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Conserved domains on  [gi|1658117666|ref|XP_018581823|]
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receptor-type tyrosine-protein phosphatase zeta-like isoform X6 [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 ...
 928-1196 3.06e-158

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


The actual alignment was detected with superfamily member cd17667:

Pssm-ID: 475123 [Multi-domain]  Cd Length: 274  Bit Score: 479.53  E-value: 3.06e-158
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  928 ECYEEIQACTVDLGITADSSIHPENKNKNRYINILAYDHSRVKLSSSSDRNGWSADYINANYVDGFTQPKAYIATQGPLK 1007
Cdd:cd17667      3 EDFEEVQRCTADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSKHSDYINANYVDGYNKAKAYIATQGPLK 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1008 SSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQEEYGSFLVTLRSTKVLAYYTQRTFTLKNTRAKKGSQ--- 1084
Cdd:cd17667     83 STFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTKVKKGQKgnp 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1085 KEQTHERTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNIL 1164
Cdd:cd17667    163 KGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVL 242

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1658117666 1165 GFLKHIRTQRNYLVQTEEQYIFIHDALVEAIL 1196
Cdd:cd17667    243 GFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 274
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 1279-1479 9.09e-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: 378.59  E-value: 9.09e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1279 YINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGlDLAEDECIYWPTKSQPIRFDTFTVTFMGEDH 1358
Cdd:cd14550      1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDN-ELNEDEPIYWPTKEKPLECETFKVTLSGEDH 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1359 MCLSNEDMLIVQDFILEATQDDYVLEVRQYRAPRWPNPDGPISNTFELINIIKEESVSRDGPIVVHDKRGGNIAGTFCAL 1438
Cdd:cd14550     80 SCLSNEIRLIVRDFILESTQDDYVLEVRQFQCPSWPNPCSPIHTVFELINTVQEWAQQRDGPIVVHDRYGGVQAATFCAL 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1658117666 1439 MTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYK 1479
Cdd:cd14550    160 TTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200
alpha_CARP_receptor_like cd03122
Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related ...
 48-301 1.87e-105

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: 335.86  E-value: 1.87e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666   48 NQNNWAKKYPSCNNA-KQSPINIDDDlSQVK-MQFQKLKLEGFEQETSNTTtIHNDGKTVAINLND---EYYISGGGLRS 122
Cdd:cd03122      1 NPKHWAKKYPACGEGrQQSPIDIVED-TQVQrQGLQPLHFDGYEELTASTT-LENTGKTVILRLEGnssDPFVSGGPLLG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  123 RFKVGRITFHWGQCNasSDGSEHSLDGIKFPLEMQIYGYeAHKFQSLDSALKDGGRLTALSVLFEVSAEDNENYVAIIDG 202
Cdd:cd03122     79 RYKFSEITFHWGTCN--SDGSEHSIDGHKFPLEMQILHR-NTDFFDSFEAIKSPGGVLALAYLFELSHEDNPFLDPIIEG 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  203 VKTVTRLGKTAVLEPFSLLGLLPNSTEKYYIYNGSLTTPPCSETVEWIVFRNTVDISDVQLETFCEVMTMQQAGyVMLMD 282
Cdd:cd03122    156 LRNVSRPGKEVELPPFPLSDLLPPFTDKYYSYEGSLTTPPCSETVEWIVFREPVPISSRQLEAFRELLTRRQDG-VMSGD 234

                          250
                   ....*....|....*....
gi 1658117666  283 YLQNNFREQQLKFVGQVFS 301
Cdd:cd03122    235 YLPNNGRPQQPLGSRTVFS 253
fn3 pfam00041
Fibronectin type III domain;
316-398 4.43e-11

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 60.51  E-value: 4.43e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  316 SEPENVEADPYNYTSLLVTWERPRAVYDVgIERYLVSYQPVGDEDlPKNEYLTDGDQDvGAIIQDLSANTSYVVQVVAVC 395
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGP-ITGYEVEYRPKNSGE-PWNEITVPGTTT-SVTLTGLKPGTEYEVRVQAVN 77


                   ...
gi 1658117666  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 ...
 928-1196 3.06e-158

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


Pssm-ID: 350505 [Multi-domain]  Cd Length: 274  Bit Score: 479.53  E-value: 3.06e-158
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  928 ECYEEIQACTVDLGITADSSIHPENKNKNRYINILAYDHSRVKLSSSSDRNGWSADYINANYVDGFTQPKAYIATQGPLK 1007
Cdd:cd17667      3 EDFEEVQRCTADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSKHSDYINANYVDGYNKAKAYIATQGPLK 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1008 SSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQEEYGSFLVTLRSTKVLAYYTQRTFTLKNTRAKKGSQ--- 1084
Cdd:cd17667     83 STFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTKVKKGQKgnp 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1085 KEQTHERTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNIL 1164
Cdd:cd17667    163 KGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVL 242

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1658117666 1165 GFLKHIRTQRNYLVQTEEQYIFIHDALVEAIL 1196
Cdd:cd17667    243 GFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 274
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 1279-1479 9.09e-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: 378.59  E-value: 9.09e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1279 YINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGlDLAEDECIYWPTKSQPIRFDTFTVTFMGEDH 1358
Cdd:cd14550      1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDN-ELNEDEPIYWPTKEKPLECETFKVTLSGEDH 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1359 MCLSNEDMLIVQDFILEATQDDYVLEVRQYRAPRWPNPDGPISNTFELINIIKEESVSRDGPIVVHDKRGGNIAGTFCAL 1438
Cdd:cd14550     80 SCLSNEIRLIVRDFILESTQDDYVLEVRQFQCPSWPNPCSPIHTVFELINTVQEWAQQRDGPIVVHDRYGGVQAATFCAL 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1658117666 1439 MTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYK 1479
Cdd:cd14550    160 TTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
919-1193 5.38e-114

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 359.67  E-value: 5.38e-114
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666   919 FSQEFEILKECYEEIQACTVdlgitadsSIHPENKNKNRYINILAYDHSRVKLSsssDRNGWSADYINANYVDGFTQPKA 998
Cdd:smart00194    2 LEEEFEKLDRLKPDDESCTV--------AAFPENRDKNRYKDVLPYDHTRVKLK---PPPGEGSDYINASYIDGPNGPKA 70

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666   999 YIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQE--EYGSFLVTLRSTKVLAYYTQRTFTLKN 1076
Cdd:smart00194   71 YIATQGPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEplTYGDITVTLKSVEKVDDYTIRTLEVTN 150

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  1077 TrakkgsqkEQTHERTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIK 1156
Cdd:smart00194  151 T--------GCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLE 222

                           250       260       270
                    ....*....|....*....|....*....|....*..
gi 1658117666  1157 EQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVE 1193
Cdd:smart00194  223 AGKEVDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
952-1193 1.97e-110

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 348.85  E-value: 1.97e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  952 NKNKNRYINILAYDHSRVKLSSSSDRNgwsaDYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNL 1031
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGPS----DYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTEL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1032 VEKGRRKCDQYWPLDSQE--EYGSFLVTLRSTK-VLAYYTQRTFTLKNTRAKkgsqkeqtHERTVVQYHYTQWPDMGVPE 1108
Cdd:pfam00102   77 EEKGREKCAQYWPEEEGEslEYGDFTVTLKKEKeDEKDYTVRTLEVSNGGSE--------ETRTVKHFHYTGWPDHGVPE 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1109 YTLPVLTFVRK-SSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFI 1187
Cdd:pfam00102  149 SPNSLLDLLRKvRKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFL 228


                   ....*.
gi 1658117666 1188 HDALVE 1193
Cdd:pfam00102  229 YDAILE 234
alpha_CARP_receptor_like cd03122
Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related ...
 48-301 1.87e-105

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: 335.86  E-value: 1.87e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666   48 NQNNWAKKYPSCNNA-KQSPINIDDDlSQVK-MQFQKLKLEGFEQETSNTTtIHNDGKTVAINLND---EYYISGGGLRS 122
Cdd:cd03122      1 NPKHWAKKYPACGEGrQQSPIDIVED-TQVQrQGLQPLHFDGYEELTASTT-LENTGKTVILRLEGnssDPFVSGGPLLG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  123 RFKVGRITFHWGQCNasSDGSEHSLDGIKFPLEMQIYGYeAHKFQSLDSALKDGGRLTALSVLFEVSAEDNENYVAIIDG 202
Cdd:cd03122     79 RYKFSEITFHWGTCN--SDGSEHSIDGHKFPLEMQILHR-NTDFFDSFEAIKSPGGVLALAYLFELSHEDNPFLDPIIEG 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  203 VKTVTRLGKTAVLEPFSLLGLLPNSTEKYYIYNGSLTTPPCSETVEWIVFRNTVDISDVQLETFCEVMTMQQAGyVMLMD 282
Cdd:cd03122    156 LRNVSRPGKEVELPPFPLSDLLPPFTDKYYSYEGSLTTPPCSETVEWIVFREPVPISSRQLEAFRELLTRRQDG-VMSGD 234

                          250
                   ....*....|....*....
gi 1658117666  283 YLQNNFREQQLKFVGQVFS 301
Cdd:cd03122    235 YLPNNGRPQQPLGSRTVFS 253
Carb_anhydrase pfam00194
Eukaryotic-type carbonic anhydrase;
47-303 8.03e-86

Eukaryotic-type carbonic anhydrase;


Pssm-ID: 459707 [Multi-domain]  Cd Length: 252  Bit Score: 280.69  E-value: 8.03e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666   47 LNQNNWAKKYPSCNNAKQSPINIDDDLSQVKMQFQKLKLEGFEQeTSNTTTIHNDGKTVAINLNDEY--YISGGGLRSRF 124
Cdd:pfam00194    1 LGPEHWGKVYPSCGGKRQSPINIDTRKVRYDPSLPPLTFQGYDV-PPGKNTLTNNGHTVQVSLDDGDpsTISGGPLATRY 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  125 KVGRITFHWGQCNasSDGSEHSLDGIKFPLEMQIYGYEAhKFQSLDSALKDGGRLTALSVLFEVSAEDNENYVAIIDGVK 204
Cdd:pfam00194   80 RLVQFHFHWGSTD--SRGSEHTIDGKRYPAELHIVHYNS-KYKSFDEAAKHPDGLAVLGVFFEVGDENNPYLQPIVSALD 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  205 TVTRLGKTAVLEPFSLLGLLPNSTEKYYIYNGSLTTPPCSETVEWIVFRNTVDISDVQLETFCEVMTMQQAGYvmlMDYL 284
Cdd:pfam00194  157 NIKYKGKSVLLPPFDLSDLLPEDLTSYYTYNGSLTTPPCSESVTWIVFKEPISISEEQLEAFRTLLFSDGGEE---PRPL 233

                          250
                   ....*....|....*....
gi 1658117666  285 QNNFREQQLKFVGQVFSSY 303
Cdd:pfam00194  234 VNNFRPTQPLNGRVVFASF 252
Carb_anhydrase smart01057
Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse ...
 41-292 2.42e-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: 2.42e-81
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666    41 WSYAGTLNQNNWAKKYPSCNNAK-QSPINIDDDLSQVKMQFQKLKlegFEQETSNTTTIHNDGKTVAINLNDE-YYISGG 118
Cdd:smart01057    1 WGYEGKNGPEHWGKLDPPFCGGKrQSPIDIVTAEAQYDPSLKPLK---LSYDQPTAKRILNNGHTVQVNFDDDgSTLSGG 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666   119 GLRSRFKVGRITFHWGQCNasSDGSEHSLDGIKFPLEMQIYGYEAHKfqSLDSALKDGGRLTALSVLFEVSAEDNENYVA 198
Cdd:smart01057   78 PLPGRYRLKQFHFHWGGSD--SEGSEHTIDGKRFPLELHLVHYNSKG--SFSEAVSKPGGLAVVAVFFKVGAEENPALQA 153

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666   199 IIDGVKTVTRLGKTAVLEPFSLLGLLPNSTEKYYIYNGSLTTPPCSETVEWIVFRNTVDISDVQLETFCEVMTMQQAgyv 278
Cdd:smart01057  154 ILDHLPLIKYKGQETELTPFDLSSLLPASTRHYYTYNGSLTTPPCSEGVTWIVFKEPITISTEQLEKFRTLLPMEGN--- 230

                           250
                    ....*....|....
gi 1658117666   279 mlmDYLQNNFREQQ 292
Cdd:smart01057  231 ---EPLVNNARPLQ 241
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1225-1482 4.07e-70

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 236.02  E-value: 4.07e-70
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  1225 LEKQFKMITQSNAKQCDYSAALKQCNRDKNRNSSLLPVERSRVHLSTTAGEISDYINASYIMGYQQSNEFIITQNPLPST 1304
Cdd:smart00194    2 LEEEFEKLDRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGPLPST 81

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  1305 MKDFWKMIWDHSTQVVIALPDGLDL-AEDECIYWPTK-SQPIRFDTFTVTFMGEDHMclsneDMLIVQDFILEATQDDYV 1382
Cdd:smart00194   82 VEDFWRMVWEQKVTVIVMLTELVEKgREKCAQYWPDEeGEPLTYGDITVTLKSVEKV-----DDYTIRTLEVTNTGCSET 156

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  1383 LEVRQYRAPRWP---NPDGPISnTFELINIIKEESVSRDGPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKM 1459
Cdd:smart00194  157 RTVTHYHYTNWPdhgVPESPES-ILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKE 235

                           250       260
                    ....*....|....*....|...
gi 1658117666  1460 INLMRPGIFTDIDQYQFLYKVIM 1482
Cdd:smart00194  236 LRSQRPGMVQTEEQYIFLYRAIL 258
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1250-1482 1.71e-63

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 215.95  E-value: 1.71e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1250 NRDKNRNSSLLPVERSRVHLSTTAGEiSDYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDL 1329
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGP-SDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1330 AEDEC-IYWPTKS-QPIRFDTFTVTFMGEDhmclSNEDMLIVQDFILEATQDDYVLEVRQYRAPRWPNPDGP--ISNTFE 1405
Cdd:pfam00102   80 GREKCaQYWPEEEgESLEYGDFTVTLKKEK----EDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPesPNSLLD 155

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1658117666 1406 LINIIKEESV-SRDGPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIM 1482
Cdd:pfam00102  156 LLRKVRKSSLdGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233
PHA02738 PHA02738
hypothetical protein; Provisional
 924-1191 6.23e-52

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 185.90  E-value: 6.23e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  924 EILKECYEEIQACTVDLGITADSsihpENKNKNRYINILAYDHSRVKLSSSSDRngwsADYINANYVDGFTQPKAYIATQ 1003
Cdd:PHA02738    25 EVITREHQKVISEKVDGTFNAEK----KNRKLNRYLDAVCFDHSRVILPAERNR----GDYINANYVDGFEYKKKFICGQ 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1004 GPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQEE--YGSFLVTLRSTKVLAYYTQRTFTLKNtrakk 1081
Cdd:PHA02738    97 APTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDVEQGSirFGKFKITTTQVETHPHYVKSTLLLTD----- 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1082 GSQKEQtherTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQA-------------NLGNMGPVVVHCSAGVGRTGTYIVL 1148
Cdd:PHA02738   172 GTSATQ----TVTHFNFTAWPDHDVPKNTSEFLNFVLEVRQCqkelaqeslqighNRLQPPPIVVHCNAGLGRTPCYCVV 247

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1658117666 1149 DSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDAL 1191
Cdd:PHA02738   248 DISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAV 290
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
950-1187 2.72e-43

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 159.87  E-value: 2.72e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  950 PENKNKNRYINILAYDHSRVklsSSSDRngwsadYINANYVDGfTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMIT 1029
Cdd:COG5599     40 INGSPLNRFRDIQPYKETAL---RANLG------YLNANYIQV-IGNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLA 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1030 NLVE--KGRRKCDQYWPLDsqEEYGSFLVTLRSTKVLAYYTQ---RTFTLKntraKKGSQKEQtheRTVVQYHYTQWPDM 1104
Cdd:COG5599    110 SDDEisKPKVKMPVYFRQD--GEYGKYEVSSELTESIQLRDGieaRTYVLT----IKGTGQKK---IEIPVLHVKNWPDH 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1105 GVP--EYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKE--QGTVNILGFLKHIRTQRNY-LVQ 1179
Cdd:COG5599    181 GAIsaEALKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINAlvQITLSVEEIVIDMRTSRNGgMVQ 260


                   ....*...
gi 1658117666 1180 TEEQYIFI 1187
Cdd:COG5599    261 TSEQLDVL 268
Cah COG3338
Carbonic anhydrase [Inorganic ion transport and metabolism];
36-266 4.25e-33

Carbonic anhydrase [Inorganic ion transport and metabolism];


Pssm-ID: 442567 [Multi-domain]  Cd Length: 247  Bit Score: 129.23  E-value: 4.25e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666   36 KEDIDWSYAGTLNQNNWAK---KYPSCNNAK-QSPINIDD----DLSQVKMQFQKLKLEgfeqetsntttIHNDGKTVAI 107
Cdd:COG3338     23 ASAPHWSYEGETGPEHWGElspEFATCATGKnQSPIDIRTaikaDLPPLKFDYKPTPLE-----------IVNNGHTIQV 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  108 NLNDEYYISGGGlrSRFKVGRITFHwgqcnassDGSEHSLDGIKFPLEMQIygyeAHKfqsldsalKDGGRLTALSVLFE 187
Cdd:COG3338     92 NVDPGSTLTVDG--KRYELKQFHFH--------TPSEHTINGKSYPMEAHL----VHK--------DADGELAVVGVLFE 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  188 VSAEdNENYVAIIDGVKTvtRLGKTAVL-EPFSLLGLLPNSTEkYYIYNGSLTTPPCSETVEWIVFRNTVDISDVQLETF 266
Cdd:COG3338    150 EGAE-NPALAKLWANLPL--EAGEEVALdATIDLNDLLPEDRS-YYRYSGSLTTPPCSEGVLWIVLKQPITVSAEQIEAF 225
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 1243-1481 1.12e-25

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 109.73  E-value: 1.12e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1243 SAALKQCNRDKNRNSSLLPVERSRVHLS--------------------TTAGEISDYINASYIMGYQQSNEFIITQNPLP 1302
Cdd:PHA02746    44 NHFLKKENLKKNRFHDIPCWDHSRVVINaheslkmfdvgdsdgkkievTSEDNAENYIHANFVDGFKEANKFICAQGPKE 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1303 STMKDFWKMIWDHSTQVVIALPDGLDLAEDECIYWPT-KSQPIRFDTFTVTFMGEDHMCLSNEDMLIVQDFILEATQddy 1381
Cdd:PHA02746   124 DTSEDFFKLISEHESQVIVSLTDIDDDDEKCFELWTKeEDSELAFGRFVAKILDIIEELSFTKTRLMITDKISDTSR--- 200

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1382 vlEVRQYRAPRWP---NPDGPiSNTFELINIIKEESV----------SRDGPIVVHDKRGGNIAGTFCALMTLLHQLEME 1448
Cdd:PHA02746   201 --EIHHFWFPDWPdngIPTGM-AEFLELINKVNEEQAelikqadndpQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKE 277

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1658117666 1449 SSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVI 1481
Cdd:PHA02746   278 KEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
fn3 pfam00041
Fibronectin type III domain;
316-398 4.43e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 60.51  E-value: 4.43e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  316 SEPENVEADPYNYTSLLVTWERPRAVYDVgIERYLVSYQPVGDEDlPKNEYLTDGDQDvGAIIQDLSANTSYVVQVVAVC 395
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGP-ITGYEVEYRPKNSGE-PWNEITVPGTTT-SVTLTGLKPGTEYEVRVQAVN 77


                   ...
gi 1658117666  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 1.57e-08

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 53.00  E-value: 1.57e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666   316 SEPENVEADPYNYTSLLVTWERPRavyDVGIERYLVSYQPVGDEDLPKNEYLTDGDQDVGAIIQDLSANTSYVVQVVAVC 395
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPP---DDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78


                    ...
gi 1658117666   396 ING 398
Cdd:smart00060   79 GAG 81
PLN02179 PLN02179
carbonic anhydrase
 52-263 2.41e-08

carbonic anhydrase


Pssm-ID: 177835  Cd Length: 235  Bit Score: 56.53  E-value: 2.41e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666   52 WAKKYPS---CNNAK-QSPINIDDDLSQVkMQFQKLKlegfEQETSNTTTIHNDGKTVAINLNDEyyisggglrsrfkVG 127
Cdd:PLN02179    50 WGKLNPQwkvCSTGKyQSPIDLTDERVSL-IHDQALS----RHYKPAPAVIQSRGHDVMVSWKGD-------------AG 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  128 RITFHWG-----QCNASSDgSEHSLDGIKFPLEMQIYGYEAHkfqsldsalkdgGRLTALSVLFEVsAEDNENYVAIIDG 202
Cdd:PLN02179   112 KITIHQTdyklvQCHWHSP-SEHTINGTSYDLELHMVHTSAS------------GKTAVVGVLYKL-GEPDEFLTKLLNG 177

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1658117666  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 1.13e-07

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 50.96  E-value: 1.13e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  316 SEPENVEADPYNYTSLLVTWERPRAvYDVGIERYLVSYQPVGDEDLpkNEYLTDGDQDVGAIIQDLSANTSYVVQVVAVC 395
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPPED-DGGPITGYVVEYREKGSGDW--KEVEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78


                   ...
gi 1658117666  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 ...
 928-1196 3.06e-158

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


Pssm-ID: 350505 [Multi-domain]  Cd Length: 274  Bit Score: 479.53  E-value: 3.06e-158
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  928 ECYEEIQACTVDLGITADSSIHPENKNKNRYINILAYDHSRVKLSSSSDRNGWSADYINANYVDGFTQPKAYIATQGPLK 1007
Cdd:cd17667      3 EDFEEVQRCTADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSKHSDYINANYVDGYNKAKAYIATQGPLK 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1008 SSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQEEYGSFLVTLRSTKVLAYYTQRTFTLKNTRAKKGSQ--- 1084
Cdd:cd17667     83 STFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTKVKKGQKgnp 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1085 KEQTHERTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNIL 1164
Cdd:cd17667    163 KGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVL 242

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1658117666 1165 GFLKHIRTQRNYLVQTEEQYIFIHDALVEAIL 1196
Cdd:cd17667    243 GFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 274
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 984-1192 3.89e-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: 423.24  E-value: 3.89e-138
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  984 YINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQEEYGSFLVTLRSTKV 1063
Cdd:cd17668      1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1064 LAYYTQRTFTLKNTRAKKGSQKEQTHERTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVGRTG 1143
Cdd:cd17668     81 LAYYTVRNFTLRNTKIKKGSQKGRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVGPVVVHCSAGVGRTG 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1658117666 1144 TYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALV 1192
Cdd:cd17668    161 TYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 984-1189 2.46e-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: 420.99  E-value: 2.46e-137
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  984 YINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQEEYGSFLVTLRSTKV 1063
Cdd:cd14549      1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTETYGNIQVTLLSTEV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1064 LAYYTQRTFTLKNTRAKKGsqKEQTHERTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVGRTG 1143
Cdd:cd14549     81 LATYTVRTFSLKNLKLKKV--KGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAGVGRTG 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1658117666 1144 TYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHD 1189
Cdd:cd14549    159 TYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 1279-1479 9.09e-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: 378.59  E-value: 9.09e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1279 YINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGlDLAEDECIYWPTKSQPIRFDTFTVTFMGEDH 1358
Cdd:cd14550      1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDN-ELNEDEPIYWPTKEKPLECETFKVTLSGEDH 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1359 MCLSNEDMLIVQDFILEATQDDYVLEVRQYRAPRWPNPDGPISNTFELINIIKEESVSRDGPIVVHDKRGGNIAGTFCAL 1438
Cdd:cd14550     80 SCLSNEIRLIVRDFILESTQDDYVLEVRQFQCPSWPNPCSPIHTVFELINTVQEWAQQRDGPIVVHDRYGGVQAATFCAL 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1658117666 1439 MTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYK 1479
Cdd:cd14550    160 TTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 1279-1482 4.33e-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: 374.33  E-value: 4.33e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1279 YINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDECIYWPTKSQPIRFDTFTVTFMGEDH 1358
Cdd:cd17669      1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFVYWPNKDEPINCETFKVTLIAEEH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1359 MCLSNEDMLIVQDFILEATQDDYVLEVRQYRAPRWPNPDGPISNTFELINIIKEESVSRDGPIVVHDKRGGNIAGTFCAL 1438
Cdd:cd17669     81 KCLSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTFELISIIKEEAANRDGPMIVHDEHGGVTAGTFCAL 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1658117666 1439 MTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIM 1482
Cdd:cd17669    161 TTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
919-1193 5.38e-114

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 359.67  E-value: 5.38e-114
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666   919 FSQEFEILKECYEEIQACTVdlgitadsSIHPENKNKNRYINILAYDHSRVKLSsssDRNGWSADYINANYVDGFTQPKA 998
Cdd:smart00194    2 LEEEFEKLDRLKPDDESCTV--------AAFPENRDKNRYKDVLPYDHTRVKLK---PPPGEGSDYINASYIDGPNGPKA 70

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666   999 YIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQE--EYGSFLVTLRSTKVLAYYTQRTFTLKN 1076
Cdd:smart00194   71 YIATQGPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEplTYGDITVTLKSVEKVDDYTIRTLEVTN 150

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  1077 TrakkgsqkEQTHERTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIK 1156
Cdd:smart00194  151 T--------GCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLE 222

                           250       260       270
                    ....*....|....*....|....*....|....*..
gi 1658117666  1157 EQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVE 1193
Cdd:smart00194  223 AGKEVDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
952-1193 1.97e-110

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 348.85  E-value: 1.97e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  952 NKNKNRYINILAYDHSRVKLSSSSDRNgwsaDYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNL 1031
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGPS----DYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTEL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1032 VEKGRRKCDQYWPLDSQE--EYGSFLVTLRSTK-VLAYYTQRTFTLKNTRAKkgsqkeqtHERTVVQYHYTQWPDMGVPE 1108
Cdd:pfam00102   77 EEKGREKCAQYWPEEEGEslEYGDFTVTLKKEKeDEKDYTVRTLEVSNGGSE--------ETRTVKHFHYTGWPDHGVPE 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1109 YTLPVLTFVRK-SSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFI 1187
Cdd:pfam00102  149 SPNSLLDLLRKvRKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFL 228


                   ....*.
gi 1658117666 1188 HDALVE 1193
Cdd:pfam00102  229 YDAILE 234
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 1279-1483 2.04e-109

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: 344.74  E-value: 2.04e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1279 YINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDECIYWPTKSQPIRFDTFTVTFMGEDH 1358
Cdd:cd17670      1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQGLAEDEFVYWPSREESMNCEAFTVTLISKDR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1359 MCLSNEDMLIVQDFILEATQDDYVLEVRQYRAPRWPNPDGPISNTFELINIIKEESVSRDGPIVVHDKRGGNIAGTFCAL 1438
Cdd:cd17670     81 LCLSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISSTFELINVIKEEALTRDGPTIVHDEFGAVSAGTLCAL 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1658117666 1439 MTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIMS 1483
Cdd:cd17670    161 TTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAMLS 205
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 952-1197 3.89e-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: 345.54  E-value: 3.89e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  952 NKNKNRYINILAYDHSRVKLSSSSDRNGwsADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNL 1031
Cdd:cd14553      3 NKPKNRYANVIAYDHSRVILQPIEGVPG--SDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1032 VEKGRRKCDQYWPLDSQEEYGSFLVTLRSTKVLAYYTQRTFTLKntraKKGSqkeqTHERTVVQYHYTQWPDMGVPEYTL 1111
Cdd:cd14553     81 EERSRVKCDQYWPTRGTETYGLIQVTLLDTVELATYTVRTFALH----KNGS----SEKREVRQFQFTAWPDHGVPEHPT 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1112 PVLTFVRKSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDAL 1191
Cdd:cd14553    153 PFLAFLRRVKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDAL 232


                   ....*.
gi 1658117666 1192 VEAILS 1197
Cdd:cd14553    233 LEAVTC 238
alpha_CARP_receptor_like cd03122
Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related ...
 48-301 1.87e-105

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: 335.86  E-value: 1.87e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666   48 NQNNWAKKYPSCNNA-KQSPINIDDDlSQVK-MQFQKLKLEGFEQETSNTTtIHNDGKTVAINLND---EYYISGGGLRS 122
Cdd:cd03122      1 NPKHWAKKYPACGEGrQQSPIDIVED-TQVQrQGLQPLHFDGYEELTASTT-LENTGKTVILRLEGnssDPFVSGGPLLG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  123 RFKVGRITFHWGQCNasSDGSEHSLDGIKFPLEMQIYGYeAHKFQSLDSALKDGGRLTALSVLFEVSAEDNENYVAIIDG 202
Cdd:cd03122     79 RYKFSEITFHWGTCN--SDGSEHSIDGHKFPLEMQILHR-NTDFFDSFEAIKSPGGVLALAYLFELSHEDNPFLDPIIEG 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  203 VKTVTRLGKTAVLEPFSLLGLLPNSTEKYYIYNGSLTTPPCSETVEWIVFRNTVDISDVQLETFCEVMTMQQAGyVMLMD 282
Cdd:cd03122    156 LRNVSRPGKEVELPPFPLSDLLPPFTDKYYSYEGSLTTPPCSETVEWIVFREPVPISSRQLEAFRELLTRRQDG-VMSGD 234

                          250
                   ....*....|....*....
gi 1658117666  283 YLQNNFREQQLKFVGQVFS 301
Cdd:cd03122    235 YLPNNGRPQQPLGSRTVFS 253
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 984-1189 3.23e-94

catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. The depth of the active site cleft renders the enzyme specific for phosphorylated Tyr (pTyr) residues, instead of pSer or pThr. This family has a distinctive active site signature motif, HCSAGxGRxG, and are characterized as either transmembrane, receptor-like or non-transmembrane (soluble) PTPs. Receptor-like PTP domains tend to occur in two copies in the cytoplasmic region of the transmembrane proteins, only one copy may be active.


Pssm-ID: 350343 [Multi-domain]  Cd Length: 200  Bit Score: 302.28  E-value: 3.23e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  984 YINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQE--EYGSFLVTLRST 1061
Cdd:cd00047      1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKplEYGDITVTLVSE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1062 KVLAYYTQRTFTLKNTRAKKgsqkeqthERTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVGR 1141
Cdd:cd00047     81 EELSDYTIRTLELSPKGCSE--------SREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCSAGVGR 152

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1658117666 1142 TGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHD 1189
Cdd:cd00047    153 TGTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 914-1195 2.46e-93

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: 303.11  E-value: 2.46e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  914 HDSNTFSQEFEilkecyeeiqacTVDLG--ITADSSIHPENKNKNRYINILAYDHSRVKLSSSSDRNGwsADYINANYVD 991
Cdd:cd14626     13 NDGLKFSQEYE------------SIDPGqqFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPG--SDYINANYID 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  992 GFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQEEYGSFLVTLRSTKVLAYYTQRT 1071
Cdd:cd14626     79 GYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIRGTETYGMIQVTLLDTVELATYSVRT 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1072 FTLKntraKKGSqkeqTHERTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSM 1151
Cdd:cd14626    159 FALY----KNGS----SEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVIDAM 230

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1658117666 1152 LRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVEAI 1195
Cdd:cd14626    231 LERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLEAA 274
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 957-1188 8.06e-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: 290.80  E-value: 8.06e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  957 RYINILAYDHSRVKLSSSSDRNGwsADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGR 1036
Cdd:cd14548      1 RYTNILPYDHSRVKLIPINEEEG--SDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGR 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1037 RKCDQYWPLDSQE-EYGSFLVTLRSTKVLAYYTQRTFTLKNTRAkkgsqkeqthERTVVQYHYTQWPDMGVPEYTLPVLT 1115
Cdd:cd14548     79 VKCDHYWPFDQDPvYYGDITVTMLSESVLPDWTIREFKLERGDE----------VRSVRQFHFTAWPDHGVPEAPDSLLR 148

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1658117666 1116 FVRKSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIH 1188
Cdd:cd14548    149 FVRLVRDYIKQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLH 221
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 925-1188 4.22e-89

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: 290.81  E-value: 4.22e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  925 ILKEcYEEIQACTVdlGITADSSIHPENKNKNRYINILAYDHSRVKLSS-SSDRNgwsADYINANYVDGFTQPKAYIATQ 1003
Cdd:cd14543      5 IYEE-YEDIRREPP--AGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPKrNGDER---TDYINANFMDGYKQKNAYIATQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1004 GPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLD--SQEEYGSFLVTLRSTKVLAYYTQRTFTLKNTrakk 1081
Cdd:cd14543     79 GPLPKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEegSSLRYGDLTVTNLSVENKEHYKKTTLEIHNT---- 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1082 gsqkeQTHE-RTVVQYHYTQWPDMGVPEYTLPVLTF---VRKSSQANLGNMG----------PVVVHCSAGVGRTGTYIV 1147
Cdd:cd14543    155 -----ETDEsRQVTHFQFTSWPDFGVPSSAAALLDFlgeVRQQQALAVKAMGdrwkghppgpPIVVHCSAGIGRTGTFCT 229

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1658117666 1148 LDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIH 1188
Cdd:cd14543    230 LDICLSQLEDVGTLNVMQTVRRMRTQRAFSIQTPDQYYFCY 270
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 898-1195 1.18e-86

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: 284.29  E-value: 1.18e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  898 HEALPIKQFVKHVAEL--HDSNTFSQEFEilkecyeeiqacTVDLG--ITADSSIHPENKNKNRYINILAYDHSRVKLSS 973
Cdd:cd14625      1 HPPIPISELAEHTERLkaNDNLKLSQEYE------------SIDPGqqFTWEHSNLEVNKPKNRYANVIAYDHSRVILQP 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  974 SSDRNGwsADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQEEYGS 1053
Cdd:cd14625     69 IEGIMG--SDYINANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSRGTETYGM 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1054 FLVTLRSTKVLAYYTQRTFTLKntraKKGSqkeqTHERTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVV 1133
Cdd:cd14625    147 IQVTLLDTIELATFCVRTFSLH----KNGS----SEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPPDAGPIVV 218

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1658117666 1134 HCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVEAI 1195
Cdd:cd14625    219 HCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEAV 280
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 898-1195 5.65e-86

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: 282.39  E-value: 5.65e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  898 HEALPIKQFVKHVAEL--HDSNTFSQEFEilkecyeeiqacTVDLG--ITADSSIHPENKNKNRYINILAYDHSRVKLSS 973
Cdd:cd14624      1 HPPIPILELADHIERLkaNDNLKFSQEYE------------SIDPGqqFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSA 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  974 SSDRNGwsADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQEEYGS 1053
Cdd:cd14624     69 IEGIPG--SDYINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSRGTETYGL 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1054 FLVTLRSTKVLAYYTQRTFTLkntrAKKGSqkeqTHERTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVV 1133
Cdd:cd14624    147 IQVTLLDTVELATYCVRTFAL----YKNGS----SEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPPDAGPMVV 218

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1658117666 1134 HCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVEAI 1195
Cdd:cd14624    219 HCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLEAV 280
Carb_anhydrase pfam00194
Eukaryotic-type carbonic anhydrase;
47-303 8.03e-86

Eukaryotic-type carbonic anhydrase;


Pssm-ID: 459707 [Multi-domain]  Cd Length: 252  Bit Score: 280.69  E-value: 8.03e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666   47 LNQNNWAKKYPSCNNAKQSPINIDDDLSQVKMQFQKLKLEGFEQeTSNTTTIHNDGKTVAINLNDEY--YISGGGLRSRF 124
Cdd:pfam00194    1 LGPEHWGKVYPSCGGKRQSPINIDTRKVRYDPSLPPLTFQGYDV-PPGKNTLTNNGHTVQVSLDDGDpsTISGGPLATRY 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  125 KVGRITFHWGQCNasSDGSEHSLDGIKFPLEMQIYGYEAhKFQSLDSALKDGGRLTALSVLFEVSAEDNENYVAIIDGVK 204
Cdd:pfam00194   80 RLVQFHFHWGSTD--SRGSEHTIDGKRYPAELHIVHYNS-KYKSFDEAAKHPDGLAVLGVFFEVGDENNPYLQPIVSALD 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  205 TVTRLGKTAVLEPFSLLGLLPNSTEKYYIYNGSLTTPPCSETVEWIVFRNTVDISDVQLETFCEVMTMQQAGYvmlMDYL 284
Cdd:pfam00194  157 NIKYKGKSVLLPPFDLSDLLPEDLTSYYTYNGSLTTPPCSESVTWIVFKEPISISEEQLEAFRTLLFSDGGEE---PRPL 233

                          250
                   ....*....|....*....
gi 1658117666  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 ...
 951-1196 3.70e-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: 269.59  E-value: 3.70e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  951 ENKNKNRYINILAYDHSRVKLSSSSDRNgwSADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITN 1030
Cdd:cd14630      2 ENRNKNRYGNIISYDHSRVRLQLLDGDP--HSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTN 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1031 LVEKGRRKCDQYWPlDSQEEYGSFLVTLRSTKVLAYYTQRTFTLkntrakkgsQKEQTHE-RTVVQYHYTQWPDMGVPEY 1109
Cdd:cd14630     80 LVEVGRVKCVRYWP-DDTEVYGDIKVTLIETEPLAEYVIRTFTV---------QKKGYHEiREIRQFHFTSWPDHGVPCY 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1110 TLPVLTFVRKSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHD 1189
Cdd:cd14630    150 ATGLLGFVRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHD 229


                   ....*..
gi 1658117666 1190 ALVEAIL 1196
Cdd:cd14630    230 AILEACL 236
Carb_anhydrase smart01057
Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse ...
 41-292 2.42e-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: 2.42e-81
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666    41 WSYAGTLNQNNWAKKYPSCNNAK-QSPINIDDDLSQVKMQFQKLKlegFEQETSNTTTIHNDGKTVAINLNDE-YYISGG 118
Cdd:smart01057    1 WGYEGKNGPEHWGKLDPPFCGGKrQSPIDIVTAEAQYDPSLKPLK---LSYDQPTAKRILNNGHTVQVNFDDDgSTLSGG 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666   119 GLRSRFKVGRITFHWGQCNasSDGSEHSLDGIKFPLEMQIYGYEAHKfqSLDSALKDGGRLTALSVLFEVSAEDNENYVA 198
Cdd:smart01057   78 PLPGRYRLKQFHFHWGGSD--SEGSEHTIDGKRFPLELHLVHYNSKG--SFSEAVSKPGGLAVVAVFFKVGAEENPALQA 153

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666   199 IIDGVKTVTRLGKTAVLEPFSLLGLLPNSTEKYYIYNGSLTTPPCSETVEWIVFRNTVDISDVQLETFCEVMTMQQAgyv 278
Cdd:smart01057  154 ILDHLPLIKYKGQETELTPFDLSSLLPASTRHYYTYNGSLTTPPCSEGVTWIVFKEPITISTEQLEKFRTLLPMEGN--- 230

                           250
                    ....*....|....
gi 1658117666   279 mlmDYLQNNFREQQ 292
Cdd:smart01057  231 ---EPLVNNARPLQ 241
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 956-1187 2.98e-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: 255.13  E-value: 2.98e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  956 NRYINILAYDHSRVKLSSSSDRngwSADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKG 1035
Cdd:cd14615      1 NRYNNVLPYDISRVKLSVQSHS---TDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1036 RRKCDQYWPLDSQEEYGSFLVTLRSTKVLAYYTQRTFTLKNTrakkgsqkeQTHE-RTVVQYHYTQWPDMGVPEYTLPVL 1114
Cdd:cd14615     78 RTKCEEYWPSKQKKDYGDITVTMTSEIVLPEWTIRDFTVKNA---------QTNEsRTVRHFHFTSWPDHGVPETTDLLI 148

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1658117666 1115 TF---VRKSSQANLGNmGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFI 1187
Cdd:cd14615    149 NFrhlVREYMKQNPPN-SPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFL 223
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 945-1196 1.22e-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: 255.35  E-value: 1.22e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  945 DSSIHPENKNKNRYINILAYDHSRVKLSSSSDRNGwsADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASV 1024
Cdd:cd14633     33 DSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETS--SDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTAS 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1025 IVMITNLVEKGRRKCDQYWPlDSQEEYGSFLVTLRSTKVLAYYTQRTFTLkntrakkgsQKEQTHE-RTVVQYHYTQWPD 1103
Cdd:cd14633    111 IIMVTNLVEVGRVKCCKYWP-DDTEIYKDIKVTLIETELLAEYVIRTFAV---------EKRGVHEiREIRQFHFTGWPD 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1104 MGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQ 1183
Cdd:cd14633    181 HGVPYHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQ 260

                          250
                   ....*....|...
gi 1658117666 1184 YIFIHDALVEAIL 1196
Cdd:cd14633    261 YVFIHDAILEACL 273
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 984-1196 2.91e-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: 251.37  E-value: 2.91e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  984 YINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSqEEYGSFLVTLRSTKV 1063
Cdd:cd14555      1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDDT-EVYGDIKVTLVETEP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1064 LAYYTQRTFTLkntrakkgsQKEQTHE-RTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVGRT 1142
Cdd:cd14555     80 LAEYVVRTFAL---------ERRGYHEiREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAGPIVVHCSAGAGRT 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1658117666 1143 GTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVEAIL 1196
Cdd:cd14555    151 GCYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILEACL 204
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 956-1188 1.07e-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: 250.99  E-value: 1.07e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  956 NRYINILAYDHSRVKLSSSSDRNGwsADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKG 1035
Cdd:cd14617      1 NRYNNILPYDSTRVKLSNVDDDPC--SDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1036 RRKCDQYWPLDSQE-EYGSFLVTLRSTKVLAYYTQRTFtlkntraKKGSQKEQTHERTVVQYHYTQWPDMGVPEYTLPVL 1114
Cdd:cd14617     79 RVKCDHYWPADQDSlYYGDLIVQMLSESVLPEWTIREF-------KICSEEQLDAPRLVRHFHYTVWPDHGVPETTQSLI 151

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1658117666 1115 TFVR--KSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIH 1188
Cdd:cd14617    152 QFVRtvRDYINRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 227
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 956-1195 2.36e-75

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


Pssm-ID: 350467 [Multi-domain]  Cd Length: 233  Bit Score: 250.19  E-value: 2.36e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  956 NRYINILAYDHSRVKLSSSSDRNGwsADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKG 1035
Cdd:cd14619      1 NRFRNVLPYDWSRVPLKPIHEEPG--SDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1036 RRKCDQYWPLDSQE-EYGSFLVTLRSTKVLAYYTQRTFTLKNtrakkgsqKEQTHERTVVQYHYTQWPDMGVPEYTLPVL 1114
Cdd:cd14619     79 RVKCEHYWPLDYTPcTYGHLRVTVVSEEVMENWTVREFLLKQ--------VEEQKTLSVRHFHFTAWPDHGVPSSTDTLL 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1115 TFVRKSSQANLGNM--GPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALV 1192
Cdd:cd14619    151 AFRRLLRQWLDQTMsgGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCIL 230


                   ...
gi 1658117666 1193 EAI 1195
Cdd:cd14619    231 DFL 233
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 915-1202 2.69e-75

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: 252.25  E-value: 2.69e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  915 DSNTFSQEFEILKECyeEIQActvdlgiTADSSIHPENKNKNRYINILAYDHSRVKLSSSSDRNgwSADYINANYVDGFT 994
Cdd:cd14621     24 DNKLFREEFNALPAC--PIQA-------TCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVP--DSDYINASFINGYQ 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  995 QPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQEEYGSFLVTLRSTKVLAYYTQRTFTL 1074
Cdd:cd14621     93 EKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQGCWTYGNIRVSVEDVTVLVDYTVRKFCI 172

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1075 KNTrakkGSQKEQTHERTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQ 1154
Cdd:cd14621    173 QQV----GDVTNKKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFIVIDAMLDM 248

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1658117666 1155 IKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVEAILSKETEV 1202
Cdd:cd14621    249 MHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEHYLYGDTEL 296
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 956-1188 1.39e-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: 1.39e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  956 NRYINILAYDHSRVKLSSSSdrNGWSADYINANYVDGFT-QPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEK 1034
Cdd:cd14547      1 NRYKTILPNEHSRVCLPSVD--DDPLSSYINANYIRGYDgEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1035 gRRKCDQYWPLDSQEEYGSFLVTLRSTKVLAYYTQRTFTLKNtrakkgsqkeQTHERTVVQYHYTQWPDMGVPEYTLPVL 1114
Cdd:cd14547     79 -KEKCAQYWPEEENETYGDFEVTVQSVKETDGYTVRKLTLKY----------GGEKRYLKHYWYTSWPDHKTPEAAQPLL 147

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1658117666 1115 TFVRKSSQA--NLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIH 1188
Cdd:cd14547    148 SLVQEVEEArqTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVH 223
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 952-1195 3.18e-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: 244.68  E-value: 3.18e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  952 NKNKNRYINILAYDHSRVKLSSSsDRNGWSADYINANYV-------DGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASV 1024
Cdd:cd14544      1 NKGKNRYKNILPFDHTRVILKDR-DPNVPGSDYINANYIrnenegpTTDENAKTYIATQGCLENTVSDFWSMVWQENSRV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1025 IVMITNLVEKGRRKCDQYWP-LDSQEEYGSFLVTLRSTKVLAYYTQRTFTLKNTrakkgsqKEQTHERTVVQYHYTQWPD 1103
Cdd:cd14544     80 IVMTTKEVERGKNKCVRYWPdEGMQKQYGPYRVQNVSEHDTTDYTLRELQVSKL-------DQGDPIREIWHYQYLSWPD 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1104 MGVPEYTLPVLTFVRK--SSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQG---TVNILGFLKHIRTQRNYLV 1178
Cdd:cd14544    153 HGVPSDPGGVLNFLEDvnQRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGldcDIDIQKTIQMVRSQRSGMV 232

                          250
                   ....*....|....*..
gi 1658117666 1179 QTEEQYIFIHDALVEAI 1195
Cdd:cd14544    233 QTEAQYKFIYVAVAQYI 249
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 950-1188 1.03e-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: 240.18  E-value: 1.03e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  950 PENKNKNRYINILAYDHSRVKLSSSSDRNGwsADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMIT 1029
Cdd:cd14614     10 PVNRCKNRYTNILPYDFSRVKLVSMHEEEG--SDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLT 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1030 NLVEKGRRKCDQYWPLDSQE-EYGSFLVTLRSTKVLAYYTQRTFTLkntrakkgSQKEQTHErtVVQYHYTQWPDMGVPE 1108
Cdd:cd14614     88 QCNEKRRVKCDHYWPFTEEPvAYGDITVEMLSEEEQPDWAIREFRV--------SYADEVQD--VMHFNYTAWPDHGVPT 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1109 YTL--PVLTFVRKSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIF 1186
Cdd:cd14614    158 ANAaeSILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIF 237


                   ..
gi 1658117666 1187 IH 1188
Cdd:cd14614    238 IH 239
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 981-1196 2.09e-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: 2.09e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  981 SADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPlDSQEEYGSFLVTLRS 1060
Cdd:cd14631     12 SSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWP-DDTEVYGDFKVTCVE 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1061 TKVLAYYTQRTFTLKntraKKGSQKEqtheRTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVG 1140
Cdd:cd14631     91 MEPLAEYVVRTFTLE----RRGYNEI----REVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVHCSAGAG 162

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1658117666 1141 RTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVEAIL 1196
Cdd:cd14631    163 RTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACL 218
alpha_CA cd00326
Carbonic anhydrase alpha (vertebrate-like) group. Carbonic anhydrases (CAs) are ...
 63-292 9.59e-71

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: 236.41  E-value: 9.59e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666   63 KQSPINIDDDLSQVKMQFQKLKLEGFEQETsntTTIHNDGKTVAINLNDE-YYISGGGLRSRFKVGRITFHWGQCNasSD 141
Cdd:cd00326      3 RQSPINIVTSAVVYDPSLPPLNFDYYPTTS---LTLVNNGHTVQVNFDDDgGTLSGGGLPGRYKLVQFHFHWGSEN--SP 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  142 GSEHSLDGIKFPLEMQIYGYEAHKFQSldSALKDGGRLTALSVLFEVSAEDNENYVAIIDGVKTVTRLGKTAVLEPFSLL 221
Cdd:cd00326     78 GSEHTIDGKRYPLELHLVHYNSDYYSS--EAAKKPGGLAVLGVFFEVGEKENPFLKKILDALPKIKYKGKETTLPPFDLS 155

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1658117666  222 GLLPNSTEKYYIYNGSLTTPPCSETVEWIVFRNTVDISDVQLETFCEVMTMQqagyvmlMDYLQNNFREQQ 292
Cdd:cd00326    156 DLLPSSLRDYYTYEGSLTTPPCSEGVTWIVFKEPITISKEQLEAFRSLLDRE-------GKPLVNNYRPVQ 219
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 956-1192 2.38e-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: 2.38e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  956 NRYINILAYDHSRVKLSSSSDRNgwSADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKG 1035
Cdd:cd14618      1 NRYPHVLPYDHSRVRLSQLGGEP--HSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1036 RRKCDQYWPLDSQE-EYGSFLVTLRSTKVLAYYTQRTFTLKNTRAKKgsqkeqthERTVVQYHYTQWPDMGVPEYTLPVL 1114
Cdd:cd14618     79 RVLCDHYWPSESTPvSYGHITVHLLAQSSEDEWTRREFKLWHEDLRK--------ERRVKHLHYTAWPDHGIPESTSSLM 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1115 TF---VRKSSQANLGNmGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDAL 1191
Cdd:cd14618    151 AFrelVREHVQATKGK-GPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCI 229


                   .
gi 1658117666 1192 V 1192
Cdd:cd14618    230 L 230
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1225-1482 4.07e-70

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 236.02  E-value: 4.07e-70
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  1225 LEKQFKMITQSNAKQCDYSAALKQCNRDKNRNSSLLPVERSRVHLSTTAGEISDYINASYIMGYQQSNEFIITQNPLPST 1304
Cdd:smart00194    2 LEEEFEKLDRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGPLPST 81

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  1305 MKDFWKMIWDHSTQVVIALPDGLDL-AEDECIYWPTK-SQPIRFDTFTVTFMGEDHMclsneDMLIVQDFILEATQDDYV 1382
Cdd:smart00194   82 VEDFWRMVWEQKVTVIVMLTELVEKgREKCAQYWPDEeGEPLTYGDITVTLKSVEKV-----DDYTIRTLEVTNTGCSET 156

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  1383 LEVRQYRAPRWP---NPDGPISnTFELINIIKEESVSRDGPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKM 1459
Cdd:smart00194  157 RTVTHYHYTNWPdhgVPESPES-ILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKE 235

                           250       260
                    ....*....|....*....|...
gi 1658117666  1460 INLMRPGIFTDIDQYQFLYKVIM 1482
Cdd:smart00194  236 LRSQRPGMVQTEEQYIFLYRAIL 258
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 984-1196 4.40e-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: 4.40e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  984 YINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPlDSQEEYGSFLVTLRSTKV 1063
Cdd:cd14632      1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWP-DDSDTYGDIKITLLKTET 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1064 LAYYTQRTFTLKntraKKGSQKEqtHErtVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVGRTG 1143
Cdd:cd14632     80 LAEYSVRTFALE----RRGYSAR--HE--VKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTG 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1658117666 1144 TYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVEAIL 1196
Cdd:cd14632    152 CYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILEACL 204
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 958-1193 8.92e-70

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: 234.06  E-value: 8.92e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  958 YINILAYDHSRVKLSSSSdrNGWSADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRR 1037
Cdd:cd14620      1 YPNILPYDHSRVILSQLD--GIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1038 KCDQYWPLDSQEEYGSFLVTLRSTKVLAYYTQRTFTLKnTRAKKGSQKEqtheRTVVQYHYTQWPDMGVPEYTLPVLTFV 1117
Cdd:cd14620     79 KCYQYWPDQGCWTYGNIRVAVEDCVVLVDYTIRKFCIQ-PQLPDGCKAP----RLVTQLHFTSWPDFGVPFTPIGMLKFL 153

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1658117666 1118 RKSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVE 1193
Cdd:cd14620    154 KKVKSVNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 950-1190 2.17e-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: 2.17e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  950 PENKNKNRYINILAYDHSRVKLSSSSDRNGwsADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMIT 1029
Cdd:cd14554      4 PCNKFKNRLVNILPYESTRVCLQPIRGVEG--SDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLT 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1030 NLVEKGRRKCDQYWPLDSQEEYGSFLVTLRSTKVLAYYTQRTFtlKNTRAKKGSQkeqtheRTVVQYHYTQWPDMGVPEY 1109
Cdd:cd14554     82 KLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREF--KVTDARDGQS------RTVRQFQFTDWPEQGVPKS 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1110 TLPVLTFVRK--SSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFI 1187
Cdd:cd14554    154 GEGFIDFIGQvhKTKEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFC 233


                   ...
gi 1658117666 1188 HDA 1190
Cdd:cd14554    234 YRA 236
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 984-1189 2.86e-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: 228.67  E-value: 2.86e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  984 YINANYVD-GFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDS-QEEYGSFLVTLRST 1061
Cdd:cd18533      1 YINASYITlPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEyEGEYGDLTVELVSE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1062 KVL--AYYTQRTFTLKntrakkgsqKEQTHERTVVQYHYTQWPDMGVPEYTLPVLTFVR--KSSQANLGNMGPVVVHCSA 1137
Cdd:cd18533     81 EENddGGFIVREFELS---------KEDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKlkRELNDSASLDPPIIVHCSA 151

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1658117666 1138 GVGRTGTYIVLDSMLRQIKEQGTVN---------ILGFLKHIRTQRNYLVQTEEQYIFIHD 1189
Cdd:cd18533    152 GVGRTGTFIALDSLLDELKRGLSDSqdledsedpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 984-1188 2.65e-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: 222.87  E-value: 2.65e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  984 YINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQEEYGSFLVTLRSTKV 1063
Cdd:cd14551      1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCWTYGNLRVRVEDTVV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1064 LAYYTQRTFTLKNTRAKKGSQKEqtheRTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVGRTG 1143
Cdd:cd14551     81 LVDYTTRKFCIQKVNRGIGEKRV----RLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAGPIVVHCSAGVGRTG 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1658117666 1144 TYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIH 1188
Cdd:cd14551    157 TFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 984-1188 2.26e-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: 220.08  E-value: 2.26e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  984 YINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPL--DSQEEYGSFLVTLRST 1061
Cdd:cd14557      1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSmeEGSRAFGDVVVKINEE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1062 KVLAYYTQRTFTLKNTRaKKGSQKEQTHertvVQYhyTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVGR 1141
Cdd:cd14557     81 KICPDYIIRKLNINNKK-EKGSGREVTH----IQF--TSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGR 153

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1658117666 1142 TGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIH 1188
Cdd:cd14557    154 TGTYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIH 200
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 951-1191 5.07e-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: 5.07e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  951 ENKNKNRYINILAYDHSRVKLSSSsDRNGWSADYINANYV--------DGFTQPKAYIATQGPLKSSMEDFWRMVWEQNA 1022
Cdd:cd14605      1 ENKNKNRYKNILPFDHTRVVLHDG-DPNEPVSDYINANIImpefetkcNNSKPKKSYIATQGCLQNTVNDFWRMVFQENS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1023 SVIVMITNLVEKGRRKCDQYWPLD-SQEEYGSFLVtlRSTKVLAYYTQRTFTLKNTRAKKGSQkeqthERTVVQYHYTQW 1101
Cdd:cd14605     80 RVIVMTTKEVERGKSKCVKYWPDEyALKEYGVMRV--RNVKESAAHDYILRELKLSKVGQGNT-----ERTVWQYHFRTW 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1102 PDMGVPEYTLPVLTFVR--KSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGT---VNILGFLKHIRTQRNY 1176
Cdd:cd14605    153 PDHGVPSDPGGVLDFLEevHHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRSG 232

                          250
                   ....*....|....*
gi 1658117666 1177 LVQTEEQYIFIHDAL 1191
Cdd:cd14605    233 MVQTEAQYRFIYMAV 247
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 953-1186 7.37e-64

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


Pssm-ID: 350393 [Multi-domain]  Cd Length: 231  Bit Score: 216.87  E-value: 7.37e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  953 KNKNRYINILAYDHSRVKLssssdrNGWSADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLV 1032
Cdd:cd14545      1 LNRYRDRDPYDHDRSRVKL------KQGDNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLM 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1033 EKGRRKCDQYWPLDSQE----EYGSFLVTLRSTKVLAYYTQRTFTLKNtraKKGSQkeqthERTVVQYHYTQWPDMGVPE 1108
Cdd:cd14545     75 EKGQIKCAQYWPQGEGNamifEDTGLKVTLLSEEDKSYYTVRTLELEN---LKTQE-----TREVLHFHYTTWPDFGVPE 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1109 YTLPVLTFVRKSSQANL--GNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGT--VNILGFLKHIRTQRNYLVQTEEQY 1184
Cdd:cd14545    147 SPAAFLNFLQKVRESGSlsSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYRMGLIQTPDQL 226


                   ..
gi 1658117666 1185 IF 1186
Cdd:cd14545    227 RF 228
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1250-1482 1.71e-63

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 215.95  E-value: 1.71e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1250 NRDKNRNSSLLPVERSRVHLSTTAGEiSDYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDL 1329
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGP-SDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1330 AEDEC-IYWPTKS-QPIRFDTFTVTFMGEDhmclSNEDMLIVQDFILEATQDDYVLEVRQYRAPRWPNPDGP--ISNTFE 1405
Cdd:pfam00102   80 GREKCaQYWPEEEgESLEYGDFTVTLKKEK----EDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPesPNSLLD 155

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1658117666 1406 LINIIKEESV-SRDGPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIM 1482
Cdd:pfam00102  156 LLRKVRKSSLdGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 950-1193 2.14e-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: 2.14e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  950 PENKNKNRYINILAYDHSRVKLSSSSDRNGwsADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMIT 1029
Cdd:cd14627     51 PCNKFKNRLVNIMPYETTRVCLQPIRGVEG--SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLT 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1030 NLVEKGRRKCDQYWPLDSQEEYGSFLVTLRSTKVLAYYTQRTFtlKNTRAKKGsqkeqtHERTVVQYHYTQWPDMGVPEY 1109
Cdd:cd14627    129 KLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREF--KVTDARDG------QSRTVRQFQFTDWPEQGVPKS 200

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1110 TLPVLTFVRK--SSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFI 1187
Cdd:cd14627    201 GEGFIDFIGQvhKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFC 280


                   ....*.
gi 1658117666 1188 HDALVE 1193
Cdd:cd14627    281 YQAALE 286
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 931-1193 2.31e-63

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


Pssm-ID: 350477 [Multi-domain]  Cd Length: 291  Bit Score: 218.06  E-value: 2.31e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  931 EEIQACTVDLGITADSSIH---------PENKNKNRYINILAYDHSRVKLSSSSDRNGwsADYINANYVDGFTQPKAYIA 1001
Cdd:cd14629     23 ESVTAMELEFKLLANSKAHtsrfisanlPCNKFKNRLVNIMPYELTRVCLQPIRGVEG--SDYINASFIDGYRQQKAYIA 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1002 TQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQEEYGSFLVTLRSTKVLAYYTQRTFtlKNTRAKK 1081
Cdd:cd14629    101 TQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREF--KVTDARD 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1082 GsqkeqtHERTVVQYHYTQWPDMGVPEYTLPVLTFVRK--SSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQG 1159
Cdd:cd14629    179 G------QSRTIRQFQFTDWPEQGVPKTGEGFIDFIGQvhKTKEQFGQDGPITVHCSAGVGRTGVFITLSIVLERMRYEG 252

                          250       260       270
                   ....*....|....*....|....*....|....
gi 1658117666 1160 TVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVE 1193
Cdd:cd14629    253 VVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALE 286
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 950-1193 2.51e-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: 218.06  E-value: 2.51e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  950 PENKNKNRYINILAYDHSRVKLSSSSDRNGwsADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMIT 1029
Cdd:cd14628     50 PCNKFKNRLVNIMPYESTRVCLQPIRGVEG--SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLT 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1030 NLVEKGRRKCDQYWPLDSQEEYGSFLVTLRSTKVLAYYTQRTFtlKNTRAKKGsqkeqtHERTVVQYHYTQWPDMGVPEY 1109
Cdd:cd14628    128 KLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREF--KVTDARDG------QSRTVRQFQFTDWPEQGVPKS 199

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1110 TLPVLTFVRK--SSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFI 1187
Cdd:cd14628    200 GEGFIDFIGQvhKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFC 279


                   ....*.
gi 1658117666 1188 HDALVE 1193
Cdd:cd14628    280 YRAALE 285
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 950-1197 3.15e-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: 216.67  E-value: 3.15e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  950 PENKNKNRYINILAYDHSRVKLSSSsDRNGWSADYINANYVD----GFTQP-KAYIATQGPLKSSMEDFWRMVWEQNASV 1024
Cdd:cd14606     16 PENKSKNRYKNILPFDHSRVILQGR-DSNIPGSDYINANYVKnqllGPDENaKTYIASQGCLEATVNDFWQMAWQENSRV 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1025 IVMITNLVEKGRRKCDQYWP-LDSQEEYGSFLVTLRSTKVLAYYTQRTF---TLKNTRAKkgsqkeqtheRTVVQYHYTQ 1100
Cdd:cd14606     95 IVMTTREVEKGRNKCVPYWPeVGMQRAYGPYSVTNCGEHDTTEYKLRTLqvsPLDNGELI----------REIWHYQYLS 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1101 WPDMGVPEYTLPVLTFVRK--SSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGT---VNILGFLKHIRTQRN 1175
Cdd:cd14606    165 WPDHGVPSEPGGVLSFLDQinQRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVRAQRS 244

                          250       260
                   ....*....|....*....|..
gi 1658117666 1176 YLVQTEEQYIFIHDALVEAILS 1197
Cdd:cd14606    245 GMVQTEAQYKFIYVAIAQFIET 266
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 913-1195 1.28e-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: 209.51  E-value: 1.28e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  913 LHDSNTFSQEFEILKECYEEIQACTVDLGITadssihpeNKNKNRYINILAYDHSRVKLSSssDRNGWSADYINAN-YVD 991
Cdd:cd14609     11 LRNRDRLAKEWQALCAYQAEPNTCSTAQGEA--------NVKKNRNPDFVPYDHARIKLKA--ESNPSRSDYINASpIIE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  992 GFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQEEYGSFLVTLRSTKVLAY-YTQR 1070
Cdd:cd14609     81 HDPRMPAYIATQGPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHIYEVNLVSEHIWCEdFLVR 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1071 TFTLKNTrakkgsqkeQTHE-RTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVGRTGTYIVLD 1149
Cdd:cd14609    161 SFYLKNV---------QTQEtRTLTQFHFLSWPAEGIPSSTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILID 231

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1658117666 1150 SML-RQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVEAI 1195
Cdd:cd14609    232 MVLnRMAKGVKEIDIAATLEHVRDQRPGMVRTKDQFEFALTAVAEEV 278
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 913-1195 2.12e-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: 209.14  E-value: 2.12e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  913 LHDSNTFSQEFEILKECYEEIQACTVdlgitadsSIHPENKNKNRYINILAYDHSRVKLSSSSDRNgwSADYINANYV-D 991
Cdd:cd14610     13 LKNKNRLEKEWEALCAYQAEPNATNV--------AQREENVQKNRSLAVLPYDHSRIILKAENSHS--HSDYINASPImD 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  992 GFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQEEYGSFLVTLRSTKVLAY-YTQR 1070
Cdd:cd14610     83 HDPRNPAYIATQGPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEGSNLYHIYEVNLVSEHIWCEdFLVR 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1071 TFTLKNTrakkgsqkeQTHE-RTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVGRTGTYIVLD 1149
Cdd:cd14610    163 SFYLKNL---------QTNEtRTVTQFHFLSWNDQGVPASTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILID 233

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1658117666 1150 SMLRQI-KEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVEAI 1195
Cdd:cd14610    234 MVLNKMaKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAEEV 280
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 983-1197 1.95e-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: 203.33  E-value: 1.95e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  983 DYINANYVDGFTqPKA-----YIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWP-LDSQEEYGSFLV 1056
Cdd:cd14541      1 DYINANYVNMEI-PGSgivnrYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPdLGETMQFGNLQI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1057 TLRSTKVLAYYTQRTFTLKNTrakkgsqkEQTHERTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCS 1136
Cdd:cd14541     80 TCVSEEVTPSFAFREFILTNT--------NTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVEPTVVHCS 151

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1658117666 1137 AGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIhdalVEAILS 1197
Cdd:cd14541    152 AGIGRTGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFV----CEAILR 208
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 950-1191 2.03e-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: 204.68  E-value: 2.03e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  950 PENKNKNRYINILAYDHSRVKLSSSSDRNGwSADYINANYVDGFT-QPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMI 1028
Cdd:cd14612     13 PGHASKDRYKTILPNPQSRVCLRRAGSQEE-EGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMI 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1029 TNLVEKgRRKCDQYWPlDSQEEYGSFLVTLRSTKVLAYYTQRTFTLKNtrakkgsqkeQTHERTVVQYHYTQWPDMGVPE 1108
Cdd:cd14612     92 TKLKEK-KEKCVHYWP-EKEGTYGRFEIRVQDMKECDGYTIRDLTIQL----------EEESRSVKHYWFSSWPDHQTPE 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1109 YTLPVLTFVRK--SSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIF 1186
Cdd:cd14612    160 SAGPLLRLVAEveESRQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQF 239


                   ....*
gi 1658117666 1187 IHDAL 1191
Cdd:cd14612    240 LHHTL 244
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 984-1192 3.11e-59

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


Pssm-ID: 350400 [Multi-domain]  Cd Length: 202  Bit Score: 202.50  E-value: 3.11e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  984 YINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQEEYGSFLVTLRSTKV 1063
Cdd:cd14552      1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGSVSSGDITVELKDQTD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1064 LAYYTQRTFTLKNTRAKKgsqkeqthERTVVQYHYTQWPDMGVPEY---TLPVLTFVRKSSQANlGNmGPVVVHCSAGVG 1140
Cdd:cd14552     81 YEDYTLRDFLVTKGKGGS--------TRTVRQFHFHGWPEVGIPDNgkgMIDLIAAVQKQQQQS-GN-HPITVHCSAGAG 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1658117666 1141 RTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALV 1192
Cdd:cd14552    151 RTGTFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVVQ 202
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 984-1195 6.00e-59

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


Pssm-ID: 350386 [Multi-domain]  Cd Length: 207  Bit Score: 201.83  E-value: 6.00e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  984 YINANYV--DGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQE---EYGSFLVTL 1058
Cdd:cd14538      1 YINASHIriPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDSLNKpliCGGRLEVSL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1059 RSTKVLAYYTQRTFTLKntrakkgsQKEQTHERTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQanLGNMGPVVVHCSAG 1138
Cdd:cd14538     81 EKYQSLQDFVIRRISLR--------DKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRR--IHNSGPIVVHCSAG 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1658117666 1139 VGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVEAI 1195
Cdd:cd14538    151 IGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEVL 207
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 903-1193 6.11e-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: 6.11e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  903 IKQFVKHVAELHDS-----NTFSQEFEILKECYEEIQACTVDLGITADSSihpENKNKNRYINILAYDHSRVKLS---SS 974
Cdd:cd14604      6 LKKFIERVQAMKSTdhngeDNFASDFMRLRRLSTKYRTEKIYPTATGEKE---ENVKKNRYKDILPFDHSRVKLTlktSS 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  975 SDrngwsADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQE--EYG 1052
Cdd:cd14604     83 QD-----SDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFEMGRKKCERYWPLYGEEpmTFG 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1053 SFLVTLRSTKVLAYYTQRTFTLKNtrakkgsqkeQTHERTVVQYHYTQWPDMGVP---EYTLPVLTFVRKSSQAnlgNMG 1129
Cdd:cd14604    158 PFRISCEAEQARTDYFIRTLLLEF----------QNETRRLYQFHYVNWPDHDVPssfDSILDMISLMRKYQEH---EDV 224

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1658117666 1130 PVVVHCSAGVGRTGTYIVLD---SMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVE 1193
Cdd:cd14604    225 PICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQ 291
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 956-1188 7.23e-59

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: 202.44  E-value: 7.23e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  956 NRYINILAYDHSRVKLSSSSDRNGwsADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKG 1035
Cdd:cd14616      1 NRFPNIKPYNNNRVKLIADAGVPG--SDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1036 RRKCDQYWPLDSQ--EEYGSFLVTLRSTKVLAYYTQRTFTLKntraKKGsqkeqtHERTVVQYHYTQWPDMGVPEYTLPV 1113
Cdd:cd14616     79 RIRCHQYWPEDNKpvTVFGDIVITKLMEDVQIDWTIRDLKIE----RHG------DYMMVRQCNFTSWPEHGVPESSAPL 148

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1658117666 1114 LTFVRKSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIH 1188
Cdd:cd14616    149 IHFVKLVRASRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLH 223
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 930-1193 9.51e-59

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


Pssm-ID: 350451 [Multi-domain]  Cd Length: 266  Bit Score: 203.52  E-value: 9.51e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  930 YEEIQACTV----DLGITADSSIHPENKNKNRYINILAYDHSRVKLSSSSDRNGwsADYINANYVDGFTQPKAYIATQGP 1005
Cdd:cd14603      4 FSEIRACSAafkaDYVCSTVAGGRKENVKKNRYKDILPYDQTRVILSLLQEEGH--SDYINANFIKGVDGSRAYIATQGP 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1006 LKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQE-EYGSFLVT-LRSTKVLAYYTQRTFTLKntrakkgS 1083
Cdd:cd14603     82 LSHTVLDFWRMIWQYGVKVILMACREIEMGKKKCERYWAQEQEPlQTGPFTITlVKEKRLNEEVILRTLKVT-------F 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1084 QKEqthERTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVGRTGTYIVLD---SMLRQIKEQGT 1160
Cdd:cd14603    155 QKE---SRSVSHFQYMAWPDHGIPDSPDCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDyvrQLLLTQRIPPD 231

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1658117666 1161 VNILGFLKHIRTQRNYLVQTEEQYIFIHDALVE 1193
Cdd:cd14603    232 FSIFDVVLEMRKQRPAAVQTEEQYEFLYHTVAQ 264
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 955-1193 5.27e-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: 200.45  E-value: 5.27e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  955 KNRYINILAYDHSRVKLS-SSSDRNgwsADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVE 1033
Cdd:cd14602      1 KNRYKDILPYDHSRVELSlITSDED---SDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1034 KGRRKCDQYW--PLDSQEEYGSFLVTLRSTKVLAYYTQRTFtlkntRAKKGSQKeqtheRTVVQYHYTQWPDMGVPEYTL 1111
Cdd:cd14602     78 MGKKKCERYWaePGEMQLEFGPFSVTCEAEKRKSDYIIRTL-----KVKFNSET-----RTIYQFHYKNWPDHDVPSSID 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1112 PVLTFVRKSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEqGTV----NILGFLKHIRTQRNYLVQTEEQYIFI 1187
Cdd:cd14602    148 PILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKD-GIIpenfSVFSLIQEMRTQRPSLVQTKEQYELV 226


                   ....*.
gi 1658117666 1188 HDALVE 1193
Cdd:cd14602    227 YNAVIE 232
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 949-1191 8.74e-58

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: 200.58  E-value: 8.74e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  949 HPENKNKNRYINILAYDHSRVKLSSSSDrngwsaDYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMI 1028
Cdd:cd14607     21 YPENRNRNRYRDVSPYDHSRVKLQNTEN------DYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVML 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1029 TNLVEKGRRKCDQYWPLDSQEEYG----SFLVTLRSTKVLAYYTQRTFTLKNtrAKKGSQKEQTHertvvqYHYTQWPDM 1104
Cdd:cd14607     95 NRIVEKDSVKCAQYWPTDEEEVLSfketGFSVKLLSEDVKSYYTVHLLQLEN--INSGETRTISH------FHYTTWPDF 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1105 GVPEYTLPVLTF---VRKSSQANLGNmGPVVVHCSAGVGRTGTYIVLDS--MLRQIKEQGTVNILGFLKHIRTQRNYLVQ 1179
Cdd:cd14607    167 GVPESPASFLNFlfkVRESGSLSPEH-GPAVVHCSAGIGRSGTFSLVDTclVLMEKKDPDSVDIKQVLLDMRKYRMGLIQ 245

                          250
                   ....*....|..
gi 1658117666 1180 TEEQYIFIHDAL 1191
Cdd:cd14607    246 TPDQLRFSYMAV 257
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 984-1195 1.66e-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: 197.67  E-value: 1.66e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  984 YINANYV-DGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQEEYGSFLVTLRSTK 1062
Cdd:cd14546      1 YINASTIyDHDPRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEVYHIYEVHLVSEH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1063 VL-AYYTQRTFTLKNTrakkgsqkeQTHE-RTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVG 1140
Cdd:cd14546     81 IWcDDYLVRSFYLKNL---------QTSEtRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYRGRSCPIVVHCSDGAG 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1658117666 1141 RTGTYIVLD----SMLRQIKEqgtVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVEAI 1195
Cdd:cd14546    152 RTGTYILIDmvlnRMAKGAKE---IDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAEEV 207
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 955-1188 2.06e-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: 2.06e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  955 KNRYINILAYDHSRVKLSSSSDRNGWSAdYINANYVDGFT-QPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVE 1033
Cdd:cd14611      2 KNRYKTILPNPHSRVCLKPKNSNDSLST-YINANYIRGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1034 KGRrKCDQYWPlDSQEEYGSFLVTLRSTKVLAYYTQRTFTLKNtrakkGSQKeqtheRTVVQYHYTQWPDMGVPEYTLPV 1113
Cdd:cd14611     81 KNE-KCVLYWP-EKRGIYGKVEVLVNSVKECDNYTIRNLTLKQ-----GSQS-----RSVKHYWYTSWPDHKTPDSAQPL 148

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1658117666 1114 LTF---VRKSSQANLGNmGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIH 1188
Cdd:cd14611    149 LQLmldVEEDRLASPGR-GPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 950-1196 3.29e-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: 3.29e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  950 PENKNKNRYINILAYDHSRVKLSSSSDrngwsadYINANYVDgfTQPKA------YIATQGPLKSSMEDFWRMVWEQNAS 1023
Cdd:cd14600     38 PQNMDKNRYKDVLPYDATRVVLQGNED-------YINASYVN--MEIPSanivnkYIATQGPLPHTCAQFWQVVWEQKLS 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1024 VIVMITNLVEKGRRKCDQYWPlDSQE--EYGSFLVTLRSTKVLAYYTQRTFTLKNTrakkgsqkEQTHERTVVQYHYTQW 1101
Cdd:cd14600    109 LIVMLTTLTERGRTKCHQYWP-DPPDvmEYGGFRVQCHSEDCTIAYVFREMLLTNT--------QTGEERTVTHLQYVAW 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1102 PDMGVPEYTLPVLTFVRKSSQANLGNMgPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTE 1181
Cdd:cd14600    180 PDHGVPDDSSDFLEFVNYVRSKRVENE-PVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTS 258

                          250
                   ....*....|....*
gi 1658117666 1182 EQYIFIhdalVEAIL 1196
Cdd:cd14600    259 SQYKFV----CEAIL 269
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 930-1193 3.90e-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: 199.48  E-value: 3.90e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  930 YEEIQACTVDLgiTADSSIHPENKNKNRYINILAYDHSRVKLSSSSDrngwsaDYINANYVDGFTQPKAYIATQGPLKSS 1009
Cdd:cd14608      5 YQDIRHEASDF--PCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQEDN------DYINASLIKMEEAQRSYILTQGPLPNT 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1010 MEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQEEY----GSFLVTLRSTKVLAYYTQRTFTLKNTRAKKgsqk 1085
Cdd:cd14608     77 CGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMifedTNLKLTLISEDIKSYYTVRQLELENLTTQE---- 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1086 eqthERTVVQYHYTQWPDMGVPEYTLPVLTF---VRKSSQANlGNMGPVVVHCSAGVGRTGTYIVLDS---MLRQIKEQG 1159
Cdd:cd14608    153 ----TREILHFHYTTWPDFGVPESPASFLNFlfkVRESGSLS-PEHGPVVVHCSAGIGRSGTFCLADTcllLMDKRKDPS 227

                          250       260       270
                   ....*....|....*....|....*....|....
gi 1658117666 1160 TVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVE 1193
Cdd:cd14608    228 SVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIE 261
alpha_CA_IV_XV_like cd03117
Carbonic anhydrase alpha, CA_IV, CA_XV, like isozymes. Carbonic anhydrases (CAs) are ...
 63-292 2.12e-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: 2.12e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666   63 KQSPINIDDDLSQVKMQFQKLKLEGFeQETSNTTTIHNDGKTVAINLNDEYYISGGGLRSRFKVGRITFHWGqcNASSDG 142
Cdd:cd03117      3 RQSPINIVTKKVQYDENLTPFTFTGY-DDTTTNWTITNNGHTVQVTLPDGAKISGGGLPGTYKALQFHFHWG--SNGSPG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  143 SEHSLDGIKFPLEMQIYGYEAhKFQSLDSALKDGGRLTALSVLFEVSAEDNENYVAIIDGVKTVTRLGKTAVLEPFSLLG 222
Cdd:cd03117     80 SEHTIDGERYPMELHIVHIKE-SYNSLLEALKDSDGLAVLGFFIEEGEEENTNFDPLISALSNIPQKGGSTNLTPFSLRS 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1658117666  223 LLP-NSTEKYYIYNGSLTTPPCSETVEWIVFRNTVDISDVQLETFCEVMTMQQAGYVMLMdylqNNFREQQ 292
Cdd:cd03117    159 LLPsVLLTKYYRYNGSLTTPGCNEAVIWTVFEEPIPISRAQLDAFSTVLFFDTDNGQPMV----NNFRPVQ 225
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 955-1191 2.14e-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: 196.62  E-value: 2.14e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  955 KNRYINILAYDHSRVKLSSSSDRNGWSAdYINANYVDGF-TQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVE 1033
Cdd:cd14613     28 KNRYKTILPNPHSRVCLTSPDQDDPLSS-YINANYIRGYgGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEE 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1034 KGRrKCDQYWPlDSQEEYGSFLVTLRSTKVLAYYTQRTFTLKNtrakkgsqkeQTHERTVVQYHYTQWPDMGVPEYTLPV 1113
Cdd:cd14613    107 MNE-KCTEYWP-EEQVTYEGIEITVKQVIHADDYRLRLITLKS----------GGEERGLKHYWYTSWPDQKTPDNAPPL 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1114 LTFVRK---SSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDA 1190
Cdd:cd14613    175 LQLVQEveeARQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVHHV 254


                   .
gi 1658117666 1191 L 1191
Cdd:cd14613    255 L 255
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 957-1193 6.13e-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: 194.11  E-value: 6.13e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  957 RYINILAYDHSRVKLSSSsdRNGWSADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGR 1036
Cdd:cd14623      1 RVLQIIPYEFNRVIIPVK--RGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1037 RKCDQYWPLDSQEEYGSFLVTLRSTKVLAYYTQRTFTLKNTRAKKgsqkeqthERTVVQYHYTQWPDMGVP---EYTLPV 1113
Cdd:cd14623     79 EKCAQYWPSDGSVSYGDITIELKKEEECESYTVRDLLVTNTRENK--------SRQIRQFHFHGWPEVGIPsdgKGMINI 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1114 LTFVRKSSQANlGNMgPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVE 1193
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 9.52e-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: 194.45  E-value: 9.52e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666   49 QNNWAKKYPSCNNAKQSPINIDDDLSQVKMQFQKLKLEGFEQETSNTTTIHNDGKTVAINLNDEYYIsGGGLRSRFKVGR 128
Cdd:cd03123      2 EDHWPKKYPACGGKRQSPIDIQTDIVQFDPSLPPLELVGYDLPGTEEFTLTNNGHTVQLSLPPTMHI-RGGPGTEYTAAQ 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  129 ITFHWGQCNASSdGSEHSLDGIKFPLEMQIYGYEAHKFQSLDSALKDGGRLTALSVLFEVSAEDNENYVAIIDGVKTVTR 208
Cdd:cd03123     81 LHLHWGGRGSLS-GSEHTIDGIRFAAELHIVHYNSDKYSSFDEAADKPDGLAVLAILIEVGYPENTYYEKIISHLHEIKY 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  209 LGKTAVLEPFSLLGLLPNSTEKYYIYNGSLTTPPCSETVEWIVFRNTVDISDVQLEtfcevmTMQQAgyvmLMDY----L 284
Cdd:cd03123    160 KGQETTVPGFNVRELLPEDLSHYYRYEGSLTTPPCYESVLWTVFRDPVTLSKEQLE------TLENT----LMDThnktL 229


                   ....*...
gi 1658117666  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; ...
 984-1188 1.35e-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: 192.25  E-value: 1.35e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  984 YINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPlDSQEE---YGSFLVTLRS 1060
Cdd:cd14542      1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWP-EEGEEqlqFGPFKISLEK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1061 TKVLAY-YTQRtfTLKNTRakkgsQKEqthERTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSAGV 1139
Cdd:cd14542     80 EKRVGPdFLIR--TLKVTF-----QKE---SRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDVPICVHCSAGC 149

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1658117666 1140 GRTGTYIVLD---SMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIH 1188
Cdd:cd14542    150 GRTGTICAIDyvwNLLKTGKIPEEFSLFDLVREMRKQRPAMVQTKEQYELVY 201
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 983-1188 3.69e-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: 185.21  E-value: 3.69e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  983 DYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQEEYGSFLVTLRSTK 1062
Cdd:cd14622      1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEGSVTHGEITIEIKNDT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1063 VLAYYTQRTFTLKNtrakkgSQKEQTheRTVVQYHYTQWPDMGVP---EYTLPVLTFVRKSSQANlGNmGPVVVHCSAGV 1139
Cdd:cd14622     81 LLETISIRDFLVTY------NQEKQT--RLVRQFHFHGWPEIGIPaegKGMIDLIAAVQKQQQQT-GN-HPIVVHCSAGA 150

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1658117666 1140 GRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIH 1188
Cdd:cd14622    151 GRTGTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCY 199
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 951-1186 5.74e-53

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: 185.80  E-value: 5.74e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  951 ENKNKNRYINILAYDHSRVKLssssdrnGWSADYINANYVD---GFTQpKAYIATQGPLKSSMEDFWRMVWEQNASVIVM 1027
Cdd:cd14597      2 ENRKKNRYKNILPYDTTRVPL-------GDEGGYINASFIKmpvGDEE-FVYIACQGPLPTTVADFWQMVWEQKSTVIAM 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1028 ITNLVEKGRRKCDQYWPldsqEEYGSFL-------VTLRSTKVLAYYTQRTFTLKNTrakkgsqkeQTHE-RTVVQYHYT 1099
Cdd:cd14597     74 MTQEVEGGKIKCQRYWP----EILGKTTmvdnrlqLTLVRMQQLKNFVIRVLELEDI---------QTREvRHITHLNFT 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1100 QWPDMGVPEYTLPVLTFVrkSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQ 1179
Cdd:cd14597    141 AWPDHDTPSQPEQLLTFI--SYMRHIHKSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQ 218


                   ....*..
gi 1658117666 1180 TEEQYIF 1186
Cdd:cd14597    219 TEDQYIF 225
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 984-1189 9.76e-53

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: 184.12  E-value: 9.76e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  984 YINANYVDGFTQPKA-YIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLD--SQEEYGSFLVTLRS 1060
Cdd:cd14539      1 YINASLIEDLTPYCPrFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTErgQALVYGAITVSLQS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1061 TKVLAYYTQRTFTLKNtrakkgsqKEQTHERTVVQYHYTQWPDMGVPEYTLPVLTF---VRKSSQANLGNMGPVVVHCSA 1137
Cdd:cd14539     81 VRTTPTHVERIISIQH--------KDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFieeVHSHYLQQRSLQTPIVVHCSS 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1658117666 1138 GVGRTGTYIVLDSMLRQIKE-QGTVNILGFLKHIRTQRNYLVQTEEQYIFIHD 1189
Cdd:cd14539    153 GVGRTGAFCLLYAAVQEIEAgNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 1279-1479 1.03e-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: 183.64  E-value: 1.03e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1279 YINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDECI-YWPTK-SQPIRFDTFTVTFMGE 1356
Cdd:cd00047      1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCErYWPEEgGKPLEYGDITVTLVSE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1357 DHMclsneDMLIVQDFILEATQDDYVLEVRQYRAPRWPNPDGP--ISNTFELINIIKEESVSRDGPIVVHDKRGGNIAGT 1434
Cdd:cd00047     81 EEL-----SDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPssPEDLLALVRRVRKEARKPNGPIVVHCSAGVGRTGT 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1658117666 1435 FCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYK 1479
Cdd:cd00047    156 FIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 984-1193 1.77e-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: 183.81  E-value: 1.77e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  984 YINANYVDGFTQPKA--YIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQEE----YGSFLVT 1057
Cdd:cd14540      1 YINASHITATVGGKQrfYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGGEHdaltFGEYKVS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1058 LRSTKVLAYYTQRTFTLKNTRAKKgsqkeqthERTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMG-------- 1129
Cdd:cd14540     81 TKFSVSSGCYTTTGLRVKHTLSGQ--------SRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINSVRRHTNQdvaghnrn 152

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1658117666 1130 -PVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVE 1193
Cdd:cd14540    153 pPTLVHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQ 217
PHA02738 PHA02738
hypothetical protein; Provisional
 924-1191 6.23e-52

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 185.90  E-value: 6.23e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  924 EILKECYEEIQACTVDLGITADSsihpENKNKNRYINILAYDHSRVKLSSSSDRngwsADYINANYVDGFTQPKAYIATQ 1003
Cdd:PHA02738    25 EVITREHQKVISEKVDGTFNAEK----KNRKLNRYLDAVCFDHSRVILPAERNR----GDYINANYVDGFEYKKKFICGQ 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1004 GPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQEE--YGSFLVTLRSTKVLAYYTQRTFTLKNtrakk 1081
Cdd:PHA02738    97 APTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDVEQGSirFGKFKITTTQVETHPHYVKSTLLLTD----- 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1082 GSQKEQtherTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQA-------------NLGNMGPVVVHCSAGVGRTGTYIVL 1148
Cdd:PHA02738   172 GTSATQ----TVTHFNFTAWPDHDVPKNTSEFLNFVLEVRQCqkelaqeslqighNRLQPPPIVVHCNAGLGRTPCYCVV 247

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1658117666 1149 DSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDAL 1191
Cdd:PHA02738   248 DISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAV 290
alpha_CA_XII_XIV cd03126
Carbonic anhydrase alpha, isozymes XII and XIV. Carbonic anhydrases (CAs) are zinc-containing ...
 49-292 7.79e-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: 177.34  E-value: 7.79e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666   49 QNNWAKKYPSCNNAKQSPINIDDDLSQVKMQFQKLKLEGFEQETSNTTTIHNDGKTVAINLNDEYYIsgGGLRSRFKVGR 128
Cdd:cd03126      2 ENSWPKKYPFCGGVAQSPIDIHTDILQYDSSLPPLEFHGYNVSGTEQFTLTNNGHTVQLSLPPTMHI--GGLPFKYTASQ 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  129 ITFHWGQCNaSSDGSEHSLDGIKFPLEMQIYGYEAHKFQSLDSALKDGGRLTALSVLFEVsAEDNENYVAIIDGVKTVTR 208
Cdd:cd03126     80 LHLHWGQRG-SPEGSEHTISGKHFAAELHIVHYNSDKYPDISTAMNKSQGLAVLGILIEV-GPFNPSYEKIFSHLHEVKY 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  209 LGKTAVLEPFSLLGLLPNSTEKYYIYNGSLTTPPCSETVEWIVFRNTVDISDVQLEtfcevmTMQQAGYVMLMD---YLQ 285
Cdd:cd03126    158 KDQKVSVPGFNVQELLPKRLDEYYRYEGSLTTPPCYPSVLWTVFRNPVQISQEQLL------ALETALYSTEEDesrEMV 231


                   ....*..
gi 1658117666  286 NNFREQQ 292
Cdd:cd03126    232 NNYRQVQ 238
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 943-1188 1.82e-49

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 178.66  E-value: 1.82e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  943 TADSSIHPENKNKNRYINILAYDHSRVKLSSSSdrnGWSADYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNA 1022
Cdd:PHA02747    42 LIANFEKPENQPKNRYWDIPCWDHNRVILDSGG---GSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHC 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1023 SVIVMIT-NLVEKGRRKCDQYWPL--DSQEEYGSFLVTLRSTKVLAYYTQRTFTLKNtrakkgsqKEQTHERTVVQYHYT 1099
Cdd:PHA02747   119 SIIVMLTpTKGTNGEEKCYQYWCLneDGNIDMEDFRIETLKTSVRAKYILTLIEITD--------KILKDSRKISHFQCS 190

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1100 QWPDMGVPEYTLPVLTF------VRKSSQANLGN----MGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKH 1169
Cdd:PHA02747   191 EWFEDETPSDHPDFIKFikiidiNRKKSGKLFNPkdalLCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEK 270

                          250
                   ....*....|....*....
gi 1658117666 1170 IRTQRNYLVQTEEQYIFIH 1188
Cdd:PHA02747   271 IREQRHAGIMNFDDYLFIQ 289
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 931-1196 7.36e-49

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 177.14  E-value: 7.36e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  931 EEIQACTVDLGITADSSIHPENKNKNRYINILAYDHSRVKLSS-----SSDRNGW------------SADYINANYVDGF 993
Cdd:PHA02746    30 EHAEVMDIPIRGTTNHFLKKENLKKNRFHDIPCWDHSRVVINAheslkMFDVGDSdgkkievtsednAENYIHANFVDGF 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  994 TQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNlVEKGRRKCDQYW--PLDSQEEYGSFLVtlrstKVLAYYTQRT 1071
Cdd:PHA02746   110 KEANKFICAQGPKEDTSEDFFKLISEHESQVIVSLTD-IDDDDEKCFELWtkEEDSELAFGRFVA-----KILDIIEELS 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1072 FTlkNTRAKKGSQKEQThERTVVQYHYTQWPDMGVPEYTLPVLTFV----------RKSSQANLGNMGPVVVHCSAGVGR 1141
Cdd:PHA02746   184 FT--KTRLMITDKISDT-SREIHHFWFPDWPDNGIPTGMAEFLELInkvneeqaelIKQADNDPQTLGPIVVHCSAGIGR 260

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1658117666 1142 TGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVEAIL 1196
Cdd:PHA02746   261 AGTFCAIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKALKYAII 315
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 983-1196 1.66e-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: 172.05  E-value: 1.66e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  983 DYINANYVD----GFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDS-QEEYGSFLVT 1057
Cdd:cd14601      1 DYINANYINmeipSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSgSSSYGGFQVT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1058 LRSTKVLAYYTQRTFTLKNTrakkgsqkEQTHERTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSA 1137
Cdd:cd14601     81 CHSEEGNPAYVFREMTLTNL--------EKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDEPVVVHCSA 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1658117666 1138 GVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIhdalVEAIL 1196
Cdd:cd14601    153 GIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFV----CEAIL 207
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 930-1193 2.37e-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: 174.42  E-value: 2.37e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  930 YEEIQACTVDlGITADSSIhPENKNKNRYINILAYDHSRVKLSSSSDRNgwsADYINANYVDGFTQPKA--YIATQGPLK 1007
Cdd:cd14599     18 YEQIPKKKAD-GVFTTATL-PENAERNRIREVVPYEENRVELVPTKENN---TGYINASHIKVTVGGEEwhYIATQGPLP 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1008 SSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWP----LDSQEEYGSFLVTLRSTKVLAYYTQRTFTLKNTRAKKgs 1083
Cdd:cd14599     93 HTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPklgsKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQ-- 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1084 qkeqthERTVVQYHYTQWPDMGVPEYTLPVLTF------VRKSSQANLGNMG----PVVVHCSAGVGRTGTYIVLDSMLR 1153
Cdd:cd14599    171 ------ERTVWHLQYTDWPDHGCPEEVQGFLSYleeiqsVRRHTNSMLDSTKncnpPIVVHCSAGVGRTGVVILTELMIG 244

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1658117666 1154 QIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVE 1193
Cdd:cd14599    245 CLEHNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQ 284
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 984-1195 3.40e-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: 171.08  E-value: 3.40e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  984 YINANYVdgfTQPKA-----YIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLDSQE--EYGSFLV 1056
Cdd:cd14596      1 YINASYI---TMPVGeeelfYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEpmELENYQL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1057 TLRSTKVLAYYTQRTFTLkntrakkgSQKEQTHERTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANlgNMGPVVVHCS 1136
Cdd:cd14596     78 RLENYQALQYFIIRIIKL--------VEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVH--NTGPIVVHCS 147

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1658117666 1137 AGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVEAI 1195
Cdd:cd14596    148 AGIGRAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVL 206
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 984-1189 7.84e-48

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: 169.88  E-value: 7.84e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  984 YINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPlDSQEEYGSFLVTLRSTKV 1063
Cdd:cd14558      1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWG-DEKKTYGDIEVELKDTEK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1064 LAYYTQRTFTLKNTRAKKgsqkeqthERTVVQYHYTQWPDMGVPEYTLPVLTFVR------KSSQANLGNMGPVVVHCSA 1137
Cdd:cd14558     80 SPTYTVRVFEITHLKRKD--------SRTVYQYQYHKWKGEELPEKPKDLVDMIKsikqklPYKNSKHGRSVPIVVHCSD 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1658117666 1138 GVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHD 1189
Cdd:cd14558    152 GSSRTGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 984-1188 8.60e-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: 169.95  E-value: 8.60e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  984 YINANYV--DGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRR-KCDQYWPLD--SQEEYGSFLVTL 1058
Cdd:cd17658      1 YINASLVetPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTaKCADYFPAEenESREFGRISVTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1059 RSTKvlayYTQRTFTLKNTRAKKGSQKEQTheRTVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANlGNMGPVVVHCSAG 1138
Cdd:cd17658     81 KKLK----HSQHSITLRVLEVQYIESEEPP--LSVLHIQYPEWPDHGVPKDTRSVRELLKRLYGIP-PSAGPIVVHCSAG 153

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1658117666 1139 VGRTGTYIVLDSMLRQIKE--QGTVNILGFLKHIRTQRNYLVQTEEQYIFIH 1188
Cdd:cd17658    154 IGRTGAYCTIHNTIRRILEgdMSAVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 1200-1482 5.59e-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: 162.21  E-value: 5.59e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1200 TEVHSSHIHTYVNELL-IPGPSGQTPLEKQFKMITQSNAKQCDYSAALKQCNRDKNRNSSLLPVERSRVHLSTTAG-EIS 1277
Cdd:cd14628      1 TEVPARNLYAYIQKLTqIETGENVTGMELEFKRLASSKAHTSRFISANLPCNKFKNRLVNIMPYESTRVCLQPIRGvEGS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1278 DYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDEC-IYWPTKsQPIRFDTFTVTFMGE 1356
Cdd:cd14628     81 DYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKChQYWPAE-RSARYQYFVVDPMAE 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1357 DHMclsneDMLIVQDFILEATQDDYVLEVRQYRAPRWPNPDGPISNTfELINIIKE-----ESVSRDGPIVVHDKRGGNI 1431
Cdd:cd14628    160 YNM-----PQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGE-GFIDFIGQvhktkEQFGQDGPISVHCSAGVGR 233

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1658117666 1432 AGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIM 1482
Cdd:cd14628    234 TGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAAL 284
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 984-1189 9.53e-44

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


Pssm-ID: 350404 [Multi-domain]  Cd Length: 201  Bit Score: 157.95  E-value: 9.53e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  984 YINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMItNLVEKGRRKCDQYWPLDSQEEYGSFLVTLRSTKV 1063
Cdd:cd14556      1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVML-NQLDPKDQSCPQYWPDEGSGTYGPIQVEFVSTTI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1064 LAYYTQRTFTLKNTRakkgsqKEQTHERTVVQYHYTQWPDMG----VPEYTLPVLTFVRKsSQANLGNmGPVVVHCSAGV 1139
Cdd:cd14556     80 DEDVISRIFRLQNTT------RPQEGYRMVQQFQFLGWPRDRdtppSKRALLKLLSEVEK-WQEQSGE-GPIVVHCLNGV 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1140 GRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHD 1189
Cdd:cd14556    152 GRSGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
950-1187 2.72e-43

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 159.87  E-value: 2.72e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  950 PENKNKNRYINILAYDHSRVklsSSSDRngwsadYINANYVDGfTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMIT 1029
Cdd:COG5599     40 INGSPLNRFRDIQPYKETAL---RANLG------YLNANYIQV-IGNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLA 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1030 NLVE--KGRRKCDQYWPLDsqEEYGSFLVTLRSTKVLAYYTQ---RTFTLKntraKKGSQKEQtheRTVVQYHYTQWPDM 1104
Cdd:COG5599    110 SDDEisKPKVKMPVYFRQD--GEYGKYEVSSELTESIQLRDGieaRTYVLT----IKGTGQKK---IEIPVLHVKNWPDH 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1105 GVP--EYTLPVLTFVRKSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKE--QGTVNILGFLKHIRTQRNY-LVQ 1179
Cdd:COG5599    181 GAIsaEALKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINAlvQITLSVEEIVIDMRTSRNGgMVQ 260


                   ....*...
gi 1658117666 1180 TEEQYIFI 1187
Cdd:COG5599    261 TSEQLDVL 268
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 924-1186 3.20e-43

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 160.17  E-value: 3.20e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  924 EILKECYEEIQACTVdlGITADSSIHPENKNKNRYINILAYDHSRVKLSSssdRNGWSaDYINANYVDGFTQPKAYIATQ 1003
Cdd:PHA02742    26 EILKEEHEHIMQEIV--AFSCNESLELKNMKKCRYPDAPCFDRNRVILKI---EDGGD-DFINASYVDGHNAKGRFICTQ 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1004 GPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWPLD--SQEEYGSFLVTLRSTKVLAYYTQRTFTLKNTRAkk 1081
Cdd:PHA02742   100 APLEETALDFWQAIFQDQVRVIVMITKIMEDGKEACYPYWMPHerGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNT-- 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1082 GSQKEQTHertvvqYHYTQWPDMGVPEYTLPVLTFVRKSSQA-----------NLGNMGPVVVHCSAGVGRTGTYIVLDS 1150
Cdd:PHA02742   178 GASLDIKH------FAYEDWPHGGLPRDPNKFLDFVLAVREAdlkadvdikgeNIVKEPPILVHCSAGLDRAGAFCAIDI 251

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1658117666 1151 MLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIF 1186
Cdd:PHA02742   252 CISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIF 287
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 1200-1482 9.03e-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: 158.36  E-value: 9.03e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1200 TEVHSSHIHTYVNELLIPGPSGQ-TPLEKQFKMITQSNAKQCDYSAALKQCNRDKNRNSSLLPVERSRVHLSTTAG-EIS 1277
Cdd:cd14627      2 TEVPARNLYSYIQKLAQVEVGEHvTGMELEFKRLANSKAHTSRFISANLPCNKFKNRLVNIMPYETTRVCLQPIRGvEGS 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1278 DYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDEC-IYWPTKsQPIRFDTFTVTFMGE 1356
Cdd:cd14627     82 DYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGREKChQYWPAE-RSARYQYFVVDPMAE 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1357 DHMclsneDMLIVQDFILEATQDDYVLEVRQYRAPRWPNPDGPISNTfELINIIKE-----ESVSRDGPIVVHDKRGGNI 1431
Cdd:cd14627    161 YNM-----PQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGE-GFIDFIGQvhktkEQFGQDGPISVHCSAGVGR 234

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1658117666 1432 AGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIM 1482
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 ...
 1249-1479 1.21e-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: 1.21e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1249 CNRDKNRNSSLLPVERSRVHLSTTAG-EISDYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGL 1327
Cdd:cd14554      5 CNKFKNRLVNILPYESTRVCLQPIRGvEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTKLR 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1328 DLAEDECI-YWPTKsQPIRFDTFTVTFMGEDHMclsneDMLIVQDFILEATQDDYVLEVRQYRAPRWPNPDGPISNTfEL 1406
Cdd:cd14554     85 EMGREKCHqYWPAE-RSARYQYFVVDPMAEYNM-----PQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGE-GF 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1658117666 1407 INIIKE-----ESVSRDGPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYK 1479
Cdd:cd14554    158 IDFIGQvhktkEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYR 235
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 1200-1482 1.14e-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: 1.14e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1200 TEVHSSHIHTYVNEL-LIPGPSGQTPLEKQFKMITQSNAKQCDYSAALKQCNRDKNRNSSLLPVERSRVHLSTTAG-EIS 1277
Cdd:cd14629      2 TEVPARNLYAHIQKLtQVPPGESVTAMELEFKLLANSKAHTSRFISANLPCNKFKNRLVNIMPYELTRVCLQPIRGvEGS 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1278 DYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDEC-IYWPTKsQPIRFDTFTVTFMGE 1356
Cdd:cd14629     82 DYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKChQYWPAE-RSARYQYFVVDPMAE 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1357 DHMclsneDMLIVQDFILEATQDDYVLEVRQYRAPRWPNPDGPISNTfELINIIKE-----ESVSRDGPIVVHDKRGGNI 1431
Cdd:cd14629    161 YNM-----PQYILREFKVTDARDGQSRTIRQFQFTDWPEQGVPKTGE-GFIDFIGQvhktkEQFGQDGPITVHCSAGVGR 234

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1658117666 1432 AGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIM 1482
Cdd:cd14629    235 TGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAAL 285
alpha_CA_IX cd03150
Carbonic anhydrase alpha, isozyme IX. Carbonic anhydrases (CAs) are zinc-containing enzymes ...
 48-293 1.98e-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: 150.11  E-value: 1.98e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666   48 NQNNWAKKYPSCNNAKQSPINIDDDLSQVKMQFQKLKLEGFEQETSNTTTIHNDGKTVAINLNDEYYISGGGLRSrFKVG 127
Cdd:cd03150      1 GQPPWPSVSPACAGRFQSPVDIRPHLVAFCPALRPLELLGFDLPPSPSLRLLNNGHTVQLSLPSGLRMALGPGQE-YRAL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  128 RITFHWGQcnASSDGSEHSLDGIKFPLEMQIYGYEAhKFQSLDSALKDGGRLTALSVLFEVSAEDNENYVAIIDGVKTVT 207
Cdd:cd03150     80 QLHLHWGA--AGRPGSEHTVDGHRFPAEIHVVHLST-AFANLDEALGRPGGLAVLAAFLAEGLHENSAYEQLLSRLSEIS 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  208 RLGKTAVLEPFSLLGLLPNSTEKYYIYNGSLTTPPCSETVEWIVFRNTVDISDVQLETFCEVMTMQQAgyvmlmDYLQNN 287
Cdd:cd03150    157 EEESETVVPGLDVSALLPSDLSRYFRYEGSLTTPPCAQGVIWTVFNQTVRLSAKQLHTLSDSLWGPHD------SRLQLN 230


                   ....*.
gi 1658117666  288 FREQQL 293
Cdd:cd03150    231 FRATQP 236
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 984-1193 3.33e-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: 3.33e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  984 YINANYVDGFTQPKA--YIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCDQYWP-LDSQEE---YGSFLVT 1057
Cdd:cd14598      1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPrLGSRHNtvtYGRFKIT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1058 LRSTKVLAYYTQRTFTLKNTRAKKgsqkeqthERTVVQYHYTQWPDMGVPEYTLPVLTF------VRKSSQANLGNMG-- 1129
Cdd:cd14598     81 TRFRTDSGCYATTGLKIKHLLTGQ--------ERTVWHLQYTDWPEHGCPEDLKGFLSYleeiqsVRRHTNSTIDPKSpn 152

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1658117666 1130 -PVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVE 1193
Cdd:cd14598    153 pPVLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQ 217
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 1255-1479 3.87e-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: 148.66  E-value: 3.87e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1255 RNSSLLPVERSRVHLSTTAGEI-SDYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDE 1333
Cdd:cd14548      1 RYTNILPYDHSRVKLIPINEEEgSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1334 CI-YWPTKSQPIRFDTFTVTFMGEDHMclsneDMLIVQDFILEatQDDYVLEVRQYRAPRWPN---PDGPISntfeLINI 1409
Cdd:cd14548     81 CDhYWPFDQDPVYYGDITVTMLSESVL-----PDWTIREFKLE--RGDEVRSVRQFHFTAWPDhgvPEAPDS----LLRF 149

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1658117666 1410 IK---EESVSRDGPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYK 1479
Cdd:cd14548    150 VRlvrDYIKQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLHQ 222
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1092-1193 9.75e-40

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 142.88  E-value: 9.75e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  1092 TVVQYHYTQWPDMGVPEYTLPVLTFVR--KSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQI-KEQGTVNILGFLK 1168
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDSILELLRavKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLeAEAGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 1658117666  1169 HIRTQRNYLVQTEEQYIFIHDALVE 1193
Cdd:smart00404   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 1092-1193 9.75e-40

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: 142.88  E-value: 9.75e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  1092 TVVQYHYTQWPDMGVPEYTLPVLTFVR--KSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQI-KEQGTVNILGFLK 1168
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDSILELLRavKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLeAEAGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 1658117666  1169 HIRTQRNYLVQTEEQYIFIHDALVE 1193
Cdd:smart00012   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 1279-1481 3.58e-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: 3.58e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1279 YINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDEC-IYWPTKSQpIRFDTFTVTFMGEd 1357
Cdd:cd14552      1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCaQYWPEDGS-VSSGDITVELKDQ- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1358 hmclSNEDMLIVQDFILEATQDDYVLEVRQYRAPRWPNPDGPiSNTFELINII----KEESVSRDGPIVVHDKRGGNIAG 1433
Cdd:cd14552     79 ----TDYEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIP-DNGKGMIDLIaavqKQQQQSGNHPITVHCSAGAGRTG 153

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1658117666 1434 TFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVI 1481
Cdd:cd14552    154 TFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 1254-1485 6.80e-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: 6.80e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1254 NRNSSLLPVERSRVHLSTT-AGEISDYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAED 1332
Cdd:cd14619      1 NRFRNVLPYDWSRVPLKPIhEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1333 EC-IYWPTKSQPIRFDTFTVTFMGEDHMclsneDMLIVQDFILEATQDDYVLEVRQYRAPRWPNPDGPiSNTFELI---N 1408
Cdd:cd14619     81 KCeHYWPLDYTPCTYGHLRVTVVSEEVM-----ENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVP-SSTDTLLafrR 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1658117666 1409 IIKE--ESVSRDGPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIMSLV 1485
Cdd:cd14619    155 LLRQwlDQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILDFL 233
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 1254-1482 7.50e-38

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


Pssm-ID: 350466 [Multi-domain]  Cd Length: 230  Bit Score: 142.39  E-value: 7.50e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1254 NRNSSLLPVERSRVHLSTTAGEI-SDYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAED 1332
Cdd:cd14618      1 NRYPHVLPYDHSRVRLSQLGGEPhSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1333 ECI-YWPTKSQPIRFDTFTVTFMGEdhmclSNEDMLIVQDFILEATQDDYVLEVRQYRAPRWPN---PDGPiSNTFELIN 1408
Cdd:cd14618     81 LCDhYWPSESTPVSYGHITVHLLAQ-----SSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDhgiPEST-SSLMAFRE 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1658117666 1409 IIKEE--SVSRDGPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIM 1482
Cdd:cd14618    155 LVREHvqATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 1254-1482 7.96e-38

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: 142.26  E-value: 7.96e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1254 NRNSSLLPVERSRVHLSTTAGEISDYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDE 1333
Cdd:cd14615      1 NRYNNVLPYDISRVKLSVQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRTK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1334 C-IYWPTKsQPIRFDTFTVTfmgedhmcLSNEDML---IVQDFILEATQDDYVLEVRQYRAPRWpnPDGPISNTFELI-- 1407
Cdd:cd14615     81 CeEYWPSK-QKKDYGDITVT--------MTSEIVLpewTIRDFTVKNAQTNESRTVRHFHFTSW--PDHGVPETTDLLin 149

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1658117666 1408 --NIIKE--ESVSRDGPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIM 1482
Cdd:cd14615    150 frHLVREymKQNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCAL 228
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 1279-1478 2.46e-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: 139.84  E-value: 2.46e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1279 YINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDECI-YWPTKSQpirfdtftvTFmGED 1357
Cdd:cd14558      1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAqYWGDEKK---------TY-GDI 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1358 HMCLSNEDM---LIVQDFILEATQDDYVLEVRQYRAPRWpNPDGPISNTFELINIIKE---------ESVSRDGPIVVHD 1425
Cdd:cd14558     71 EVELKDTEKsptYTVRVFEITHLKRKDSRTVYQYQYHKW-KGEELPEKPKDLVDMIKSikqklpyknSKHGRSVPIVVHC 149

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1658117666 1426 KRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLY 1478
Cdd:cd14558    150 SDGSSRTGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 1278-1481 9.25e-37

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type tyrosine-protein phosphatase E (PTPRE), also known as receptor-type tyrosine-protein phosphatase epsilon (R-PTP-epsilon), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. The PTPRE gene contains two distinct promoters that generate the two major isoforms: transmembrane (receptor type RPTPe or PTPeM) and cytoplasmic (cyt-PTPe or PTPeC). Receptor type RPTPe plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells, and may also play a role in osteoclast formation and function. It also negatively regulates PDGFRbeta-mediated signaling pathways that are crucial for the pathogenesis of atherosclerosis. cyt-PTPe acts as a negative regulator of insulin receptor signaling in skeletal muscle. It regulates insulin-induced phosphorylation of proteins downstream of the insulin receptor. Receptor type RPTPe contains a small extracellular region, a single transmembrane segment, and an intracellular region two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350470 [Multi-domain]  Cd Length: 205  Bit Score: 138.21  E-value: 9.25e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1278 DYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDECI-YWPTKSqpirfdtfTVTFmGE 1356
Cdd:cd14622      1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVqYWPSEG--------SVTH-GE 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1357 DHMCLSNE---DMLIVQDFILEATQDDYVLEVRQYRAPRWPNPDGPiSNTFELINII----KEESVSRDGPIVVHDKRGG 1429
Cdd:cd14622     72 ITIEIKNDtllETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIP-AEGKGMIDLIaavqKQQQQTGNHPIVVHCSAGA 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1658117666 1430 NIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVI 1481
Cdd:cd14622    151 GRTGTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 1279-1478 1.59e-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: 134.46  E-value: 1.59e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1279 YINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDgLDLAEDECI-YWPTKSQPiRFDTFTVTFMGED 1357
Cdd:cd14556      1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQ-LDPKDQSCPqYWPDEGSG-TYGPIQVEFVSTT 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1358 hmclsNEDMLIVQDFILEAT---QDDYVLeVRQYRAPRWP-NPDGPIS--NTFELINII-KEESVSRDGPIVVHDKRGGN 1430
Cdd:cd14556     79 -----IDEDVISRIFRLQNTtrpQEGYRM-VQQFQFLGWPrDRDTPPSkrALLKLLSEVeKWQEQSGEGPIVVHCLNGVG 152

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1658117666 1431 IAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLY 1478
Cdd:cd14556    153 RSGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCY 200
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 1259-1481 1.61e-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: 1.61e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1259 LLPVERSRVHLSTTAGEI-SDYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDECI-Y 1336
Cdd:cd14623      5 IIPYEFNRVIIPVKRGEEnTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEKCAqY 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1337 WPTKSQpIRFDTFTVTFMGEDHmCLSnedmLIVQDFILEATQDDYVLEVRQYRAPRWPNPDGPiSNTFELINII----KE 1412
Cdd:cd14623     85 WPSDGS-VSYGDITIELKKEEE-CES----YTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIP-SDGKGMINIIaavqKQ 157

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1658117666 1413 ESVSRDGPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVI 1481
Cdd:cd14623    158 QQQSGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVV 226
alpha_CA_VI cd03125
Carbonic anhydrase alpha, isozyme VI. Carbonic anhydrases (CAs) are zinc-containing enzymes ...
 48-292 1.86e-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: 1.86e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666   48 NQNNWAKKYPSCNNAKQSPINIDDDLSQVKMQFQKLKLEGFEQETSnTTTIHNDGKTVAINLNDEYYISGGgLRSRFKVG 127
Cdd:cd03125      1 DESHWPEKYPACGGKRQSPIDIQRREVRFNPSLLQLELVGYEKEQG-EFTMTNNGHTVQIDLPPTMSITTG-DGTVYTAV 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  128 RITFHWGQCNASSDGSEHSLDGIKFPLEMQIYGYEAhKFQSLDSALKDGGRLTALSVLFEVSAE-DNENYVAIIDGVKTV 206
Cdd:cd03125     79 QMHFHWGGRDSEISGSEHTIDGMRYVAELHIVHYNS-KYKSYEEAKDKPDGLAVLAFLYKVGHYaENTYYSDFISKLAKI 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  207 TRLGKTAVLEPFSLLGLLPNSTEKYYIYNGSLTTPPCSETVEWIVFRNTVDISDVQLETFCEVmtmqqagyvmLMDY--- 283
Cdd:cd03125    158 KYAGQTTTLTSLDVRDMLPENLHHYYTYQGSLTTPPCTENVLWFVFDDPVTLSKTQIVKLENT----------LMDHhnk 227

                          250
                   ....*....|
gi 1658117666  284 -LQNNFREQQ 292
Cdd:cd03125    228 tIRNDYRRTQ 237
Cah COG3338
Carbonic anhydrase [Inorganic ion transport and metabolism];
36-266 4.25e-33

Carbonic anhydrase [Inorganic ion transport and metabolism];


Pssm-ID: 442567 [Multi-domain]  Cd Length: 247  Bit Score: 129.23  E-value: 4.25e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666   36 KEDIDWSYAGTLNQNNWAK---KYPSCNNAK-QSPINIDD----DLSQVKMQFQKLKLEgfeqetsntttIHNDGKTVAI 107
Cdd:COG3338     23 ASAPHWSYEGETGPEHWGElspEFATCATGKnQSPIDIRTaikaDLPPLKFDYKPTPLE-----------IVNNGHTIQV 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  108 NLNDEYYISGGGlrSRFKVGRITFHwgqcnassDGSEHSLDGIKFPLEMQIygyeAHKfqsldsalKDGGRLTALSVLFE 187
Cdd:COG3338     92 NVDPGSTLTVDG--KRYELKQFHFH--------TPSEHTINGKSYPMEAHL----VHK--------DADGELAVVGVLFE 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  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 ...
 1227-1484 5.95e-33

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


Pssm-ID: 350451 [Multi-domain]  Cd Length: 266  Bit Score: 129.17  E-value: 5.95e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1227 KQFKMI-TQSNAKQCDYS----AALKQCNRDKNRNSSLLPVERSRVHLSTTAGEI-SDYINASYIMGYQQSNEFIITQNP 1300
Cdd:cd14603      2 GEFSEIrACSAAFKADYVcstvAGGRKENVKKNRYKDILPYDQTRVILSLLQEEGhSDYINANFIKGVDGSRAYIATQGP 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1301 LPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDEC-IYWPTKSQPIRFDTFTVTFMGEDHMclsNEDmLIVQDFILEATQD 1379
Cdd:cd14603     82 LSHTVLDFWRMIWQYGVKVILMACREIEMGKKKCeRYWAQEQEPLQTGPFTITLVKEKRL---NEE-VILRTLKVTFQKE 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1380 DYVLEVRQYRAprWPN---PDGPiSNTFELINIIKEESVSRDGPIVVHDKRGGNIAGTFCAL---MTLLHQLEMESSFDV 1453
Cdd:cd14603    158 SRSVSHFQYMA--WPDhgiPDSP-DCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVdyvRQLLLTQRIPPDFSI 234

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1658117666 1454 YWVAKMINLMRPGIFTDIDQYQFLYKVIMSL 1484
Cdd:cd14603    235 FDVVLEMRKQRPAAVQTEEQYEFLYHTVAQM 265
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 984-1187 1.43e-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: 125.90  E-value: 1.43e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  984 YINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGrrKCDQYWPLDSQE-EYGSFLVTLRSTK 1062
Cdd:cd14550      1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNE--DEPIYWPTKEKPlECETFKVTLSGED 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1063 VLAY-----YTQRTFTLKNTrakkgsqkEQTHERTVVQYHYTQWPDMGVPEYTlpVLTFVRKSSQANLGNMGPVVVHCSA 1137
Cdd:cd14550     79 HSCLsneirLIVRDFILEST--------QDDYVLEVRQFQCPSWPNPCSPIHT--VFELINTVQEWAQQRDGPIVVHDRY 148

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1138 GVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFI 1187
Cdd:cd14550    149 GGVQAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFL 198
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 1250-1481 2.45e-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: 126.93  E-value: 2.45e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1250 NRDKNRNSSLLPVERSRVHL-STTAGEISDYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLD 1328
Cdd:cd14614     12 NRCKNRYTNILPYDFSRVKLvSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNE 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1329 LAEDECI-YWPTKSQPIRFDTFTVTFMGEdhmclSNEDMLIVQDFILeaTQDDYVLEVRQYRAPRWPNPDGPISNTFE-- 1405
Cdd:cd14614     92 KRRVKCDhYWPFTEEPVAYGDITVEMLSE-----EEQPDWAIREFRV--SYADEVQDVMHFNYTAWPDHGVPTANAAEsi 164

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1658117666 1406 --LINIIKEESVSRDGPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVI 1481
Cdd:cd14614    165 lqFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 242
alpha_CA_prokaryotic_like cd03124
Carbonic anhydrase alpha, prokaryotic-like subfamily. Carbonic anhydrases (CAs) are ...
 51-270 3.90e-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: 125.08  E-value: 3.90e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666   51 NWA---KKYPSCNNAK-QSPINIDDDLSQVKmqfqklKLEGFEQETSNTT-TIHNDGKTVAINLNDEyyisGGGLR---S 122
Cdd:cd03124      4 HWGnldPEFALCATGKnQSPIDITTKAVVSD------KLPPLNYNYKPTSaTLVNNGHTIQVNFEGN----GGTLTidgE 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  123 RFKVGRITFHwgqcnassDGSEHSLDGIKFPLEMQIygyeAHKfqsldsalKDGGRLTALSVLFEVSAEdNENYVAIIDG 202
Cdd:cd03124     74 TYQLLQFHFH--------SPSEHLINGKRYPLEAHL----VHK--------SKDGQLAVVAVLFEEGKE-NPFLKKILDN 132

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1658117666  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 ...
 984-1193 1.76e-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: 1.76e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  984 YINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLveKGRRKCDQYWPLDSQEEYGSFLVTLRSTKV 1063
Cdd:cd14634      1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEM--DAAQLCMQYWPEKTSCCYGPIQVEFVSADI 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1064 LAYYTQRTFTLKNTrakkgsQKEQTHERTVVQYHYTQWPDM-GVPEYTLPVLTFVR---KSSQANLGNMGPVVVHCSAGV 1139
Cdd:cd14634     79 DEDIISRIFRICNM------ARPQDGYRIVQHLQYIGWPAYrDTPPSKRSILKVVRrleKWQEQYDGREGRTVVHCLNGG 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1658117666 1140 GRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVE 1193
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 2.66e-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: 2.66e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666   40 DWSYAGTLNQNNWAKKYPSCNNAKQSPINIDDDLSQVKMQFQKLKlegFEQETSNTTTIHNDGKTVAINLNDEYYIS--- 116
Cdd:cd03119      4 HWGYDSHNGPEHWHELFPIAKGDRQSPIDIKTKDAKHDPSLKPLS---VSYDPATAKTILNNGHSFNVEFDDTDDRSvlr 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  117 GGGLRSRFKVGRITFHWGQCNasSDGSEHSLDGIKFPLEMQIYGYEAhKFQSLDSALKDGGRLTALSVLFEVSAEdNENY 196
Cdd:cd03119     81 GGPLTGSYRLRQFHFHWGSSD--DHGSEHTVDGVKYAAELHLVHWNS-KYGSFGEAAKQPDGLAVVGVFLKVGEA-NPEL 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  197 VAIIDGVKTVTRLGKTAVLEPFSLLGLLPNSTEkYYIYNGSLTTPPCSETVEWIVFRNTVDISDVQLETF 266
Cdd:cd03119    157 QKVLDALDSIKTKGKQAPFTNFDPSCLLPASLD-YWTYPGSLTTPPLLECVTWIVLKEPISVSSEQMAKF 225
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 1242-1479 1.06e-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: 122.86  E-value: 1.06e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1242 YSAALKQCNRDKNRNSSLLPVERSRVHLSTTAG-EISDYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVV 1320
Cdd:cd14543     21 FLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNGdERTDYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKVLVI 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1321 IALPDGLDLAEDEC-IYWP-TKSQPIRFDTFTVTFMG----EDHM---------------CLSNEDMLIVQDFIL---EA 1376
Cdd:cd14543    101 VMTTRVVERGRVKCgQYWPlEEGSSLRYGDLTVTNLSvenkEHYKkttleihntetdesrQVTHFQFTSWPDFGVpssAA 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1377 TQDDYVLEVRQYRA-------PRWP-NPDGPisntfeliniikeesvsrdgPIVVHDKRGGNIAGTFCALMTLLHQLEME 1448
Cdd:cd14543    181 ALLDFLGEVRQQQAlavkamgDRWKgHPPGP--------------------PIVVHCSAGIGRTGTFCTLDICLSQLEDV 240

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1658117666 1449 SSFDVYWVAKMINLMRPGIFTDIDQYQFLYK 1479
Cdd:cd14543    241 GTLNVMQTVRRMRTQRAFSIQTPDQYYFCYK 271
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 1248-1486 1.82e-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: 1.82e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1248 QCNRDKNRNSSLLPVERSRVHLSTTAG-EISDYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDG 1326
Cdd:cd14553      1 EVNKPKNRYANVIAYDHSRVILQPIEGvPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1327 LDLAEDEC-IYWPTKSQPIrFDTFTVTFMgeDHMCLSNedmLIVQDFILEATQDDYVLEVRQYRAPRWPN---PDGPISn 1402
Cdd:cd14553     81 EERSRVKCdQYWPTRGTET-YGLIQVTLL--DTVELAT---YTVRTFALHKNGSSEKREVRQFQFTAWPDhgvPEHPTP- 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1403 TFELINIIKEESVSRDGPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIM 1482
Cdd:cd14553    154 FLAFLRRVKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALL 233


                   ....
gi 1658117666 1483 SLVA 1486
Cdd:cd14553    234 EAVT 237
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 1254-1479 1.93e-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: 118.10  E-value: 1.93e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1254 NRNSSLLPVERSRVHLSTTAGE-ISDYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAED 1332
Cdd:cd14617      1 NRYNNILPYDSTRVKLSNVDDDpCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1333 ECI-YWPTKSQPIRFDTFTVTFMGEdhmclSNEDMLIVQDF-ILEATQDDYVLEVRQYRAPRWPNPDGPiSNTFELINII 1410
Cdd:cd14617     81 KCDhYWPADQDSLYYGDLIVQMLSE-----SVLPEWTIREFkICSEEQLDAPRLVRHFHYTVWPDHGVP-ETTQSLIQFV 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1658117666 1411 K--EESVSRD---GPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYK 1479
Cdd:cd14617    155 RtvRDYINRTpgsGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 1239-1482 2.51e-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: 2.51e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1239 QCDYSAALKQCNRDKNRNSSLLPVERSRVHLSTTAG-EISDYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHST 1317
Cdd:cd14621     41 QATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGvPDSDYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNT 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1318 QVVIALPDGLDLAEDECI-YWPtksqpirfDTFTVTFmgeDHMCLSNEDMLIVQDFIL---------EATQDDYVLEVRQ 1387
Cdd:cd14621    121 ATIVMVTNLKERKECKCAqYWP--------DQGCWTY---GNIRVSVEDVTVLVDYTVrkfciqqvgDVTNKKPQRLITQ 189

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1388 YRAPRWPN---PDGPISnTFELINIIKEESVSRDGPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMR 1464
Cdd:cd14621    190 FHFTSWPDfgvPFTPIG-MLKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQR 268

                          250
                   ....*....|....*...
gi 1658117666 1465 PGIFTDIDQYQFLYKVIM 1482
Cdd:cd14621    269 CQMVQTDMQYVFIYQALL 286
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 1254-1479 3.64e-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: 116.93  E-value: 3.64e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1254 NRNSSLLPVERSRVHLSTTAGEI-SDYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAED 1332
Cdd:cd14616      1 NRFPNIKPYNNNRVKLIADAGVPgSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1333 EC-IYWPTKSQPIR-FDTFTVTFMGEDhmclsNEDMLIVQDFILEaTQDDYVLeVRQYRAPRWPNPDGPiSNTFELINII 1410
Cdd:cd14616     81 RChQYWPEDNKPVTvFGDIVITKLMED-----VQIDWTIRDLKIE-RHGDYMM-VRQCNFTSWPEHGVP-ESSAPLIHFV 152

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1658117666 1411 KEESVSRDG---PIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYK 1479
Cdd:cd14616    153 KLVRASRAHdntPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLHQ 224
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 1279-1478 3.81e-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: 116.58  E-value: 3.81e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1279 YINASYI-MGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDEC-IYWPTKSQPIRFDTFTVTFMGE 1356
Cdd:cd18533      1 YINASYItLPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCdQYWPSGEYEGEYGDLTVELVSE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1357 DHmclsNEDM-LIVQDFILeATQDDYVLEVRQYRAPRWPN---PDGPISnTFELINIIKE--ESVSRDGPIVVHDKRGGN 1430
Cdd:cd18533     81 EE----NDDGgFIVREFEL-SKEDGKVKKVYHIQYKSWPDfgvPDSPED-LLTLIKLKRElnDSASLDPPIIVHCSAGVG 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1658117666 1431 IAGTFCALMTLLHQLEMESSFDVYW------VAKMINLM---RPGIFTDIDQYQFLY 1478
Cdd:cd18533    155 RTGTFIALDSLLDELKRGLSDSQDLedsedpVYEIVNQLrkqRMSMVQTLRQYIFLY 211
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 1253-1484 1.13e-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: 115.71  E-value: 1.13e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1253 KNRNSSLLPVERSRVHLS-TTAGEISDYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAE 1331
Cdd:cd14602      1 KNRYKDILPYDHSRVELSlITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1332 DEC-IYWP-TKSQPIRFDTFTVTFMGEDhmclsNEDMLIVQdfILEATQDDYVLEVRQYRAPRWPNPDGP--ISNTFELI 1407
Cdd:cd14602     81 KKCeRYWAePGEMQLEFGPFSVTCEAEK-----RKSDYIIR--TLKVKFNSETRTIYQFHYKNWPDHDVPssIDPILELI 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1408 NIIKEESVSRDGPIVVHDKRGGNIAGTFCAL---MTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIMSL 1484
Cdd:cd14602    154 WDVRCYQEDDSVPICIHCSAGCGRTGVICAIdytWMLLKDGIIPENFSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIEL 233
alpha_CA_VII cd03149
Carbonic anhydrase alpha, CA isozyme VII_like subgroup. Carbonic anhydrases (CAs) are ...
 63-292 2.02e-28

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: 115.32  E-value: 2.02e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666   63 KQSPINIDDDLSQVKMQFQKLKLEgFEQETSntTTIHNDGKTVAINLND---EYYISGGGLRSRFKVGRITFHWGQcnAS 139
Cdd:cd03149      3 RQSPIDIVSSEAVYDPKLKPLSLS-YDPCTS--LSISNNGHSVMVEFDDsddKTVITGGPLENPYRLKQFHFHWGA--KH 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  140 SDGSEHSLDGIKFPLEMQIYGYEAHKFQSLDSALKDGGRLTALSVLFEVSAEdNENYVAIIDGVKTVTRLGKTAVLEPFS 219
Cdd:cd03149     78 GSGSEHTVDGKTFPSELHLVHWNAKKYKSFGEAAAAPDGLAVLGVFLETGDE-HPGLNRLTDALYMVRFKGTKAQFLDFN 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1658117666  220 LLGLLPNSTEkYYIYNGSLTTPPCSETVEWIVFRNTVDISDVQLETFCEVMTMQQAGYVMLMdylQNNFREQQ 292
Cdd:cd03149    157 PKCLLPKSLD-YWTYPGSLTTPPLNESVTWIVLKEPIPVSEKQMGKFRELLFTSEEDQRNHM---VNNFRPPQ 225
alpha_CARP_X_XI_like cd03121
Carbonic anhydrase alpha related protein: groups X, XI and related proteins. This subgroup ...
 59-292 2.26e-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: 115.59  E-value: 2.26e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666   59 CNNAK-QSPINIDDDlsqvKMQFQ----KLKLEGFEQETSnttTIHNDGKTVAINLNDEY--YISGGGLRSRFKVGRITF 131
Cdd:cd03121     15 CSKGRrQSPVDIEPS----RLLFDpfltPLRIDTGRKVSG---TFYNTGRHVSFRPDKDPvvNISGGPLSYRYRLEEIRL 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  132 HWGQCNasSDGSEHSLDGIKFPLEMQIYGYEAHKFQSLDSALKDGGRLTALSVLFEVSAEDNE--NYVAIIDGVKTVTRL 209
Cdd:cd03121     88 HFGRED--EQGSEHTVNGQAFPGEVQLIHYNSELYPNFSEASKSPNGLVIVSLFVKIGETSNPelRRLTNRDTITSIRYK 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  210 GKTAVLEPFSLLGLLPNsTEKYYIYNGSLTTPPCSETVEWIVFRNTVDISDVQLEtfcEVMTMQQAGYVMLMDYLQNNFR 289
Cdd:cd03121    166 GDAYFLQDLSIELLLPE-TDHYITYEGSLTSPGCHETVTWIILNKPIYITKEQMH---SLRLLSQNSPSQEKAPMSPNFR 241


                   ...
gi 1658117666  290 EQQ 292
Cdd:cd03121    242 PVQ 244
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 1254-1478 2.97e-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: 2.97e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1254 NRNSSLLPVERSRVHL-STTAGEISDYINASYIMGYQQSNE-FIITQNPLPSTMKDFWKMIWDHSTQVVIALPDgLDLAE 1331
Cdd:cd14547      1 NRYKTILPNEHSRVCLpSVDDDPLSSYINANYIRGYDGEEKaYIATQGPLPNTVADFWRMVWQEKTPIIVMITN-LTEAK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1332 DECI-YWPTKsQPIRFDTFTVTFMGEDHmclsnEDMLIVQDFILEatqddYVLEVR---QYRAPRWPN---PD--GPISN 1402
Cdd:cd14547     80 EKCAqYWPEE-ENETYGDFEVTVQSVKE-----TDGYTVRKLTLK-----YGGEKRylkHYWYTSWPDhktPEaaQPLLS 148

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1658117666 1403 TFELINIIKEESVSRdGPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLY 1478
Cdd:cd14547    149 LVQEVEEARQTEPHR-GPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVH 223
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 1242-1482 4.05e-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: 115.53  E-value: 4.05e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1242 YSAALKQCNRDKNRNSSLLPVERSRVHLSTTAGEI-SDYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVV 1320
Cdd:cd14633     32 WDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETsSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASI 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1321 IALPDGLDLAEDECI-YWPTKSQPIRfdTFTVTFMGEDHMClsnedMLIVQDFILEATQDDYVLEVRQYRAPRWPNPDGP 1399
Cdd:cd14633    112 IMVTNLVEVGRVKCCkYWPDDTEIYK--DIKVTLIETELLA-----EYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVP 184

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1400 ISNT--FELINIIKEESVSRDGPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFL 1477
Cdd:cd14633    185 YHATglLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFI 264


                   ....*
gi 1658117666 1478 YKVIM 1482
Cdd:cd14633    265 HDAIL 269
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 1247-1488 4.18e-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: 4.18e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1247 KQCNRDKNRNSSLLPVERSRVHLS-TTAGEISDYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPD 1325
Cdd:cd14604     54 KEENVKKNRYKDILPFDHSRVKLTlKTSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACR 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1326 GLDLAEDEC-IYWPT-KSQPIRFDTFTVTFMGEDhmclSNEDMLIvQDFILEATQDDYvlEVRQYRAPRWPNPDGPIS-- 1401
Cdd:cd14604    134 EFEMGRKKCeRYWPLyGEEPMTFGPFRISCEAEQ----ARTDYFI-RTLLLEFQNETR--RLYQFHYVNWPDHDVPSSfd 206

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1402 NTFELINIIKEESVSRDGPIVVHDKRGGNIAGTFCAL---MTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLY 1478
Cdd:cd14604    207 SILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIdytWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVH 286

                          250
                   ....*....|
gi 1658117666 1479 KVIMSLVAKK 1488
Cdd:cd14604    287 RAIAQLFEKQ 296
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 1250-1481 8.33e-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: 114.10  E-value: 8.33e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1250 NRDKNRNSSLLPVERSRVHL----STTAGeiSDYINASYIM-------GYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQ 1318
Cdd:cd14544      1 NKGKNRYKNILPFDHTRVILkdrdPNVPG--SDYINANYIRnenegptTDENAKTYIATQGCLENTVSDFWSMVWQENSR 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1319 VVIALPDGLDLAEDECI-YWPTKSQPIRFDTFTVTFMGEDhmclSNEDMlIVQDFILEAT-QDDYVLEVRQYRAPRWPN- 1395
Cdd:cd14544     79 VIVMTTKEVERGKNKCVrYWPDEGMQKQYGPYRVQNVSEH----DTTDY-TLRELQVSKLdQGDPIREIWHYQYLSWPDh 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1396 --PDGP--ISNTFELINiIKEESVSRDGPIVVHDKRGGNIAGTFCALMTLLHQLE---MESSFDVYWVAKMINLMRPGIF 1468
Cdd:cd14544    154 gvPSDPggVLNFLEDVN-QRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKrkgLDCDIDIQKTIQMVRSQRSGMV 232

                          250
                   ....*....|...
gi 1658117666 1469 TDIDQYQFLYKVI 1481
Cdd:cd14544    233 QTEAQYKFIYVAV 245
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 1248-1482 8.74e-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: 8.74e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1248 QCNRDKNRNSSLLPVERSRVHLSTTAG-EISDYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDG 1326
Cdd:cd14626     39 EVNKPKNRYANVIAYDHSRVILTSVDGvPGSDYINANYIDGYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRL 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1327 LDLAEDEC-IYWPTKSQPIrFDTFTVTFMgeDHMCLSNedmLIVQDFILEATQDDYVLEVRQYRAPRWPN---PDGPiSN 1402
Cdd:cd14626    119 EEKSRVKCdQYWPIRGTET-YGMIQVTLL--DTVELAT---YSVRTFALYKNGSSEKREVRQFQFMAWPDhgvPEYP-TP 191

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1403 TFELINIIKEESVSRDGPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIM 1482
Cdd:cd14626    192 ILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALL 271
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 1250-1485 1.16e-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: 114.36  E-value: 1.16e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1250 NRDKNRNSSLLPVERSRVHLSTTAGEIS---DYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDG 1326
Cdd:cd17667     27 NKHKNRYINILAYDHSRVKLRPLPGKDSkhsDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNL 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1327 LDLAEDEC-IYWPTKSQPiRFDTFTVTFMGED-HMCLSnedmliVQDFILEATQDDYVLE-----------VRQYRAPRW 1393
Cdd:cd17667    107 VEKGRRKCdQYWPTENSE-EYGNIIVTLKSTKiHACYT------VRRFSIRNTKVKKGQKgnpkgrqnertVIQYHYTQW 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1394 PNPDGPiSNTFELINIIKEESVSRD---GPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTD 1470
Cdd:cd17667    180 PDMGVP-EYALPVLTFVRRSSAARTpemGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQT 258

                          250
                   ....*....|....*
gi 1658117666 1471 IDQYQFLYKVIMSLV 1485
Cdd:cd17667    259 EEQYIFIHDALLEAI 273
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 1250-1482 1.17e-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: 113.20  E-value: 1.17e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1250 NRDKNRNSSLLPVERSRVHLSTTAGEI-SDYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLD 1328
Cdd:cd14630      3 NRNKNRYGNIISYDHSRVRLQLLDGDPhSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVE 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1329 LAEDECI-YWPTKSQPirFDTFTVTFMGEDHMClsnedMLIVQDFILEATQDDYVLEVRQYRAPRWPNPDGPISNT--FE 1405
Cdd:cd14630     83 VGRVKCVrYWPDDTEV--YGDIKVTLIETEPLA-----EYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATglLG 155

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1658117666 1406 LINIIKEESVSRDGPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIM 1482
Cdd:cd14630    156 FVRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAIL 232
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 1250-1482 2.74e-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: 111.85  E-value: 2.74e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1250 NRDKNRNSSLLPVERSRVHLsttaGEISDYINASYIMGYQQSNEF--IITQNPLPSTMKDFWKMIWDHSTQVVIALPDGL 1327
Cdd:cd14597      3 NRKKNRYKNILPYDTTRVPL----GDEGGYINASFIKMPVGDEEFvyIACQGPLPTTVADFWQMVWEQKSTVIAMMTQEV 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1328 DLAEDECI-YWPtksqpirfDTFTVTFMGEDHMCLSNEDMLIVQDFI-----LEATQDDYVLEVRQYRAPRWPNPDGPiS 1401
Cdd:cd14597     79 EGGKIKCQrYWP--------EILGKTTMVDNRLQLTLVRMQQLKNFVirvleLEDIQTREVRHITHLNFTAWPDHDTP-S 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1402 NTFELINIIK-EESVSRDGPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKV 1480
Cdd:cd14597    150 QPEQLLTFISyMRHIHKSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQV 229


                   ..
gi 1658117666 1481 IM 1482
Cdd:cd14597    230 IL 231
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 1248-1486 4.25e-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: 112.88  E-value: 4.25e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1248 QCNRDKNRNSSLLPVERSRVHLSTTAGEI-SDYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDG 1326
Cdd:cd14625     45 EVNKPKNRYANVIAYDHSRVILQPIEGIMgSDYINANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKL 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1327 LDLAEDEC-IYWPTKSQPIrFDTFTVTFMgeDHMCLSNedmLIVQDFILEATQDDYVLEVRQYRAPRWPNPDGPISNT-- 1403
Cdd:cd14625    125 EEKSRIKCdQYWPSRGTET-YGMIQVTLL--DTIELAT---FCVRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTpf 198

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1404 FELINIIKEESVSRDGPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIMS 1483
Cdd:cd14625    199 LAFLRRVKTCNPPDAGPIVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLE 278


                   ...
gi 1658117666 1484 LVA 1486
Cdd:cd14625    279 AVA 281
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 1258-1482 7.13e-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: 110.42  E-value: 7.13e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1258 SLLPVERSRVHLSTTAGEI-SDYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDECI- 1335
Cdd:cd14620      3 NILPYDHSRVILSQLDGIPcSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKCYq 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1336 YWPTKSQPIrfdtftvtfMGEDHMCLsnEDMLIVQDFILEATQDDYVLEvRQYRAPR---------WPN---PDGPISnT 1403
Cdd:cd14620     83 YWPDQGCWT---------YGNIRVAV--EDCVVLVDYTIRKFCIQPQLP-DGCKAPRlvtqlhftsWPDfgvPFTPIG-M 149

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1658117666 1404 FELINIIKEESVSRDGPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIM 1482
Cdd:cd14620    150 LKFLKKVKSVNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALL 228
alpha_CARP_VIII cd03120
Carbonic anhydrase alpha related protein, group VIII. Carbonic anhydrase related proteins ...
 52-292 8.52e-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: 8.52e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666   52 WAKKYPSCNNAKQSPINIDDDLSQVKMQFQKLKLEGFEQETSNTTTIhNDGKTVAINLNDEYYISGGGL--RSRFKVGRI 129
Cdd:cd03120      4 WGLLFPEANGEYQSPINLNSREARYDPSLLEVRLSPNYVVCRDCEVI-NDGHTIQIILKSKSVLSGGPLpqGHEFELAEV 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  130 TFHWGQCNasSDGSEHSLDGIKFPLEMQIYGYEAHKFQSLDSALKDGGRLTALSVLFEVSAEdNENYVAIIDGVKTVTRL 209
Cdd:cd03120     83 RFHWGREN--QRGSEHTVNFKAFPMELHLIHWNSTLYSSLEEAMGKPHGIAIIALFVQIGKE-HVGLKAVTEILQDIQYK 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  210 GKTAVLEPFSLLGLLPNSTEK-YYIYNGSLTTPPCSETVEWIVFRNTVDISDVQLETFCEVMT-MQQAGYVMLMDY-LQN 286
Cdd:cd03120    160 GKSKTIPCFNPNTLLPDPLLRdYWVYEGSLTTPPCSEGVTWILFRYPLTISQSQIEEFRRLRThVKGAELVEGCDGlLGD 239


                   ....*.
gi 1658117666  287 NFREQQ 292
Cdd:cd03120    240 NFRPTQ 245
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 1279-1478 9.10e-27

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


Pssm-ID: 350397 [Multi-domain]  Cd Length: 204  Bit Score: 109.36  E-value: 9.10e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1279 YINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDEC-IYWPTKSQPiRFDTFTVTFMGED 1357
Cdd:cd14549      1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCdQYWPKEGTE-TYGNIQVTLLSTE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1358 HM--------CLSNEDmlivqdfILEATQDDYVLEVRQYRAPRWPN---PDGPISntfeLINIIKEESVSRD---GPIVV 1423
Cdd:cd14549     80 VLatytvrtfSLKNLK-------LKKVKGRSSERVVYQYHYTQWPDhgvPDYTLP----VLSFVRKSSAANPpgaGPIVV 148

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1658117666 1424 HDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLY 1478
Cdd:cd14549    149 HCSAGVGRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 1225-1491 2.18e-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: 2.18e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1225 LEKQFKMITQSNAKQCDYSAALKQCNRDKNRNSSLLPVERSRVHLST-TAGEISDYINASYIMGYQQSN-EFIITQNPLP 1302
Cdd:cd14610     19 LEKEWEALCAYQAEPNATNVAQREENVQKNRSLAVLPYDHSRIILKAeNSHSHSDYINASPIMDHDPRNpAYIATQGPLP 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1303 STMKDFWKMIWDHSTQVVIALPdglDLAED---ECI-YWPTKSQPIrFDTFTVTFMGEDHMClsnEDMLiVQDFILEATQ 1378
Cdd:cd14610     99 ATVADFWQMVWESGCVVIVMLT---PLAENgvkQCYhYWPDEGSNL-YHIYEVNLVSEHIWC---EDFL-VRSFYLKNLQ 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1379 DDYVLEVRQYRAPRWPNPDGPiSNTFELINIIKEESV---SRDGPIVVHDKRGGNIAGTFCALMTLLHQL-EMESSFDVY 1454
Cdd:cd14610    171 TNETRTVTQFHFLSWNDQGVP-ASTRSLLDFRRKVNKcyrGRSCPIIVHCSDGAGRSGTYILIDMVLNKMaKGAKEIDIA 249

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1658117666 1455 WVAKMINLMRPGIFTDIDQYQFlykvimSLVAKKEEV 1491
Cdd:cd14610    250 ATLEHLRDQRPGMVQTKEQFEF------ALTAVAEEV 280
alpha_CA_V cd03118
Carbonic anhydrase alpha, CA isozyme V_like subgroup. Carbonic anhydrases (CAs) are ...
 63-303 7.69e-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: 107.62  E-value: 7.69e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666   63 KQSPINIDDDLSQVKMQFQKLKLEgfeQETSNTTTIHNDGKTVAINLND---EYYISGGGLRSRFKVGRITFHWGQCNAS 139
Cdd:cd03118      3 RQSPINIQWRDSVYDPQLAPLRVS---YDPATCLYIWNNGYSFQVEFDDstdKSGISGGPLENHYRLKQFHFHWGANNEW 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  140 sdGSEHSLDGIKFPLEMQIYGYEAHKFQSLDSALKDGGRLTALSVLFEVSAEdNENYVAIIDGVKTVTRLGKTAVLEPFS 219
Cdd:cd03118     80 --GSEHTVDGHTYPAELHLVHWNSVKYENFEEAVMEENGLAVIGVFLKLGAH-HEGLQKLVDALPEVRHKDTVVEFNPFD 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  220 LLGLLPNSTEkYYIYNGSLTTPPCSETVEWIVFRNTVDISDVQLETFcEVMTMQQAGYVmlMDYLQNNFREQQLKFVGQV 299
Cdd:cd03118    157 PSCLLPACRD-YWTYPGSLTTPPLTESVTWIIQKQPIEVSPSQLSVF-RTLLFTSRGEE--EKVMVNNFRPLQPLMNRKV 232


                   ....
gi 1658117666  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 ...
 984-1193 8.73e-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: 8.73e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  984 YINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNL-VEKGrrkCDQYWPLDSQEEYGSFLVTLRSTK 1062
Cdd:cd14636      1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVdLAQG---CPQYWPEEGMLRYGPIQVECMSCS 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1063 VLAYYTQRTFTLKN-TRAKKGSQkeqtherTVVQYHYTQWPDM----GVPEYTLPVLTFVRKSSQANLGNMGPVVVHCSA 1137
Cdd:cd14636     78 MDCDVISRIFRICNlTRPQEGYL-------MVQQFQYLGWASHrevpGSKRSFLKLILQVEKWQEECDEGEGRTIIHCLN 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1658117666 1138 GVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVE 1193
Cdd:cd14636    151 GGGRSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 1277-1482 9.59e-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: 9.59e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1277 SDYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDECI-YWPTKSQpiRFDTFTVTFMG 1355
Cdd:cd14631     13 SDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYkYWPDDTE--VYGDFKVTCVE 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1356 EDHMClsnedMLIVQDFILEATQDDYVLEVRQYRAPRWPNPDGPISNT--FELINIIKEESVSRDGPIVVHDKRGGNIAG 1433
Cdd:cd14631     91 MEPLA-----EYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATglLSFIRRVKLSNPPSAGPIVVHCSAGAGRTG 165

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1658117666 1434 TFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIM 1482
Cdd:cd14631    166 CYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAIL 214
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 1279-1482 9.93e-26

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: 106.54  E-value: 9.93e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1279 YINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDECI-YWPTKSQPirFDTFTVTfmged 1357
Cdd:cd14555      1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSrYWPDDTEV--YGDIKVT----- 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1358 hmCLSNEDM--LIVQDFILEATQDDYVLEVRQYRAPRWPNPDGPISNT--FELINIIKEESVSRDGPIVVHDKRGGNIAG 1433
Cdd:cd14555     74 --LVETEPLaeYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATglLGFIRRVKASNPPSAGPIVVHCSAGAGRTG 151

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1658117666 1434 TFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIM 1482
Cdd:cd14555    152 CYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAIL 200
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 1225-1491 1.04e-25

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: 1.04e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1225 LEKQFKMITQSNAKQCDYSAALKQCNRDKNRNSSLLPVERSRVHL-STTAGEISDYINASYIMGYQ-QSNEFIITQNPLP 1302
Cdd:cd14609     17 LAKEWQALCAYQAEPNTCSTAQGEANVKKNRNPDFVPYDHARIKLkAESNPSRSDYINASPIIEHDpRMPAYIATQGPLS 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1303 STMKDFWKMIWDHSTQVVIALPDGLDLAEDEC-IYWPTKSQPIrFDTFTVTFMGEDHMClsnEDMLiVQDFILEATQDDY 1381
Cdd:cd14609     97 HTIADFWQMVWENGCTVIVMLTPLVEDGVKQCdRYWPDEGSSL-YHIYEVNLVSEHIWC---EDFL-VRSFYLKNVQTQE 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1382 VLEVRQYRAPRWPnPDGPISNTFELINIIKEESVS---RDGPIVVHDKRGGNIAGTFCAL-MTLLHQLEMESSFDVYWVA 1457
Cdd:cd14609    172 TRTLTQFHFLSWP-AEGIPSSTRPLLDFRRKVNKCyrgRSCPIIVHCSDGAGRTGTYILIdMVLNRMAKGVKEIDIAATL 250

                          250       260       270
                   ....*....|....*....|....*....|....
gi 1658117666 1458 KMINLMRPGIFTDIDQYQFlykvimSLVAKKEEV 1491
Cdd:cd14609    251 EHVRDQRPGMVRTKDQFEF------ALTAVAEEV 278
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 1243-1481 1.12e-25

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 109.73  E-value: 1.12e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1243 SAALKQCNRDKNRNSSLLPVERSRVHLS--------------------TTAGEISDYINASYIMGYQQSNEFIITQNPLP 1302
Cdd:PHA02746    44 NHFLKKENLKKNRFHDIPCWDHSRVVINaheslkmfdvgdsdgkkievTSEDNAENYIHANFVDGFKEANKFICAQGPKE 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1303 STMKDFWKMIWDHSTQVVIALPDGLDLAEDECIYWPT-KSQPIRFDTFTVTFMGEDHMCLSNEDMLIVQDFILEATQddy 1381
Cdd:PHA02746   124 DTSEDFFKLISEHESQVIVSLTDIDDDDEKCFELWTKeEDSELAFGRFVAKILDIIEELSFTKTRLMITDKISDTSR--- 200

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1382 vlEVRQYRAPRWP---NPDGPiSNTFELINIIKEESV----------SRDGPIVVHDKRGGNIAGTFCALMTLLHQLEME 1448
Cdd:PHA02746   201 --EIHHFWFPDWPdngIPTGM-AEFLELINKVNEEQAelikqadndpQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKE 277

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1658117666 1449 SSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVI 1481
Cdd:PHA02746   278 KEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 1248-1485 1.42e-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: 108.28  E-value: 1.42e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1248 QCNRDKNRNSSLLPVERSRVHLSTTAG-EISDYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDG 1326
Cdd:cd14624     45 EVNKPKNRYANVIAYDHSRVLLSAIEGiPGSDYINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKL 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1327 LDLAEDEC-IYWPTKSQPIRfDTFTVTFMgeDHMCLSNedmLIVQDFILEATQDDYVLEVRQYRAPRWPN---PDGPiSN 1402
Cdd:cd14624    125 EERSRVKCdQYWPSRGTETY-GLIQVTLL--DTVELAT---YCVRTFALYKNGSSEKREVRQFQFTAWPDhgvPEHP-TP 197

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1403 TFELINIIKEESVSRDGPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIM 1482
Cdd:cd14624    198 FLAFLRRVKTCNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALL 277


                   ...
gi 1658117666 1483 SLV 1485
Cdd:cd14624    278 EAV 280
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 1253-1478 1.61e-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: 107.23  E-value: 1.61e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1253 KNRNSSLLPVERSRVHLSTTA--GEISDYINASYIMGYQ-QSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDgLDL 1329
Cdd:cd14612     18 KDRYKTILPNPQSRVCLRRAGsqEEEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMITK-LKE 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1330 AEDECI-YWPTKSQPirFDTFTVTFMGedhmcLSNEDMLIVQDFILEATQDDYvlEVRQYRAPRWPNPDGPISnTFELIN 1408
Cdd:cd14612     97 KKEKCVhYWPEKEGT--YGRFEIRVQD-----MKECDGYTIRDLTIQLEEESR--SVKHYWFSSWPDHQTPES-AGPLLR 166

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1658117666 1409 IIKEESVSRD-----GPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLY 1478
Cdd:cd14612    167 LVAEVEESRQtaaspGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLH 241
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 984-1193 4.27e-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: 104.61  E-value: 4.27e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  984 YINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRR-KCDQYWPLDSQEEYGSFLVTLRSTK 1062
Cdd:cd14637      1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWPEPGLQQYGPMEVEFVSGS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1063 VLAYYTQRTFTLKN-TRAKKGsqkeqthERTVVQYHYTQW-PDMGVPEYT---LPVLTFVRKsSQANLGNmGPVVVHCSA 1137
Cdd:cd14637     81 ADEDIVTRLFRVQNiTRLQEG-------HLMVRHFQFLRWsAYRDTPDSKkafLHLLASVEK-WQRESGE-GRTVVHCLN 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1658117666 1138 GVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVE 1193
Cdd:cd14637    152 GGGRSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 1250-1478 4.92e-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: 4.92e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1250 NRDKNRNSSLLPVERSRVHLSTtagEISDYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDL 1329
Cdd:cd14608     25 NKNRNRYRDVSPFDHSRIKLHQ---EDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEK 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1330 AEDECI-YWPTKSQ-PIRFD--TFTVTFMGEDhmclsNEDMLIVQDFILEATQDDYVLEVRQYRAPRWPN---PDGPISN 1402
Cdd:cd14608    102 GSLKCAqYWPQKEEkEMIFEdtNLKLTLISED-----IKSYYTVRQLELENLTTQETREILHFHYTTWPDfgvPESPASF 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1403 TFELINIIKEESVSRD-GPIVVHDKRGGNIAGTFCALMT---LLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLY 1478
Cdd:cd14608    177 LNFLFKVRESGSLSPEhGPVVVHCSAGIGRSGTFCLADTcllLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSY 256
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 984-1193 5.61e-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: 104.38  E-value: 5.61e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  984 YINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLveKGRRKCDQYWPLDSQEEYGSFLVTLRSTKV 1063
Cdd:cd14635      1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDV--DPAQLCPQYWPENGVHRHGPIQVEFVSADL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1064 LAYYTQRTFTLKNtrakkgSQKEQTHERTVVQYHYTQWP---DMGVPEYT-LPVLTFVRKSSQANLGNMGPVVVHCSAGV 1139
Cdd:cd14635     79 EEDIISRIFRIYN------AARPQDGYRMVQQFQFLGWPmyrDTPVSKRSfLKLIRQVDKWQEEYNGGEGRTVVHCLNGG 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1658117666 1140 GRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALVE 1193
Cdd:cd14635    153 GRSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 1279-1479 1.27e-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: 103.27  E-value: 1.27e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1279 YINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDEC-IYWPTKSQP-IRFDTFTVTFMGE 1356
Cdd:cd14542      1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCeRYWPEEGEEqLQFGPFKISLEKE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1357 DHMClsnEDMLIVQdfiLEATQDDYVLEVRQYRAPRWPNPDGPISNT--FELINIIKEESVSRDGPIVVHDKRGGNIAGT 1434
Cdd:cd14542     81 KRVG---PDFLIRT---LKVTFQKESRTVYQFHYTAWPDHGVPSSVDpiLDLVRLVRDYQGSEDVPICVHCSAGCGRTGT 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1658117666 1435 FCAL---MTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYK 1479
Cdd:cd14542    155 ICAIdyvWNLLKTGKIPEEFSLFDLVREMRKQRPAMVQTKEQYELVYR 202
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 1279-1482 1.41e-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: 1.41e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1279 YINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDgLDLAEDECIYWPTKSQ----PIRfdtftVTFM 1354
Cdd:cd14634      1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNE-MDAAQLCMQYWPEKTSccygPIQ-----VEFV 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1355 GEDhmclSNEDML--IVQDFILEATQDDYVLeVRQYRAPRWPN-PDGPISNTFEL-----INIIKEESVSRDGPIVVHDK 1426
Cdd:cd14634     75 SAD----IDEDIIsrIFRICNMARPQDGYRI-VQHLQYIGWPAyRDTPPSKRSILkvvrrLEKWQEQYDGREGRTVVHCL 149

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1658117666 1427 RGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIM 1482
Cdd:cd14634    150 NGGGRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVAL 205
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 1279-1482 1.81e-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: 102.84  E-value: 1.81e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1279 YINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDgLDLAEDECIYWPTKSQPiRFDTFTVTFMGEDh 1358
Cdd:cd14635      1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLND-VDPAQLCPQYWPENGVH-RHGPIQVEFVSAD- 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1359 mclSNEDML--IVQDFILEATQDDYVLeVRQYRAPRWP-NPDGPISNT--FELINII---KEESVSRDGPIVVHDKRGGN 1430
Cdd:cd14635     78 ---LEEDIIsrIFRIYNAARPQDGYRM-VQQFQFLGWPmYRDTPVSKRsfLKLIRQVdkwQEEYNGGEGRTVVHCLNGGG 153

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1658117666 1431 IAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIM 1482
Cdd:cd14635    154 RSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVAL 205
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 1279-1482 2.05e-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: 2.05e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1279 YINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDECI-YWPTKSqpirfDTFtvtfmGED 1357
Cdd:cd14632      1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSkYWPDDS-----DTY-----GDI 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1358 HMCLSNEDML---IVQDFILEATQDDYVLEVRQYRAPRWPNPDGPISNT--FELINIIKEESVSRDGPIVVHDKRGGNIA 1432
Cdd:cd14632     71 KITLLKTETLaeySVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATglLAFIRRVKASTPPDAGPVVVHCSAGAGRT 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1433 GTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIM 1482
Cdd:cd14632    151 GCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAIL 200
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 1253-1484 2.22e-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: 104.17  E-value: 2.22e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1253 KNRNSSLLPVERSRVHLSTTAGE--ISDYINASYIMGY-QQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDL 1329
Cdd:cd14613     28 KNRYKTILPNPHSRVCLTSPDQDdpLSSYINANYIRGYgGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEM 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1330 AEDECIYWPTKSqpirfdtftVTFMGEDhmclsnedmLIVQDFILEatqDDYVLEV------------RQYRAPRWPNPD 1397
Cdd:cd14613    108 NEKCTEYWPEEQ---------VTYEGIE---------ITVKQVIHA---DDYRLRLitlksggeerglKHYWYTSWPDQK 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1398 GPiSNTFELINIIKEESVSR------DGPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDI 1471
Cdd:cd14613    167 TP-DNAPPLLQLVQEVEEARqqaepnCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTC 245

                          250
                   ....*....|...
gi 1658117666 1472 DQYQFLYKViMSL 1484
Cdd:cd14613    246 EQYQFVHHV-LSL 257
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 1251-1479 3.66e-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: 102.86  E-value: 3.66e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1251 RDKNRNSSLLPVERSRVHLSttaGEISDYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLA 1330
Cdd:cd14545      1 LNRYRDRDPYDHDRSRVKLK---QGDNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1331 EDECI-YWPTKSQP---IRFDTFTVTFMGEDhmclSNEDmLIVQDFILEATQDDYVLEVRQYRAPRWPN---PDGPISNT 1403
Cdd:cd14545     78 QIKCAqYWPQGEGNamiFEDTGLKVTLLSEE----DKSY-YTVRTLELENLKTQETREVLHFHYTTWPDfgvPESPAAFL 152

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1658117666 1404 FELINIIKEESVSRD-GPIVVHDKRGGNIAGTFCALMTLLHQLEME--SSFDVYWVAKMINLMRPGIFTDIDQYQFLYK 1479
Cdd:cd14545    153 NFLQKVRESGSLSSDvGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGnpSSVDVKKVLLEMRKYRMGLIQTPDQLRFSYL 231
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 1242-1491 1.36e-23

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 103.16  E-value: 1.36e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1242 YSAALKQCNRDKNRNSSLLPVERSRVHLSTTAGEISDYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVI 1321
Cdd:PHA02747    43 IANFEKPENQPKNRYWDIPCWDHNRVILDSGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIV 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1322 AL-PDGLDLAEDECI-YWptksqpirfdtftvtfmgedhmCLSNEDMLIVQDFILE----ATQDDYVL------------ 1383
Cdd:PHA02747   123 MLtPTKGTNGEEKCYqYW----------------------CLNEDGNIDMEDFRIEtlktSVRAKYILtlieitdkilkd 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1384 --EVRQYRAPRWPNPDGPISNT-----FELINIIKEESVSRDG-------PIVVHDKRGGNIAGTFCALMTLLHQLEMES 1449
Cdd:PHA02747   181 srKISHFQCSEWFEDETPSDHPdfikfIKIIDINRKKSGKLFNpkdallcPIVVHCSDGVGKTGIFCAVDICLNQLVKRK 260

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1658117666 1450 SFDVYWVAKMINLMRPGIFTDIDQYQFL---YKVIMSLVAKKEEV 1491
Cdd:PHA02747   261 AICLAKTAEKIREQRHAGIMNFDDYLFIqpgYEVLHYFLSKIKAI 305
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 1250-1481 3.22e-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: 100.81  E-value: 3.22e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1250 NRDKNRNSSLLPVERSRVHLSTTAgeiSDYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDL 1329
Cdd:cd14607     24 NRNRNRYRDVSPYDHSRVKLQNTE---NDYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEK 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1330 AEDECI-YWPTKSQPIRF--DT-FTVTFMGEDHMCLSNEDMLIVQDFILEATQDdyvleVRQYRAPRWPN---PDGPISN 1402
Cdd:cd14607    101 DSVKCAqYWPTDEEEVLSfkETgFSVKLLSEDVKSYYTVHLLQLENINSGETRT-----ISHFHYTTWPDfgvPESPASF 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1403 TFELINIIKEESVSRD-GPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINL--MRPGIFTDIDQYQFLYK 1479
Cdd:cd14607    176 LNFLFKVRESGSLSPEhGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDPDSVDIKQVLLDMrkYRMGLIQTPDQLRFSYM 255


                   ..
gi 1658117666 1480 VI 1481
Cdd:cd14607    256 AV 257
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 1279-1479 5.98e-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: 98.45  E-value: 5.98e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1279 YINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDECI-YWPTKSQpirfdtftvTFMGED 1357
Cdd:cd14551      1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSqYWPDQGC---------WTYGNL 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1358 HMCLsnEDMLIVQDFILEATQDDYVLEVRQYRAPR---------WPN---PDGPISnTFELINIIKEESVSRDGPIVVHD 1425
Cdd:cd14551     72 RVRV--EDTVVLVDYTTRKFCIQKVNRGIGEKRVRlvtqfhftsWPDfgvPFTPIG-MLKFLKKVKSANPPRAGPIVVHC 148

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1658117666 1426 KRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYK 1479
Cdd:cd14551    149 SAGVGRTGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 1250-1481 7.43e-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: 7.43e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1250 NRDKNRNSSLLPVERSRV--HLSTTAGEISDYINASYIM--------GYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQV 1319
Cdd:cd14605      2 NKNKNRYKNILPFDHTRVvlHDGDPNEPVSDYINANIIMpefetkcnNSKPKKSYIATQGCLQNTVNDFWRMVFQENSRV 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1320 VIALPDGLDLAEDECI-YWPtksqpirfDTFTVTFMGEdhMCLSNEDMLIVQDFIL------EATQDDYVLEVRQYRAPR 1392
Cdd:cd14605     82 IVMTTKEVERGKSKCVkYWP--------DEYALKEYGV--MRVRNVKESAAHDYILrelklsKVGQGNTERTVWQYHFRT 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1393 WPN---PDGP--ISNTFELINIiKEESVSRDGPIVVHDKRGGNIAGTFCA---LMTLLHQLEMESSFDVYWVAKMINLMR 1464
Cdd:cd14605    152 WPDhgvPSDPggVLDFLEEVHH-KQESIMDAGPVVVHCSAGIGRTGTFIVidiLIDIIREKGVDCDIDVPKTIQMVRSQR 230

                          250
                   ....*....|....*..
gi 1658117666 1465 PGIFTDIDQYQFLYKVI 1481
Cdd:cd14605    231 SGMVQTEAQYRFIYMAV 247
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 1250-1485 2.19e-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: 2.19e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1250 NRDKNRNSSLLPVERSRVHLSTTAGEI--SDYINASYI----MGYQQSNE-FIITQNPLPSTMKDFWKMIWDHSTQVVIA 1322
Cdd:cd14606     18 NKSKNRYKNILPFDHSRVILQGRDSNIpgSDYINANYVknqlLGPDENAKtYIASQGCLEATVNDFWQMAWQENSRVIVM 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1323 LPDGLDLAEDECI-YWPTKSQPIRFDTFTVTFMGEdhMCLSNEDMLIVQDFILEATqdDYVLEVRQYRAPRWP------N 1395
Cdd:cd14606     98 TTREVEKGRNKCVpYWPEVGMQRAYGPYSVTNCGE--HDTTEYKLRTLQVSPLDNG--ELIREIWHYQYLSWPdhgvpsE 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1396 PDGPISnTFELINiIKEESVSRDGPIVVHDKRGGNIAGTFCALMTLLHQLEM---ESSFDVYWVAKMINLMRPGIFTDID 1472
Cdd:cd14606    174 PGGVLS-FLDQIN-QRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTkglDCDIDIQKTIQMVRAQRSGMVQTEA 251

                          250
                   ....*....|...
gi 1658117666 1473 QYQFLYKVIMSLV 1485
Cdd:cd14606    252 QYKFIYVAIAQFI 264
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 1279-1482 2.74e-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: 96.59  E-value: 2.74e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1279 YINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDEC-IYWPTKSQPiRFDTFTVTFMGED 1357
Cdd:cd17668      1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCdQYWPADGSE-EYGNFLVTQKSVQ 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1358 HMCLSNEDMLIVQDF-ILEATQDDYVLE--VRQYRAPRWPNPDGPiSNTFELINIIKEESVSRD---GPIVVHDKRGGNI 1431
Cdd:cd17668     80 VLAYYTVRNFTLRNTkIKKGSQKGRPSGrvVTQYHYTQWPDMGVP-EYTLPVLTFVRKASYAKRhavGPVVVHCSAGVGR 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1658117666 1432 AGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIM 1482
Cdd:cd17668    159 TGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 984-1192 2.79e-22

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


Pssm-ID: 350507 [Multi-domain]  Cd Length: 204  Bit Score: 96.60  E-value: 2.79e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  984 YINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKGRRKCdQYWPldSQEE---YGSFLVTLRS 1060
Cdd:cd17669      1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEF-VYWP--NKDEpinCETFKVTLIA 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1061 TKVLAYYTQRTFTLKNTrAKKGSQKEQTHErtVVQYHYTQWPDMGVPEYTLPVLTFVRKSSQANlgNMGPVVVHCSAGVG 1140
Cdd:cd17669     78 EEHKCLSNEEKLIIQDF-ILEATQDDYVLE--VRHFQCPKWPNPDSPISKTFELISIIKEEAAN--RDGPMIVHDEHGGV 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1658117666 1141 RTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALV 1192
Cdd:cd17669    153 TAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 984-1192 1.04e-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: 94.75  E-value: 1.04e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  984 YINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNASVIVMITN---LVEkgrrkcDQ--YWPldSQEEY---GSFL 1055
Cdd:cd17670      1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDnqgLAE------DEfvYWP--SREESmncEAFT 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1056 VTLRSTKVLAYYTQRTFTLKNTRAkkgsqkEQTHERTVVQYHYTQ---WPDMGVP-EYTLPVLTFVRKSSqanLGNMGPV 1131
Cdd:cd17670     73 VTLISKDRLCLSNEEQIIIHDFIL------EATQDDYVLEVRHFQcpkWPNPDAPiSSTFELINVIKEEA---LTRDGPT 143

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1658117666 1132 VVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHIRTQRNYLVQTEEQYIFIHDALV 1192
Cdd:cd17670    144 IVHDEFGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 1279-1480 1.86e-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: 1.86e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1279 YINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDgLDLAEDECIYWPTKSQpIRFDTFTVTFMGedh 1358
Cdd:cd14636      1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNE-VDLAQGCPQYWPEEGM-LRYGPIQVECMS--- 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1359 mCLSNEDML--IVQDFILEATQDDYVLeVRQYRAPRWPNPDGPISNTFELINII------KEESVSRDGPIVVHDKRGGN 1430
Cdd:cd14636     76 -CSMDCDVIsrIFRICNLTRPQEGYLM-VQQFQYLGWASHREVPGSKRSFLKLIlqvekwQEECDEGEGRTIIHCLNGGG 153

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1431 IAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKV 1480
Cdd:cd14636    154 RSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDV 203
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 1279-1482 2.40e-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: 93.98  E-value: 2.40e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1279 YINASYIMGYQQSNEF--IITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDECI-YWPtksqpirfDTFTVTFMG 1355
Cdd:cd14538      1 YINASHIRIPVGGDTYhyIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHrYWP--------DSLNKPLIC 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1356 EDHMCLSNEDMLIVQDFI-----LEATQDDYVLEVRQYRAPRWPNPDGPiSNTFELINIIKE-ESVSRDGPIVVHDKRGG 1429
Cdd:cd14538     73 GGRLEVSLEKYQSLQDFVirrisLRDKETGEVHHITHLNFTTWPDHGTP-QSADPLLRFIRYmRRIHNSGPIVVHCSAGI 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1658117666 1430 NIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIM 1482
Cdd:cd14538    152 GRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACL 204
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 1279-1482 2.73e-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: 93.82  E-value: 2.73e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1279 YINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALpDGLDLAEDE--CI-YWPtKSQPIRFDTFTVTFMG 1355
Cdd:cd14637      1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVML-NQLNQSNSAwpCLqYWP-EPGLQQYGPMEVEFVS 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1356 edhmcLSNEDMLIVQDFILE--ATQDDYVLEVRQYRAPRWP----NPDGPISNTFELINIIKEESVSRDGPIVVHDKRGG 1429
Cdd:cd14637     79 -----GSADEDIVTRLFRVQniTRLQEGHLMVRHFQFLRWSayrdTPDSKKAFLHLLASVEKWQRESGEGRTVVHCLNGG 153

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1658117666 1430 NIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIM 1482
Cdd:cd14637    154 GRSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIAL 206
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 1253-1478 5.07e-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: 5.07e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1253 KNRNSSLLPVERSRVHLST--TAGEISDYINASYIMGYQ-QSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDL 1329
Cdd:cd14611      2 KNRYKTILPNPHSRVCLKPknSNDSLSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1330 AEDECIYWPTKSQPIRFDTFTVTfmgedhmCLSNEDMLIVQDFILEatQDDYVLEVRQYRAPRWPNPDGPISNT--FELI 1407
Cdd:cd14611     82 NEKCVLYWPEKRGIYGKVEVLVN-------SVKECDNYTIRNLTLK--QGSQSRSVKHYWYTSWPDHKTPDSAQplLQLM 152

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1658117666 1408 NIIKEE---SVSRdGPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLY 1478
Cdd:cd14611    153 LDVEEDrlaSPGR-GPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225
PHA02738 PHA02738
hypothetical protein; Provisional
 1242-1481 2.10e-20

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 94.22  E-value: 2.10e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1242 YSAALKqcNRDKNRNSSLLPVERSRVHLSTTAGEiSDYINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVI 1321
Cdd:PHA02738    43 FNAEKK--NRKLNRYLDAVCFDHSRVILPAERNR-GDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIV 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1322 ALPDGLDLAEDECI-YWPTKSQ-PIRFDTFTVTFMGEDHMCLSNEDMLIVQDFIlEATQddyvlEVRQYRAPRWPNPDGP 1399
Cdd:PHA02738   120 MLCKKKENGREKCFpYWSDVEQgSIRFGKFKITTTQVETHPHYVKSTLLLTDGT-SATQ-----TVTHFNFTAWPDHDVP 193

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1400 iSNTFELINIIKE----------------ESVSRDGPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLM 1463
Cdd:PHA02738   194 -KNTSEFLNFVLEvrqcqkelaqeslqigHNRLQPPPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQ 272

                          250
                   ....*....|....*...
gi 1658117666 1464 RPGIFTDIDQYQFLYKVI 1481
Cdd:PHA02738   273 RYYSLFIPFQYFFCYRAV 290
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 1279-1482 3.62e-20

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


Pssm-ID: 350444 [Multi-domain]  Cd Length: 207  Bit Score: 90.58  E-value: 3.62e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1279 YINASYIMGYQQSNE--FIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDECI-YWP-TKSQPIRFDTFtvtfm 1354
Cdd:cd14596      1 YINASYITMPVGEEElfYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHrYWPeTLQEPMELENY----- 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1355 gedHMCLSNEDMLivQDFILEATQddyVLE--------VRQYRAPRWPNPDGPISNTFELINIIKEESVSRDGPIVVHDK 1426
Cdd:cd14596     76 ---QLRLENYQAL--QYFIIRIIK---LVEketgenrlIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHNTGPIVVHCS 147

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1658117666 1427 RGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIM 1482
Cdd:cd14596    148 AGIGRAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVL 203
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 946-1197 3.84e-20

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 92.72  E-value: 3.84e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  946 SSIHPENKNK--NRYINILAYDHSRVKLSSSSDrngwsadYINANYVDGFTQPKAYIATQGPLKSSMEDFWRMVWEQNAS 1023
Cdd:PHA02740    45 ACAQAENKAKdeNLALHITRLLHRRIKLFNDEK-------VLDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQ 117

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1024 VIVMITNLVEKgrrKC-DQYWPLDSQ--EEYGSFLVtlrstKVLAYYTQRTF--TLKNTRAKKGSQKEQTHertvvqYHY 1098
Cdd:PHA02740   118 IIVLISRHADK---KCfNQFWSLKEGcvITSDKFQI-----ETLEIIIKPHFnlTLLSLTDKFGQAQKISH------FQY 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1099 TQWPDMGVPEYTLPVLTF--------VRKSSQANLGNMGPVVVHCSAGVGRTGTYIVLDSMLRQIKEQGTVNILGFLKHI 1170
Cdd:PHA02740   184 TAWPADGFSHDPDAFIDFfcniddlcADLEKHKADGKIAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKV 263

                          250       260
                   ....*....|....*....|....*..
gi 1658117666 1171 RTQRNYLVQTEEQYIFIHDaLVEAILS 1197
Cdd:PHA02740   264 RQKKYGCMNCLDDYVFCYH-LIAAYLK 289
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 1225-1482 4.06e-20

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 92.76  E-value: 4.06e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1225 LEKQFKMITQSN-AKQCDYSAALKqcNRDKNRNSSLLPVERSRVHLSTTAGeISDYINASYIMGYQQSNEFIITQNPLPS 1303
Cdd:PHA02742    28 LKEEHEHIMQEIvAFSCNESLELK--NMKKCRYPDAPCFDRNRVILKIEDG-GDDFINASYVDGHNAKGRFICTQAPLEE 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1304 TMKDFWKMIWDHSTQVVIALPDGLDLAEDECI-YWPTKSQ--------PIR------FDTFTVTfmgedHMCLSNedmli 1368
Cdd:PHA02742   105 TALDFWQAIFQDQVRVIVMITKIMEDGKEACYpYWMPHERgkathgefKIKtkkiksFRNYAVT-----NLCLTD----- 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1369 vqdfileaTQDDYVLEVRQYRAPRWPNPDGP--ISNTFELINIIKE-----------ESVSRDGPIVVHDKRGGNIAGTF 1435
Cdd:PHA02742   175 --------TNTGASLDIKHFAYEDWPHGGLPrdPNKFLDFVLAVREadlkadvdikgENIVKEPPILVHCSAGLDRAGAF 246

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1658117666 1436 CALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIM 1482
Cdd:PHA02742   247 CAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIFCYFIVL 293
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 1279-1491 8.93e-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: 89.43  E-value: 8.93e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1279 YINASYIMGYQQSNE-FIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDECI-YWPTKSQPIrFDTFTVTFMGE 1356
Cdd:cd14546      1 YINASTIYDHDPRNPaYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCArYWPEEGSEV-YHIYEVHLVSE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1357 DHMClsneDMLIVQDFILEATQDDYVLEVRQYRAPRWPNPDGPIS--NTFELINIIKEESVSRDGPIVVHDKRGGNIAGT 1434
Cdd:cd14546     80 HIWC----DDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASakPLLEFRRKVNKSYRGRSCPIVVHCSDGAGRTGT 155

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1658117666 1435 FCAL-MTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFlykvimSLVAKKEEV 1491
Cdd:cd14546    156 YILIdMVLNRMAKGAKEIDIAATLEHLRDQRPGMVKTKDQFEF------VLTAVAEEV 207
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 1279-1459 1.04e-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: 1.04e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1279 YINASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDECI-YWPTKSQPIR-FDTFTVTFMGE 1356
Cdd:cd14557      1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAqYWPSMEEGSRaFGDVVVKINEE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1357 DHMclsnEDMLIVQDFILEATQDDYVLEVRQYRAPRWPN---PDGPiSNTFELINIIKEESVSRDGPIVVHDKRGGNIAG 1433
Cdd:cd14557     81 KIC----PDYIIRKLNINNKKEKGSGREVTHIQFTSWPDhgvPEDP-HLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRTG 155

                          170       180
                   ....*....|....*....|....*..
gi 1658117666 1434 TFCALMTLLHQLEMESSFDVY-WVAKM 1459
Cdd:cd14557    156 TYIGIDAMLEGLEAEGRVDVYgYVVKL 182
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1384-1483 1.14e-18

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 82.79  E-value: 1.14e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  1384 EVRQYRAPRWPNPDGPISNT--FELINIIKEESVSRD--GPIVVHDKRGGNIAGTFCALMTLLHQLEMES-SFDVYWVAK 1458
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDsiLELLRAVKKNLNQSEssGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAgEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 1658117666  1459 MINLMRPGIFTDIDQYQFLYKVIMS 1483
Cdd:smart00404   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 1384-1483 1.14e-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: 82.79  E-value: 1.14e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  1384 EVRQYRAPRWPNPDGPISNT--FELINIIKEESVSRD--GPIVVHDKRGGNIAGTFCALMTLLHQLEMES-SFDVYWVAK 1458
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDsiLELLRAVKKNLNQSEssGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAgEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 1658117666  1459 MINLMRPGIFTDIDQYQFLYKVIMS 1483
Cdd:smart00012   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 1250-1482 1.04e-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: 1.04e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1250 NRDKNRNSSLLPVERSRVHLSttagEISDYINASY----IMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPD 1325
Cdd:cd14600     40 NMDKNRYKDVLPYDATRVVLQ----GNEDYINASYvnmeIPSANIVNKYIATQGPLPHTCAQFWQVVWEQKLSLIVMLTT 115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1326 GLDLAEDEC-IYWPTKSQPIRFDTFTVTFMGED-HMCLSNEDMLIVQdfiLEATQDDYVLEVrQYRAprWPN---PDGPi 1400
Cdd:cd14600    116 LTERGRTKChQYWPDPPDVMEYGGFRVQCHSEDcTIAYVFREMLLTN---TQTGEERTVTHL-QYVA--WPDhgvPDDS- 188

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1401 SNTFELINIIKEESVSRDgPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKV 1480
Cdd:cd14600    189 SDFLEFVNYVRSKRVENE-PVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEA 267


                   ..
gi 1658117666 1481 IM 1482
Cdd:cd14600    268 IL 269
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 1278-1482 2.08e-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: 2.08e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1278 DYINASYI-MGYQQS---NEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDEC-IYWPTKSQPIRFDTFTVT 1352
Cdd:cd14601      1 DYINANYInMEIPSSsiiNRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKChQYWPEPSGSSSYGGFQVT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1353 fmgedhmCLSNE--DMLIVQDFILEATQDDYVLEVRQYRAPRWPN---PDGPiSNTFELINIIKEESVSRDGPIVVHDKR 1427
Cdd:cd14601     81 -------CHSEEgnPAYVFREMTLTNLEKNESRPLTQIQYIAWPDhgvPDDS-SDFLDFVCLVRNKRAGKDEPVVVHCSA 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1658117666 1428 GGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIM 1482
Cdd:cd14601    153 GIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAIL 207
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 1279-1478 6.34e-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: 78.28  E-value: 6.34e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1279 YINASYIMGYQQSN--EFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLD-LAEDECI-YWPTKS-QPIRFDTFTVTF 1353
Cdd:cd17658      1 YINASLVETPASESlpKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDnYSTAKCAdYFPAEEnESREFGRISVTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1354 MGEDHMCLSNE-DMLIVQDFILEatqdDYVLEVRQYRAPRWPNPDGPiSNTFELINIIKEESVSRD--GPIVVHDKRGGN 1430
Cdd:cd17658     81 KKLKHSQHSITlRVLEVQYIESE----EPPLSVLHIQYPEWPDHGVP-KDTRSVRELLKRLYGIPPsaGPIVVHCSAGIG 155

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1658117666 1431 IAGTFCALMTLLHQLeME---SSFDVYWVAKMINLMRPGIFTDIDQYQFLY 1478
Cdd:cd17658    156 RTGAYCTIHNTIRRI-LEgdmSAVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 1243-1485 9.78e-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: 9.78e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1243 SAALKQcNRDKNRNSSLLPVERSRVHLSTTAGEISDYINASYIMGYQQSNE--FIITQNPLPSTMKDFWKMIWDHSTQVV 1320
Cdd:cd14599     32 TATLPE-NAERNRIREVVPYEENRVELVPTKENNTGYINASHIKVTVGGEEwhYIATQGPLPHTCHDFWQMVWEQGVNVI 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1321 ialpdGLDLAEDEC------IYWP---TKSQPIRFDTFTVTF-MGEDHMCLSNEDMLIVQdfiLEATQDDYVLEVrQYra 1390
Cdd:cd14599    111 -----AMVTAEEEGgrskshRYWPklgSKHSSATYGKFKVTTkFRTDSGCYATTGLKVKH---LLSGQERTVWHL-QY-- 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1391 PRWPN---PD---GPISNTFEL------INIIKEESVSRDGPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAK 1458
Cdd:cd14599    180 TDWPDhgcPEevqGFLSYLEEIqsvrrhTNSMLDSTKNCNPPIVVHCSAGVGRTGVVILTELMIGCLEHNEKVEVPVMLR 259

                          250       260
                   ....*....|....*....|....*..
gi 1658117666 1459 MINLMRPGIFTDIDQYQFLYKVIMSLV 1485
Cdd:cd14599    260 HLREQRMFMIQTIAQYKFVYQVLIQFL 286
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 1279-1479 1.04e-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: 77.42  E-value: 1.04e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1279 YINASYIMGYQQ-SNEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDECI-YWPT-KSQPIRFDTFTVTFMG 1355
Cdd:cd14539      1 YINASLIEDLTPyCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHrYWPTeRGQALVYGAITVSLQS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1356 EDHMCLSNEDMLIVQDfileatqddyvLEVRQYRA------PRWPNPDGPiSNTFELINIIKE------ESVSRDGPIVV 1423
Cdd:cd14539     81 VRTTPTHVERIISIQH-----------KDTRLSRSvvhlqfTTWPELGLP-DSPNPLLRFIEEvhshylQQRSLQTPIVV 148

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1658117666 1424 HDKRGGNIAGTFCALMTLLHQLEMESSF-DVYWVAKMINLMRPGIFTDIDQYQFLYK 1479
Cdd:cd14539    149 HCSSGVGRTGAFCLLYAAVQEIEAGNGIpDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 956-1184 9.91e-15

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


Pssm-ID: 350407 [Multi-domain]  Cd Length: 227  Bit Score: 75.13  E-value: 9.91e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  956 NRYINIlaydHSRVKLSsssDRNGwsadyINANYVDGFTQPKAyIATQGPLKSSMEDFWRMVWEQNASVIVMITNLVEKG 1035
Cdd:cd14559      1 NRFTNI----QTRVSTP---VGKN-----LNANRVQIGNKNVA-IACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQ 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1036 RRKCDQYWPLDSQeeYGSflVTLRSTKVLAYYtQRTFTLKNTRAKKGSQKEQTHERTVvqYHYTQWPDMGV--PEYTLPV 1113
Cdd:cd14559     68 RKGLPPYFRQSGT--YGS--VTVKSKKTGKDE-LVDGLKADMYNLKITDGNKTITIPV--VHVTNWPDHTAisSEGLKEL 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1114 LTFVRKSSQANLG-------------NMGPVVVHCSAGVGRTGTYIVLDSMlrqIKEQGTVNILGFLKHIRTQRN-YLVQ 1179
Cdd:cd14559    141 ADLVNKSAEEKRNfykskgssaindkNKLLPVIHCRAGVGRTGQLAAAMEL---NKSPNNLSVEDIVSDMRTSRNgKMVQ 217


                   ....*
gi 1658117666 1180 TEEQY 1184
Cdd:cd14559    218 KDEQL 222
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1278-1424 1.47e-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: 74.29  E-value: 1.47e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1278 DYINASYI-MGYQQS---NEFIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDEC-IYWPTKSQPIRFDTFTVT 1352
Cdd:cd14541      1 DYINANYVnMEIPGSgivNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKChQYWPDLGETMQFGNLQIT 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1658117666 1353 fmgedhmCLSNED--MLIVQDFILEATQDDYVLEVRQYRAPRWPNPDGPiSNTFELINIIKEESVSRDG---PIVVH 1424
Cdd:cd14541     81 -------CVSEEVtpSFAFREFILTNTNTGEERHITQMQYLAWPDHGVP-DDSSDFLDFVKRVRQNRVGmvePTVVH 149
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1279-1482 8.21e-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: 69.41  E-value: 8.21e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1279 YINASYIMGYQQSNE--FIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDECI-YWPtksqpirfdtftvtFMG 1355
Cdd:cd14540      1 YINASHITATVGGKQrfYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFrYWP--------------TLG 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1356 EDHMCLSNEDMLIVQDFILEAtqDDYV--------LEVRQYRA------PRWPN---PDGPisNTF----ELINIIKEES 1414
Cdd:cd14540     67 GEHDALTFGEYKVSTKFSVSS--GCYTttglrvkhTLSGQSRTvwhlqyTDWPDhgcPEDV--SGFldflEEINSVRRHT 142

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1658117666 1415 VS------RDGPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIM 1482
Cdd:cd14540    143 NQdvaghnRNPPTLVHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLI 216
fn3 pfam00041
Fibronectin type III domain;
316-398 4.43e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 60.51  E-value: 4.43e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  316 SEPENVEADPYNYTSLLVTWERPRAVYDVgIERYLVSYQPVGDEDlPKNEYLTDGDQDvGAIIQDLSANTSYVVQVVAVC 395
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGP-ITGYEVEYRPKNSGE-PWNEITVPGTTT-SVTLTGLKPGTEYEVRVQAVN 77


                   ...
gi 1658117666  396 ING 398
Cdd:pfam00041   78 GGG 80
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 1247-1488 3.67e-10

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 63.06  E-value: 3.67e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1247 KQCNRDKNR---NSSLLPVER---SRVHLSTTaGEISDyinASYIMGYQQSNEFIITQNPLPSTMKDFWKMIWDHSTQVV 1320
Cdd:PHA02740    44 KACAQAENKakdENLALHITRllhRRIKLFND-EKVLD---ARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQII 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1321 IALPdglDLAEDECI--YWPTKSQPIR-FDTF---TVTFMGEDHMCLSnedMLIVQDFILEATQddyvLEVRQYRAprWP 1394
Cdd:PHA02740   120 VLIS---RHADKKCFnqFWSLKEGCVItSDKFqieTLEIIIKPHFNLT---LLSLTDKFGQAQK----ISHFQYTA--WP 187

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1395 ------NPDGPISNTFEL----INIIKEESVSRDGPIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMR 1464
Cdd:PHA02740   188 adgfshDPDAFIDFFCNIddlcADLEKHKADGKIAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKK 267

                          250       260
                   ....*....|....*....|....
gi 1658117666 1465 PGIFTDIDQYQFLYKVIMSLVAKK 1488
Cdd:PHA02740   268 YGCMNCLDDYVFCYHLIAAYLKEK 291
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 1279-1485 1.52e-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: 1.52e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1279 YINASYIMGYQQSNE--FIITQNPLPSTMKDFWKMIWDHSTQVVIALPDGLDLAEDECI-YWP---TKSQPIRFDTFTVT 1352
Cdd:cd14598      1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFrYWPrlgSRHNTVTYGRFKIT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1353 F-MGEDHMCLSNEDMLIVQdfiLEATQDDYVLEVrQYraPRWPNPDGPiSNTFELINIIKE-ESVSR-----------DG 1419
Cdd:cd14598     81 TrFRTDSGCYATTGLKIKH---LLTGQERTVWHL-QY--TDWPEHGCP-EDLKGFLSYLEEiQSVRRhtnstidpkspNP 153

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1658117666 1420 PIVVHDKRGGNIAGTFCALMTLLHQLEMESSFDVYWVAKMINLMRPGIFTDIDQYQFLYKVIMSLV 1485
Cdd:cd14598    154 PVLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFL 219
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 316-398 1.57e-08

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 53.00  E-value: 1.57e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666   316 SEPENVEADPYNYTSLLVTWERPRavyDVGIERYLVSYQPVGDEDLPKNEYLTDGDQDVGAIIQDLSANTSYVVQVVAVC 395
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPP---DDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78


                    ...
gi 1658117666   396 ING 398
Cdd:smart00060   79 GAG 81
PLN02179 PLN02179
carbonic anhydrase
 52-263 2.41e-08

carbonic anhydrase


Pssm-ID: 177835  Cd Length: 235  Bit Score: 56.53  E-value: 2.41e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666   52 WAKKYPS---CNNAK-QSPINIDDDLSQVkMQFQKLKlegfEQETSNTTTIHNDGKTVAINLNDEyyisggglrsrfkVG 127
Cdd:PLN02179    50 WGKLNPQwkvCSTGKyQSPIDLTDERVSL-IHDQALS----RHYKPAPAVIQSRGHDVMVSWKGD-------------AG 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  128 RITFHWG-----QCNASSDgSEHSLDGIKFPLEMQIYGYEAHkfqsldsalkdgGRLTALSVLFEVsAEDNENYVAIIDG 202
Cdd:PLN02179   112 KITIHQTdyklvQCHWHSP-SEHTINGTSYDLELHMVHTSAS------------GKTAVVGVLYKL-GEPDEFLTKLLNG 177

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1658117666  203 VKTVtrlGKTAVLepfslLGLL-PN----STEKYYIYNGSLTTPPCSETVEWIVFRNTVDISDVQL 263
Cdd:PLN02179   178 IKGV---GKKEIN-----LGIVdPRdirfETNNFYRYIGSLTIPPCTEGVIWTVVKRVVWFFDFNV 235
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
1094-1189 6.02e-08

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 53.05  E-value: 6.02e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1094 VQYHYTQWPDMGVPEYT--LPVLTFVRKSSQANlgnmGPVVVHCSAGVGRTGT----YIVLDSM-LRQIkeqgtvnilgf 1166
Cdd:COG2453     48 LEYLHLPIPDFGAPDDEqlQEAVDFIDEALREG----KKVLVHCRGGIGRTGTvaaaYLVLLGLsAEEA----------- 112

                           90       100
                   ....*....|....*....|...
gi 1658117666 1167 LKHIRTQRNYLVQTEEQYIFIHD 1189
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 1.13e-07

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 50.96  E-value: 1.13e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  316 SEPENVEADPYNYTSLLVTWERPRAvYDVGIERYLVSYQPVGDEDLpkNEYLTDGDQDVGAIIQDLSANTSYVVQVVAVC 395
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPPED-DGGPITGYVVEYREKGSGDW--KEVEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78


                   ...
gi 1658117666  396 ING 398
Cdd:cd00063     79 GGG 81
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 1113-1189 1.70e-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: 1.70e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1658117666 1113 VLTFVRKSSQANLGNmGPVVVHCSAGVGRTGTYIVLDSMLRQIKeqgtvNILGFLKHIRTQR-NYLVQTEEQYIFIHD 1189
Cdd:cd14494     42 VDRFLEVLDQAEKPG-EPVLVHCKAGVGRTGTLVACYLVLLGGM-----SAEEAVRIVRLIRpGGIPQTIEQLDFLIK 113
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 1094-1187 4.40e-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: 4.40e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1094 VQYHYTQWPDMGVPeyTLPVLT-FVRKSSQANLGNmGPVVVHCSAGVGRTGT----YIVLDSMLR---QIKEqgtvnilg 1165
Cdd:cd14504     50 LRYHHIPIEDYTPP--TLEQIDeFLDIVEEANAKN-EAVLVHCLAGKGRTGTmlacYLVKTGKISavdAINE-------- 118

                           90       100
                   ....*....|....*....|..
gi 1658117666 1166 flkhIRTQRNYLVQTEEQYIFI 1187
Cdd:cd14504    119 ----IRRIRPGSIETSEQEKFV 136
PLN02202 PLN02202
carbonate dehydratase
 9-264 4.50e-07

carbonate dehydratase


Pssm-ID: 177853 [Multi-domain]  Cd Length: 284  Bit Score: 53.14  E-value: 4.50e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666    9 LMMLCQICFIcQIANLAHGYYRTQrkfKEDIDWSYAGTLNQNNWAKKYP---SCNNAK-QSPINIdddlsQVKMQFQKLK 84
Cdd:PLN02202     3 IMMMIKLCFF-AIALICIAPADAQ---TEGVVFGYKGKNGPNQWGHLNPhftKCAVGKlQSPIDI-----QRRQIFYNHK 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666   85 LEGFEQETSNTT-TIHNDGKTVAInlndeYYISGGG--LRSRFKVGRITFHWgqcnasSDGSEHSLDGIKFPLEMQ-IYG 160
Cdd:PLN02202    74 LESIHRDYYFTNaTLVNHVCNVAM-----FFGEGAGdvIIDNKNYTLLQMHW------HTPSEHHLHGVQYAAELHmVHQ 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666  161 YEAHKFQSLDSALKDGGRLTALSVLFEVSAEDNE-----NYVAIIDGVKTVTRLgktavlepfsllglLPNSTEKYYIYN 235
Cdd:PLN02202   143 AKDGSFAVVASLFKIGTEEPFLSQMKDKLVKLKEerfkgNHTAQVEVGKIDTRH--------------IERKTRKYFRYI 208

                          250       260
                   ....*....|....*....|....*....
gi 1658117666  236 GSLTTPPCSETVEWIVFRNTVDISDVQLE 264
Cdd:PLN02202   209 GSLTTPPCSENVSWTILGKVRSMSKEQVE 237
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 1096-1189 3.08e-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: 3.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1096 YHYT-QWPDMGVPEYTLpVLTFVRKSSQAnLGNMGPVVVHCSAGVGRTGTYI--VLDSMLRQIKEQGtvnILGFlkhiRT 1172
Cdd:cd14506     78 YFYNfGWKDYGVPSLTT-ILDIVKVMAFA-LQEGGKVAVHCHAGLGRTGVLIacYLVYALRMSADQA---IRLV----RS 148

                           90
                   ....*....|....*..
gi 1658117666 1173 QRNYLVQTEEQYIFIHD 1189
Cdd:cd14506    149 KRPNSIQTRGQVLCVRE 165
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 1102-1189 1.90e-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: 1.90e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1102 PDMGVP---EYTLPVLTFVRKssqaNLGNMGPVVVHCSAGVGRTGTyiVLDSMLRQIKEQGTVNILgfLKHIRTQRNYLV 1178
Cdd:cd14505     81 PDGGVPsdiAQWQELLEELLS----ALENGKKVLIHCKGGLGRTGL--IAACLLLELGDTLDPEQA--IAAVRALRPGAI 152

                           90
                   ....*....|.
gi 1658117666 1179 QTEEQYIFIHD 1189
Cdd:cd14505    153 QTPKQENFLHQ 163
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 1412-1479 1.36e-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: 1.36e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658117666 1412 EESVSRDGPIVVHDKRGGNIAGTFCALMTLLHQLE-MESSFDVYWVAkminlmRPGIFTD-IDQYQFLYK 1479
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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