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Conserved domains on  [gi|1387264124|ref|XP_024846259|]
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receptor-type tyrosine-protein phosphatase zeta isoform X1 [Bos taurus]

Protein Classification

fibronectin type III domain-containing protein; tyrosine-protein phosphatase( domain architecture ID 12931151)

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 ...
 1725-2002 3.65e-161

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


The actual alignment was detected with superfamily member cd17667:

Pssm-ID: 475123 [Multi-domain]  Cd Length: 274  Bit Score: 497.25  E-value: 3.65e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1725 FTEEFEtlkefyqEVQSCTVDLGITADSSNHPDNKHKNRYINIVAYDHSRVKLAQLAEKDGKLTDYINANYVDGYNRPKA 1804
Cdd:cd17667      1 FSEDFE-------EVQRCTADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSKHSDYINANYVDGYNKAKA 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1805 YIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPVDGSEEYGNFLVTQKSIQVLAYYTVRNFTLRNTK 1884
Cdd:cd17667     74 YIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTK 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1885 IKKGSQ---KGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQI 1961
Cdd:cd17667    154 VKKGQKgnpKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQI 233

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1387264124 1962 QHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDALVEAIL 2002
Cdd:cd17667    234 KDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 274
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 2085-2301 2.70e-149

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: 461.00  E-value: 2.70e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2085 YINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDGQNMvspsghfwhflfrAEDEFVYWPNKDEPIN 2164
Cdd:cd17669      1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNM-------------AEDEFVYWPNKDEPIN 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2165 CESFKVTLMAEEHKCLSNEEKLIMQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTFELISIIKEEAATRDGPMIVHD 2244
Cdd:cd17669     68 CETFKVTLIAEEHKCLSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTFELISIIKEEAANRDGPMIVHD 147

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1387264124 2245 EHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAVL 2301
Cdd:cd17669    148 EHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
alpha_CARP_receptor_like cd03122
Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related ...
 45-298 9.18e-112

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: 355.89  E-value: 9.18e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124   45 NQKNWGKKYPTCNS-PKQSPINIDEDlTQVNVN-LKKLKFQDWDKTSLEnTFIHNTGKTVEINLTN---DYRLSGGVSET 119
Cdd:cd03122      1 NPKHWAKKYPACGEgRQQSPIDIVED-TQVQRQgLQPLHFDGYEELTAS-TTLENTGKTVILRLEGnssDPFVSGGPLLG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124  120 VFKASKIAFHWGKCNmsSDGSEHSLEGQKFPLEMQIYCFDADRFSSFEeAIKGKGKLRALSILFEVGIEENLDYKAIIDG 199
Cdd:cd03122     79 RYKFSEITFHWGTCN--SDGSEHSIDGHKFPLEMQILHRNTDFFDSFE-AIKSPGGVLALAYLFELSHEDNPFLDPIIEG 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124  200 VERVSRFGKQAALDPFTLLNLLPNSTDKYYTYNGSLTSPPCTDTVDWIIFKDTVSISESQLAVFCEVLTMQQSGyVMLMD 279
Cdd:cd03122    156 LRNVSRPGKEVELPPFPLSDLLPPFTDKYYSYEGSLTTPPCSETVEWIVFREPVPISSRQLEAFRELLTRRQDG-VMSGD 234

                          250
                   ....*....|....*....
gi 1387264124  280 YLQNNFREQQYKFSRQVFS 298
Cdd:cd03122    235 YLPNNGRPQQPLGSRTVFS 253
fn3 pfam00041
Fibronectin type III domain;
313-401 5.89e-09

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 55.11  E-value: 5.89e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124  313 SEPENVQADPENYTSLLVTWERPRVVYDTmIEKFAVLYQQLEGEDQtKHEFLTDGYQDlGAILNNLLPNMSYVLQIVAIC 392
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGP-ITGYEVEYRPKNSGEP-WNEITVPGTTT-SVTLTGLKPGTEYEVRVQAVN 77


                   ....*....
gi 1387264124  393 TNGlYGKYS 401
Cdd:pfam00041   78 GGG-EGPPS 85
 
Name Accession Description Interval E-value
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 1725-2002 3.65e-161

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


Pssm-ID: 350505 [Multi-domain]  Cd Length: 274  Bit Score: 497.25  E-value: 3.65e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1725 FTEEFEtlkefyqEVQSCTVDLGITADSSNHPDNKHKNRYINIVAYDHSRVKLAQLAEKDGKLTDYINANYVDGYNRPKA 1804
Cdd:cd17667      1 FSEDFE-------EVQRCTADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSKHSDYINANYVDGYNKAKA 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1805 YIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPVDGSEEYGNFLVTQKSIQVLAYYTVRNFTLRNTK 1884
Cdd:cd17667     74 YIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTK 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1885 IKKGSQ---KGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQI 1961
Cdd:cd17667    154 VKKGQKgnpKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQI 233

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1387264124 1962 QHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDALVEAIL 2002
Cdd:cd17667    234 KDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 274
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 2085-2301 2.70e-149

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: 461.00  E-value: 2.70e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2085 YINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDGQNMvspsghfwhflfrAEDEFVYWPNKDEPIN 2164
Cdd:cd17669      1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNM-------------AEDEFVYWPNKDEPIN 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2165 CESFKVTLMAEEHKCLSNEEKLIMQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTFELISIIKEEAATRDGPMIVHD 2244
Cdd:cd17669     68 CETFKVTLIAEEHKCLSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTFELISIIKEEAANRDGPMIVHD 147

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1387264124 2245 EHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAVL 2301
Cdd:cd17669    148 EHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1724-1999 2.73e-119

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 377.77  E-value: 2.73e-119
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124  1724 GFTEEFETLKEFYQEVQSCTVdlgitadsSNHPDNKHKNRYINIVAYDHSRVKLAQLaekDGKLTDYINANYVDGYNRPK 1803
Cdd:smart00194    1 GLEEEFEKLDRLKPDDESCTV--------AAFPENRDKNRYKDVLPYDHTRVKLKPP---PGEGSDYINASYIDGPNGPK 69

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124  1804 AYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPVDGSE--EYGNFLVTQKSIQVLAYYTVRNFTLR 1881
Cdd:smart00194   70 AYIATQGPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEplTYGDITVTLKSVEKVDDYTIRTLEVT 149

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124  1882 NTkikkgsqkGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQI 1961
Cdd:smart00194  150 NT--------GCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQL 221

                           250       260       270
                    ....*....|....*....|....*....|....*...
gi 1387264124  1962 QHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDALVE 1999
Cdd:smart00194  222 EAGKEVDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1758-1999 2.76e-113

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 359.25  E-value: 2.76e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1758 NKHKNRYINIVAYDHSRVKLaqlaEKDGKLTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNL 1837
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKL----TGDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTEL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1838 VEKGRRKCDQYWP--VDGSEEYGNFLVTQKSI-QVLAYYTVRNFTLRNtkikkgsqKGRPSGRVVTQYHYTQWPDMGVPE 1914
Cdd:pfam00102   77 EEKGREKCAQYWPeeEGESLEYGDFTVTLKKEkEDEKDYTVRTLEVSN--------GGSEETRTVKHFHYTGWPDHGVPE 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1915 YSLPVLTFVRKASHAKRHA-VGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFI 1993
Cdd:pfam00102  149 SPNSLLDLLRKVRKSSLDGrSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFL 228


                   ....*.
gi 1387264124 1994 HDALVE 1999
Cdd:pfam00102  229 YDAILE 234
alpha_CARP_receptor_like cd03122
Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related ...
 45-298 9.18e-112

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: 355.89  E-value: 9.18e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124   45 NQKNWGKKYPTCNS-PKQSPINIDEDlTQVNVN-LKKLKFQDWDKTSLEnTFIHNTGKTVEINLTN---DYRLSGGVSET 119
Cdd:cd03122      1 NPKHWAKKYPACGEgRQQSPIDIVED-TQVQRQgLQPLHFDGYEELTAS-TTLENTGKTVILRLEGnssDPFVSGGPLLG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124  120 VFKASKIAFHWGKCNmsSDGSEHSLEGQKFPLEMQIYCFDADRFSSFEeAIKGKGKLRALSILFEVGIEENLDYKAIIDG 199
Cdd:cd03122     79 RYKFSEITFHWGTCN--SDGSEHSIDGHKFPLEMQILHRNTDFFDSFE-AIKSPGGVLALAYLFELSHEDNPFLDPIIEG 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124  200 VERVSRFGKQAALDPFTLLNLLPNSTDKYYTYNGSLTSPPCTDTVDWIIFKDTVSISESQLAVFCEVLTMQQSGyVMLMD 279
Cdd:cd03122    156 LRNVSRPGKEVELPPFPLSDLLPPFTDKYYSYEGSLTTPPCSETVEWIVFREPVPISSRQLEAFRELLTRRQDG-VMSGD 234

                          250
                   ....*....|....*....
gi 1387264124  280 YLQNNFREQQYKFSRQVFS 298
Cdd:cd03122    235 YLPNNGRPQQPLGSRTVFS 253
Carb_anhydrase smart01057
Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse ...
 38-295 2.01e-86

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: 283.05  E-value: 2.01e-86
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124    38 WSYTGALNQKNWGKKYPT-CNSPKQSPINIDEDLTQVNVNLKKLKFqDWDKTSleNTFIHNTGKTVEINL-TNDYRLSGG 115
Cdd:smart01057    1 WGYEGKNGPEHWGKLDPPfCGGKRQSPIDIVTAEAQYDPSLKPLKL-SYDQPT--AKRILNNGHTVQVNFdDDGSTLSGG 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124   116 VSETVFKASKIAFHWGKCNmsSDGSEHSLEGQKFPLEMQIYCFDADrfSSFEEAIKGKGKLRALSILFEVGIEENLDYKA 195
Cdd:smart01057   78 PLPGRYRLKQFHFHWGGSD--SEGSEHTIDGKRFPLELHLVHYNSK--GSFSEAVSKPGGLAVVAVFFKVGAEENPALQA 153

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124   196 IIDGVERVSRFGKQAALDPFTLLNLLPNSTDKYYTYNGSLTSPPCTDTVDWIIFKDTVSISESQLAVFCEVLTMQQSgyv 275
Cdd:smart01057  154 ILDHLPLIKYKGQETELTPFDLSSLLPASTRHYYTYNGSLTTPPCSEGVTWIVFKEPITISTEQLEKFRTLLPMEGN--- 230

                           250       260
                    ....*....|....*....|
gi 1387264124   276 mlmDYLQNNFREQQYKFSRQ 295
Cdd:smart01057  231 ---EPLVNNARPLQPLNGRV 247
Carb_anhydrase pfam00194
Eukaryotic-type carbonic anhydrase;
44-300 9.14e-85

Eukaryotic-type carbonic anhydrase;


Pssm-ID: 459707 [Multi-domain]  Cd Length: 252  Bit Score: 278.38  E-value: 9.14e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124   44 LNQKNWGKKYPTCNSPKQSPINIDEDLTQVNVNLKKLKFQDWDKTSLENTfIHNTGKTVEINLTNDYR--LSGGVSETVF 121
Cdd:pfam00194    1 LGPEHWGKVYPSCGGKRQSPINIDTRKVRYDPSLPPLTFQGYDVPPGKNT-LTNNGHTVQVSLDDGDPstISGGPLATRY 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124  122 KASKIAFHWGKCNmsSDGSEHSLEGQKFPLEMQIYCFDADRfSSFEEAIKGKGKLRALSILFEVGIEENLDYKAIIDGVE 201
Cdd:pfam00194   80 RLVQFHFHWGSTD--SRGSEHTIDGKRYPAELHIVHYNSKY-KSFDEAAKHPDGLAVLGVFFEVGDENNPYLQPIVSALD 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124  202 RVSRFGKQAALDPFTLLNLLPNSTDKYYTYNGSLTSPPCTDTVDWIIFKDTVSISESQLAVFCEVLTMQQSGYvmlMDYL 281
Cdd:pfam00194  157 NIKYKGKSVLLPPFDLSDLLPEDLTSYYTYNGSLTTPPCSESVTWIVFKEPISISEEQLEAFRTLLFSDGGEE---PRPL 233

                          250
                   ....*....|....*....
gi 1387264124  282 QNNFREQQYKFSRQVFSSY 300
Cdd:pfam00194  234 VNNFRPTQPLNGRVVFASF 252
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
2030-2301 5.85e-75

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 250.65  E-value: 5.85e-75
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124  2030 KLEKQFKLLSQSNIQQSDYSTALKQCNREKNRTSSIIPVERSRVGISSLSGEGADYINASYIMGYYQSNEFIITQHPLLH 2109
Cdd:smart00194    1 GLEEEFEKLDRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGPLPS 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124  2110 TIQDFWRMIWDHNAQLVVMLpdgqNMVSPSGhfwhflfrAEDEFVYWPNK-DEPINCESFKVTLMAEEHKclsneEKLIM 2188
Cdd:smart00194   81 TVEDFWRMVWEQKVTVIVML----TELVEKG--------REKCAQYWPDEeGEPLTYGDITVTLKSVEKV-----DDYTI 143

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124  2189 QDFILEATQDDYVLEVRHFQCPKWP---NPDSPISkTFELISIIKEEAATRDGPMIVHDEHGGVTAGTFCALTTLMHQLE 2265
Cdd:smart00194  144 RTLEVTNTGCSETRTVTHYHYTNWPdhgVPESPES-ILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLE 222

                           250       260       270
                    ....*....|....*....|....*....|....*.
gi 1387264124  2266 KENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAVL 2301
Cdd:smart00194  223 AGKEVDIFEIVKELRSQRPGMVQTEEQYIFLYRAIL 258
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
2056-2301 6.01e-73

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 243.69  E-value: 6.01e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2056 NREKNRTSSIIPVERSRVGISSLSGeGADYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDGQNM 2135
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPG-PSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2136 VSPSGHfwhflfraedefVYWPNK-DEPINCESFKVTLMAEEhkclSNEEKLIMQDFILEATQDDYVLEVRHFQCPKWPN 2214
Cdd:pfam00102   80 GREKCA------------QYWPEEeGESLEYGDFTVTLKKEK----EDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPD 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2215 ---PDSPISkTFELISIIKE-EAATRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADI 2290
Cdd:pfam00102  144 hgvPESPNS-LLDLLRKVRKsSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTL 222

                          250
                   ....*....|.
gi 1387264124 2291 EQYQFLYKAVL 2301
Cdd:pfam00102  223 EQYIFLYDAIL 233
PHA02738 PHA02738
hypothetical protein; Provisional
 1730-2008 6.22e-54

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 192.45  E-value: 6.22e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1730 ETLKEFYQEVQSCTVDLGITADSSNhpdnKHKNRYINIVAYDHSRVKLAqlAEKDgkLTDYINANYVDGYNRPKAYIAAQ 1809
Cdd:PHA02738    25 EVITREHQKVISEKVDGTFNAEKKN----RKLNRYLDAVCFDHSRVILP--AERN--RGDYINANYVDGFEYKKKFICGQ 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1810 GPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWP-VDGSE-EYGNFLVTQKSIQVLAYYTVRNFTLRNtkikk 1887
Cdd:PHA02738    97 APTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSdVEQGSiRFGKFKITTTQVETHPHYVKSTLLLTD----- 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1888 gsqkGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFV------RKASHAKRHAVG-------PVVVHCSAGVGRTGTYIVL 1954
Cdd:PHA02738   172 ----GTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVlevrqcQKELAQESLQIGhnrlqppPIVVHCNAGLGRTPCYCVV 247

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1387264124 1955 DSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDALVEAILSKETEV 2008
Cdd:PHA02738   248 DISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAVKRYVNLTVNKV 301
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
1733-1993 4.72e-40

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 151.01  E-value: 4.72e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1733 KEFYQEVQSCTVDLGITADSSNHPDN---KHKNRYINIVAYDHSRVklaqlaEKDGKltdYINANYVDGYNrPKAYIAAQ 1809
Cdd:COG5599     14 EKINSRLSTLTNELAPSHNDPQYLQNingSPLNRFRDIQPYKETAL------RANLG---YLNANYIQVIG-NHRYIATQ 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1810 GPLKSTAEDFWRMIWEHNVEVIVMITNLVE--KGRRKCDQYWPVDGseEYGNFLVTQKSIQVlaYYTVRNFTLRNTKIK- 1886
Cdd:COG5599     84 YPLEEQLEDFFQMLFDNNTPVLVVLASDDEisKPKVKMPVYFRQDG--EYGKYEVSSELTES--IQLRDGIEARTYVLTi 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1887 KGS-QKGRPsgrvVTQYHYTQWPDMGVP--EYSLPVLTFVRKASHAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQ- 1962
Cdd:COG5599    160 KGTgQKKIE----IPVLHVKNWPDHGAIsaEALKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINa 235

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1387264124 1963 -HEGTVNVFGFLKHIRSQRNY-LVQTEEQYVFI 1993
Cdd:COG5599    236 lVQITLSVEEIVIDMRTSRNGgMVQTSEQLDVL 268
Cah COG3338
Carbonic anhydrase [Inorganic ion transport and metabolism];
38-263 1.22e-31

Carbonic anhydrase [Inorganic ion transport and metabolism];


Pssm-ID: 442567 [Multi-domain]  Cd Length: 247  Bit Score: 125.38  E-value: 1.22e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124   38 WSYTGALNQKNWGK---KYPTCNS-PKQSPINIDedlTQVNVNLKKLKFqDWDKTSLEntfIHNTGKTVEINLTNDYRLS 113
Cdd:COG3338     28 WSYEGETGPEHWGElspEFATCATgKNQSPIDIR---TAIKADLPPLKF-DYKPTPLE---IVNNGHTIQVNVDPGSTLT 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124  114 ggVSETVFKASKIAFHwgkcnmssDGSEHSLEGQKFPLEMQiycF---DADrfssfeeaikgkGKLRALSILFEVGiEEN 190
Cdd:COG3338    101 --VDGKRYELKQFHFH--------TPSEHTINGKSYPMEAH---LvhkDAD------------GELAVVGVLFEEG-AEN 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387264124  191 LDYKAIIDGV--ERvsrfGKQAALD-PFTLLNLLPNSTDkYYTYNGSLTSPPCTDTVDWIIFKDTVSISESQLAVF 263
Cdd:COG3338    155 PALAKLWANLplEA----GEEVALDaTIDLNDLLPEDRS-YYRYSGSLTTPPCSEGVLWIVLKQPITVSAEQIEAF 225
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 2049-2300 1.20e-25

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 110.12  E-value: 1.20e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2049 STALKQCNREKNRTSSIIPVERSRVGISS------------------LSGEGAD--YINASYIMGYYQSNEFIITQHPLL 2108
Cdd:PHA02746    44 NHFLKKENLKKNRFHDIPCWDHSRVVINAheslkmfdvgdsdgkkieVTSEDNAenYIHANFVDGFKEANKFICAQGPKE 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2109 HTIQDFWRMIWDHNAQLVVMLPDGQNmvspsghfwhflfraEDE--FVYWPN-KDEPINCESFKVTLMAEEHKCLSNEEK 2185
Cdd:PHA02746   124 DTSEDFFKLISEHESQVIVSLTDIDD---------------DDEkcFELWTKeEDSELAFGRFVAKILDIIEELSFTKTR 188

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2186 LIMQDFILEATQddyvlEVRHFQCPKWP---NPDSPiSKTFELISIIKEEAA----------TRDGPMIVHDEHGGVTAG 2252
Cdd:PHA02746   189 LMITDKISDTSR-----EIHHFWFPDWPdngIPTGM-AEFLELINKVNEEQAelikqadndpQTLGPIVVHCSAGIGRAG 262

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1387264124 2253 TFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAV 2300
Cdd:PHA02746   263 TFCAIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
fn3 pfam00041
Fibronectin type III domain;
313-401 5.89e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 55.11  E-value: 5.89e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124  313 SEPENVQADPENYTSLLVTWERPRVVYDTmIEKFAVLYQQLEGEDQtKHEFLTDGYQDlGAILNNLLPNMSYVLQIVAIC 392
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGP-ITGYEVEYRPKNSGEP-WNEITVPGTTT-SVTLTGLKPGTEYEVRVQAVN 77


                   ....*....
gi 1387264124  393 TNGlYGKYS 401
Cdd:pfam00041   78 GGG-EGPPS 85
PLN02179 PLN02179
carbonic anhydrase
 49-253 8.76e-08

carbonic anhydrase


Pssm-ID: 177835  Cd Length: 235  Bit Score: 55.37  E-value: 8.76e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124   49 WGKKYP---TCNSPK-QSPInideDLTQVNVNLkkLKFQDWDKT-SLENTFIHNTGKTVEINLTNDyrlsGG---VSETV 120
Cdd:PLN02179    50 WGKLNPqwkVCSTGKyQSPI----DLTDERVSL--IHDQALSRHyKPAPAVIQSRGHDVMVSWKGD----AGkitIHQTD 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124  121 FKAskIAFHWgkcnmsSDGSEHSLEGQKFPLEMQIYCFDAdrfssfeeaikgKGKLRALSILFEVGiEENLDYKAIIDGV 200
Cdd:PLN02179   120 YKL--VQCHW------HSPSEHTINGTSYDLELHMVHTSA------------SGKTAVVGVLYKLG-EPDEFLTKLLNGI 178

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1387264124  201 ERVsrfGKQ----AALDPFTLlnllPNSTDKYYTYNGSLTSPPCTDTVDWIIFKDTV 253
Cdd:PLN02179   179 KGV---GKKeinlGIVDPRDI----RFETNNFYRYIGSLTIPPCTEGVIWTVVKRVV 228
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 313-406 3.39e-05

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: 44.41  E-value: 3.39e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124  313 SEPENVQADPENYTSLLVTWERPRvVYDTMIEKFAVLYQQLEGEDQTKHEflTDGYQDLGAILNNLLPNMSYVLQIVAIC 392
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPPE-DDGGPITGYVVEYREKGSGDWKEVE--VTPGSETSYTLTGLKPGTEYEFRVRAVN 78

                           90
                   ....*....|....
gi 1387264124  393 TNGlYGKYSDQLIV 406
Cdd:cd00063     79 GGG-ESPPSESVTV 91
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 313-395 5.51e-05

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: 43.76  E-value: 5.51e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124   313 SEPENVQADPENYTSLLVTWERPRvvyDTMIEKFAVLYQQLEGEDQTKHEFLTDGYQDLGAILNNLLPNMSYVLQIVAIC 392
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPP---DDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78


                    ...
gi 1387264124   393 TNG 395
Cdd:smart00060   79 GAG 81
 
Name Accession Description Interval E-value
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 1725-2002 3.65e-161

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


Pssm-ID: 350505 [Multi-domain]  Cd Length: 274  Bit Score: 497.25  E-value: 3.65e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1725 FTEEFEtlkefyqEVQSCTVDLGITADSSNHPDNKHKNRYINIVAYDHSRVKLAQLAEKDGKLTDYINANYVDGYNRPKA 1804
Cdd:cd17667      1 FSEDFE-------EVQRCTADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSKHSDYINANYVDGYNKAKA 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1805 YIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPVDGSEEYGNFLVTQKSIQVLAYYTVRNFTLRNTK 1884
Cdd:cd17667     74 YIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTK 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1885 IKKGSQ---KGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQI 1961
Cdd:cd17667    154 VKKGQKgnpKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQI 233

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1387264124 1962 QHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDALVEAIL 2002
Cdd:cd17667    234 KDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 274
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 1790-1998 6.87e-155

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: 476.78  E-value: 6.87e-155
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1790 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPVDGSEEYGNFLVTQKSIQV 1869
Cdd:cd17668      1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1870 LAYYTVRNFTLRNTKIKKGSQKGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAKRHAVGPVVVHCSAGVGRTG 1949
Cdd:cd17668     81 LAYYTVRNFTLRNTKIKKGSQKGRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVGPVVVHCSAGVGRTG 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1387264124 1950 TYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDALV 1998
Cdd:cd17668    161 TYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 2085-2301 2.70e-149

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: 461.00  E-value: 2.70e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2085 YINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDGQNMvspsghfwhflfrAEDEFVYWPNKDEPIN 2164
Cdd:cd17669      1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNM-------------AEDEFVYWPNKDEPIN 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2165 CESFKVTLMAEEHKCLSNEEKLIMQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTFELISIIKEEAATRDGPMIVHD 2244
Cdd:cd17669     68 CETFKVTLIAEEHKCLSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTFELISIIKEEAANRDGPMIVHD 147

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1387264124 2245 EHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAVL 2301
Cdd:cd17669    148 EHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 1790-1995 2.89e-142

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: 441.02  E-value: 2.89e-142
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1790 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPVDGSEEYGNFLVTQKSIQV 1869
Cdd:cd14549      1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTETYGNIQVTLLSTEV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1870 LAYYTVRNFTLRNTKIKKGsqKGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAKRHAVGPVVVHCSAGVGRTG 1949
Cdd:cd14549     81 LATYTVRTFSLKNLKLKKV--KGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAGVGRTG 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1387264124 1950 TYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHD 1995
Cdd:cd14549    159 TYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 2085-2302 3.69e-124

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: 389.42  E-value: 3.69e-124
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2085 YINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDGQNMvspsghfwhflfrAEDEFVYWPNKDEPIN 2164
Cdd:cd17670      1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQGL-------------AEDEFVYWPSREESMN 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2165 CESFKVTLMAEEHKCLSNEEKLIMQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTFELISIIKEEAATRDGPMIVHD 2244
Cdd:cd17670     68 CEAFTVTLISKDRLCLSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISSTFELINVIKEEALTRDGPTIVHD 147

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1387264124 2245 EHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAVLS 2302
Cdd:cd17670    148 EFGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAMLS 205
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 2085-2298 6.71e-123

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: 385.52  E-value: 6.71e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2085 YINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDGQnmvspsghfwhflfRAEDEFVYWPNKDEPIN 2164
Cdd:cd14550      1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNE--------------LNEDEPIYWPTKEKPLE 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2165 CESFKVTLMAEEHKCLSNEEKLIMQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTFELISIIKEEAATRDGPMIVHD 2244
Cdd:cd14550     67 CETFKVTLSGEDHSCLSNEIRLIVRDFILESTQDDYVLEVRQFQCPSWPNPCSPIHTVFELINTVQEWAQQRDGPIVVHD 146

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1387264124 2245 EHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYK 2298
Cdd:cd14550    147 RYGGVQAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1724-1999 2.73e-119

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 377.77  E-value: 2.73e-119
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124  1724 GFTEEFETLKEFYQEVQSCTVdlgitadsSNHPDNKHKNRYINIVAYDHSRVKLAQLaekDGKLTDYINANYVDGYNRPK 1803
Cdd:smart00194    1 GLEEEFEKLDRLKPDDESCTV--------AAFPENRDKNRYKDVLPYDHTRVKLKPP---PGEGSDYINASYIDGPNGPK 69

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124  1804 AYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPVDGSE--EYGNFLVTQKSIQVLAYYTVRNFTLR 1881
Cdd:smart00194   70 AYIATQGPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEplTYGDITVTLKSVEKVDDYTIRTLEVT 149

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124  1882 NTkikkgsqkGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQI 1961
Cdd:smart00194  150 NT--------GCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQL 221

                           250       260       270
                    ....*....|....*....|....*....|....*...
gi 1387264124  1962 QHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDALVE 1999
Cdd:smart00194  222 EAGKEVDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1758-1999 2.76e-113

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 359.25  E-value: 2.76e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1758 NKHKNRYINIVAYDHSRVKLaqlaEKDGKLTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNL 1837
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKL----TGDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTEL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1838 VEKGRRKCDQYWP--VDGSEEYGNFLVTQKSI-QVLAYYTVRNFTLRNtkikkgsqKGRPSGRVVTQYHYTQWPDMGVPE 1914
Cdd:pfam00102   77 EEKGREKCAQYWPeeEGESLEYGDFTVTLKKEkEDEKDYTVRTLEVSN--------GGSEETRTVKHFHYTGWPDHGVPE 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1915 YSLPVLTFVRKASHAKRHA-VGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFI 1993
Cdd:pfam00102  149 SPNSLLDLLRKVRKSSLDGrSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFL 228


                   ....*.
gi 1387264124 1994 HDALVE 1999
Cdd:pfam00102  229 YDAILE 234
alpha_CARP_receptor_like cd03122
Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related ...
 45-298 9.18e-112

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: 355.89  E-value: 9.18e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124   45 NQKNWGKKYPTCNS-PKQSPINIDEDlTQVNVN-LKKLKFQDWDKTSLEnTFIHNTGKTVEINLTN---DYRLSGGVSET 119
Cdd:cd03122      1 NPKHWAKKYPACGEgRQQSPIDIVED-TQVQRQgLQPLHFDGYEELTAS-TTLENTGKTVILRLEGnssDPFVSGGPLLG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124  120 VFKASKIAFHWGKCNmsSDGSEHSLEGQKFPLEMQIYCFDADRFSSFEeAIKGKGKLRALSILFEVGIEENLDYKAIIDG 199
Cdd:cd03122     79 RYKFSEITFHWGTCN--SDGSEHSIDGHKFPLEMQILHRNTDFFDSFE-AIKSPGGVLALAYLFELSHEDNPFLDPIIEG 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124  200 VERVSRFGKQAALDPFTLLNLLPNSTDKYYTYNGSLTSPPCTDTVDWIIFKDTVSISESQLAVFCEVLTMQQSGyVMLMD 279
Cdd:cd03122    156 LRNVSRPGKEVELPPFPLSDLLPPFTDKYYSYEGSLTTPPCSETVEWIVFREPVPISSRQLEAFRELLTRRQDG-VMSGD 234

                          250
                   ....*....|....*....
gi 1387264124  280 YLQNNFREQQYKFSRQVFS 298
Cdd:cd03122    235 YLPNNGRPQQPLGSRTVFS 253
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 1758-2003 1.39e-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: 349.00  E-value: 1.39e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1758 NKHKNRYINIVAYDHSRVKLAQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNL 1837
Cdd:cd14553      3 NKPKNRYANVIAYDHSRVILQPIEGVPG--SDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1838 VEKGRRKCDQYWPVDGSEEYGNFLVTQKSIQVLAYYTVRNFTLRNTkikkgsqkGRPSGRVVTQYHYTQWPDMGVPEYSL 1917
Cdd:cd14553     81 EERSRVKCDQYWPTRGTETYGLIQVTLLDTVELATYTVRTFALHKN--------GSSEKREVRQFQFTAWPDHGVPEHPT 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1918 PVLTFVRKASHAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDAL 1997
Cdd:cd14553    153 PFLAFLRRVKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDAL 232


                   ....*.
gi 1387264124 1998 VEAILS 2003
Cdd:cd14553    233 LEAVTC 238
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 1790-1995 2.94e-95

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: 306.13  E-value: 2.94e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1790 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPVDGSE--EYGNFLVTQKSI 1867
Cdd:cd00047      1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKplEYGDITVTLVSE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1868 QVLAYYTVRNFTLRNTKIKKGsqkgrpsgRVVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAKRHAVGPVVVHCSAGVGR 1947
Cdd:cd00047     81 EELSDYTIRTLELSPKGCSES--------REVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCSAGVGR 152

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1387264124 1948 TGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHD 1995
Cdd:cd00047    153 TGTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 1723-2001 3.75e-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: 303.50  E-value: 3.75e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1723 SGFTEEFETLK-----EFYQEVQSCTVDLGITADSSNHPDNKHKNRYINIVAYDHSRVKLAQLAEKDGklTDYINANYVD 1797
Cdd:cd14626      1 SDLADNIERLKandglKFSQEYESIDPGQQFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPG--SDYINANYID 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1798 GYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPVDGSEEYGNFLVTQKSIQVLAYYTVRN 1877
Cdd:cd14626     79 GYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIRGTETYGMIQVTLLDTVELATYSVRT 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1878 FTLRntkiKKGSQKGRPsgrvVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAKRHAVGPVVVHCSAGVGRTGTYIVLDSM 1957
Cdd:cd14626    159 FALY----KNGSSEKRE----VRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVIDAM 230

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1387264124 1958 LQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDALVEAI 2001
Cdd:cd14626    231 LERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLEAA 274
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 1763-1994 6.76e-92

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: 297.73  E-value: 6.76e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1763 RYINIVAYDHSRVKLAQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGR 1842
Cdd:cd14548      1 RYTNILPYDHSRVKLIPINEEEG--SDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGR 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1843 RKCDQYWPVDGSE-EYGNFLVTQKSIQVLAYYTVRNFTLrntkikkgsqKGRPSGRVVTQYHYTQWPDMGVPEYSLPVLT 1921
Cdd:cd14548     79 VKCDHYWPFDQDPvYYGDITVTMLSESVLPDWTIREFKL----------ERGDEVRSVRQFHFTAWPDHGVPEAPDSLLR 148

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387264124 1922 FVRKASHAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIH 1994
Cdd:cd14548    149 FVRLVRDYIKQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLH 221
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 1749-1994 6.95e-91

catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein phosphatase non-receptor type 9 (PTPN9), also called protein-tyrosine phosphatase MEG2, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN9 plays an important role in promoting intracellular secretary vesicle fusion in hematopoietic cells and promotes the dephosphorylation of ErbB2 and EGFR in breast cancer cells, leading to impaired activation of STAT5 and STAT3. It also directly dephosphorylates STAT3 at the Tyr705 residue, resulting in its inactivation. PTPN9 has been found to be dysregulated in various human cancers, including breast, colorectal, and gastric cancer.


Pssm-ID: 350391 [Multi-domain]  Cd Length: 271  Bit Score: 296.58  E-value: 6.95e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1749 TADSSNHPDNKHKNRYINIVAYDHSRVKLAQLAEKDgkLTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNV 1828
Cdd:cd14543     20 TFLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDE--RTDYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKV 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1829 EVIVMITNLVEKGRRKCDQYWPVDG--SEEYGNFLVTQKSIQVLAYYTVRNFTLRNTKIKkgsqkgrpSGRVVTQYHYTQ 1906
Cdd:cd14543     98 LVIVMTTRVVERGRVKCGQYWPLEEgsSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETD--------ESRQVTHFQFTS 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1907 WPDMGVPEYSLPVLTFVRKASHAKRHAVG-------------PVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFL 1973
Cdd:cd14543    170 WPDFGVPSSAAALLDFLGEVRQQQALAVKamgdrwkghppgpPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQTV 249

                          250       260
                   ....*....|....*....|.
gi 1387264124 1974 KHIRSQRNYLVQTEEQYVFIH 1994
Cdd:cd14543    250 RRMRTQRAFSIQTPDQYYFCY 270
Carb_anhydrase smart01057
Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse ...
 38-295 2.01e-86

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: 283.05  E-value: 2.01e-86
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124    38 WSYTGALNQKNWGKKYPT-CNSPKQSPINIDEDLTQVNVNLKKLKFqDWDKTSleNTFIHNTGKTVEINL-TNDYRLSGG 115
Cdd:smart01057    1 WGYEGKNGPEHWGKLDPPfCGGKRQSPIDIVTAEAQYDPSLKPLKL-SYDQPT--AKRILNNGHTVQVNFdDDGSTLSGG 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124   116 VSETVFKASKIAFHWGKCNmsSDGSEHSLEGQKFPLEMQIYCFDADrfSSFEEAIKGKGKLRALSILFEVGIEENLDYKA 195
Cdd:smart01057   78 PLPGRYRLKQFHFHWGGSD--SEGSEHTIDGKRFPLELHLVHYNSK--GSFSEAVSKPGGLAVVAVFFKVGAEENPALQA 153

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124   196 IIDGVERVSRFGKQAALDPFTLLNLLPNSTDKYYTYNGSLTSPPCTDTVDWIIFKDTVSISESQLAVFCEVLTMQQSgyv 275
Cdd:smart01057  154 ILDHLPLIKYKGQETELTPFDLSSLLPASTRHYYTYNGSLTTPPCSEGVTWIVFKEPITISTEQLEKFRTLLPMEGN--- 230

                           250       260
                    ....*....|....*....|
gi 1387264124   276 mlmDYLQNNFREQQYKFSRQ 295
Cdd:smart01057  231 ---EPLVNNARPLQPLNGRV 247
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 1707-2001 7.07e-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: 282.75  E-value: 7.07e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1707 IPIKHFPKHVADLHASsgfteefETLKeFYQEVQSCTVDLGITADSSNHPDNKHKNRYINIVAYDHSRVKLAQLAEKDGk 1786
Cdd:cd14625      4 IPISELAEHTERLKAN-------DNLK-LSQEYESIDPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMG- 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1787 lTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPVDGSEEYGNFLVTQKS 1866
Cdd:cd14625     75 -SDYINANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSRGTETYGMIQVTLLD 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1867 IQVLAYYTVRNFTLRntkiKKGSQKGRPsgrvVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAKRHAVGPVVVHCSAGVG 1946
Cdd:cd14625    154 TIELATFCVRTFSLH----KNGSSEKRE----VRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPPDAGPIVVHCSAGVG 225

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1387264124 1947 RTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDALVEAI 2001
Cdd:cd14625    226 RTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEAV 280
Carb_anhydrase pfam00194
Eukaryotic-type carbonic anhydrase;
44-300 9.14e-85

Eukaryotic-type carbonic anhydrase;


Pssm-ID: 459707 [Multi-domain]  Cd Length: 252  Bit Score: 278.38  E-value: 9.14e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124   44 LNQKNWGKKYPTCNSPKQSPINIDEDLTQVNVNLKKLKFQDWDKTSLENTfIHNTGKTVEINLTNDYR--LSGGVSETVF 121
Cdd:pfam00194    1 LGPEHWGKVYPSCGGKRQSPINIDTRKVRYDPSLPPLTFQGYDVPPGKNT-LTNNGHTVQVSLDDGDPstISGGPLATRY 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124  122 KASKIAFHWGKCNmsSDGSEHSLEGQKFPLEMQIYCFDADRfSSFEEAIKGKGKLRALSILFEVGIEENLDYKAIIDGVE 201
Cdd:pfam00194   80 RLVQFHFHWGSTD--SRGSEHTIDGKRYPAELHIVHYNSKY-KSFDEAAKHPDGLAVLGVFFEVGDENNPYLQPIVSALD 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124  202 RVSRFGKQAALDPFTLLNLLPNSTDKYYTYNGSLTSPPCTDTVDWIIFKDTVSISESQLAVFCEVLTMQQSGYvmlMDYL 281
Cdd:pfam00194  157 NIKYKGKSVLLPPFDLSDLLPEDLTSYYTYNGSLTTPPCSESVTWIVFKEPISISEEQLEAFRTLLFSDGGEE---PRPL 233

                          250
                   ....*....|....*....
gi 1387264124  282 QNNFREQQYKFSRQVFSSY 300
Cdd:pfam00194  234 VNNFRPTQPLNGRVVFASF 252
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 1693-2001 1.28e-84

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: 279.31  E-value: 1.28e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1693 PPTPIFPISDdvgaipikhfpkHVADLHASSGFteefetlkEFYQEVQSCTVDLGITADSSNHPDNKHKNRYINIVAYDH 1772
Cdd:cd14624      2 PPIPILELAD------------HIERLKANDNL--------KFSQEYESIDPGQQFTWEHSNLEVNKPKNRYANVIAYDH 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1773 SRVKLAQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPVD 1852
Cdd:cd14624     62 SRVLLSAIEGIPG--SDYINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSR 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1853 GSEEYGNFLVTQKSIQVLAYYTVRNFTLrntkIKKGSQKGRPsgrvVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAKRH 1932
Cdd:cd14624    140 GTETYGLIQVTLLDTVELATYCVRTFAL----YKNGSSEKRE----VRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPP 211

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387264124 1933 AVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDALVEAI 2001
Cdd:cd14624    212 DAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLEAV 280
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 1757-2002 4.95e-84

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: 275.75  E-value: 4.95e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1757 DNKHKNRYINIVAYDHSRVKLAQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITN 1836
Cdd:cd14630      2 ENRNKNRYGNIISYDHSRVRLQLLDGDPH--SDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTN 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1837 LVEKGRRKCDQYWPvDGSEEYGNFLVTQKSIQVLAYYTVRNFTLRntkiKKGSQKGRPsgrvVTQYHYTQWPDMGVPEYS 1916
Cdd:cd14630     80 LVEVGRVKCVRYWP-DDTEVYGDIKVTLIETEPLAEYVIRTFTVQ----KKGYHEIRE----IRQFHFTSWPDHGVPCYA 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1917 LPVLTFVRKASHAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDA 1996
Cdd:cd14630    151 TGLLGFVRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDA 230


                   ....*.
gi 1387264124 1997 LVEAIL 2002
Cdd:cd14630    231 ILEACL 236
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 1762-1993 3.15e-80

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: 264.37  E-value: 3.15e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1762 NRYINIVAYDHSRVKLAQLAEKdgkLTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKG 1841
Cdd:cd14615      1 NRYNNVLPYDISRVKLSVQSHS---TDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1842 RRKCDQYWPVDGSEEYGNFLVTQKSIQVLAYYTVRNFTLRNtkiKKGSQKgrpsgRVVTQYHYTQWPDMGVPEYSLPVLT 1921
Cdd:cd14615     78 RTKCEEYWPSKQKKDYGDITVTMTSEIVLPEWTIRDFTVKN---AQTNES-----RTVRHFHFTSWPDHGVPETTDLLIN 149

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387264124 1922 F---VRKasHAKRHAV-GPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFI 1993
Cdd:cd14615    150 FrhlVRE--YMKQNPPnSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFL 223
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 1693-2008 7.81e-80

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: 266.12  E-value: 7.81e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1693 PPTPIFPISDDVGaipikhfpKHVADlhASSGFTEEFETLKefyqevqSCTVDlgITADSSNHPDNKHKNRYINIVAYDH 1772
Cdd:cd14621      6 PPLPVDKLEEEIN--------RRMAD--DNKLFREEFNALP-------ACPIQ--ATCEAASKEENKEKNRYVNILPYDH 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1773 SRVKLAQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPVD 1852
Cdd:cd14621     67 SRVHLTPVEGVPD--SDYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQ 144

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1853 GSEEYGNFLVTQKSIQVLAYYTVRNFTLRNTkikkGSQKGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAKRH 1932
Cdd:cd14621    145 GCWTYGNIRVSVEDVTVLVDYTVRKFCIQQV----GDVTNKKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQ 220

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387264124 1933 AVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDALVEAILSKETEV 2008
Cdd:cd14621    221 YAGAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEHYLYGDTEL 296
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 1714-2002 2.31e-79

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: 263.83  E-value: 2.31e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1714 KHVADLHASSG--FTEEFETlkefYQEVQSCTvdlgitADSSNHPDNKHKNRYINIVAYDHSRVKLAQLAEKDGklTDYI 1791
Cdd:cd14633      4 QHITQMKCAEGygFKEEYES----FFEGQSAP------WDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETS--SDYI 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1792 NANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPvDGSEEYGNFLVTQKSIQVLA 1871
Cdd:cd14633     72 NGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWP-DDTEIYKDIKVTLIETELLA 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1872 YYTVRNFTLRntkikkgsQKGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAKRHAVGPVVVHCSAGVGRTGTY 1951
Cdd:cd14633    151 EYVIRTFAVE--------KRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCF 222

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1387264124 1952 IVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDALVEAIL 2002
Cdd:cd14633    223 IVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILEACL 273
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 1790-2002 6.18e-77

catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The type II (or R2B) subfamily of receptor protein tyrosine phosphatases (RPTPs) include the prototypical member PTPmu (or PTPRM), PCP-2 (or PTPRU), PTPrho (or PTPRT), and PTPkappa (or PTPRK). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Type IIb RPTPs mediate cell-cell adhesion though homophilic interactions; their ligand is an identical molecule on an adjacent cell. No heterophilic interactions between the subfamily members have been observed. They also commonly function as tumor suppressors. They contain an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350403 [Multi-domain]  Cd Length: 204  Bit Score: 254.07  E-value: 6.18e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1790 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPvDGSEEYGNFLVTQKSIQV 1869
Cdd:cd14555      1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWP-DDTEVYGDIKVTLVETEP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1870 LAYYTVRNFTLRntkikkgsQKGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAKRHAVGPVVVHCSAGVGRTG 1949
Cdd:cd14555     80 LAEYVVRTFALE--------RRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAGPIVVHCSAGAGRTG 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1387264124 1950 TYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDALVEAIL 2002
Cdd:cd14555    152 CYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILEACL 204
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 1762-2001 7.45e-77

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: 254.81  E-value: 7.45e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1762 NRYINIVAYDHSRVKLAQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKG 1841
Cdd:cd14619      1 NRFRNVLPYDWSRVPLKPIHEEPG--SDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1842 RRKCDQYWPVDGSE-EYGNFLVTQKSIQVLAYYTVRNFTLRNTKIKKgsqkgrpsGRVVTQYHYTQWPDMGVPEYSLPVL 1920
Cdd:cd14619     79 RVKCEHYWPLDYTPcTYGHLRVTVVSEEVMENWTVREFLLKQVEEQK--------TLSVRHFHFTAWPDHGVPSSTDTLL 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1921 TF---VRKASHAKRHAvGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDAL 1997
Cdd:cd14619    151 AFrrlLRQWLDQTMSG-GPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCI 229


                   ....
gi 1387264124 1998 VEAI 2001
Cdd:cd14619    230 LDFL 233
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 1764-1999 1.91e-76

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: 253.71  E-value: 1.91e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1764 YINIVAYDHSRVKLAQLaekDGKL-TDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGR 1842
Cdd:cd14620      1 YPNILPYDHSRVILSQL---DGIPcSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1843 RKCDQYWPVDGSEEYGNFLVTQKSIQVLAYYTVRNFTLRntkiKKGSQKGRPSgRVVTQYHYTQWPDMGVPEYSLPVLTF 1922
Cdd:cd14620     78 EKCYQYWPDQGCWTYGNIRVAVEDCVVLVDYTIRKFCIQ----PQLPDGCKAP-RLVTQLHFTSWPDFGVPFTPIGMLKF 152

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387264124 1923 VRKASHAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDALVE 1999
Cdd:cd14620    153 LKKVKSVNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 1762-1994 3.51e-76

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: 252.92  E-value: 3.51e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1762 NRYINIVAYDHSRVKLAQLaeKDGKLTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKG 1841
Cdd:cd14617      1 NRYNNILPYDSTRVKLSNV--DDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1842 RRKCDQYWPVD-GSEEYGNFLVTQKSIQVLAYYTVRNFtlrntKIKKGSQKGRPsgRVVTQYHYTQWPDMGVPEYSLPVL 1920
Cdd:cd14617     79 RVKCDHYWPADqDSLYYGDLIVQMLSESVLPEWTIREF-----KICSEEQLDAP--RLVRHFHYTVWPDHGVPETTQSLI 151

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387264124 1921 TFVRKASH--AKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIH 1994
Cdd:cd14617    152 QFVRTVRDyiNRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 227
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
2030-2301 5.85e-75

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 250.65  E-value: 5.85e-75
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124  2030 KLEKQFKLLSQSNIQQSDYSTALKQCNREKNRTSSIIPVERSRVGISSLSGEGADYINASYIMGYYQSNEFIITQHPLLH 2109
Cdd:smart00194    1 GLEEEFEKLDRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGPLPS 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124  2110 TIQDFWRMIWDHNAQLVVMLpdgqNMVSPSGhfwhflfrAEDEFVYWPNK-DEPINCESFKVTLMAEEHKclsneEKLIM 2188
Cdd:smart00194   81 TVEDFWRMVWEQKVTVIVML----TELVEKG--------REKCAQYWPDEeGEPLTYGDITVTLKSVEKV-----DDYTI 143

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124  2189 QDFILEATQDDYVLEVRHFQCPKWP---NPDSPISkTFELISIIKEEAATRDGPMIVHDEHGGVTAGTFCALTTLMHQLE 2265
Cdd:smart00194  144 RTLEVTNTGCSETRTVTHYHYTNWPdhgVPESPES-ILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLE 222

                           250       260       270
                    ....*....|....*....|....*....|....*.
gi 1387264124  2266 KENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAVL 2301
Cdd:smart00194  223 AGKEVDIFEIVKELRSQRPGMVQTEEQYIFLYRAIL 258
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 1753-1996 1.52e-73

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: 245.51  E-value: 1.52e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1753 SNHPDNKHKNRYINIVAYDHSRVKLAQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIV 1832
Cdd:cd14554      1 ANLPCNKFKNRLVNILPYESTRVCLQPIRGVEG--SDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIV 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1833 MITNLVEKGRRKCDQYWPVDGSEEYGNFLVtqksiQVLAYYTVRNFTLRNTKIKKGSQKgrpSGRVVTQYHYTQWPDMGV 1912
Cdd:cd14554     79 MLTKLREMGREKCHQYWPAERSARYQYFVV-----DPMAEYNMPQYILREFKVTDARDG---QSRTVRQFQFTDWPEQGV 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1913 PEYSLPVLTFVRKASHAKRH--AVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQY 1990
Cdd:cd14554    151 PKSGEGFIDFIGQVHKTKEQfgQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQY 230


                   ....*.
gi 1387264124 1991 VFIHDA 1996
Cdd:cd14554    231 QFCYRA 236
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 1783-2002 1.94e-73

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: 244.54  E-value: 1.94e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1783 KDGKLTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPvDGSEEYGNFLV 1862
Cdd:cd14631      8 EDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWP-DDTEVYGDFKV 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1863 TQKSIQVLAYYTVRNFTLrntkikkgSQKGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAKRHAVGPVVVHCS 1942
Cdd:cd14631     87 TCVEMEPLAEYVVRTFTL--------ERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVHCS 158

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1943 AGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDALVEAIL 2002
Cdd:cd14631    159 AGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACL 218
alpha_CA cd00326
Carbonic anhydrase alpha (vertebrate-like) group. Carbonic anhydrases (CAs) are ...
 60-297 3.39e-73

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: 244.11  E-value: 3.39e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124   60 KQSPINIDEDLTQVNVNLKKLKFQDWDKTSLEntfIHNTGKTVEINL-TNDYRLSGGVSETVFKASKIAFHWGKCNmsSD 138
Cdd:cd00326      3 RQSPINIVTSAVVYDPSLPPLNFDYYPTTSLT---LVNNGHTVQVNFdDDGGTLSGGGLPGRYKLVQFHFHWGSEN--SP 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124  139 GSEHSLEGQKFPLEMQIYCFDADRFSSfeEAIKGKGKLRALSILFEVGIEENLDYKAIIDGVERVSRFGKQAALDPFTLL 218
Cdd:cd00326     78 GSEHTIDGKRYPLELHLVHYNSDYYSS--EAAKKPGGLAVLGVFFEVGEKENPFLKKILDALPKIKYKGKETTLPPFDLS 155

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387264124  219 NLLPNSTDKYYTYNGSLTSPPCTDTVDWIIFKDTVSISESQLAVFCEVLTMQqsgyvmlMDYLQNNFREQQYKFSRQVF 297
Cdd:cd00326    156 DLLPSSLRDYYTYEGSLTTPPCSEGVTWIVFKEPITISKEQLEAFRSLLDRE-------GKPLVNNYRPVQPLNGRVVY 227
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
2056-2301 6.01e-73

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 243.69  E-value: 6.01e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2056 NREKNRTSSIIPVERSRVGISSLSGeGADYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDGQNM 2135
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPG-PSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2136 VSPSGHfwhflfraedefVYWPNK-DEPINCESFKVTLMAEEhkclSNEEKLIMQDFILEATQDDYVLEVRHFQCPKWPN 2214
Cdd:pfam00102   80 GREKCA------------QYWPEEeGESLEYGDFTVTLKKEK----EDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPD 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2215 ---PDSPISkTFELISIIKE-EAATRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADI 2290
Cdd:pfam00102  144 hgvPESPNS-LLDLLRKVRKsSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTL 222

                          250
                   ....*....|.
gi 1387264124 2291 EQYQFLYKAVL 2301
Cdd:pfam00102  223 EQYIFLYDAIL 233
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 1790-1994 2.11e-72

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: 240.97  E-value: 2.11e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1790 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPVDGSEEYGNFLVTQKSIQV 1869
Cdd:cd14551      1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCWTYGNLRVRVEDTVV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1870 LAYYTVRNFTLRntkiKKGSQKGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAKRHAVGPVVVHCSAGVGRTG 1949
Cdd:cd14551     81 LVDYTTRKFCIQ----KVNRGIGEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAGPIVVHCSAGVGRTG 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1387264124 1950 TYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIH 1994
Cdd:cd14551    157 TFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 1762-1994 1.92e-71

catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; The kinase interaction motif (KIM) family of protein-tyrosine phosphatases (PTPs) includes tyrosine-protein phosphatases non-receptor type 7 (PTPN7) and non-receptor type 5 (PTPN5), and protein-tyrosine phosphatase receptor type R (PTPRR). PTPN7 is also called hematopoietic protein-tyrosine phosphatase (HePTP) while PTPN5 is also called striatal-enriched protein-tyrosine phosphatase (STEP). They belong to the family of classical tyrosine-specific PTPs (EC 3.1.3.48) that catalyze the dephosphorylation of phosphotyrosine peptides. KIM-PTPs are characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. They are highly specific to the MAPKs ERK1/2 (extracellular-signal-regulated kinase 1/2) and p38, over JNK (c-Jun N-terminal kinase); they dephosphorylate these kinases and thereby critically modulate cell proliferation and differentiation.


Pssm-ID: 350395 [Multi-domain]  Cd Length: 224  Bit Score: 238.84  E-value: 1.92e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1762 NRYINIVAYDHSRVKLAQlaEKDGKLTDYINANYVDGYN-RPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEK 1840
Cdd:cd14547      1 NRYKTILPNEHSRVCLPS--VDDDPLSSYINANYIRGYDgEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1841 gRRKCDQYWPVDGSEEYGNFLVTQKSIQVLAYYTVRNFTLRNtkikkGSQKgrpsgRVVTQYHYTQWPDMGVPEYSLPVL 1920
Cdd:cd14547     79 -KEKCAQYWPEEENETYGDFEVTVQSVKETDGYTVRKLTLKY-----GGEK-----RYLKHYWYTSWPDHKTPEAAQPLL 147

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387264124 1921 TFVRKASHAKRHAV--GPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIH 1994
Cdd:cd14547    148 SLVQEVEEARQTEPhrGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVH 223
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 1790-2002 4.64e-71

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: 237.26  E-value: 4.64e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1790 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPvDGSEEYGNFLVTQKSIQV 1869
Cdd:cd14632      1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWP-DDSDTYGDIKITLLKTET 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1870 LAYYTVRNFTLRntkikkgsQKGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAKRHAVGPVVVHCSAGVGRTG 1949
Cdd:cd14632     80 LAEYSVRTFALE--------RRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTG 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1387264124 1950 TYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDALVEAIL 2002
Cdd:cd14632    152 CYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILEACL 204
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 1758-2001 4.55e-70

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: 236.21  E-value: 4.55e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1758 NKHKNRYINIVAYDHSRVKLaQLAEKDGKLTDYINANYVDGYN-------RPKAYIAAQGPLKSTAEDFWRMIWEHNVEV 1830
Cdd:cd14544      1 NKGKNRYKNILPFDHTRVIL-KDRDPNVPGSDYINANYIRNENegpttdeNAKTYIATQGCLENTVSDFWSMVWQENSRV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1831 IVMITNLVEKGRRKCDQYWPVDG-SEEYGNFlvtqkSIQVLAYYTVRNFTLRNTKIKKGSQKGRPsgRVVTQYHYTQWPD 1909
Cdd:cd14544     80 IVMTTKEVERGKNKCVRYWPDEGmQKQYGPY-----RVQNVSEHDTTDYTLRELQVSKLDQGDPI--REIWHYQYLSWPD 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1910 MGVPEYSLPVLTFVRKASHAKRH--AVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEG---TVNVFGFLKHIRSQRNYLV 1984
Cdd:cd14544    153 HGVPSDPGGVLNFLEDVNQRQESlpHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGldcDIDIQKTIQMVRSQRSGMV 232

                          250
                   ....*....|....*..
gi 1387264124 1985 QTEEQYVFIHDALVEAI 2001
Cdd:cd14544    233 QTEAQYKFIYVAVAQYI 249
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 1748-1994 1.16e-69

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


Pssm-ID: 350462 [Multi-domain]  Cd Length: 245  Bit Score: 234.78  E-value: 1.16e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1748 ITADSSNHPDNKHKNRYINIVAYDHSRVKLAQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHN 1827
Cdd:cd14614      2 IPHFAADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEG--SDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1828 VEVIVMITNLVEKGRRKCDQYWPVdgSEE---YGNFLVTQKSIQVLAYYTVRNFtlrntKIKKGSQKGRpsgrvVTQYHY 1904
Cdd:cd14614     80 SQIIVMLTQCNEKRRVKCDHYWPF--TEEpvaYGDITVEMLSEEEQPDWAIREF-----RVSYADEVQD-----VMHFNY 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1905 TQWPDMGVPEYSL--PVLTFVRKASHAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNY 1982
Cdd:cd14614    148 TAWPDHGVPTANAaeSILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMS 227

                          250
                   ....*....|..
gi 1387264124 1983 LVQTEEQYVFIH 1994
Cdd:cd14614    228 MVQTEEQYIFIH 239
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 1762-1998 1.80e-67

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


Pssm-ID: 350466 [Multi-domain]  Cd Length: 230  Bit Score: 227.90  E-value: 1.80e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1762 NRYINIVAYDHSRVKLAQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKG 1841
Cdd:cd14618      1 NRYPHVLPYDHSRVRLSQLGGEPH--SDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1842 RRKCDQYWPVDGSE-EYGnflvtQKSIQVLAYYTVRNFTLRNTKIKKGSQKGRpsgRVVTQYHYTQWPDMGVPEYSLPVL 1920
Cdd:cd14618     79 RVLCDHYWPSESTPvSYG-----HITVHLLAQSSEDEWTRREFKLWHEDLRKE---RRVKHLHYTAWPDHGIPESTSSLM 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1921 TF---VRKASHAKRHAvGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDAL 1997
Cdd:cd14618    151 AFrelVREHVQATKGK-GPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCI 229


                   .
gi 1387264124 1998 V 1998
Cdd:cd14618    230 L 230
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 1790-1995 2.63e-67

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: 226.75  E-value: 2.63e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1790 YINANYVD-GYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPVDGSE-EYGNFLVTQKSI 1867
Cdd:cd18533      1 YINASYITlPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEgEYGDLTVELVSE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1868 QVL--AYYTVRNFTLRNTKIKKgsqkgrpsgRVVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAKRHA--VGPVVVHCSA 1943
Cdd:cd18533     81 EENddGGFIVREFELSKEDGKV---------KKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRELNDSAslDPPIIVHCSA 151

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387264124 1944 GVGRTGTYIVLDSMLQQIQ--HEGTVN-------VFGFLKHIRSQRNYLVQTEEQYVFIHD 1995
Cdd:cd18533    152 GVGRTGTFIALDSLLDELKrgLSDSQDledsedpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 1752-2003 1.11e-66

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


Pssm-ID: 350476 [Multi-domain]  Cd Length: 292  Bit Score: 228.08  E-value: 1.11e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1752 SSNHPDNKHKNRYINIVAYDHSRVKLAQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVI 1831
Cdd:cd14628     46 SANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEG--SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIV 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1832 VMITNLVEKGRRKCDQYWPVDGSEEYGNFLVTQksiqvLAYYTVRNFTLRNTKIKKgSQKGRpsGRVVTQYHYTQWPDMG 1911
Cdd:cd14628    124 VMLTKLREMGREKCHQYWPAERSARYQYFVVDP-----MAEYNMPQYILREFKVTD-ARDGQ--SRTVRQFQFTDWPEQG 195

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1912 VPEYSLPVLTFVRKASHAKRH--AVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQ 1989
Cdd:cd14628    196 VPKSGEGFIDFIGQVHKTKEQfgQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQ 275

                          250
                   ....*....|....
gi 1387264124 1990 YVFIHDALVEAILS 2003
Cdd:cd14628    276 YQFCYRAALEYLGS 289
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 1790-1994 5.01e-66

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: 222.39  E-value: 5.01e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1790 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPV--DGSEEYGNFLVTQKSI 1867
Cdd:cd14557      1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSmeEGSRAFGDVVVKINEE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1868 QVLAYYTVRNFTLRNTKIKKgsqkgrpSGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAKRHAVGPVVVHCSAGVGR 1947
Cdd:cd14557     81 KICPDYIIRKLNINNKKEKG-------SGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGR 153

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1387264124 1948 TGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIH 1994
Cdd:cd14557    154 TGTYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIH 200
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 1752-2003 1.31e-65

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


Pssm-ID: 350475 [Multi-domain]  Cd Length: 290  Bit Score: 225.00  E-value: 1.31e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1752 SSNHPDNKHKNRYINIVAYDHSRVKLAQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVI 1831
Cdd:cd14627     47 SANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEG--SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIV 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1832 VMITNLVEKGRRKCDQYWPVDGSEEYGNFLVTQksiqvLAYYTVRNFTLRNTKIKKgSQKGRpsGRVVTQYHYTQWPDMG 1911
Cdd:cd14627    125 VMLTKLREMGREKCHQYWPAERSARYQYFVVDP-----MAEYNMPQYILREFKVTD-ARDGQ--SRTVRQFQFTDWPEQG 196

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1912 VPEYSLPVLTFVRKASHAKRH--AVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQ 1989
Cdd:cd14627    197 VPKSGEGFIDFIGQVHKTKEQfgQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDE 276

                          250
                   ....*....|....
gi 1387264124 1990 YVFIHDALVEAILS 2003
Cdd:cd14627    277 YQFCYQAALEYLGS 290
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 1752-2003 6.34e-65

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: 223.06  E-value: 6.34e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1752 SSNHPDNKHKNRYINIVAYDHSRVKLAQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVI 1831
Cdd:cd14629     47 SANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEG--SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIV 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1832 VMITNLVEKGRRKCDQYWPVDGSEEYGNFLVTQksiqvLAYYTVRNFTLRNTKIKKgSQKGRpsGRVVTQYHYTQWPDMG 1911
Cdd:cd14629    125 VMLTKLREMGREKCHQYWPAERSARYQYFVVDP-----MAEYNMPQYILREFKVTD-ARDGQ--SRTIRQFQFTDWPEQG 196

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1912 VPEYSLPVLTFVRKASHAKRH--AVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQ 1989
Cdd:cd14629    197 VPKTGEGFIDFIGQVHKTKEQfgQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQ 276

                          250
                   ....*....|....
gi 1387264124 1990 YVFIHDALVEAILS 2003
Cdd:cd14629    277 YQLCYRAALEYLGS 290
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 1733-1999 5.41e-62

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


Pssm-ID: 350451 [Multi-domain]  Cd Length: 266  Bit Score: 213.53  E-value: 5.41e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1733 KEFyQEVQSCTV----DLGITADSSNHPDNKHKNRYINIVAYDHSRVKLAQLAEKDGklTDYINANYVDGYNRPKAYIAA 1808
Cdd:cd14603      2 GEF-SEIRACSAafkaDYVCSTVAGGRKENVKKNRYKDILPYDQTRVILSLLQEEGH--SDYINANFIKGVDGSRAYIAT 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1809 QGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPV-DGSEEYGNFLVTQ-KSIQVLAYYTVRNFTLrntKIK 1886
Cdd:cd14603     79 QGPLSHTVLDFWRMIWQYGVKVILMACREIEMGKKKCERYWAQeQEPLQTGPFTITLvKEKRLNEEVILRTLKV---TFQ 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1887 KGSqkgrpsgRVVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAKRHAVGPVVVHCSAGVGRTGTYIVLDS-----MLQQI 1961
Cdd:cd14603    156 KES-------RSVSHFQYMAWPDHGIPDSPDCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYvrqllLTQRI 228

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1387264124 1962 QHEgtVNVFGFLKHIRSQRNYLVQTEEQYVFIHDALVE 1999
Cdd:cd14603    229 PPD--FSIFDVVLEMRKQRPAAVQTEEQYEFLYHTVAQ 264
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 1751-2003 5.96e-62

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


Pssm-ID: 350454 [Multi-domain]  Cd Length: 266  Bit Score: 213.59  E-value: 5.96e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1751 DSSNHPDNKHKNRYINIVAYDHSRVKLaQLAEKDGKLTDYINANYVDGY-----NRPKAYIAAQGPLKSTAEDFWRMIWE 1825
Cdd:cd14606     11 LEGQRPENKSKNRYKNILPFDHSRVIL-QGRDSNIPGSDYINANYVKNQllgpdENAKTYIASQGCLEATVNDFWQMAWQ 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1826 HNVEVIVMITNLVEKGRRKCDQYWP-VDGSEEYGNFLVTQKSIQVLAYYTVRnfTLRNTKIKKGSQKgrpsgRVVTQYHY 1904
Cdd:cd14606     90 ENSRVIVMTTREVEKGRNKCVPYWPeVGMQRAYGPYSVTNCGEHDTTEYKLR--TLQVSPLDNGELI-----REIWHYQY 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1905 TQWPDMGVPEYSLPVLTF---VRKASHAKRHAvGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGT---VNVFGFLKHIRS 1978
Cdd:cd14606    163 LSWPDHGVPSEPGGVLSFldqINQRQESLPHA-GPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVRA 241

                          250       260
                   ....*....|....*....|....*
gi 1387264124 1979 QRNYLVQTEEQYVFIHDALVEAILS 2003
Cdd:cd14606    242 QRSGMVQTEAQYKFIYVAIAQFIET 266
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 1790-2001 1.57e-61

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: 209.92  E-value: 1.57e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1790 YINANYV--DGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPvDGSEE----YGNFLVT 1863
Cdd:cd14538      1 YINASHIriPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWP-DSLNKplicGGRLEVS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1864 QKSIQVLAYYTVRNFTLRNTKIKKGsqkgrpsgRVVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAkrHAVGPVVVHCSA 1943
Cdd:cd14538     80 LEKYQSLQDFVIRRISLRDKETGEV--------HHITHLNFTTWPDHGTPQSADPLLRFIRYMRRI--HNSGPIVVHCSA 149

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1387264124 1944 GVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDALVEAI 2001
Cdd:cd14538    150 GIGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEVL 207
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 1790-1998 4.51e-61

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: 208.28  E-value: 4.51e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1790 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPVDGSEEYGNFLVTQKSIQV 1869
Cdd:cd14552      1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGSVSSGDITVELKDQTD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1870 LAYYTVRNFTLRNTKIKKgsqkgrpsGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAKRHA-VGPVVVHCSAGVGRT 1948
Cdd:cd14552     81 YEDYTLRDFLVTKGKGGS--------TRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQSgNHPITVHCSAGAGRT 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1949 GTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDALV 1998
Cdd:cd14552    153 GTFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVVQ 202
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 1790-1994 2.35e-60

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: 206.51  E-value: 2.35e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1790 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPVDGSEE--YGNFLVTQKSI 1867
Cdd:cd14542      1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQlqFGPFKISLEKE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1868 QVLAyytvRNFTLRNTKIKKGSQKgrpsgRVVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAKRHAVGPVVVHCSAGVGR 1947
Cdd:cd14542     81 KRVG----PDFLIRTLKVTFQKES-----RTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDVPICVHCSAGCGR 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1948 TGTYIVLDSMLQQIQHEG---TVNVFGFLKHIRSQRNYLVQTEEQYVFIH 1994
Cdd:cd14542    152 TGTICAIDYVWNLLKTGKipeEFSLFDLVREMRKQRPAMVQTKEQYELVY 201
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 1762-1994 2.73e-60

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: 207.07  E-value: 2.73e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1762 NRYINIVAYDHSRVKLAQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKG 1841
Cdd:cd14616      1 NRFPNIKPYNNNRVKLIADAGVPG--SDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1842 RRKCDQYWPVDGS--EEYGNFLVTQksiqvLAYYTVRNFTLRNTKIKKGSQKgrpsgRVVTQYHYTQWPDMGVPEYSLPV 1919
Cdd:cd14616     79 RIRCHQYWPEDNKpvTVFGDIVITK-----LMEDVQIDWTIRDLKIERHGDY-----MMVRQCNFTSWPEHGVPESSAPL 148

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1387264124 1920 LTFVRKASHAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIH 1994
Cdd:cd14616    149 IHFVKLVRASRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLH 223
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 1757-1999 2.95e-60

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


Pssm-ID: 350452 [Multi-domain]  Cd Length: 297  Bit Score: 209.79  E-value: 2.95e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1757 DNKHKNRYINIVAYDHSRVKLA-QLAEKDgklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMIT 1835
Cdd:cd14604     56 ENVKKNRYKDILPFDHSRVKLTlKTSSQD---SDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMAC 132

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1836 NLVEKGRRKCDQYWPVDGSE--EYGNFLVTQKSIQVLAYYTVRNFTLrntkikkgsqKGRPSGRVVTQYHYTQWPDMGVP 1913
Cdd:cd14604    133 REFEMGRKKCERYWPLYGEEpmTFGPFRISCEAEQARTDYFIRTLLL----------EFQNETRRLYQFHYVNWPDHDVP 202

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1914 EYSLPVLTFVRKASHAKRHAVGPVVVHCSAGVGRTGTYIVLD---SMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQY 1990
Cdd:cd14604    203 SSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQY 282


                   ....*....
gi 1387264124 1991 VFIHDALVE 1999
Cdd:cd14604    283 ELVHRAIAQ 291
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 1759-1992 7.05e-60

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: 206.09  E-value: 7.05e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1759 KHKNRYINIVAYDHSRVKLaqlaeKDGKlTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLV 1838
Cdd:cd14545      1 LNRYRDRDPYDHDRSRVKL-----KQGD-NDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLM 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1839 EKGRRKCDQYWPVDGSE----EYGNFLVTQKSIQVLAYYTVRNFTLRNTKIkkgsqkgrPSGRVVTQYHYTQWPDMGVPE 1914
Cdd:cd14545     75 EKGQIKCAQYWPQGEGNamifEDTGLKVTLLSEEDKSYYTVRTLELENLKT--------QETREVLHFHYTTWPDFGVPE 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1915 YSLPVLTF---VRKASHAKRHaVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGT--VNVFGFLKHIRSQRNYLVQTEEQ 1989
Cdd:cd14545    147 SPAAFLNFlqkVRESGSLSSD-VGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYRMGLIQTPDQ 225


                   ...
gi 1387264124 1990 YVF 1992
Cdd:cd14545    226 LRF 228
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1789-2003 7.53e-60

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: 205.26  E-value: 7.53e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1789 DYINANYVDgYNRPKA-----YIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWP-VDGSEEYGNFLV 1862
Cdd:cd14541      1 DYINANYVN-MEIPGSgivnrYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPdLGETMQFGNLQI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1863 TQKSIQVLAYYTVRNFTLRNTKIKKGsqkgrpsgRVVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAKRHAVGPVVVHCS 1942
Cdd:cd14541     80 TCVSEEVTPSFAFREFILTNTNTGEE--------RHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVEPTVVHCS 151

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387264124 1943 AGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIhdalVEAILS 2003
Cdd:cd14541    152 AGIGRTGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFV----CEAILR 208
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 1727-2001 4.84e-59

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: 205.66  E-value: 4.84e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1727 EEFETLKEFYQEVQSCtvdlgitaDSSNHPDNKHKNRYINIVAYDHSRVKLAqlAEKDGKLTDYINAN-YVDGYNRPKAY 1805
Cdd:cd14609     19 KEWQALCAYQAEPNTC--------STAQGEANVKKNRNPDFVPYDHARIKLK--AESNPSRSDYINASpIIEHDPRMPAY 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1806 IAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPVDGSEEYGNFLVTQKSIQVLAY-YTVRNFTLRNTK 1884
Cdd:cd14609     89 IATQGPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHIYEVNLVSEHIWCEdFLVRSFYLKNVQ 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1885 IKKgsqkgrpsGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQhE 1964
Cdd:cd14609    169 TQE--------TRTLTQFHFLSWPAEGIPSSTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMA-K 239

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1387264124 1965 GT--VNVFGFLKHIRSQRNYLVQTEEQYVFIHDALVEAI 2001
Cdd:cd14609    240 GVkeIDIAATLEHVRDQRPGMVRTKDQFEFALTAVAEEV 278
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 1757-1997 5.33e-59

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: 204.48  E-value: 5.33e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1757 DNKHKNRYINIVAYDHSRVKLAQlAEKDGKLTDYINANYVDGYN-------RPK-AYIAAQGPLKSTAEDFWRMIWEHNV 1828
Cdd:cd14605      1 ENKNKNRYKNILPFDHTRVVLHD-GDPNEPVSDYINANIIMPEFetkcnnsKPKkSYIATQGCLQNTVNDFWRMVFQENS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1829 EVIVMITNLVEKGRRKCDQYWPVDGS-EEYGNFLVTQKSIQVLAYYTVRNFTLrnTKIKKGSQKgrpsgRVVTQYHYTQW 1907
Cdd:cd14605     80 RVIVMTTKEVERGKSKCVKYWPDEYAlKEYGVMRVRNVKESAAHDYILRELKL--SKVGQGNTE-----RTVWQYHFRTW 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1908 PDMGVPEYSLPVLTFVRKASHaKRHAV---GPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGT---VNVFGFLKHIRSQRN 1981
Cdd:cd14605    153 PDHGVPSDPGGVLDFLEEVHH-KQESImdaGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRS 231

                          250
                   ....*....|....*.
gi 1387264124 1982 YLVQTEEQYVFIHDAL 1997
Cdd:cd14605    232 GMVQTEAQYRFIYMAV 247
alpha_CA_VI_IX_XII_XIV cd03123
Carbonic anhydrase alpha, isozymes VI, IX, XII and XIV. Carbonic anhydrases (CAs) are ...
 46-300 9.03e-59

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: 203.69  E-value: 9.03e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124   46 QKNWGKKYPTCNSPKQSPINIDEDLTQVNVNLKKLKFQDWDKTSLENTFIHNTGKTVEINLTNDYRLSGGVSeTVFKASK 125
Cdd:cd03123      2 EDHWPKKYPACGGKRQSPIDIQTDIVQFDPSLPPLELVGYDLPGTEEFTLTNNGHTVQLSLPPTMHIRGGPG-TEYTAAQ 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124  126 IAFHWGKCNMSSdGSEHSLEGQKFPLEMQIYCFDADRFSSFEEAIKGKGKLRALSILFEVGIEENLDYKAIIDGVERVSR 205
Cdd:cd03123     81 LHLHWGGRGSLS-GSEHTIDGIRFAAELHIVHYNSDKYSSFDEAADKPDGLAVLAILIEVGYPENTYYEKIISHLHEIKY 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124  206 FGKQAALDPFTLLNLLPNSTDKYYTYNGSLTSPPCTDTVDWIIFKDTVSISESQLavfcevLTMQQSgyvmLMDY----L 281
Cdd:cd03123    160 KGQETTVPGFNVRELLPEDLSHYYRYEGSLTTPPCYESVLWTVFRDPVTLSKEQL------ETLENT----LMDThnktL 229

                          250
                   ....*....|....*....
gi 1387264124  282 QNNFREQQYKFSRQVFSSY 300
Cdd:cd03123    230 QNNYRATQPLNGRVVEASF 248
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 1727-2001 1.86e-58

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: 204.13  E-value: 1.86e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1727 EEFETLKEFYQEVQSCTVDLgitadssnHPDNKHKNRYINIVAYDHSRVKLAqlAEKDGKLTDYINANYV-DGYNRPKAY 1805
Cdd:cd14610     21 KEWEALCAYQAEPNATNVAQ--------REENVQKNRSLAVLPYDHSRIILK--AENSHSHSDYINASPImDHDPRNPAY 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1806 IAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPVDGSEEYGNFLVTQKSIQVLAY-YTVRNFTLRNTK 1884
Cdd:cd14610     91 IATQGPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEGSNLYHIYEVNLVSEHIWCEdFLVRSFYLKNLQ 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1885 IKKgsqkgrpsGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQI-QH 1963
Cdd:cd14610    171 TNE--------TRTVTQFHFLSWNDQGVPASTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLNKMaKG 242

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1387264124 1964 EGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDALVEAI 2001
Cdd:cd14610    243 AKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAEEV 280
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 1748-1997 2.23e-58

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: 202.37  E-value: 2.23e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1748 ITADSSNHPDNKHKNRYINIVAYDHSRVKLAQLAEKDgKLTDYINANYVDGYN-RPKAYIAAQGPLKSTAEDFWRMIWEH 1826
Cdd:cd14612      5 VSPEELDIPGHASKDRYKTILPNPQSRVCLRRAGSQE-EEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQE 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1827 NVEVIVMITNLVEKgRRKCDQYWPvDGSEEYGNFLVTQKSIQVLAYYTVRNFTlrntkIKKGSQKgrpsgRVVTQYHYTQ 1906
Cdd:cd14612     84 ECPIIVMITKLKEK-KEKCVHYWP-EKEGTYGRFEIRVQDMKECDGYTIRDLT-----IQLEEES-----RSVKHYWFSS 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1907 WPDMGVPEYSLPVLTFVRKASHAKRHAV--GPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLV 1984
Cdd:cd14612    152 WPDHQTPESAGPLLRLVAEVEESRQTAAspGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMI 231

                          250
                   ....*....|...
gi 1387264124 1985 QTEEQYVFIHDAL 1997
Cdd:cd14612    232 QTSEQYQFLHHTL 244
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 1763-1999 5.61e-58

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: 200.66  E-value: 5.61e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1763 RYINIVAYDHSRVKLAqlAEKDGKLTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGR 1842
Cdd:cd14623      1 RVLQIIPYEFNRVIIP--VKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1843 RKCDQYWPVDGSEEYGNFLVTQKSIQVLAYYTVRNFTLRNTKIKKgsqkgrpsGRVVTQYHYTQWPDMGVPEYSLPVLTF 1922
Cdd:cd14623     79 EKCAQYWPSDGSVSYGDITIELKKEEECESYTVRDLLVTNTRENK--------SRQIRQFHFHGWPEVGIPSDGKGMINI 150

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387264124 1923 VRKASHAKRHAVG-PVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDALVE 1999
Cdd:cd14623    151 IAAVQKQQQQSGNhPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 1761-1999 1.90e-57

catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein phosphatase non-receptor type 22 (PTPN22), also called lymphoid phosphatase (LyP), PEST-domain phosphatase (PEP), or hematopoietic cell protein-tyrosine phosphatase 70Z-PEP, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN22 is expressed in hematopoietic cells and it functions as a key regulator of immune homeostasis by inhibiting T-cell receptor signaling through the direct dephosphorylation of Src family kinases (Lck and Fyn), ITAMs of the TCRz/CD3 complex, and other signaling molecules. Mutations in the PTPN22 gene are associated with multiple connective tissue and autoimmune diseases including type 1 diabetes mellitus, rheumatoid arthritis, and systemic lupus erythematosus. PTPN22 contains an N-terminal catalytic PTP domain and four proline-rich regions at the C-terminus.


Pssm-ID: 350450 [Multi-domain]  Cd Length: 234  Bit Score: 199.30  E-value: 1.90e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1761 KNRYINIVAYDHSRVKLAQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEK 1840
Cdd:cd14602      1 KNRYKDILPYDHSRVELSLITSDED--SDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEM 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1841 GRRKCDQYWPVDGSE--EYGNFLVTQKSIQVLAYYTVRnfTLrntKIKKGSQKgrpsgRVVTQYHYTQWPDMGVPEYSLP 1918
Cdd:cd14602     79 GKKKCERYWAEPGEMqlEFGPFSVTCEAEKRKSDYIIR--TL---KVKFNSET-----RTIYQFHYKNWPDHDVPSSIDP 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1919 VLTFVRKASHAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQhEGTV----NVFGFLKHIRSQRNYLVQTEEQYVFIH 1994
Cdd:cd14602    149 ILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLK-DGIIpenfSVFSLIQEMRTQRPSLVQTKEQYELVY 227


                   ....*
gi 1387264124 1995 DALVE 1999
Cdd:cd14602    228 NAVIE 232
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 1790-2001 1.07e-56

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: 196.13  E-value: 1.07e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1790 YINANYVDGYN-RPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPVDGSEEYGNFLVTQKSIQ 1868
Cdd:cd14546      1 YINASTIYDHDpRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEVYHIYEVHLVSEH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1869 VL-AYYTVRNFTLRNTKIKKgsqkgrpsGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAKRHAVGPVVVHCSAGVGR 1947
Cdd:cd14546     81 IWcDDYLVRSFYLKNLQTSE--------TRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYRGRSCPIVVHCSDGAGR 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1387264124 1948 TGTYIVLDSMLQQIQhEGT--VNVFGFLKHIRSQRNYLVQTEEQYVFIHDALVEAI 2001
Cdd:cd14546    153 TGTYILIDMVLNRMA-KGAkeIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAEEV 207
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 1756-2002 1.49e-56

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: 198.15  E-value: 1.49e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1756 PDNKHKNRYINIVAYDHSRVKLaqlaekDGKlTDYINANYVD----GYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVI 1831
Cdd:cd14600     38 PQNMDKNRYKDVLPYDATRVVL------QGN-EDYINASYVNmeipSANIVNKYIATQGPLPHTCAQFWQVVWEQKLSLI 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1832 VMITNLVEKGRRKCDQYWPvDGSE--EYGNFLVTQKSIQVLAYYTVRNFTLrnTKIKKGSQkgrpsgRVVTQYHYTQWPD 1909
Cdd:cd14600    111 VMLTTLTERGRTKCHQYWP-DPPDvmEYGGFRVQCHSEDCTIAYVFREMLL--TNTQTGEE------RTVTHLQYVAWPD 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1910 MGVPEYSLPVLTFVrKASHAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQ 1989
Cdd:cd14600    182 HGVPDDSSDFLEFV-NYVRSKRVENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQ 260

                          250
                   ....*....|...
gi 1387264124 1990 YVFIhdalVEAIL 2002
Cdd:cd14600    261 YKFV----CEAIL 269
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1790-1999 1.61e-56

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


Pssm-ID: 350388 [Multi-domain]  Cd Length: 219  Bit Score: 196.14  E-value: 1.61e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1790 YINANYVDGY--NRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPVDGSEE----YGNFLVT 1863
Cdd:cd14540      1 YINASHITATvgGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGGEHdaltFGEYKVS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1864 QKSIQVLAYYTVRNFTLRNTkikkgsqkgrPSGRVVTQYH--YTQWPDMGVPEYSLPVLTFVRKASHAKRHAVG------ 1935
Cdd:cd14540     81 TKFSVSSGCYTTTGLRVKHT----------LSGQSRTVWHlqYTDWPDHGCPEDVSGFLDFLEEINSVRRHTNQdvaghn 150

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387264124 1936 ---PVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDALVE 1999
Cdd:cd14540    151 rnpPTLVHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQ 217
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 1761-1994 4.74e-56

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: 195.14  E-value: 4.74e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1761 KNRYINIVAYDHSRVKLAQLAEKDgKLTDYINANYVDGY-NRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVE 1839
Cdd:cd14611      2 KNRYKTILPNPHSRVCLKPKNSND-SLSTYINANYIRGYgGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1840 KGRrKCDQYWPvDGSEEYGNFLVTQKSIQVLAYYTVRNFTLrntkiKKGSQKgrpsgRVVTQYHYTQWPDMGVPEYSLPV 1919
Cdd:cd14611     81 KNE-KCVLYWP-EKRGIYGKVEVLVNSVKECDNYTIRNLTL-----KQGSQS-----RSVKHYWYTSWPDHKTPDSAQPL 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1920 LTFV------RKASHAKrhavGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFI 1993
Cdd:cd14611    149 LQLMldveedRLASPGR----GPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFV 224


                   .
gi 1387264124 1994 H 1994
Cdd:cd14611    225 H 225
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 2085-2298 2.75e-55

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: 191.73  E-value: 2.75e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2085 YINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPD----GQNMVSPsghfwhflfraedefvYWPNK- 2159
Cdd:cd00047      1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNlvekGREKCER----------------YWPEEg 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2160 DEPINCESFKVTLMAEEHKclsneEKLIMQDFILEATQDDYVLEVRHFQCPKWPN---PDSPISkTFELISIIKEEAATR 2236
Cdd:cd00047     65 GKPLEYGDITVTLVSEEEL-----SDYTIRTLELSPKGCSESREVTHLHYTGWPDhgvPSSPED-LLALVRRVRKEARKP 138

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387264124 2237 DGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYK 2298
Cdd:cd00047    139 NGPIVVHCSAGVGRTGTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 1761-1997 2.94e-55

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: 193.93  E-value: 2.94e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1761 KNRYINIVAYDHSRVKLAQlAEKDGKLTDYINANYVDGYN-RPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVE 1839
Cdd:cd14613     28 KNRYKTILPNPHSRVCLTS-PDQDDPLSSYINANYIRGYGgEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEE 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1840 KGRrKCDQYWPVDgSEEYGNFLVTQKSIQVLAYYTVRNFTLrntkiKKGSQKgrpsgRVVTQYHYTQWPDMGVPEYSLPV 1919
Cdd:cd14613    107 MNE-KCTEYWPEE-QVTYEGIEITVKQVIHADDYRLRLITL-----KSGGEE-----RGLKHYWYTSWPDQKTPDNAPPL 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1920 LTFVRKASHAKRHA---VGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDA 1996
Cdd:cd14613    175 LQLVQEVEEARQQAepnCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVHHV 254


                   .
gi 1387264124 1997 L 1997
Cdd:cd14613    255 L 255
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 1789-1994 3.00e-54

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: 189.06  E-value: 3.00e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1789 DYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPVDGSEEYGNFLVTQKSIQ 1868
Cdd:cd14622      1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEGSVTHGEITIEIKNDT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1869 VLAYYTVRNFTLRNTKIKKgsqkgrpsGRVVTQYHYTQWPDMGVPEYSLPVLTFVrKASHAKRHAVG--PVVVHCSAGVG 1946
Cdd:cd14622     81 LLETISIRDFLVTYNQEKQ--------TRLVRQFHFHGWPEIGIPAEGKGMIDLI-AAVQKQQQQTGnhPIVVHCSAGAG 151

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1387264124 1947 RTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIH 1994
Cdd:cd14622    152 RTGTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCY 199
PHA02738 PHA02738
hypothetical protein; Provisional
 1730-2008 6.22e-54

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 192.45  E-value: 6.22e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1730 ETLKEFYQEVQSCTVDLGITADSSNhpdnKHKNRYINIVAYDHSRVKLAqlAEKDgkLTDYINANYVDGYNRPKAYIAAQ 1809
Cdd:PHA02738    25 EVITREHQKVISEKVDGTFNAEKKN----RKLNRYLDAVCFDHSRVILP--AERN--RGDYINANYVDGFEYKKKFICGQ 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1810 GPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWP-VDGSE-EYGNFLVTQKSIQVLAYYTVRNFTLRNtkikk 1887
Cdd:PHA02738    97 APTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSdVEQGSiRFGKFKITTTQVETHPHYVKSTLLLTD----- 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1888 gsqkGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFV------RKASHAKRHAVG-------PVVVHCSAGVGRTGTYIVL 1954
Cdd:PHA02738   172 ----GTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVlevrqcQKELAQESLQIGhnrlqppPIVVHCNAGLGRTPCYCVV 247

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1387264124 1955 DSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDALVEAILSKETEV 2008
Cdd:PHA02738   248 DISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAVKRYVNLTVNKV 301
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 1736-1999 3.85e-53

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: 188.70  E-value: 3.85e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1736 YQEVQSCTVDLgiTADSSNHPDNKHKNRYINIVAYDHSRVKLAQlaekdgKLTDYINANYVDGYNRPKAYIAAQGPLKST 1815
Cdd:cd14608      5 YQDIRHEASDF--PCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQ------EDNDYINASLIKMEEAQRSYILTQGPLPNT 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1816 AEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPVDGSEEY----GNFLVTQKSIQVLAYYTVRNFTLRNTKIKKgsqk 1891
Cdd:cd14608     77 CGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMifedTNLKLTLISEDIKSYYTVRQLELENLTTQE---- 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1892 grpsGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKA--SHAKRHAVGPVVVHCSAGVGRTGTYIVLDS---MLQQIQHEGT 1966
Cdd:cd14608    153 ----TREILHFHYTTWPDFGVPESPASFLNFLFKVreSGSLSPEHGPVVVHCSAGIGRSGTFCLADTcllLMDKRKDPSS 228

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1387264124 1967 VNVFGFLKHIRSQRNYLVQTEEQYVFIHDALVE 1999
Cdd:cd14608    229 VDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIE 261
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 1757-1992 7.75e-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: 186.19  E-value: 7.75e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1757 DNKHKNRYINIVAYDHSRVKLAQlaekDGkltDYINANYVD---GyNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVM 1833
Cdd:cd14597      2 ENRKKNRYKNILPYDTTRVPLGD----EG---GYINASFIKmpvG-DEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAM 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1834 ITNLVEKGRRKCDQYWPvdgsEEYGNFLVTQKSIQV--LAYYTVRNFTLRNTKIKKgSQKGRPsgRVVTQYHYTQWPDMG 1911
Cdd:cd14597     74 MTQEVEGGKIKCQRYWP----EILGKTTMVDNRLQLtlVRMQQLKNFVIRVLELED-IQTREV--RHITHLNFTAWPDHD 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1912 VPEYSLPVLTFVRKASHAkrHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYV 1991
Cdd:cd14597    147 TPSQPEQLLTFISYMRHI--HKSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYI 224


                   .
gi 1387264124 1992 F 1992
Cdd:cd14597    225 F 225
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 1736-1997 1.17e-51

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: 183.63  E-value: 1.17e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1736 YQEVQSCTVDLGITAdsSNHPDNKHKNRYINIVAYDHSRVKLaQLAEkdgklTDYINANYVDGYNRPKAYIAAQGPLKST 1815
Cdd:cd14607      4 YLEIRNESHDYPHRV--AKYPENRNRNRYRDVSPYDHSRVKL-QNTE-----NDYINASLVVIEEAQRSYILTQGPLPNT 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1816 AEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPVDGSEEYG----NFLVTQKSIQVLAYYTVRNFTLRNtkIKKGSQk 1891
Cdd:cd14607     76 CCHFWLMVWQQKTKAVVMLNRIVEKDSVKCAQYWPTDEEEVLSfketGFSVKLLSEDVKSYYTVHLLQLEN--INSGET- 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1892 grpsgRVVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAKRHAV--GPVVVHCSAGVGRTGTYIVLDS--MLQQIQHEGTV 1967
Cdd:cd14607    153 -----RTISHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSPehGPAVVHCSAGIGRSGTFSLVDTclVLMEKKDPDSV 227

                          250       260       270
                   ....*....|....*....|....*....|
gi 1387264124 1968 NVFGFLKHIRSQRNYLVQTEEQYVFIHDAL 1997
Cdd:cd14607    228 DIKQVLLDMRKYRMGLIQTPDQLRFSYMAV 257
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 1790-1995 2.56e-51

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: 180.28  E-value: 2.56e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1790 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPvDGSEEYGNFLVTQKSIQV 1869
Cdd:cd14558      1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWG-DEKKTYGDIEVELKDTEK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1870 LAYYTVRNFTLRNTKIKKgsqkgrpsGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKASH------AKRHAVGPVVVHCSA 1943
Cdd:cd14558     80 SPTYTVRVFEITHLKRKD--------SRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQklpyknSKHGRSVPIVVHCSD 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1387264124 1944 GVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHD 1995
Cdd:cd14558    152 GSSRTGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203
alpha_CA_IV_XV_like cd03117
Carbonic anhydrase alpha, CA_IV, CA_XV, like isozymes. Carbonic anhydrases (CAs) are ...
 59-298 1.46e-50

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: 179.39  E-value: 1.46e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124   59 PKQSPINIDEDLTQVNVNLKKLKFQDWDKTSLeNTFIHNTGKTVEINLTNDYRLSGGVSETVFKASKIAFHWGkcNMSSD 138
Cdd:cd03117      2 KRQSPINIVTKKVQYDENLTPFTFTGYDDTTT-NWTITNNGHTVQVTLPDGAKISGGGLPGTYKALQFHFHWG--SNGSP 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124  139 GSEHSLEGQKFPLEMQIYCFDADrFSSFEEAIKGKGKLRALSILFEVGIEENLDYKAIIDGVERVSRFGKQAALDPFTLL 218
Cdd:cd03117     79 GSEHTIDGERYPMELHIVHIKES-YNSLLEALKDSDGLAVLGFFIEEGEEENTNFDPLISALSNIPQKGGSTNLTPFSLR 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124  219 NLLP-NSTDKYYTYNGSLTSPPCTDTVDWIIFKDTVSISESQLAVFCEVLTMQQSGYVMLMdylqNNFREQQYKFSRQVF 297
Cdd:cd03117    158 SLLPsVLLTKYYRYNGSLTTPGCNEAVIWTVFEEPIPISRAQLDAFSTVLFFDTDNGQPMV----NNFRPVQPLNGRVVY 233


                   .
gi 1387264124  298 S 298
Cdd:cd03117    234 A 234
alpha_CA_XII_XIV cd03126
Carbonic anhydrase alpha, isozymes XII and XIV. Carbonic anhydrases (CAs) are zinc-containing ...
 46-300 2.13e-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: 179.65  E-value: 2.13e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124   46 QKNWGKKYPTCNSPKQSPINIDEDLTQVNVNLKKLKFQDWDKTSLENTFIHNTGKTVEINLTNDYRLSGGVSEtvFKASK 125
Cdd:cd03126      2 ENSWPKKYPFCGGVAQSPIDIHTDILQYDSSLPPLEFHGYNVSGTEQFTLTNNGHTVQLSLPPTMHIGGLPFK--YTASQ 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124  126 IAFHWGKCNmSSDGSEHSLEGQKFPLEMQIYCFDADRFSSFEEAIKGKGKLRALSILFEVGiEENLDYKAIIDGVERVSR 205
Cdd:cd03126     80 LHLHWGQRG-SPEGSEHTISGKHFAAELHIVHYNSDKYPDISTAMNKSQGLAVLGILIEVG-PFNPSYEKIFSHLHEVKY 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124  206 FGKQAALDPFTLLNLLPNSTDKYYTYNGSLTSPPCTDTVDWIIFKDTVSISESQLavfcevLTMQQSGYVMLMD---YLQ 282
Cdd:cd03126    158 KDQKVSVPGFNVQELLPKRLDEYYRYEGSLTTPPCYPSVLWTVFRNPVQISQEQL------LALETALYSTEEDesrEMV 231

                          250
                   ....*....|....*...
gi 1387264124  283 NNFREQQYKFSRQVFSSY 300
Cdd:cd03126    232 NNYRQVQPFNERLVFASF 249
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 1790-2001 2.75e-50

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: 177.63  E-value: 2.75e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1790 YINANYVDGYNRPKA--YIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPVDGSE--EYGNFLVTQK 1865
Cdd:cd14596      1 YINASYITMPVGEEElfYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEpmELENYQLRLE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1866 SIQVLAYYTVRNFTLrntkikkgSQKGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAkrHAVGPVVVHCSAGV 1945
Cdd:cd14596     81 NYQALQYFIIRIIKL--------VEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKV--HNTGPIVVHCSAGI 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1387264124 1946 GRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDALVEAI 2001
Cdd:cd14596    151 GRAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVL 206
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 1789-2002 6.35e-49

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


Pssm-ID: 350449 [Multi-domain]  Cd Length: 212  Bit Score: 173.98  E-value: 6.35e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1789 DYINANYVDG-------YNRpkaYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWP-VDGSEEYGNF 1860
Cdd:cd14601      1 DYINANYINMeipsssiINR---YIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPePSGSSSYGGF 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1861 LVTQKSIQVLAYYTVRNFTLRNTKikkgSQKGRPsgrvVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAKRHAVGPVVVH 1940
Cdd:cd14601     78 QVTCHSEEGNPAYVFREMTLTNLE----KNESRP----LTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDEPVVVH 149

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387264124 1941 CSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIhdalVEAIL 2002
Cdd:cd14601    150 CSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFV----CEAIL 207
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 1756-1999 9.23e-49

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: 176.34  E-value: 9.23e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1756 PDNKHKNRYINIVAYDHSRVKLAQLAEKDgklTDYINANYVDGYNRPKA--YIAAQGPLKSTAEDFWRMIWEHNVEVIVM 1833
Cdd:cd14599     36 PENAERNRIREVVPYEENRVELVPTKENN---TGYINASHIKVTVGGEEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAM 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1834 ITNLVEKGRRKCDQYWPVDG----SEEYGNFLVTQKSIQVLAYYTVRNFTLRNtkIKKGSQkgrpsgRVVTQYHYTQWPD 1909
Cdd:cd14599    113 VTAEEEGGRSKSHRYWPKLGskhsSATYGKFKVTTKFRTDSGCYATTGLKVKH--LLSGQE------RTVWHLQYTDWPD 184

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1910 MGVPEYSLPVLTFVRKASHAKRHAVG----------PVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQ 1979
Cdd:cd14599    185 HGCPEEVQGFLSYLEEIQSVRRHTNSmldstkncnpPIVVHCSAGVGRTGVVILTELMIGCLEHNEKVEVPVMLRHLREQ 264

                          250       260
                   ....*....|....*....|
gi 1387264124 1980 RNYLVQTEEQYVFIHDALVE 1999
Cdd:cd14599    265 RMFMIQTIAQYKFVYQVLIQ 284
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 2006-2306 1.89e-47

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: 172.61  E-value: 1.89e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2006 TEVPDSHIHAYVNGLL-IPGPTGKTKLEKQFKLLSQSNIQQSDYSTALKQCNREKNRTSSIIPVERSRVGISSLSG-EGA 2083
Cdd:cd14628      1 TEVPARNLYAYIQKLTqIETGENVTGMELEFKRLASSKAHTSRFISANLPCNKFKNRLVNIMPYESTRVCLQPIRGvEGS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2084 DYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDGQNMVSPSGHfwhflfraedefVYWPnKDEPI 2163
Cdd:cd14628     81 DYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCH------------QYWP-AERSA 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2164 NCESFKVTLMAEehkclSNEEKLIMQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKT--FELISII--KEEAATRDGP 2239
Cdd:cd14628    148 RYQYFVVDPMAE-----YNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEgfIDFIGQVhkTKEQFGQDGP 222

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387264124 2240 MIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAVLSLVST 2306
Cdd:cd14628    223 ISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEYLGS 289
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 1749-1994 1.97e-46

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 170.57  E-value: 1.97e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1749 TADSSNHPDNKHKNRYINIVAYDHSRVKLAQlaeKDGKLTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNV 1828
Cdd:PHA02747    42 LIANFEKPENQPKNRYWDIPCWDHNRVILDS---GGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHC 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1829 EVIVMIT-NLVEKGRRKCDQYWPV--DGSEEYGNFLVTQKSIQVLAYYTVRNFTLRNtKIKKGSQKgrpsgrvVTQYHYT 1905
Cdd:PHA02747   119 SIIVMLTpTKGTNGEEKCYQYWCLneDGNIDMEDFRIETLKTSVRAKYILTLIEITD-KILKDSRK-------ISHFQCS 190

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1906 QWPDMGVPEYSLPVLTF------VRKAS----HAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKH 1975
Cdd:PHA02747   191 EWFEDETPSDHPDFIKFikiidiNRKKSgklfNPKDALLCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEK 270

                          250
                   ....*....|....*....
gi 1387264124 1976 IRSQRNYLVQTEEQYVFIH 1994
Cdd:PHA02747   271 IREQRHAGIMNFDDYLFIQ 289
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 1758-1992 1.99e-46

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 170.18  E-value: 1.99e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1758 NKHKNRYINIVAYDHSRVKLAQlaeKDGkLTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNL 1837
Cdd:PHA02742    52 NMKKCRYPDAPCFDRNRVILKI---EDG-GDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKI 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1838 VEKGRRKCDQYWPVD--GSEEYGNFLVTQKSIQVLAYYTVRNFTLRNTKikkgsqkgrpSGRV--VTQYHYTQWPDMGVP 1913
Cdd:PHA02742   128 MEDGKEACYPYWMPHerGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTN----------TGASldIKHFAYEDWPHGGLP 197

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1914 EYSLPVLTFVRKASHAK-----------RHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNY 1982
Cdd:PHA02742   198 RDPNKFLDFVLAVREADlkadvdikgenIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHN 277

                          250
                   ....*....|
gi 1387264124 1983 LVQTEEQYVF 1992
Cdd:PHA02742   278 CLSLPQQYIF 287
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 1790-1995 2.23e-46

PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein phosphatase non-receptor type 23 (PTPN23), also called His domain-containing protein tyrosine phosphatase (HD-PTP) or protein tyrosine phosphatase TD14 (PTP-TD14), is a catalytically inactive member of the tyrosine-specific protein tyrosine phosphatase (PTP) family. Human PTPN23 may be involved in the regulation of small nuclear ribonucleoprotein assembly and pre-mRNA splicing by modifying the survival motor neuron (SMN) complex. It plays a role in ciliogenesis and is part of endosomal sorting complex required for transport (ESCRT) pathways. PTPN23 contains five domains: a BRO1-like domain that plays a role in endosomal sorting; a V-domain that interacts with Lys63-linked polyubiquitinated substrates; a central proline-rich region that might recruit SH3-containing proteins; a PTP-like domain; and a proteolytic degradation-targeting motif, also known as a PEST sequence.


Pssm-ID: 350387 [Multi-domain]  Cd Length: 205  Bit Score: 166.41  E-value: 2.23e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1790 YINANYVDGY-NRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPVD-GSE-EYGNFLVTQKS 1866
Cdd:cd14539      1 YINASLIEDLtPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTErGQAlVYGAITVSLQS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1867 IQVLAYYTVRNFTlrntkIKKGSQKGRpsgRVVTQYHYTQWPDMGVPEYSLPVLTFVRKA-SH--AKRHAVGPVVVHCSA 1943
Cdd:cd14539     81 VRTTPTHVERIIS-----IQHKDTRLS---RSVVHLQFTTWPELGLPDSPNPLLRFIEEVhSHylQQRSLQTPIVVHCSS 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1387264124 1944 GVGRTGTYIVLDSMLQQIQHE-GTVNVFGFLKHIRSQRNYLVQTEEQYVFIHD 1995
Cdd:cd14539    153 GVGRTGAFCLLYAAVQEIEAGnGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 2006-2306 7.46e-46

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: 167.99  E-value: 7.46e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2006 TEVPDSHIHAYVNGLLIPGPTGK-TKLEKQFKLLSQSNIQQSDYSTALKQCNREKNRTSSIIPVERSRVGISSLSG-EGA 2083
Cdd:cd14627      2 TEVPARNLYSYIQKLAQVEVGEHvTGMELEFKRLANSKAHTSRFISANLPCNKFKNRLVNIMPYETTRVCLQPIRGvEGS 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2084 DYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDGQNMVSPSGHfwhflfraedefVYWPnKDEPI 2163
Cdd:cd14627     82 DYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGREKCH------------QYWP-AERSA 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2164 NCESFKVTLMAEehkclSNEEKLIMQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKT--FELISII--KEEAATRDGP 2239
Cdd:cd14627    149 RYQYFVVDPMAE-----YNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEgfIDFIGQVhkTKEQFGQDGP 223

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387264124 2240 MIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAVLSLVST 2306
Cdd:cd14627    224 ISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALEYLGS 290
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 2006-2306 7.93e-46

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: 167.98  E-value: 7.93e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2006 TEVPDSHIHAYVNGL-LIPGPTGKTKLEKQFKLLSQSNIQQSDYSTALKQCNREKNRTSSIIPVERSRVGISSLSG-EGA 2083
Cdd:cd14629      2 TEVPARNLYAHIQKLtQVPPGESVTAMELEFKLLANSKAHTSRFISANLPCNKFKNRLVNIMPYELTRVCLQPIRGvEGS 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2084 DYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDGQNMVSPSGHfwhflfraedefVYWPnKDEPI 2163
Cdd:cd14629     82 DYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCH------------QYWP-AERSA 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2164 NCESFKVTLMAEehkclSNEEKLIMQDFILEATQDDYVLEVRHFQCPKWPNPDSPisKTFE-LISIIKEEAATR-----D 2237
Cdd:cd14629    149 RYQYFVVDPMAE-----YNMPQYILREFKVTDARDGQSRTIRQFQFTDWPEQGVP--KTGEgFIDFIGQVHKTKeqfgqD 221

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387264124 2238 GPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAVLSLVST 2306
Cdd:cd14629    222 GPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALEYLGS 290
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 1790-1994 1.20e-45

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


Pssm-ID: 350496 [Multi-domain]  Cd Length: 206  Bit Score: 164.17  E-value: 1.20e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1790 YINANYV---DGYNRPKaYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRR-KCDQYWPVD--GSEEYGNFLVT 1863
Cdd:cd17658      1 YINASLVetpASESLPK-FIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTaKCADYFPAEenESREFGRISVT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1864 QKSIQvlayYTVRNFTLRNTKIKKGSQKGRPsgRVVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAKRHAvGPVVVHCSA 1943
Cdd:cd17658     80 NKKLK----HSQHSITLRVLEVQYIESEEPP--LSVLHIQYPEWPDHGVPKDTRSVRELLKRLYGIPPSA-GPIVVHCSA 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1387264124 1944 GVGRTGTYIVLDSMLQQIQhEG---TVNVFGFLKHIRSQRNYLVQTEEQYVFIH 1994
Cdd:cd17658    153 GIGRTGAYCTIHNTIRRIL-EGdmsAVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 1749-2002 1.92e-45

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 167.90  E-value: 1.92e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1749 TADSSNHPDNKHKNRYINIVAYDHSRV--------KLAQLAEKDGKL---------TDYINANYVDGYNRPKAYIAAQGP 1811
Cdd:PHA02746    42 TTNHFLKKENLKKNRFHDIPCWDHSRVvinaheslKMFDVGDSDGKKievtsednaENYIHANFVDGFKEANKFICAQGP 121

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1812 LKSTAEDFWRMIWEHNVEVIVMITNlVEKGRRKCDQYW--PVDGSEEYGNFLVtqKSIQVLAYYTVRNFTLRNTkikkgs 1889
Cdd:PHA02746   122 KEDTSEDFFKLISEHESQVIVSLTD-IDDDDEKCFELWtkEEDSELAFGRFVA--KILDIIEELSFTKTRLMIT------ 192

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1890 QKGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAKR----------HAVGPVVVHCSAGVGRTGTYIVLDSMLQ 1959
Cdd:PHA02746   193 DKISDTSREIHHFWFPDWPDNGIPTGMAEFLELINKVNEEQAelikqadndpQTLGPIVVHCSAGIGRAGTFCAIDNALE 272

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1387264124 1960 QIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDALVEAIL 2002
Cdd:PHA02746   273 QLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKALKYAII 315
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 1790-1995 2.60e-45

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: 162.96  E-value: 2.60e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1790 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMItNLVEKGRRKCDQYWPVDGSEEYGNFLVTQKSIQV 1869
Cdd:cd14556      1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVML-NQLDPKDQSCPQYWPDEGSGTYGPIQVEFVSTTI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1870 LAYYTVRNFTLRNTKikkgsqkgRPS--GRVVTQYHYTQWPDMG----VPEYSLPVLTFVRKAShaKRHAVGPVVVHCSA 1943
Cdd:cd14556     80 DEDVISRIFRLQNTT--------RPQegYRMVQQFQFLGWPRDRdtppSKRALLKLLSEVEKWQ--EQSGEGPIVVHCLN 149

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1387264124 1944 GVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHD 1995
Cdd:cd14556    150 GVGRSGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 2055-2301 1.08e-44

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


Pssm-ID: 350402 [Multi-domain]  Cd Length: 238  Bit Score: 162.69  E-value: 1.08e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2055 CNREKNRTSSIIPVERSRVGISSLSG-EGADYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDGQ 2133
Cdd:cd14554      5 CNKFKNRLVNILPYESTRVCLQPIRGvEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTKLR 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2134 NMvspsghfwhflfRAEDEFVYWPNkDEPINCESFKVTLMAEehkclSNEEKLIMQDFILEATQDDYVLEVRHFQCPKWP 2213
Cdd:cd14554     85 EM------------GREKCHQYWPA-ERSARYQYFVVDPMAE-----YNMPQYILREFKVTDARDGQSRTVRQFQFTDWP 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2214 NPDSPisKTFE-LISIIKEEAATR-----DGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVF 2287
Cdd:cd14554    147 EQGVP--KSGEgFIDFIGQVHKTKeqfgqEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMV 224

                          250
                   ....*....|....
gi 1387264124 2288 ADIEQYQFLYKAVL 2301
Cdd:cd14554    225 QTEDQYQFCYRAAL 238
alpha_CA_VI cd03125
Carbonic anhydrase alpha, isozyme VI. Carbonic anhydrases (CAs) are zinc-containing enzymes ...
 45-300 6.24e-41

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: 152.25  E-value: 6.24e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124   45 NQKNWGKKYPTCNSPKQSPINIDEDLTQVNVNLKKLKFQDWDKTSLENTFIHNtGKTVEINLTNDYRLSGGVSeTVFKAS 124
Cdd:cd03125      1 DESHWPEKYPACGGKRQSPIDIQRREVRFNPSLLQLELVGYEKEQGEFTMTNN-GHTVQIDLPPTMSITTGDG-TVYTAV 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124  125 KIAFHWGKCNMSSDGSEHSLEGQKFPLEMQIYCFDADrFSSFEEAIKGKGKLRALSILFEVG-IEENLDYKAIIDGVERV 203
Cdd:cd03125     79 QMHFHWGGRDSEISGSEHTIDGMRYVAELHIVHYNSK-YKSYEEAKDKPDGLAVLAFLYKVGhYAENTYYSDFISKLAKI 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124  204 SRFGKQAALDPFTLLNLLPNSTDKYYTYNGSLTSPPCTDTVDWIIFKDTVSISESQlavfceVLTMQQSgyvmLMDY--- 280
Cdd:cd03125    158 KYAGQTTTLTSLDVRDMLPENLHHYYTYQGSLTTPPCTENVLWFVFDDPVTLSKTQ------IVKLENT----LMDHhnk 227

                          250       260
                   ....*....|....*....|.
gi 1387264124  281 -LQNNFREQQYKFSRQVFSSY 300
Cdd:cd03125    228 tIRNDYRRTQPLNHRVVEANF 248
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 2061-2298 3.01e-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: 149.43  E-value: 3.01e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2061 RTSSIIPVERSRVGISSLSG-EGADYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDG--QNMVs 2137
Cdd:cd14548      1 RYTNILPYDHSRVKLIPINEeEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCmeKGRV- 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2138 psghfwhflfRAEDefvYWPNKDEPINCESFKVTLMAEEHkclsnEEKLIMQDFILEatQDDYVLEVRHFQCPKWPN--- 2214
Cdd:cd14548     80 ----------KCDH---YWPFDQDPVYYGDITVTMLSESV-----LPDWTIREFKLE--RGDEVRSVRQFHFTAWPDhgv 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2215 PDSPISktfeLISIIKEEAATRD---GPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIE 2291
Cdd:cd14548    140 PEAPDS----LLRFVRLVRDYIKqekGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEA 215


                   ....*..
gi 1387264124 2292 QYQFLYK 2298
Cdd:cd14548    216 QYIFLHQ 222
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 2085-2297 3.54e-40

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: 148.32  E-value: 3.54e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2085 YINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLpdgqNMVSPSghfwhflfrAEDEFVYWPNKdepin 2164
Cdd:cd14556      1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVML----NQLDPK---------DQSCPQYWPDE----- 62

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2165 cESFKVTLMAEEHKCLSNEEKLIMQDFILEAT---QDDYVLeVRHFQCPKWP-NPDSPISKT--FELISII-KEEAATRD 2237
Cdd:cd14556     63 -GSGTYGPIQVEFVSTTIDEDVISRIFRLQNTtrpQEGYRM-VQQFQFLGWPrDRDTPPSKRalLKLLSEVeKWQEQSGE 140

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2238 GPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLY 2297
Cdd:cd14556    141 GPIVVHCLNGVGRSGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCY 200
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
1733-1993 4.72e-40

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 151.01  E-value: 4.72e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1733 KEFYQEVQSCTVDLGITADSSNHPDN---KHKNRYINIVAYDHSRVklaqlaEKDGKltdYINANYVDGYNrPKAYIAAQ 1809
Cdd:COG5599     14 EKINSRLSTLTNELAPSHNDPQYLQNingSPLNRFRDIQPYKETAL------RANLG---YLNANYIQVIG-NHRYIATQ 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1810 GPLKSTAEDFWRMIWEHNVEVIVMITNLVE--KGRRKCDQYWPVDGseEYGNFLVTQKSIQVlaYYTVRNFTLRNTKIK- 1886
Cdd:COG5599     84 YPLEEQLEDFFQMLFDNNTPVLVVLASDDEisKPKVKMPVYFRQDG--EYGKYEVSSELTES--IQLRDGIEARTYVLTi 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1887 KGS-QKGRPsgrvVTQYHYTQWPDMGVP--EYSLPVLTFVRKASHAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQ- 1962
Cdd:COG5599    160 KGTgQKKIE----IPVLHVKNWPDHGAIsaEALKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINa 235

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1387264124 1963 -HEGTVNVFGFLKHIRSQRNY-LVQTEEQYVFI 1993
Cdd:COG5599    236 lVQITLSVEEIVIDMRTSRNGgMVQTSEQLDVL 268
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 1899-1999 6.65e-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: 144.04  E-value: 6.65e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124  1899 VTQYHYTQWPDMGVPEYSLPVLTFVR--KASHAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHE-GTVNVFGFLKH 1975
Cdd:smart00012    2 VKHYHYTGWPDHGVPESPDSILELLRavKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVKE 81

                            90       100
                    ....*....|....*....|....
gi 1387264124  1976 IRSQRNYLVQTEEQYVFIHDALVE 1999
Cdd:smart00012   82 LRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1899-1999 6.65e-40

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 144.04  E-value: 6.65e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124  1899 VTQYHYTQWPDMGVPEYSLPVLTFVR--KASHAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHE-GTVNVFGFLKH 1975
Cdd:smart00404    2 VKHYHYTGWPDHGVPESPDSILELLRavKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVKE 81

                            90       100
                    ....*....|....*....|....
gi 1387264124  1976 IRSQRNYLVQTEEQYVFIHDALVE 1999
Cdd:smart00404   82 LRSQRPGMVQTEEQYLFLYRALLE 105
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 1790-1999 7.91e-40

catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein phosphatase non-receptor type 21 (PTPN21), also called protein-tyrosine phosphatase D1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN21 is a component of a multivalent scaffold complex nucleated by focal adhesion kinase (FAK) at specific intracellular sites. It promotes cytoskeleton events that induce cell adhesion and migration by modulating Src-FAK signaling. It can also selectively associate with and stimulate Tec family kinases and modulate Stat3 activation. Human PTPN21 may also play a pathologic role in gastrointestinal tract tumorigenesis. PTPN21 contains an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350446 [Multi-domain]  Cd Length: 220  Bit Score: 148.20  E-value: 7.91e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1790 YINANYVDGYNRPKA--YIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPVDGSEE----YGNFLVT 1863
Cdd:cd14598      1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRLGSRHntvtYGRFKIT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1864 QKSIQVLAYYTVRNFTLRNtkIKKGSQkgrpsgRVVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAKRHAVG-------- 1935
Cdd:cd14598     81 TRFRTDSGCYATTGLKIKH--LLTGQE------RTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHTNStidpkspn 152

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1387264124 1936 -PVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDALVE 1999
Cdd:cd14598    153 pPVLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQ 217
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 2085-2300 1.51e-39

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: 146.65  E-value: 1.51e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2085 YINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDGQNmvspsghfwhflfRAEDE-FVYWPNkDEPI 2163
Cdd:cd14552      1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKE-------------RSQNKcAQYWPE-DGSV 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2164 NCESFKVTLMAEEhkclsNEEKLIMQDFILEATQDDYVLEVRHFQCPKWPNPDSPiSKTFELISII----KEEAATRDGP 2239
Cdd:cd14552     67 SSGDITVELKDQT-----DYEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIP-DNGKGMIDLIaavqKQQQQSGNHP 140

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387264124 2240 MIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAV 2300
Cdd:cd14552    141 ITVHCSAGAGRTGTFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 2061-2300 2.18e-39

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


Pssm-ID: 350471 [Multi-domain]  Cd Length: 228  Bit Score: 147.11  E-value: 2.18e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2061 RTSSIIPVERSRVGISSLSGE-GADYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDGQNmvsps 2139
Cdd:cd14623      1 RVLQIIPYEFNRVIIPVKRGEeNTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEE----- 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2140 ghfwhflfRAEDEFV-YWPNkDEPINCESFKVTLMAEEhKClsneEKLIMQDFILEATQDDYVLEVRHFQCPKWPNPDSP 2218
Cdd:cd14623     76 --------RGQEKCAqYWPS-DGSVSYGDITIELKKEE-EC----ESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIP 141

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2219 iSKTFELISII----KEEAATRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQ 2294
Cdd:cd14623    142 -SDGKGMINIIaavqKQQQQSGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYE 220


                   ....*.
gi 1387264124 2295 FLYKAV 2300
Cdd:cd14623    221 FCYKVV 226
alpha_CA_IX cd03150
Carbonic anhydrase alpha, isozyme IX. Carbonic anhydrases (CAs) are zinc-containing enzymes ...
 45-300 5.78e-39

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: 146.64  E-value: 5.78e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124   45 NQKNWGKKYPTCNSPKQSPINIDEDLTQVNVNLKKLKFQDWDKTSLENTFIHNTGKTVEINLTNDYRLSGGVSEtVFKAS 124
Cdd:cd03150      1 GQPPWPSVSPACAGRFQSPVDIRPHLVAFCPALRPLELLGFDLPPSPSLRLLNNGHTVQLSLPSGLRMALGPGQ-EYRAL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124  125 KIAFHWGKCNMSsdGSEHSLEGQKFPLEMQIYCFDAdRFSSFEEAIKGKGKLRALSILFEVGIEENLDYKAIIDGVERVS 204
Cdd:cd03150     80 QLHLHWGAAGRP--GSEHTVDGHRFPAEIHVVHLST-AFANLDEALGRPGGLAVLAAFLAEGLHENSAYEQLLSRLSEIS 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124  205 RFGKQAALDPFTLLNLLPNSTDKYYTYNGSLTSPPCTDTVDWIIFKDTVSISESQLAVFCEVLTMQQSgyvmlmDYLQNN 284
Cdd:cd03150    157 EEESETVVPGLDVSALLPSDLSRYFRYEGSLTTPPCAQGVIWTVFNQTVRLSAKQLHTLSDSLWGPHD------SRLQLN 230

                          250
                   ....*....|....*.
gi 1387264124  285 FREQQYKFSRQVFSSY 300
Cdd:cd03150    231 FRATQPLNGRKIEASF 246
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 2085-2297 8.88e-38

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: 141.76  E-value: 8.88e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2085 YINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPD----GQnmvspsghfwhflfraEDEFVYWPNKD 2160
Cdd:cd14558      1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTElkegDQ----------------EQCAQYWGDEK 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2161 EpiNCESFKVTLMAEEhkclsNEEKLIMQDFILEATQDDYVLEVRHFQCPKWpNPDSPISKTFELISIIKE--------- 2231
Cdd:cd14558     65 K--TYGDIEVELKDTE-----KSPTYTVRVFEITHLKRKDSRTVYQYQYHKW-KGEELPEKPKDLVDMIKSikqklpykn 136

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387264124 2232 EAATRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLY 2297
Cdd:cd14558    137 SKHGRSVPIVVHCSDGSSRTGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 2060-2301 1.03e-37

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: 1.03e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2060 NRTSSIIPVERSRVGISSLSGE-GADYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDG-QNMVS 2137
Cdd:cd14618      1 NRYPHVLPYDHSRVRLSQLGGEpHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGmENGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2138 PSGHfwhflfraedefvYWPNKDEPINCESFKVTLMAEEhkclsNEEKLIMQDFILEATQDDYVLEVRHFQCPKWPN--- 2214
Cdd:cd14618     81 LCDH-------------YWPSESTPVSYGHITVHLLAQS-----SEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDhgi 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2215 PDSPISkTFELISIIKEEA-ATRD-GPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQ 2292
Cdd:cd14618    143 PESTSS-LMAFRELVREHVqATKGkGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQ 221


                   ....*....
gi 1387264124 2293 YQFLYKAVL 2301
Cdd:cd14618    222 YIFLHSCIL 230
alpha_CA_I_II_III_XIII cd03119
Carbonic anhydrase alpha, isozymes I, II, and III and XIII. Carbonic anhydrases (CAs) are ...
 38-300 3.85e-36

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: 138.73  E-value: 3.85e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124   38 WSYTGALNQKNWGKKYPTCNSPKQSPINIDEDLTQVNVNLKKLKFqDWDKTSLENtfIHNTGKTVEINLTNDYR---LSG 114
Cdd:cd03119      5 WGYDSHNGPEHWHELFPIAKGDRQSPIDIKTKDAKHDPSLKPLSV-SYDPATAKT--ILNNGHSFNVEFDDTDDrsvLRG 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124  115 GVSETVFKASKIAFHWGKCNmsSDGSEHSLEGQKFPLEMQIYCFDAdRFSSFEEAIKGKGKLRALSILFEVGiEENLDYK 194
Cdd:cd03119     82 GPLTGSYRLRQFHFHWGSSD--DHGSEHTVDGVKYAAELHLVHWNS-KYGSFGEAAKQPDGLAVVGVFLKVG-EANPELQ 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124  195 AIIDGVERVSRFGKQAALDPFTLLNLLPNSTDkYYTYNGSLTSPPCTDTVDWIIFKDTVSISESQLAVFCEVLTMQQSGY 274
Cdd:cd03119    158 KVLDALDSIKTKGKQAPFTNFDPSCLLPASLD-YWTYPGSLTTPPLLECVTWIVLKEPISVSSEQMAKFRSLLFNAEGEP 236

                          250       260
                   ....*....|....*....|....*.
gi 1387264124  275 VMLMdylQNNFREQQYKFSRQVFSSY 300
Cdd:cd03119    237 PCPM---VDNWRPPQPLKGRKVRASF 259
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 1790-1993 5.54e-35

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: 133.60  E-value: 5.54e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1790 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGrrKCDQYWPVDGSE-EYGNFLVTQ--KS 1866
Cdd:cd14550      1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNE--DEPIYWPTKEKPlECETFKVTLsgED 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1867 IQVLAY---YTVRNFTLRNTKikkgsqkgrpSGRVVT--QYHYTQWPDMGVPEYSlpVLTFVRKASHAKRHAVGPVVVHC 1941
Cdd:cd14550     79 HSCLSNeirLIVRDFILESTQ----------DDYVLEvrQFQCPSWPNPCSPIHT--VFELINTVQEWAQQRDGPIVVHD 146

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1387264124 1942 SAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFI 1993
Cdd:cd14550    147 RYGGVQAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFL 198
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 2084-2300 5.87e-35

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: 133.59  E-value: 5.87e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2084 DYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDGQNmvspsghfwhflfRAEDE-FVYWPNKDEP 2162
Cdd:cd14622      1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQE-------------REQEKcVQYWPSEGSV 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2163 INCEsfkVTLmaeEHKCLSNEEKLIMQDFILEATQDDYVLEVRHFQCPKWPNPDSPiSKTFELISII----KEEAATRDG 2238
Cdd:cd14622     68 THGE---ITI---EIKNDTLLETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIP-AEGKGMIDLIaavqKQQQQTGNH 140

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387264124 2239 PMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAV 2300
Cdd:cd14622    141 PIVVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 2060-2301 1.03e-34

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: 133.79  E-value: 1.03e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2060 NRTSSIIPVERSRVGISSLSGEGADYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDGQNmvsps 2139
Cdd:cd14615      1 NRYNNVLPYDISRVKLSVQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVE----- 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2140 ghfwhfLFRAEDEfVYWPNKdEPINCESFKVTLMAEehkclSNEEKLIMQDFILEATQDDYVLEVRHFQCPKWpnPDSPI 2219
Cdd:cd14615     76 ------QGRTKCE-EYWPSK-QKKDYGDITVTMTSE-----IVLPEWTIRDFTVKNAQTNESRTVRHFHFTSW--PDHGV 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2220 SKTFELI----SIIKE--EAATRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQY 2293
Cdd:cd14615    141 PETTDLLinfrHLVREymKQNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQY 220


                   ....*...
gi 1387264124 2294 QFLYKAVL 2301
Cdd:cd14615    221 VFLNQCAL 228
alpha_CA_V cd03118
Carbonic anhydrase alpha, CA isozyme V_like subgroup. Carbonic anhydrases (CAs) are ...
 60-300 3.29e-34

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: 132.66  E-value: 3.29e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124   60 KQSPINIDEDLTQVNVNLKKLKFQDWDKTSLentFIHNTGKTVEINL---TNDYRLSGGVSETVFKASKIAFHWGKCNms 136
Cdd:cd03118      3 RQSPINIQWRDSVYDPQLAPLRVSYDPATCL---YIWNNGYSFQVEFddsTDKSGISGGPLENHYRLKQFHFHWGANN-- 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124  137 SDGSEHSLEGQKFPLEMQIYCFDADRFSSFEEAIKGKGKLRALSILFEVGIE-ENLdyKAIIDGVERVSRFGKQAALDPF 215
Cdd:cd03118     78 EWGSEHTVDGHTYPAELHLVHWNSVKYENFEEAVMEENGLAVIGVFLKLGAHhEGL--QKLVDALPEVRHKDTVVEFNPF 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124  216 TLLNLLPNSTDkYYTYNGSLTSPPCTDTVDWIIFKDTVSISESQLAVFCEVLTmqqSGYVMLMDYLQNNFREQQYKFSRQ 295
Cdd:cd03118    156 DPSCLLPACRD-YWTYPGSLTTPPLTESVTWIIQKQPIEVSPSQLSVFRTLLF---TSRGEEEKVMVNNFRPLQPLMNRK 231


                   ....*
gi 1387264124  296 VFSSY 300
Cdd:cd03118    232 VRSSF 236
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 2056-2301 7.55e-34

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: 131.93  E-value: 7.55e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2056 NREKNRTSSIIPVERSRVGISSLSG-EGADYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPD-GQ 2133
Cdd:cd14614     12 NRCKNRYTNILPYDFSRVKLVSMHEeEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQcNE 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2134 NMVSPSGHfwhflfraedefvYWPNKDEPINCESFKVTLMAEEhkclsNEEKLIMQDFILeaTQDDYVLEVRHFQCPKWP 2213
Cdd:cd14614     92 KRRVKCDH-------------YWPFTEEPVAYGDITVEMLSEE-----EQPDWAIREFRV--SYADEVQDVMHFNYTAWP 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2214 NPDSPISKTFE----LISIIKEEAATRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFAD 2289
Cdd:cd14614    152 DHGVPTANAAEsilqFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQT 231

                          250
                   ....*....|..
gi 1387264124 2290 IEQYQFLYKAVL 2301
Cdd:cd14614    232 EEQYIFIHQCVQ 243
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 2054-2305 1.47e-33

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: 130.59  E-value: 1.47e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2054 QCNREKNRTSSIIPVERSRVGISSLSG-EGADYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDG 2132
Cdd:cd14553      1 EVNKPKNRYANVIAYDHSRVILQPIEGvPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2133 QNmvspsghfwhflfRAE---DEfvYWPNKDEPiNCESFKVTLMAEEHkcLSNeekLIMQDFILEATQDDYVLEVRHFQC 2209
Cdd:cd14553     81 EE-------------RSRvkcDQ--YWPTRGTE-TYGLIQVTLLDTVE--LAT---YTVRTFALHKNGSSEKREVRQFQF 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2210 PKWPN---PDSPISkTFELISIIKEEAATRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGV 2286
Cdd:cd14553    140 TAWPDhgvPEHPTP-FLAFLRRVKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYM 218

                          250
                   ....*....|....*....
gi 1387264124 2287 FADIEQYQFLYKAVLSLVS 2305
Cdd:cd14553    219 VQTEDQYIFIHDALLEAVT 237
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 2060-2304 1.31e-32

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: 127.70  E-value: 1.31e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2060 NRTSSIIPVERSRVGISSLSGE-GADYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDgqnmVSP 2138
Cdd:cd14619      1 NRFRNVLPYDWSRVPLKPIHEEpGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTN----CME 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2139 SGhfwhflfRAEDEFvYWPNKDEPINCESFKVTLMAEEhkclsNEEKLIMQDFILEATQDDYVLEVRHFQCPKWPNPDSP 2218
Cdd:cd14619     77 AG-------RVKCEH-YWPLDYTPCTYGHLRVTVVSEE-----VMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVP 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2219 iSKTFELIS---IIKE--EAATRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQY 2293
Cdd:cd14619    144 -SSTDTLLAfrrLLRQwlDQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQY 222

                          250
                   ....*....|.
gi 1387264124 2294 QFLYKAVLSLV 2304
Cdd:cd14619    223 VFLHQCILDFL 233
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 2045-2300 4.37e-32

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: 127.25  E-value: 4.37e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2045 QSDYSTAL----KQCNREKNRTSSIIPVERSRVGISSLSGEG-ADYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIW 2119
Cdd:cd14603     15 KADYVCSTvaggRKENVKKNRYKDILPYDQTRVILSLLQEEGhSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIW 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2120 DHNAQLVVMlpdgqnmvsPSGHFWHFLFRAEdefVYWPNKDEPINCESFKVTLMAEEHkclSNEEKLIMQdfiLEATQDD 2199
Cdd:cd14603     95 QYGVKVILM---------ACREIEMGKKKCE---RYWAQEQEPLQTGPFTITLVKEKR---LNEEVILRT---LKVTFQK 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2200 YVLEVRHFQCPKWPN---PDSPiSKTFELISIIKEEAATRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVA 2276
Cdd:cd14603    157 ESRSVSHFQYMAWPDhgiPDSP-DCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPDFSIF 235

                          250       260
                   ....*....|....*....|....*..
gi 1387264124 2277 KMINLM---RPGVFADIEQYQFLYKAV 2300
Cdd:cd14603    236 DVVLEMrkqRPAAVQTEEQYEFLYHTV 262
alpha_CA_prokaryotic_like cd03124
Carbonic anhydrase alpha, prokaryotic-like subfamily. Carbonic anhydrases (CAs) are ...
 45-263 4.63e-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: 125.46  E-value: 4.63e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124   45 NQKNWG---KKYPTCNS-PKQSPINIDEDLTQVNVnLKKLKFQdWDKTSLEntfIHNTGKTVEINLTNDyrlsGGVSE-- 118
Cdd:cd03124      1 GPEHWGnldPEFALCATgKNQSPIDITTKAVVSDK-LPPLNYN-YKPTSAT---LVNNGHTIQVNFEGN----GGTLTid 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124  119 -TVFKASKIAFHwgkcnmssDGSEHSLEGQKFPLEMQIycfdadrfsSFEEAikgKGKLRALSILFEVGiEENLDYKAII 197
Cdd:cd03124     72 gETYQLLQFHFH--------SPSEHLINGKRYPLEAHL---------VHKSK---DGQLAVVAVLFEEG-KENPFLKKIL 130

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387264124  198 DGVErvSRFGKQAALDPFTLLN-LLPNSTDkYYTYNGSLTSPPCTDTVDWIIFKDTVSISESQLAVF 263
Cdd:cd03124    131 DNMP--KKEGTEVNLPAILDPNeLLPESRS-YYRYEGSLTTPPCSEGVRWIVLKQPITISKEQLAKF 194
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 2044-2301 5.81e-32

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: 127.47  E-value: 5.81e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2044 QQSDYSTALKQCNREKNRTSSIIPVERSRVGISSLSGE-GADYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHN 2122
Cdd:cd14633     28 QSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGEtSSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHEN 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2123 AQLVVMLpdgQNMVSpsghfwhfLFRAEDeFVYWPNKDEPIncESFKVTLMaeEHKCLSneeKLIMQDFILEATQDDYVL 2202
Cdd:cd14633    108 TASIIMV---TNLVE--------VGRVKC-CKYWPDDTEIY--KDIKVTLI--ETELLA---EYVIRTFAVEKRGVHEIR 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2203 EVRHFQCPKWPNPDSPISKT--FELISIIKEEAATRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMIN 2280
Cdd:cd14633    169 EIRQFHFTGWPDHGVPYHATglLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELR 248

                          250       260
                   ....*....|....*....|.
gi 1387264124 2281 LMRPGVFADIEQYQFLYKAVL 2301
Cdd:cd14633    249 SRRVNMVQTEEQYVFIHDAIL 269
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 2051-2298 1.02e-31

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: 126.32  E-value: 1.02e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2051 ALKQCNREKNRTSSIIPVERSRVGISSLSG-EGADYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVML 2129
Cdd:cd14543     24 SLAPANQEKNRYGDVLCLDQSRVKLPKRNGdERTDYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKVLVIVMT 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2130 PD---------GQnmvspsghfwhflfraedefvYWPNKDEpiNCESF-KVTLmaeEHKCLSNEEKLIMQDFILEATQDD 2199
Cdd:cd14543    104 TRvvergrvkcGQ---------------------YWPLEEG--SSLRYgDLTV---TNLSVENKEHYKKTTLEIHNTETD 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2200 YVLEVRHFQCPKWPN---PDSPISKTFELISIIKEEAA------------TRDGPMIVHDEHGGVTAGTFCALTTLMHQL 2264
Cdd:cd14543    158 ESRQVTHFQFTSWPDfgvPSSAAALLDFLGEVRQQQALavkamgdrwkghPPGPPIVVHCSAGIGRTGTFCTLDICLSQL 237

                          250       260       270
                   ....*....|....*....|....*....|....
gi 1387264124 2265 EKENSMDVYQVAKMINLMRPGVFADIEQYQFLYK 2298
Cdd:cd14543    238 EDVGTLNVMQTVRRMRTQRAFSIQTPDQYYFCYK 271
Cah COG3338
Carbonic anhydrase [Inorganic ion transport and metabolism];
38-263 1.22e-31

Carbonic anhydrase [Inorganic ion transport and metabolism];


Pssm-ID: 442567 [Multi-domain]  Cd Length: 247  Bit Score: 125.38  E-value: 1.22e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124   38 WSYTGALNQKNWGK---KYPTCNS-PKQSPINIDedlTQVNVNLKKLKFqDWDKTSLEntfIHNTGKTVEINLTNDYRLS 113
Cdd:COG3338     28 WSYEGETGPEHWGElspEFATCATgKNQSPIDIR---TAIKADLPPLKF-DYKPTPLE---IVNNGHTIQVNVDPGSTLT 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124  114 ggVSETVFKASKIAFHwgkcnmssDGSEHSLEGQKFPLEMQiycF---DADrfssfeeaikgkGKLRALSILFEVGiEEN 190
Cdd:COG3338    101 --VDGKRYELKQFHFH--------TPSEHTINGKSYPMEAH---LvhkDAD------------GELAVVGVLFEEG-AEN 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387264124  191 LDYKAIIDGV--ERvsrfGKQAALD-PFTLLNLLPNSTDkYYTYNGSLTSPPCTDTVDWIIFKDTVSISESQLAVF 263
Cdd:COG3338    155 PALAKLWANLplEA----GEEVALDaTIDLNDLLPEDRS-YYRYSGSLTTPPCSEGVLWIVLKQPITVSAEQIEAF 225
alpha_CA_VII cd03149
Carbonic anhydrase alpha, CA isozyme VII_like subgroup. Carbonic anhydrases (CAs) are ...
 60-300 1.83e-30

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: 121.87  E-value: 1.83e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124   60 KQSPINIDEDLTQVNVNLKKLKFQDWDKTSLEntfIHNTGKTVEINLtNDYR----LSGGVSETVFKASKIAFHWGKcnM 135
Cdd:cd03149      3 RQSPIDIVSSEAVYDPKLKPLSLSYDPCTSLS---ISNNGHSVMVEF-DDSDdktvITGGPLENPYRLKQFHFHWGA--K 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124  136 SSDGSEHSLEGQKFPLEMQIYCFDADRFSSFEEAIKGKGKLRALSILFEVGiEENLDYKAIIDGVERVSRFGKQAALDPF 215
Cdd:cd03149     77 HGSGSEHTVDGKTFPSELHLVHWNAKKYKSFGEAAAAPDGLAVLGVFLETG-DEHPGLNRLTDALYMVRFKGTKAQFLDF 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124  216 TLLNLLPNSTDkYYTYNGSLTSPPCTDTVDWIIFKDTVSISESQLAVFCEVLTMQQSGYVMLMdylQNNFREQQYKFSRQ 295
Cdd:cd03149    156 NPKCLLPKSLD-YWTYPGSLTTPPLNESVTWIVLKEPIPVSEKQMGKFRELLFTSEEDQRNHM---VNNFRPPQPLKGRT 231


                   ....*
gi 1387264124  296 VFSSY 300
Cdd:cd03149    232 VRASF 236
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 2059-2303 1.94e-30

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: 121.49  E-value: 1.94e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2059 KNRTSSIIPVERSRVGISSL-SGEGADYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMlpdgqnmvs 2137
Cdd:cd14602      1 KNRYKDILPYDHSRVELSLItSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVM--------- 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2138 psghfwhflfrAEDEFV--------YWPN-KDEPINCESFKVTLMAEEHKclsnEEKLIMqdfILEATQDDYVLEVRHFQ 2208
Cdd:cd14602     72 -----------ACMEFEmgkkkcerYWAEpGEMQLEFGPFSVTCEAEKRK----SDYIIR---TLKVKFNSETRTIYQFH 133

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2209 CPKWPNPDSP--ISKTFELISIIKEEAATRDGPMIVHDEHGGVTAGTFCALTTLMHQLEK----ENsMDVYQVAKMINLM 2282
Cdd:cd14602    134 YKNWPDHDVPssIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDgiipEN-FSVFSLIQEMRTQ 212

                          250       260
                   ....*....|....*....|.
gi 1387264124 2283 RPGVFADIEQYQFLYKAVLSL 2303
Cdd:cd14602    213 RPSLVQTKEQYELVYNAVIEL 233
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 2060-2297 7.08e-30

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: 119.42  E-value: 7.08e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2060 NRTSSIIPVERSRVGISSL-SGEGADYINASYIMGY-YQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDgqnmvs 2137
Cdd:cd14547      1 NRYKTILPNEHSRVCLPSVdDDPLSSYINANYIRGYdGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITN------ 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2138 psghfwhFLFRAEDEFVYWPNKdEPINCESFKVTLMAEEHKclsneEKLIMQDFILEatqddYVLEVR---HFQCPKWPN 2214
Cdd:cd14547     75 -------LTEAKEKCAQYWPEE-ENETYGDFEVTVQSVKET-----DGYTVRKLTLK-----YGGEKRylkHYWYTSWPD 136

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2215 PDSPiSKTFELISIIKE-----EAATRDGPMIVHDEHG-GVTaGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFA 2288
Cdd:cd14547    137 HKTP-EAAQPLLSLVQEveearQTEPHRGPIVVHCSAGiGRT-GCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQ 214


                   ....*....
gi 1387264124 2289 DIEQYQFLY 2297
Cdd:cd14547    215 TAEQYEFVH 223
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 2085-2301 1.09e-29

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: 118.47  E-value: 1.09e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2085 YINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLpdgqNMVSPSGHFWHFLfraedefVYWPnkdEPIN 2164
Cdd:cd14637      1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVML----NQLNQSNSAWPCL-------QYWP---EPGL 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2165 CesfKVTLMAEEHKCLSNEEKLIMQDFILE--ATQDDYVLEVRHFQCPKWP----NPDSPISKTFELISIIKEEAATRDG 2238
Cdd:cd14637     67 Q---QYGPMEVEFVSGSADEDIVTRLFRVQniTRLQEGHLMVRHFQFLRWSayrdTPDSKKAFLHLLASVEKWQRESGEG 143

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387264124 2239 PMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAVL 2301
Cdd:cd14637    144 RTVVHCLNGGGRSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIAL 206
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 1790-1999 1.50e-29

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


Pssm-ID: 350482 [Multi-domain]  Cd Length: 206  Bit Score: 118.20  E-value: 1.50e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1790 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLveKGRRKCDQYWPVDGSEEYGNFLVTQKSIQV 1869
Cdd:cd14634      1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEM--DAAQLCMQYWPEKTSCCYGPIQVEFVSADI 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1870 LAYYTVRNFTLRNTkikkgsqkGRPSG--RVVTQYHYTQWPDM-GVPEYSLPVLTFVRKASHAKRH---AVGPVVVHCSA 1943
Cdd:cd14634     79 DEDIISRIFRICNM--------ARPQDgyRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLEKWQEQydgREGRTVVHCLN 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1387264124 1944 GVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDALVE 1999
Cdd:cd14634    151 GGGRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
alpha_CARP_VIII cd03120
Carbonic anhydrase alpha related protein, group VIII. Carbonic anhydrase related proteins ...
 49-289 3.28e-29

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: 118.81  E-value: 3.28e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124   49 WGKKYPTCNSPKQSPINI-------DEDLTQVNVNLKKLKFQDWDKTslentfihNTGKTVEINLTNDYRLSGGV--SET 119
Cdd:cd03120      4 WGLLFPEANGEYQSPINLnsrearyDPSLLEVRLSPNYVVCRDCEVI--------NDGHTIQIILKSKSVLSGGPlpQGH 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124  120 VFKASKIAFHWGKCNMSsdGSEHSLEGQKFPLEMQIYCFDADRFSSFEEAIKGKGKLRALSILFEVGiEENLDYKAIIDG 199
Cdd:cd03120     76 EFELAEVRFHWGRENQR--GSEHTVNFKAFPMELHLIHWNSTLYSSLEEAMGKPHGIAIIALFVQIG-KEHVGLKAVTEI 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124  200 VERVSRFGKQAALDPFTLLNLLPNSTDK-YYTYNGSLTSPPCTDTVDWIIFKDTVSISESQLAVFCEvLTMQQSGYVMLM 278
Cdd:cd03120    153 LQDIQYKGKSKTIPCFNPNTLLPDPLLRdYWVYEGSLTTPPCSEGVTWILFRYPLTISQSQIEEFRR-LRTHVKGAELVE 231

                          250
                   ....*....|....
gi 1387264124  279 --DY-LQNNFREQQ 289
Cdd:cd03120    232 gcDGlLGDNFRPTQ 245
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 2056-2301 7.20e-29

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: 117.05  E-value: 7.20e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2056 NREKNRTSSIIPVERSRVGISSLSGE-GADYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLpdgQN 2134
Cdd:cd14630      3 NRNKNRYGNIISYDHSRVRLQLLDGDpHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMV---TN 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2135 MVSpsghfwhfLFRAEDeFVYWPNKDEPINceSFKVTLMAEEHKClsneeKLIMQDFILEATQDDYVLEVRHFQCPKWPN 2214
Cdd:cd14630     80 LVE--------VGRVKC-VRYWPDDTEVYG--DIKVTLIETEPLA-----EYVIRTFTVQKKGYHEIREIRQFHFTSWPD 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2215 PDSPISKT--FELISIIKEEAATRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQ 2292
Cdd:cd14630    144 HGVPCYATglLGFVRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQ 223


                   ....*....
gi 1387264124 2293 YQFLYKAVL 2301
Cdd:cd14630    224 YVFVHDAIL 232
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 2085-2297 8.94e-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: 116.19  E-value: 8.94e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2085 YINASYI-MGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVML-PDGQNMVspsghfwhflfraEDEFVYWPNKDEP 2162
Cdd:cd18533      1 YINASYItLPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLtPLVENGR-------------EKCDQYWPSGEYE 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2163 INCESFKVTLMaeehkclsNEEKLIMQDFI---LEATQDDYVL-EVRHFQCPKWPN---PDSPISkTFELISIIKE--EA 2233
Cdd:cd18533     68 GEYGDLTVELV--------SEEENDDGGFIvreFELSKEDGKVkKVYHIQYKSWPDfgvPDSPED-LLTLIKLKRElnDS 138

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387264124 2234 ATRDGPMIVHDEHG-GVTaGTFCALTTLMHQLEKENSMDVYQ------VAKMINLM---RPGVFADIEQYQFLY 2297
Cdd:cd18533    139 ASLDPPIIVHCSAGvGRT-GTFIALDSLLDELKRGLSDSQDLedsedpVYEIVNQLrkqRMSMVQTLRQYIFLY 211
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 2059-2297 2.82e-28

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: 115.70  E-value: 2.82e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2059 KNRTSSIIPVERSRVGISSL--SGEGADYINASYIMGYY-QSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDGQNm 2135
Cdd:cd14612     18 KDRYKTILPNPQSRVCLRRAgsQEEEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMITKLKE- 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2136 vspsghfwhflfRAEDEFVYWPNKDEPINCESFKVTLMAEehkClsneEKLIMQDFILEATQDDYvlEVRHFQCPKWPNP 2215
Cdd:cd14612     97 ------------KKEKCVHYWPEKEGTYGRFEIRVQDMKE---C----DGYTIRDLTIQLEEESR--SVKHYWFSSWPDH 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2216 DSPISKT--FELISIIKE--EAATRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIE 2291
Cdd:cd14612    156 QTPESAGplLRLVAEVEEsrQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSE 235


                   ....*.
gi 1387264124 2292 QYQFLY 2297
Cdd:cd14612    236 QYQFLH 241
alpha_CARP_X_XI_like cd03121
Carbonic anhydrase alpha related protein: groups X, XI and related proteins. This subgroup ...
 49-296 3.82e-28

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


Pssm-ID: 239395 [Multi-domain]  Cd Length: 256  Bit Score: 115.59  E-value: 3.82e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124   49 WGKKYPT---CNSPK-QSPINIDEDLTQVNVNLKKLKFQDWDKTSLEntfIHNTGKTVEINLTNDY--RLSGGVSETVFK 122
Cdd:cd03121      5 WGLVNSAwnlCSKGRrQSPVDIEPSRLLFDPFLTPLRIDTGRKVSGT---FYNTGRHVSFRPDKDPvvNISGGPLSYRYR 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124  123 ASKIAFHWGKCNmsSDGSEHSLEGQKFPLEMQIYCFDADRFSSFEEAIKGKGKLRALSILFEVGIEENLDYKAII--DGV 200
Cdd:cd03121     82 LEEIRLHFGRED--EQGSEHTVNGQAFPGEVQLIHYNSELYPNFSEASKSPNGLVIVSLFVKIGETSNPELRRLTnrDTI 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124  201 ERVSRFGKQAALDPFTLLNLLPNsTDKYYTYNGSLTSPPCTDTVDWIIFKDTVSISESQLAvfcEVLTMQQSGYVMLMDY 280
Cdd:cd03121    160 TSIRYKGDAYFLQDLSIELLLPE-TDHYITYEGSLTSPGCHETVTWIILNKPIYITKEQMH---SLRLLSQNSPSQEKAP 235

                          250
                   ....*....|....*.
gi 1387264124  281 LQNNFREQQYKFSRQV 296
Cdd:cd03121    236 MSPNFRPVQPLNNRPV 251
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 2044-2305 4.11e-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: 116.29  E-value: 4.11e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2044 QQSDYSTALKQCNREKNRTSSIIPVERSRVGISSLSG-EGADYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHN 2122
Cdd:cd14626     29 QQFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGvPGSDYINANYIDGYRKQNAYIATQGPLPETLSDFWRMVWEQR 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2123 AQLVVMLPdgqnmvspsghfwhflfRAEDEF-----VYWPNKDEPiNCESFKVTLM-AEEHKCLSneekliMQDFILEAT 2196
Cdd:cd14626    109 TATIVMMT-----------------RLEEKSrvkcdQYWPIRGTE-TYGMIQVTLLdTVELATYS------VRTFALYKN 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2197 QDDYVLEVRHFQCPKWPN---PDSPiSKTFELISIIKEEAATRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVY 2273
Cdd:cd14626    165 GSSEKREVRQFQFMAWPDhgvPEYP-TPILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIY 243

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1387264124 2274 QVAKMINLMRPGVFADIEQYQFLYKAVLSLVS 2305
Cdd:cd14626    244 GHVTCMRSQRNYMVQTEDQYIFIHEALLEAAT 275
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 2064-2301 1.68e-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: 113.11  E-value: 1.68e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2064 SIIPVERSRVGISSLSG-EGADYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDGQNmvspsghf 2142
Cdd:cd14620      3 NILPYDHSRVILSQLDGiPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKE-------- 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2143 whflfRAEDE-FVYWPNKdepiNCESF-KVTLMAEEHKCLSNeekLIMQDFILEATQDDYVLEVR-----HFQcpKWPN- 2214
Cdd:cd14620     75 -----RKEEKcYQYWPDQ----GCWTYgNIRVAVEDCVVLVD---YTIRKFCIQPQLPDGCKAPRlvtqlHFT--SWPDf 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2215 --PDSPISkTFELISIIKEEAATRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQ 2292
Cdd:cd14620    141 gvPFTPIG-MLKFLKKVKSVNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQ 219


                   ....*....
gi 1387264124 2293 YQFLYKAVL 2301
Cdd:cd14620    220 YSFIYQALL 228
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 2060-2298 1.78e-27

catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type tyrosine-protein phosphatase Q (PTPRQ or R-PTP-Q), also called phosphatidylinositol phosphatase PTPRQ, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRQ is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats (18 in PTPRQ) and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It displays low tyrosine-protein phosphatase activity; rather, it functions as a phosphatidylinositol phosphatase required for auditory processes. It regulates the levels of phosphatidylinositol 4,5-bisphosphate (PIP2) in the basal region of hair bundles. It can dephosphorylate a broad range of phosphatidylinositol phosphates, including phosphatidylinositol 3,4,5-trisphosphate and most phosphatidylinositol monophosphates and diphosphates.


Pssm-ID: 350464 [Multi-domain]  Cd Length: 224  Bit Score: 112.69  E-value: 1.78e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2060 NRTSSIIPVERSRVGISSLSG-EGADYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDGQNMVSP 2138
Cdd:cd14616      1 NRFPNIKPYNNNRVKLIADAGvPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2139 SGHfwhflfraedefVYWPNKDEPINCES-FKVTLMAEEhkclsNEEKLIMQDFILEaTQDDYVLeVRHFQCPKWPNPDS 2217
Cdd:cd14616     81 RCH------------QYWPEDNKPVTVFGdIVITKLMED-----VQIDWTIRDLKIE-RHGDYMM-VRQCNFTSWPEHGV 141

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2218 PISkTFELISIIKEEAATRDG---PMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQ 2294
Cdd:cd14616    142 PES-SAPLIHFVKLVRASRAHdntPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYI 220


                   ....
gi 1387264124 2295 FLYK 2298
Cdd:cd14616    221 FLHQ 224
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 2059-2303 2.30e-27

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: 113.42  E-value: 2.30e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2059 KNRTSSIIPVERSRVGISSLSGEG--ADYINASYIMGY-YQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDGQNM 2135
Cdd:cd14613     28 KNRYKTILPNPHSRVCLTSPDQDDplSSYINANYIRGYgGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEM 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2136 vspsghfwhflfrAEDEFVYWPnkDEPINCESFKVTLMAEEHkclsnEEKLIMQDFILEATQDDYVLevRHFQCPKWPNP 2215
Cdd:cd14613    108 -------------NEKCTEYWP--EEQVTYEGIEITVKQVIH-----ADDYRLRLITLKSGGEERGL--KHYWYTSWPDQ 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2216 DSPiSKTFELISIIKE------EAATRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFAD 2289
Cdd:cd14613    166 KTP-DNAPPLLQLVQEveearqQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQT 244

                          250
                   ....*....|....
gi 1387264124 2290 IEQYQFLYKaVLSL 2303
Cdd:cd14613    245 CEQYQFVHH-VLSL 257
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 2048-2303 4.21e-27

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


Pssm-ID: 350452 [Multi-domain]  Cd Length: 297  Bit Score: 113.87  E-value: 4.21e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2048 YSTAL--KQCNREKNRTSSIIPVERSRVGIS-SLSGEGADYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQ 2124
Cdd:cd14604     47 YPTATgeKEENVKKNRYKDILPFDHSRVKLTlKTSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVA 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2125 LVVMLPDGQNMvspsghfwhflFRAEDEfVYWPN-KDEPINCESFKVTLMAEEHKclsneEKLIMQDFILEATQDDYVLE 2203
Cdd:cd14604    127 IIVMACREFEM-----------GRKKCE-RYWPLyGEEPMTFGPFRISCEAEQAR-----TDYFIRTLLLEFQNETRRLY 189

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2204 VRHFQcpKWPNPDSPIS--KTFELISIIKEEAATRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINL 2281
Cdd:cd14604    190 QFHYV--NWPDHDVPSSfdSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQE 267

                          250       260
                   ....*....|....*....|....*
gi 1387264124 2282 MRPGVFADI---EQYQFLYKAVLSL 2303
Cdd:cd14604    268 MRTQRHSAVqtkEQYELVHRAIAQL 292
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 2060-2298 1.03e-26

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: 110.78  E-value: 1.03e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2060 NRTSSIIPVERSRVGISSLSGEG-ADYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPD--GQNMV 2136
Cdd:cd14617      1 NRYNNILPYDSTRVKLSNVDDDPcSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQcvEKGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2137 SpSGHfwhflfraedefvYWPNKDEPINCESFKVTLMAEehkclSNEEKLIMQDF-ILEATQDDYVLEVRHFQCPKWPNP 2215
Cdd:cd14617     81 K-CDH-------------YWPADQDSLYYGDLIVQMLSE-----SVLPEWTIREFkICSEEQLDAPRLVRHFHYTVWPDH 141

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2216 DSPiSKTFELISIIKeeaATRD--------GPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVF 2287
Cdd:cd14617    142 GVP-ETTQSLIQFVR---TVRDyinrtpgsGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMV 217

                          250
                   ....*....|.
gi 1387264124 2288 ADIEQYQFLYK 2298
Cdd:cd14617    218 QTECQYVYLHQ 228
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 2044-2301 1.24e-26

catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein phosphatase non-receptor type 1 (PTPN1), also called protein-tyrosine phosphatase 1B (PTP-1B), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN1/PTP-1B is the first PTP to be purified and characterized and is the prototypical intracellular PTP found in a wide variety of human tissues. It contains an N-terminal catalytic PTP domain, followed by two tandem proline-rich motifs that mediate interaction with SH3-domain-containing proteins, and a small hydrophobic stretch that localizes the enzyme to the endoplasmic reticulum (ER). It dephosphorylates and regulates the activity of a number of receptor tyrosine kinases, including the insulin receptor, the EGF receptor, and the PDGF receptor.


Pssm-ID: 350456 [Multi-domain]  Cd Length: 277  Bit Score: 112.04  E-value: 1.24e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2044 QQSDY--STALKQCNREKNRTSSIIPVERSRVgisSLSGEGADYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDH 2121
Cdd:cd14608     11 EASDFpcRVAKLPKNKNRNRYRDVSPFDHSRI---KLHQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQ 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2122 NAQLVVMLpdgqNMVSPSGHfwhfLFRAEdefvYWPNKDEP---INCESFKVTLMAEEHKCLSNEEKLIMQDFILEATQd 2198
Cdd:cd14608     88 KSRGVVML----NRVMEKGS----LKCAQ----YWPQKEEKemiFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETR- 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2199 dyvlEVRHFQCPKWPN---PDSPISkTFELISIIKEEAA--TRDGPMIVHDEHGGVTAGTFCALTT---LMHQLEKENSM 2270
Cdd:cd14608    155 ----EILHFHYTTWPDfgvPESPAS-FLNFLFKVRESGSlsPEHGPVVVHCSAGIGRSGTFCLADTcllLMDKRKDPSSV 229

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1387264124 2271 DVYQVAKMINLMRPGVFADIEQYQFLYKAVL 2301
Cdd:cd14608    230 DIKKVLLEMRKFRMGLIQTADQLRFSYLAVI 260
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 2085-2301 2.52e-26

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: 108.96  E-value: 2.52e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2085 YINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDgqnmvspsghfwhfLFRAEDEFVYWPNKDE--- 2161
Cdd:cd14634      1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNE--------------MDAAQLCMQYWPEKTSccy 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2162 -PINCESFKVTLmaeehkclsnEEKLIMQDFI---LEATQDDYVLeVRHFQCPKWPN-PDSPISKTfELISIIK------ 2230
Cdd:cd14634     67 gPIQVEFVSADI----------DEDIISRIFRicnMARPQDGYRI-VQHLQYIGWPAyRDTPPSKR-SILKVVRrlekwq 134

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387264124 2231 EEAATRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAVL 2301
Cdd:cd14634    135 EQYDGREGRTVVHCLNGGGRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVAL 205
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 1790-1999 3.88e-26

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: 108.46  E-value: 3.88e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1790 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRR-KCDQYWPVDGSEEYGNFLVTQKSIQ 1868
Cdd:cd14637      1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWPEPGLQQYGPMEVEFVSGS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1869 VLAYYTVRNFTLRN-TKIKKGSqkgrpsgRVVTQYHYTQW-PDMGVPEYS---LPVLTFVRKASHAKRHavGPVVVHCSA 1943
Cdd:cd14637     81 ADEDIVTRLFRVQNiTRLQEGH-------LMVRHFQFLRWsAYRDTPDSKkafLHLLASVEKWQRESGE--GRTVVHCLN 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1387264124 1944 GVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDALVE 1999
Cdd:cd14637    152 GGGRSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 2085-2297 4.43e-26

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


Pssm-ID: 350397 [Multi-domain]  Cd Length: 204  Bit Score: 107.82  E-value: 4.43e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2085 YINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLpdgQNMVSpSGHfwhflfRAEDEfvYWPNKDEPiN 2164
Cdd:cd14549      1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMI---TNLVE-RGR------RKCDQ--YWPKEGTE-T 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2165 CESFKVTLMAEEHK--------CLSNEEklimqdfILEATQDDYVLEVRHFQCPKWPN---PDSPISktfeLISIIKEEA 2233
Cdd:cd14549     68 YGNIQVTLLSTEVLatytvrtfSLKNLK-------LKKVKGRSSERVVYQYHYTQWPDhgvPDYTLP----VLSFVRKSS 136

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387264124 2234 ATRD---GPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLY 2297
Cdd:cd14549    137 AANPpgaGPIVVHCSAGVGRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 2056-2300 5.74e-26

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: 109.09  E-value: 5.74e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2056 NREKNRTSSIIPVERSRVGISSL--SGEGADYINASYIM-------GYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLV 2126
Cdd:cd14544      1 NKGKNRYKNILPFDHTRVILKDRdpNVPGSDYINANYIRnenegptTDENAKTYIATQGCLENTVSDFWSMVWQENSRVI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2127 VMLPDGQNmvspsghfwhflfRAEDEFV-YWPnkDEpincesfkVTLMAEEHKCLSNEEKLIMQDFIL------EATQDD 2199
Cdd:cd14544     81 VMTTKEVE-------------RGKNKCVrYWP--DE--------GMQKQYGPYRVQNVSEHDTTDYTLrelqvsKLDQGD 137

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2200 YVLEVRHFQCPKWPNPDSPiSKTFELISII-----KEEAATRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKEN---SMD 2271
Cdd:cd14544    138 PIREIWHYQYLSWPDHGVP-SDPGGVLNFLedvnqRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGldcDID 216

                          250       260
                   ....*....|....*....|....*....
gi 1387264124 2272 VYQVAKMINLMRPGVFADIEQYQFLYKAV 2300
Cdd:cd14544    217 IQKTIQMVRSQRSGMVQTEAQYKFIYVAV 245
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 2056-2304 5.97e-26

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: 109.74  E-value: 5.97e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2056 NREKNRTSSIIPVERSRVGISSLSGEGA---DYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLpdg 2132
Cdd:cd17667     27 NKHKNRYINILAYDHSRVKLRPLPGKDSkhsDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMI--- 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2133 QNMVSPSGhfwhflfRAEDEfvYWPNKdepiNCESFK---VTLMAEE-HKCLSneekliMQDFILEATQDDYVLE----- 2203
Cdd:cd17667    104 TNLVEKGR-------RKCDQ--YWPTE----NSEEYGniiVTLKSTKiHACYT------VRRFSIRNTKVKKGQKgnpkg 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2204 ------VRHFQCPKWPNPDSPiSKTFELISIIKEEAATRD---GPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQ 2274
Cdd:cd17667    165 rqnertVIQYHYTQWPDMGVP-EYALPVLTFVRRSSAARTpemGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLG 243

                          250       260       270
                   ....*....|....*....|....*....|
gi 1387264124 2275 VAKMINLMRPGVFADIEQYQFLYKAVLSLV 2304
Cdd:cd17667    244 FLKHIRTQRNYLVQTEEQYIFIHDALLEAI 273
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 1790-1999 6.61e-26

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


Pssm-ID: 350483 [Multi-domain]  Cd Length: 206  Bit Score: 107.47  E-value: 6.61e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1790 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLveKGRRKCDQYWPVDGSEEYGNFLVTQKSIQV 1869
Cdd:cd14635      1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDV--DPAQLCPQYWPENGVHRHGPIQVEFVSADL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1870 LAYYTVRNFTLRNTkikkgsqkGRPSG--RVVTQYHYTQWPDM-GVPEYSLPVLTFVRKASHAKRH---AVGPVVVHCSA 1943
Cdd:cd14635     79 EEDIISRIFRIYNA--------ARPQDgyRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEyngGEGRTVVHCLN 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1387264124 1944 GVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDALVE 1999
Cdd:cd14635    151 GGGRSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 2031-2301 1.01e-25

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: 109.73  E-value: 1.01e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2031 LEKQFKLLSQSNIQQSdYSTALKQCNREKNRTSSIIPVERSRVGISSLSG-EGADYINASYIMGYYQSNEFIITQHPLLH 2109
Cdd:cd14621     28 FREEFNALPACPIQAT-CEAASKEENKEKNRYVNILPYDHSRVHLTPVEGvPDSDYINASFINGYQEKNKFIAAQGPKEE 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2110 TIQDFWRMIWDHNAQLVVMLPDGQNmvspsghfwhflfRAEDEFV-YWPNKdepiNCESF-KVTLMAEEHKCLSNE--EK 2185
Cdd:cd14621    107 TVNDFWRMIWEQNTATIVMVTNLKE-------------RKECKCAqYWPDQ----GCWTYgNIRVSVEDVTVLVDYtvRK 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2186 LIMQDfILEATQDDYVLEVRHFQCPKWPN---PDSPISkTFELISIIKEEAATRDGPMIVHDEHGGVTAGTFCALTTLMH 2262
Cdd:cd14621    170 FCIQQ-VGDVTNKKPQRLITQFHFTSWPDfgvPFTPIG-MLKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFIVIDAMLD 247

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1387264124 2263 QLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAVL 2301
Cdd:cd14621    248 MMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALL 286
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 2049-2300 1.20e-25

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 110.12  E-value: 1.20e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2049 STALKQCNREKNRTSSIIPVERSRVGISS------------------LSGEGAD--YINASYIMGYYQSNEFIITQHPLL 2108
Cdd:PHA02746    44 NHFLKKENLKKNRFHDIPCWDHSRVVINAheslkmfdvgdsdgkkieVTSEDNAenYIHANFVDGFKEANKFICAQGPKE 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2109 HTIQDFWRMIWDHNAQLVVMLPDGQNmvspsghfwhflfraEDE--FVYWPN-KDEPINCESFKVTLMAEEHKCLSNEEK 2185
Cdd:PHA02746   124 DTSEDFFKLISEHESQVIVSLTDIDD---------------DDEkcFELWTKeEDSELAFGRFVAKILDIIEELSFTKTR 188

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2186 LIMQDFILEATQddyvlEVRHFQCPKWP---NPDSPiSKTFELISIIKEEAA----------TRDGPMIVHDEHGGVTAG 2252
Cdd:PHA02746   189 LMITDKISDTSR-----EIHHFWFPDWPdngIPTGM-AEFLELINKVNEEQAelikqadndpQTLGPIVVHCSAGIGRAG 262

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1387264124 2253 TFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAV 2300
Cdd:PHA02746   263 TFCAIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 2048-2305 1.91e-25

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 109.32  E-value: 1.91e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2048 YSTALKQCNREKNRTSSIIPVERSRVGISSLSGEGADYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVV 2127
Cdd:PHA02747    43 IANFEKPENQPKNRYWDIPCWDHNRVILDSGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIV 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2128 MLPDGQNMvspSGHfwhflfraEDEFVYW-PNKDEPINCESFKVTLMAEEHKCLSNEEKLIMQDFILEATQddyvlEVRH 2206
Cdd:PHA02747   123 MLTPTKGT---NGE--------EKCYQYWcLNEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILKDSR-----KISH 186

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2207 FQCPKWPNPDSPIS-----KTFELISIIKEEAAT----RDG---PMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQ 2274
Cdd:PHA02747   187 FQCSEWFEDETPSDhpdfiKFIKIIDINRKKSGKlfnpKDAllcPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAK 266

                          250       260       270
                   ....*....|....*....|....*....|....
gi 1387264124 2275 VAKMINLMRPGVFADIEQYQFL---YKAVLSLVS 2305
Cdd:PHA02747   267 TAEKIREQRHAGIMNFDDYLFIqpgYEVLHYFLS 300
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 1790-1999 2.03e-25

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


Pssm-ID: 350484 [Multi-domain]  Cd Length: 206  Bit Score: 106.26  E-value: 2.03e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1790 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNL-VEKGrrkCDQYWPVDGSEEYGNFLVTQKSIQ 1868
Cdd:cd14636      1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVdLAQG---CPQYWPEEGMLRYGPIQVECMSCS 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1869 VLAYYTVRNFTLRN-TKIKKGSQkgrpsgrVVTQYHYTQWPD-MGVPEYS---LPVLTFVRKASHAKRHAVGPVVVHCSA 1943
Cdd:cd14636     78 MDCDVISRIFRICNlTRPQEGYL-------MVQQFQYLGWAShREVPGSKrsfLKLILQVEKWQEECDEGEGRTIIHCLN 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1387264124 1944 GVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDALVE 1999
Cdd:cd14636    151 GGGRSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 2085-2298 2.41e-25

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: 105.97  E-value: 2.41e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2085 YINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDGQNMvspsGHfwhflFRAEDefvYWPNK-DEPI 2163
Cdd:cd14542      1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEM----GK-----KKCER---YWPEEgEEQL 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2164 NCESFKVTLMAEEHKClsneeklimQDFI---LEATQDDYVLEVRHFQCPKWPNPDSPISKT--FELISIIKEEAATRDG 2238
Cdd:cd14542     69 QFGPFKISLEKEKRVG---------PDFLirtLKVTFQKESRTVYQFHYTAWPDHGVPSSVDpiLDLVRLVRDYQGSEDV 139

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387264124 2239 PMIVHDEHGGVTAGTFCALT---TLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYK 2298
Cdd:cd14542    140 PICVHCSAGCGRTGTICAIDyvwNLLKTGKIPEEFSLFDLVREMRKQRPAMVQTKEQYELVYR 202
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 2028-2300 2.83e-25

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: 108.22  E-value: 2.83e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2028 KTKLEKQFKLLSQSNIQQSDYSTALKQCNREKNRTSSIIPVERSRVGISSL-SGEGADYINASYIMGYYQSN-EFIITQH 2105
Cdd:cd14610     16 KNRLEKEWEALCAYQAEPNATNVAQREENVQKNRSLAVLPYDHSRIILKAEnSHSHSDYINASPIMDHDPRNpAYIATQG 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2106 PLLHTIQDFWRMIWDHNAQLVVML-PDGQNMVSPSGHfwhflfraedefvYWPnkDEPINC-ESFKVTLMAEEHKClsne 2183
Cdd:cd14610     96 PLPATVADFWQMVWESGCVVIVMLtPLAENGVKQCYH-------------YWP--DEGSNLyHIYEVNLVSEHIWC---- 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2184 EKLIMQDFILEATQDDYVLEVRHFQCPKWPNPDSPIS--KTFELISIIKEEAATRDGPMIVHDEHGGVTAGTFCALTTLM 2261
Cdd:cd14610    157 EDFLVRSFYLKNLQTNETRTVTQFHFLSWNDQGVPAStrSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILIDMVL 236

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1387264124 2262 HQLEK-ENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAV 2300
Cdd:cd14610    237 NKMAKgAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAV 276
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 2083-2301 6.59e-25

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


Pssm-ID: 350479 [Multi-domain]  Cd Length: 218  Bit Score: 105.10  E-value: 6.59e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2083 ADYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLpdgQNMVSpsghfwhfLFRAEDeFVYWPNKDEP 2162
Cdd:cd14631     13 SDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMV---TNLVE--------VGRVKC-YKYWPDDTEV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2163 INceSFKVTLMAEEHKClsneeKLIMQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKT--FELISIIKEEAATRDGPM 2240
Cdd:cd14631     81 YG--DFKVTCVEMEPLA-----EYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATglLSFIRRVKLSNPPSAGPI 153

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387264124 2241 IVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAVL 2301
Cdd:cd14631    154 VVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAIL 214
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 2085-2301 7.81e-25

catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The type II (or R2B) subfamily of receptor protein tyrosine phosphatases (RPTPs) include the prototypical member PTPmu (or PTPRM), PCP-2 (or PTPRU), PTPrho (or PTPRT), and PTPkappa (or PTPRK). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Type IIb RPTPs mediate cell-cell adhesion though homophilic interactions; their ligand is an identical molecule on an adjacent cell. No heterophilic interactions between the subfamily members have been observed. They also commonly function as tumor suppressors. They contain an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350403 [Multi-domain]  Cd Length: 204  Bit Score: 104.61  E-value: 7.81e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2085 YINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLpdgQNMVSpsghfwhfLFRAEDeFVYWPNKDEPIN 2164
Cdd:cd14555      1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMV---TNLVE--------VGRVKC-SRYWPDDTEVYG 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2165 ceSFKVTLMAEEHKClsneeKLIMQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKT--FELISIIKEEAATRDGPMIV 2242
Cdd:cd14555     69 --DIKVTLVETEPLA-----EYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATglLGFIRRVKASNPPSAGPIVV 141

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1387264124 2243 HDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAVL 2301
Cdd:cd14555    142 HCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAIL 200
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 2085-2301 7.90e-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: 7.90e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2085 YINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDgqnmVSPsghfwhflfrAEDEFVYWP----NKD 2160
Cdd:cd14635      1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLND----VDP----------AQLCPQYWPengvHRH 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2161 EPINCESFKVTLmaeehkclsnEEKLIMQDF-ILEAT--QDDYVLeVRHFQCPKWP-NPDSPISKT--FELISII---KE 2231
Cdd:cd14635     67 GPIQVEFVSADL----------EEDIISRIFrIYNAArpQDGYRM-VQQFQFLGWPmYRDTPVSKRsfLKLIRQVdkwQE 135

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2232 EAATRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAVL 2301
Cdd:cd14635    136 EYNGGEGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVAL 205
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 2044-2305 1.29e-24

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: 106.35  E-value: 1.29e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2044 QQSDYSTALKQCNREKNRTSSIIPVERSRVGISSLSG-EGADYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHN 2122
Cdd:cd14624     35 QQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGiPGSDYINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQR 114

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2123 AQLVVMLPDGQNMVspsghfwhflfRAEDEfVYWPNKDEPINcESFKVTLMAEEHKClsneeKLIMQDFILEATQDDYVL 2202
Cdd:cd14624    115 SATVVMMTKLEERS-----------RVKCD-QYWPSRGTETY-GLIQVTLLDTVELA-----TYCVRTFALYKNGSSEKR 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2203 EVRHFQCPKWPNPDSPISKT--FELISIIKEEAATRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMIN 2280
Cdd:cd14624    177 EVRQFQFTAWPDHGVPEHPTpfLAFLRRVKTCNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMR 256

                          250       260
                   ....*....|....*....|....*
gi 1387264124 2281 LMRPGVFADIEQYQFLYKAVLSLVS 2305
Cdd:cd14624    257 AQRNYMVQTEDQYIFIHDALLEAVT 281
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 2044-2305 4.02e-24

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: 104.79  E-value: 4.02e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2044 QQSDYSTALKQCNREKNRTSSIIPVERSRVGISSLSG-EGADYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHN 2122
Cdd:cd14625     35 QQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGiMGSDYINANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQR 114

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2123 AQLVVMLPdgqnmvspsghfwhflfRAEDEF-----VYWPNKdepiNCESF---KVTLMAEEHKClsneeKLIMQDFILE 2194
Cdd:cd14625    115 SATVVMMT-----------------KLEEKSrikcdQYWPSR----GTETYgmiQVTLLDTIELA-----TFCVRTFSLH 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2195 ATQDDYVLEVRHFQCPKWPNPDSPISKT--FELISIIKEEAATRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDV 2272
Cdd:cd14625    169 KNGSSEKREVRQFQFTAWPDHGVPEYPTpfLAFLRRVKTCNPPDAGPIVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDI 248

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1387264124 2273 YQVAKMINLMRPGVFADIEQYQFLYKAVLSLVS 2305
Cdd:cd14625    249 YGHVTLMRSQRNYMVQTEDQYSFIHDALLEAVA 281
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 2057-2298 4.67e-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: 4.67e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2057 REKNRTSSIIPVERSRVgisSLSGEGADYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLpdgqNMV 2136
Cdd:cd14545      1 LNRYRDRDPYDHDRSRV---KLKQGDNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIML----NKL 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2137 SPSGhfwhfLFRAEDefvYWPNKDEPINC---ESFKVTLMAEEHKclsneEKLIMQDFILEATQDDYVLEVRHFQCPKWP 2213
Cdd:cd14545     74 MEKG-----QIKCAQ---YWPQGEGNAMIfedTGLKVTLLSEEDK-----SYYTVRTLELENLKTQETREVLHFHYTTWP 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2214 N---PDSPISKTFELISIIKEEAATRD-GPMIVHDEHGGVTAGTFCALTTLMHQLEKEN--SMDVYQVAKMINLMRPGVF 2287
Cdd:cd14545    141 DfgvPESPAAFLNFLQKVRESGSLSSDvGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNpsSVDVKKVLLEMRKYRMGLI 220

                          250
                   ....*....|.
gi 1387264124 2288 ADIEQYQFLYK 2298
Cdd:cd14545    221 QTPDQLRFSYL 231
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 1790-1998 1.81e-23

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: 100.52  E-value: 1.81e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1790 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITN---LVEkgrrkcDQ--YWPvdGSEEYGN---FL 1861
Cdd:cd17670      1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDnqgLAE------DEfvYWP--SREESMNceaFT 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1862 VTQKSIQVLAYYT-----VRNFTLRNTKIKKGSQkgrpsgrvVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAKRHavGP 1936
Cdd:cd17670     73 VTLISKDRLCLSNeeqiiIHDFILEATQDDYVLE--------VRHFQCPKWPNPDAPISSTFELINVIKEEALTRD--GP 142

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387264124 1937 VVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDALV 1998
Cdd:cd17670    143 TIVHDEFGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 2085-2301 6.27e-23

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: 98.94  E-value: 6.27e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2085 YINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDgQNMVSPSGHFWhflfRAEDEFVYWPNKDEPIN 2164
Cdd:cd14636      1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNE-VDLAQGCPQYW----PEEGMLRYGPIQVECMS 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2165 CeSFKVTLMAEehkclsneeklIMQDFILEATQDDYVLeVRHFQCPKWP-NPDSPISKTFELISII-----KEEAATRDG 2238
Cdd:cd14636     76 C-SMDCDVISR-----------IFRICNLTRPQEGYLM-VQQFQYLGWAsHREVPGSKRSFLKLILqvekwQEECDEGEG 142

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387264124 2239 PMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAVL 2301
Cdd:cd14636    143 RTIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVAL 205
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 2085-2301 6.61e-23

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: 98.97  E-value: 6.61e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2085 YINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPD----GQNMVSPsghfwhflfraedefvYWPNKD 2160
Cdd:cd14632      1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKlvevGRVKCSK----------------YWPDDS 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2161 EPINceSFKVTLMAEEhkclsNEEKLIMQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKT--FELISIIKEEAATRDG 2238
Cdd:cd14632     65 DTYG--DIKITLLKTE-----TLAEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATglLAFIRRVKASTPPDAG 137

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387264124 2239 PMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAVL 2301
Cdd:cd14632    138 PVVVHCSAGAGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAIL 200
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 2028-2300 8.46e-23

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: 100.88  E-value: 8.46e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2028 KTKLEKQFKLLSQSNIQQSDYSTALKQCNREKNRTSSIIPVERSRVGI-SSLSGEGADYINASYIMGY-YQSNEFIITQH 2105
Cdd:cd14609     14 RDRLAKEWQALCAYQAEPNTCSTAQGEANVKKNRNPDFVPYDHARIKLkAESNPSRSDYINASPIIEHdPRMPAYIATQG 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2106 PLLHTIQDFWRMIWDHNAQLVVMLP----DGQNMVSPsghfwhflfraedefvYWPNKDEPINcESFKVTLMAEEHKCls 2181
Cdd:cd14609     94 PLSHTIADFWQMVWENGCTVIVMLTplveDGVKQCDR----------------YWPDEGSSLY-HIYEVNLVSEHIWC-- 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2182 neEKLIMQDFILEATQDDYVLEVRHFQCPKWPNPDSPiSKTFELISI---IKEEAATRDGPMIVHDEHGGVTAGTFCALT 2258
Cdd:cd14609    155 --EDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGIP-SSTRPLLDFrrkVNKCYRGRSCPIIVHCSDGAGRTGTYILID 231

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1387264124 2259 TLMHQLEKE-NSMDVYQVAKMINLMRPGVFADIEQYQFLYKAV 2300
Cdd:cd14609    232 MVLNRMAKGvKEIDIAATLEHVRDQRPGMVRTKDQFEFALTAV 274
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 1790-1998 1.03e-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: 98.14  E-value: 1.03e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1790 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCdQYWPvdGSEEYGN---FLVT--- 1863
Cdd:cd17669      1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEF-VYWP--NKDEPINcetFKVTlia 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1864 --QKSIQVLAYYTVRNFTLRNTKikkgsqkgrpSGRVVTQYHYT--QWPDMGVPEYSLPVLTFVRKASHAKRHavGPVVV 1939
Cdd:cd17669     78 eeHKCLSNEEKLIIQDFILEATQ----------DDYVLEVRHFQcpKWPNPDSPISKTFELISIIKEEAANRD--GPMIV 145

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1387264124 1940 HCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDALV 1998
Cdd:cd17669    146 HDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
2203-2302 2.93e-22

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 93.58  E-value: 2.93e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124  2203 EVRHFQCPKWPNPDSPISKT--FELISIIKEE--AATRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKE-NSMDVYQVAK 2277
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDsiLELLRAVKKNlnQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 1387264124  2278 MINLMRPGVFADIEQYQFLYKAVLS 2302
Cdd:smart00404   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 2203-2302 2.93e-22

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: 93.58  E-value: 2.93e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124  2203 EVRHFQCPKWPNPDSPISKT--FELISIIKEE--AATRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKE-NSMDVYQVAK 2277
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDsiLELLRAVKKNlnQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 1387264124  2278 MINLMRPGVFADIEQYQFLYKAVLS 2302
Cdd:smart00012   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 2056-2301 4.01e-22

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: 97.59  E-value: 4.01e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2056 NREKNRTSSIIPVERSRVgissLSGEGADYINASYIMGYYQSNEF--IITQHPLLHTIQDFWRMIWDHNAQLVVMLPDgq 2133
Cdd:cd14597      3 NRKKNRYKNILPYDTTRV----PLGDEGGYINASFIKMPVGDEEFvyIACQGPLPTTVADFWQMVWEQKSTVIAMMTQ-- 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2134 nmvspsghfwhflfRAEDEFV----YWP---NKDEPINcESFKVTLMAEEHkclsnEEKLIMQDFILEATQDDYVLEVRH 2206
Cdd:cd14597     77 --------------EVEGGKIkcqrYWPeilGKTTMVD-NRLQLTLVRMQQ-----LKNFVIRVLELEDIQTREVRHITH 136

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2207 FQCPKWPNPDSPiSKTFELISIIK-EEAATRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPG 2285
Cdd:cd14597    137 LNFTAWPDHDTP-SQPEQLLTFISyMRHIHKSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHG 215

                          250
                   ....*....|....*.
gi 1387264124 2286 VFADIEQYQFLYKAVL 2301
Cdd:cd14597    216 MVQTEDQYIFCYQVIL 231
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 2085-2301 5.56e-22

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: 96.29  E-value: 5.56e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2085 YINASYIMGYYQSNEF--IITQHPLLHTIQDFWRMIWDHNAQLVVMLPdgQNMvspsghfwhflfraEDEFV----YWPn 2158
Cdd:cd14538      1 YINASHIRIPVGGDTYhyIACQGPLPNTTGDFWQMVWEQKSEVIAMVT--QDV--------------EGGKVkchrYWP- 63

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2159 kdepincESFKVTLMAEEHKCLSNEEKLIMQDFI-----LEATQDDYVLEVRHFQCPKWPNPDSPISKtfelISIIKEEA 2233
Cdd:cd14538     64 -------DSLNKPLICGGRLEVSLEKYQSLQDFVirrisLRDKETGEVHHITHLNFTTWPDHGTPQSA----DPLLRFIR 132

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387264124 2234 ATR----DGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAVL 2301
Cdd:cd14538    133 YMRrihnSGPIVVHCSAGIGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACL 204
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 2085-2301 7.99e-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: 95.82  E-value: 7.99e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2085 YINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLpdgQNMVSPSGhfwhflfRAEDEfvYWPNKDEPiN 2164
Cdd:cd17668      1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMI---TNLVEKGR-------RKCDQ--YWPADGSE-E 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2165 CESFKVTLMAEEHKCLSNEEKLIMQDF-ILEATQDDYVLE--VRHFQCPKWPNPDSPiSKTFELISIIKEEAATRD---G 2238
Cdd:cd17668     68 YGNFLVTQKSVQVLAYYTVRNFTLRNTkIKKGSQKGRPSGrvVTQYHYTQWPDMGVP-EYTLPVLTFVRKASYAKRhavG 146

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387264124 2239 PMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAVL 2301
Cdd:cd17668    147 PVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 2059-2297 8.85e-22

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: 96.14  E-value: 8.85e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2059 KNRTSSIIPVERSRVGI--SSLSGEGADYINASYIMGYY-QSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDGQNm 2135
Cdd:cd14611      2 KNRYKTILPNPHSRVCLkpKNSNDSLSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKE- 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2136 vspsghfwhflfRAEDEFVYWPNKDEPINcesfKVTLMAeehKCLSNEEKLIMQDFILEatQDDYVLEVRHFQCPKWPNP 2215
Cdd:cd14611     81 ------------KNEKCVLYWPEKRGIYG----KVEVLV---NSVKECDNYTIRNLTLK--QGSQSRSVKHYWYTSWPDH 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2216 DSPISKT--FELISIIKEE--AATRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIE 2291
Cdd:cd14611    140 KTPDSAQplLQLMLDVEEDrlASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSE 219


                   ....*.
gi 1387264124 2292 QYQFLY 2297
Cdd:cd14611    220 QYEFVH 225
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 1752-2003 1.01e-21

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 98.12  E-value: 1.01e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1752 SSNHPDNKHK--NRYINIVAYDHSRVKLaqlaEKDGKLTDyinANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVE 1829
Cdd:PHA02740    45 ACAQAENKAKdeNLALHITRLLHRRIKL----FNDEKVLD---ARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQ 117

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1830 VIVMITNLVEKgrrKC-DQYWpvdgSEEYGNFLVTQK-SIQVLAYYTVRNFTLrnTKIKKGSQKGRpsGRVVTQYHYTQW 1907
Cdd:PHA02740   118 IIVLISRHADK---KCfNQFW----SLKEGCVITSDKfQIETLEIIIKPHFNL--TLLSLTDKFGQ--AQKISHFQYTAW 186

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1908 PDMGVPEYSLPVLTF----------VRKASHAKRhaVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIR 1977
Cdd:PHA02740   187 PADGFSHDPDAFIDFfcniddlcadLEKHKADGK--IAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVR 264

                          250       260
                   ....*....|....*....|....*.
gi 1387264124 1978 SQRNYLVQTEEQYVFIHDaLVEAILS 2003
Cdd:PHA02740   265 QKKYGCMNCLDDYVFCYH-LIAAYLK 289
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 2085-2298 2.04e-21

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; Receptor-type tyrosine-protein phosphatase A (PTPRA) and E (PTPRE) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA and PTPRE share several functions including regulation of Src family kinases and voltage-gated potassium (Kv) channels. They both contain a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the first catalytic PTP domain (repeat 1).


Pssm-ID: 350399 [Multi-domain]  Cd Length: 202  Bit Score: 94.59  E-value: 2.04e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2085 YINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDGQNmvspsghfwhflfRAEDEFV-YWPNKdepi 2163
Cdd:cd14551      1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKE-------------RKEKKCSqYWPDQ---- 63

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2164 NCESFKVTLMaeehkCLSNEEKLI---MQDFILEATQDDY----VLEVRHFQCPKWPN---PDSPISkTFELISIIKEEA 2233
Cdd:cd14551     64 GCWTYGNLRV-----RVEDTVVLVdytTRKFCIQKVNRGIgekrVRLVTQFHFTSWPDfgvPFTPIG-MLKFLKKVKSAN 137

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1387264124 2234 ATRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYK 2298
Cdd:cd14551    138 PPRAGPIVVHCSAGVGRTGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 2085-2301 1.15e-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: 92.50  E-value: 1.15e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2085 YINASYIMGYYQSNE--FIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDGQNMVSPSGHfwhflfraedefVYWPNK-DE 2161
Cdd:cd14596      1 YINASYITMPVGEEElfYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCH------------RYWPETlQE 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2162 PINCESFKVTLmaeehkclsnEEKLIMQDFILEATQddyVLE--------VRHFQCPKWPNPDSPISKTFELISIIKEEA 2233
Cdd:cd14596     69 PMELENYQLRL----------ENYQALQYFIIRIIK---LVEketgenrlIKHLQFTTWPDHGTPQSSDQLVKFICYMRK 135

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387264124 2234 ATRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAVL 2301
Cdd:cd14596    136 VHNTGPIVVHCSAGIGRAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVL 203
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 2056-2300 7.55e-20

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


Pssm-ID: 350455 [Multi-domain]  Cd Length: 257  Bit Score: 91.57  E-value: 7.55e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2056 NREKNRTSSIIPVERSRVGISSLSGegaDYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLpdgqNM 2135
Cdd:cd14607     24 NRNRNRYRDVSPYDHSRVKLQNTEN---DYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVML----NR 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2136 VSPSGhfwhflfrAEDEFVYWPNKDEPINCES---FKVTLMAEEHKCLSNEEKLIMQDFILEATQDdyvleVRHFQCPKW 2212
Cdd:cd14607     97 IVEKD--------SVKCAQYWPTDEEEVLSFKetgFSVKLLSEDVKSYYTVHLLQLENINSGETRT-----ISHFHYTTW 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2213 PN---PDSPISKTFELISIIKEEAATRD-GPMIVHDEHGGVTAGTFCALTTLMHQLEKEN--SMDVYQVAKMINLMRPGV 2286
Cdd:cd14607    164 PDfgvPESPASFLNFLFKVRESGSLSPEhGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDIKQVLLDMRKYRMGL 243

                          250
                   ....*....|....
gi 1387264124 2287 FADIEQYQFLYKAV 2300
Cdd:cd14607    244 IQTPDQLRFSYMAV 257
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 2056-2301 1.46e-19

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: 91.06  E-value: 1.46e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2056 NREKNRTSSIIPVERSRVgissLSGEGADYINASY----IMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPD 2131
Cdd:cd14600     40 NMDKNRYKDVLPYDATRV----VLQGNEDYINASYvnmeIPSANIVNKYIATQGPLPHTCAQFWQVVWEQKLSLIVMLTT 115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2132 GQNMVSPSGHfwhflfraedefVYWPNKDEPINCESFKVTLMAEEHKClsneeKLIMQDFILEATQDDYVLEVRHFQCPK 2211
Cdd:cd14600    116 LTERGRTKCH------------QYWPDPPDVMEYGGFRVQCHSEDCTI-----AYVFREMLLTNTQTGEERTVTHLQYVA 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2212 WPN---PDSPiSKTFELISIIKEEAATRDgPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFA 2288
Cdd:cd14600    179 WPDhgvPDDS-SDFLEFVNYVRSKRVENE-PVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQ 256

                          250
                   ....*....|...
gi 1387264124 2289 DIEQYQFLYKAVL 2301
Cdd:cd14600    257 TSSQYKFVCEAIL 269
PHA02738 PHA02738
hypothetical protein; Provisional
 2056-2300 6.05e-19

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 90.37  E-value: 6.05e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2056 NREKNRTSSIIPVERSRVGISSLSGEGaDYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDGQNM 2135
Cdd:PHA02738    49 NRKLNRYLDAVCFDHSRVILPAERNRG-DYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKEN 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2136 VSpsghfwhflfraEDEFVYWPNKDE-PINCESFKVTLMAEEHKCLSNEEKLIMQDFIlEATQddyvlEVRHFQCPKWPN 2214
Cdd:PHA02738   128 GR------------EKCFPYWSDVEQgSIRFGKFKITTTQVETHPHYVKSTLLLTDGT-SATQ-----TVTHFNFTAWPD 189

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2215 PDSPiSKTFELISII-------KEEAATR---------DGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKM 2278
Cdd:PHA02738   190 HDVP-KNTSEFLNFVlevrqcqKELAQESlqighnrlqPPPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSS 268

                          250       260
                   ....*....|....*....|..
gi 1387264124 2279 INLMRPGVFADIEQYQFLYKAV 2300
Cdd:PHA02738   269 IRNQRYYSLFIPFQYFFCYRAV 290
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 2056-2306 1.97e-18

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: 87.38  E-value: 1.97e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2056 NREKNRTSSIIPVERSRVGISS--LSGEGADYINASYIMGYYQSN--------EFIITQHPLLHTIQDFWRMIWDHNAQL 2125
Cdd:cd14605      2 NKNKNRYKNILPFDHTRVVLHDgdPNEPVSDYINANIIMPEFETKcnnskpkkSYIATQGCLQNTVNDFWRMVFQENSRV 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2126 VVMLPDGqnmvspsghfwhfLFRAEDEFV-YWPNKDEPINCESFKVTLMAEE--HKCLSNEEKLImqdfilEATQDDYVL 2202
Cdd:cd14605     82 IVMTTKE-------------VERGKSKCVkYWPDEYALKEYGVMRVRNVKESaaHDYILRELKLS------KVGQGNTER 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2203 EVRHFQCPKWPN---PDSP--ISKTFELISiIKEEAATRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKEN---SMDVYQ 2274
Cdd:cd14605    143 TVWQYHFRTWPDhgvPSDPggVLDFLEEVH-HKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGvdcDIDVPK 221

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1387264124 2275 VAKMINLMRPGVFADIEQYQFLYKAVLSLVST 2306
Cdd:cd14605    222 TIQMVRSQRSGMVQTEAQYRFIYMAVQHYIET 253
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 2056-2306 2.50e-18

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: 87.24  E-value: 2.50e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2056 NREKNRTSSIIPVERSRVGISSLSGE--GADYINASYIMGYYQSNE-----FIITQHPLLHTIQDFWRMIWDHNAQLVVM 2128
Cdd:cd14606     18 NKSKNRYKNILPFDHSRVILQGRDSNipGSDYINANYVKNQLLGPDenaktYIASQGCLEATVNDFWQMAWQENSRVIVM 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2129 ----LPDGQNMVSPsghfwhflfraedefvYWPNKDEPINCESFKVTLMAEEHkclSNEEKL-IMQDFILEATqdDYVLE 2203
Cdd:cd14606     98 ttreVEKGRNKCVP----------------YWPEVGMQRAYGPYSVTNCGEHD---TTEYKLrTLQVSPLDNG--ELIRE 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2204 VRHFQCPKWPNPDSPiSKTFELISII-----KEEAATRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKEN---SMDVYQV 2275
Cdd:cd14606    157 IWHYQYLSWPDHGVP-SEPGGVLSFLdqinqRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGldcDIDIQKT 235

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1387264124 2276 AKMINLMRPGVFADIEQYQFLYKAVLSLVST 2306
Cdd:cd14606    236 IQMVRAQRSGMVQTEAQYKFIYVAIAQFIET 266
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 2085-2300 2.74e-18

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: 85.57  E-value: 2.74e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2085 YINASYIMGYYQSNE-FIITQHPLLHTIQDFWRMIWDHNAQLVVML-PDGQNMVSPSGHfwhflfraedefvYWPNKDEP 2162
Cdd:cd14546      1 YINASTIYDHDPRNPaYIATQGPLPHTIADFWQMIWEQGCVVIVMLtRLQENGVKQCAR-------------YWPEEGSE 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2163 INcESFKVTLMAEEHKClsneEKLIMQDFILEATQDDYVLEVRHFQCPKWPNPDSPIS-KTF-ELISIIKEEAATRDGPM 2240
Cdd:cd14546     68 VY-HIYEVHLVSEHIWC----DDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASaKPLlEFRRKVNKSYRGRSCPI 142

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387264124 2241 IVHDEHGGVTAGTFCALTTLMHQLEK-ENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAV 2300
Cdd:cd14546    143 VVHCSDGAGRTGTYILIDMVLNRMAKgAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAV 203
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 2085-2298 2.91e-18

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


Pssm-ID: 350405 [Multi-domain]  Cd Length: 201  Bit Score: 85.26  E-value: 2.91e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2085 YINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDGQNMvspsghfwhflfRAEDEFVYWPNKDEPIN 2164
Cdd:cd14557      1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEG------------NRNKCAQYWPSMEEGSR 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2165 C-ESFKVTLMAEEHkClsnEEKLIMQDFILEATQDDYVLEVRHFQCPKWPN---PDSPiSKTFELISIIKEEAATRDGPM 2240
Cdd:cd14557     69 AfGDVVVKINEEKI-C---PDYIIRKLNINNKKEKGSGREVTHIQFTSWPDhgvPEDP-HLLLKLRRRVNAFNNFFSGPI 143

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1387264124 2241 IVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYK 2298
Cdd:cd14557    144 VVHCSAGVGRTGTYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 2031-2307 4.87e-18

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 87.36  E-value: 4.87e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2031 LEKQFKLLSQSNIQQSDYsTALKQCNREKNRTSSIIPVERSRVGISSLSGeGADYINASYIMGYYQSNEFIITQHPLLHT 2110
Cdd:PHA02742    28 LKEEHEHIMQEIVAFSCN-ESLELKNMKKCRYPDAPCFDRNRVILKIEDG-GDDFINASYVDGHNAKGRFICTQAPLEET 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2111 IQDFWRMIWDHNAQLVVMLP----DGQNMVSPsghFWHFLFRAedEFVYWPNKDEPINCESF---KVTLMaeehkCLSNe 2183
Cdd:PHA02742   106 ALDFWQAIFQDQVRVIVMITkimeDGKEACYP---YWMPHERG--KATHGEFKIKTKKIKSFrnyAVTNL-----CLTD- 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2184 eklimqdfileaTQDDYVLEVRHFQCPKWPNPDSP--ISKTFELISIIKEEAATRD-----------GPMIVHDEHGGVT 2250
Cdd:PHA02742   175 ------------TNTGASLDIKHFAYEDWPHGGLPrdPNKFLDFVLAVREADLKADvdikgenivkePPILVHCSAGLDR 242

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2251 AGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAVL---SLVSTR 2307
Cdd:PHA02742   243 AGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIFCYFIVLifaKLMADK 302
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 2085-2298 2.54e-17

PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein phosphatase non-receptor type 23 (PTPN23), also called His domain-containing protein tyrosine phosphatase (HD-PTP) or protein tyrosine phosphatase TD14 (PTP-TD14), is a catalytically inactive member of the tyrosine-specific protein tyrosine phosphatase (PTP) family. Human PTPN23 may be involved in the regulation of small nuclear ribonucleoprotein assembly and pre-mRNA splicing by modifying the survival motor neuron (SMN) complex. It plays a role in ciliogenesis and is part of endosomal sorting complex required for transport (ESCRT) pathways. PTPN23 contains five domains: a BRO1-like domain that plays a role in endosomal sorting; a V-domain that interacts with Lys63-linked polyubiquitinated substrates; a central proline-rich region that might recruit SH3-containing proteins; a PTP-like domain; and a proteolytic degradation-targeting motif, also known as a PEST sequence.


Pssm-ID: 350387 [Multi-domain]  Cd Length: 205  Bit Score: 82.82  E-value: 2.54e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2085 YINASYIMGYYQ-SNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDGQNMVSPSGHfwhflfraedefVYWP-NKDEP 2162
Cdd:cd14539      1 YINASLIEDLTPyCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVH------------RYWPtERGQA 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2163 INCESFKVTLMAEEHKCLSNEEklimqdfILEATQDDYVLE--VRHFQCPKWPNPDSPISKTfELISIIKE------EAA 2234
Cdd:cd14539     69 LVYGAITVSLQSVRTTPTHVER-------IISIQHKDTRLSrsVVHLQFTTWPELGLPDSPN-PLLRFIEEvhshylQQR 140

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1387264124 2235 TRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSM-DVYQVAKMINLMRPGVFADIEQYQFLYK 2298
Cdd:cd14539    141 SLQTPIVVHCSSGVGRTGAFCLLYAAVQEIEAGNGIpDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 2084-2302 1.20e-16

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; Tyrosine-protein phosphatase non-receptor type 3 (PTPN3) and type 4 (PTPN4) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN3 and PTPN4 are large modular proteins containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain. PTPN3 interacts with mitogen-activated protein kinase p38gamma and serves as its specific phosphatase. PTPN4 functions in TCR cell signaling, apoptosis, cerebellar synaptic plasticity, and innate immune responses.


Pssm-ID: 350389 [Multi-domain]  Cd Length: 212  Bit Score: 80.84  E-value: 1.20e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2084 DYINASY----IMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDGQNMVSPSGHfwhflfraedefVYWPNK 2159
Cdd:cd14541      1 DYINANYvnmeIPGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCH------------QYWPDL 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2160 DEPINCESFKVTLMAEEhkclsNEEKLIMQDFILEATQDDYVLEVRHFQCPKWPN---PDSPiSKTFELISIIKEEAATR 2236
Cdd:cd14541     69 GETMQFGNLQITCVSEE-----VTPSFAFREFILTNTNTGEERHITQMQYLAWPDhgvPDDS-SDFLDFVKRVRQNRVGM 142

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387264124 2237 DGPMIVHDEHG-GVTaGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAVLS 2302
Cdd:cd14541    143 VEPTVVHCSAGiGRT-GVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAILR 208
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 2084-2301 2.49e-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: 79.99  E-value: 2.49e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2084 DYINASYIMGYYQS----NEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDGQNMVSPSGHfwhflfraedefVYWPNK 2159
Cdd:cd14601      1 DYINANYINMEIPSssiiNRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCH------------QYWPEP 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2160 DEPINCESFKVTLMAEEhkclsNEEKLIMQDFILEATQDDYVLEVRHFQCPKWPN---PDSPiSKTFELISIIKEEAATR 2236
Cdd:cd14601     69 SGSSSYGGFQVTCHSEE-----GNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDhgvPDDS-SDFLDFVCLVRNKRAGK 142

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1387264124 2237 DGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAVL 2301
Cdd:cd14601    143 DEPVVVHCSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAIL 207
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 2048-2304 1.51e-15

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: 1.51e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2048 YSTALKQCNREKNRTSSIIPVERSRVGISSLSGEGADYINASYIMGYYQSNE--FIITQHPLLHTIQDFWRMIWDHNAQL 2125
Cdd:cd14599     30 FTTATLPENAERNRIREVVPYEENRVELVPTKENNTGYINASHIKVTVGGEEwhYIATQGPLPHTCHDFWQMVWEQGVNV 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2126 VVMLPDGQNMVSPSGHfwhflfraedefVYWPNKDEPINCES---FKVTL-MAEEHKC-----------LSNEEKlimqd 2190
Cdd:cd14599    110 IAMVTAEEEGGRSKSH------------RYWPKLGSKHSSATygkFKVTTkFRTDSGCyattglkvkhlLSGQER----- 172

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2191 fileatqddyvlEVRHFQCPKWPNPDSP------ISKTFELISIIKEEAATRDG------PMIVHDEHGGVTAGTFCALT 2258
Cdd:cd14599    173 ------------TVWHLQYTDWPDHGCPeevqgfLSYLEEIQSVRRHTNSMLDStkncnpPIVVHCSAGVGRTGVVILTE 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1387264124 2259 TLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAVLSLV 2304
Cdd:cd14599    241 LMIGCLEHNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQFL 286
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 2085-2301 4.50e-14

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: 73.64  E-value: 4.50e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2085 YINASYIMGYYQSNE--FIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDGQNmvspSGHfwhflfraEDEFVYWPNkdep 2162
Cdd:cd14540      1 YINASHITATVGGKQrfYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEE----GGR--------EKCFRYWPT---- 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2163 incesfkvtlMAEEHKCLSNEEKLIMQDF------------ILEATQDDYVLEVRHFQCPKWPN---PDSPisKTF---- 2223
Cdd:cd14540     65 ----------LGGEHDALTFGEYKVSTKFsvssgcytttglRVKHTLSGQSRTVWHLQYTDWPDhgcPEDV--SGFldfl 132

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2224 -ELISI---IKEEAAT--RDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLY 2297
Cdd:cd14540    133 eEINSVrrhTNQDVAGhnRNPPTLVHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVY 212


                   ....
gi 1387264124 2298 KAVL 2301
Cdd:cd14540    213 NVLI 216
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 2085-2297 9.41e-14

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: 72.50  E-value: 9.41e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2085 YINASYIMGYYQSN--EFIITQHPLLHTIQDFWRMIWDHNAQLVVMLP--DGQNMVSPSGHFWHFLFRAEDEFVYWPNKD 2160
Cdd:cd17658      1 YINASLVETPASESlpKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTrlVDNYSTAKCADYFPAEENESREFGRISVTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2161 EPINCESFKVTLMAEEHKCLSNEEKlimqdfileatqddyVLEVRHFQCPKWPN---PDS--PISKTFELISIIKEEAat 2235
Cdd:cd17658     81 KKLKHSQHSITLRVLEVQYIESEEP---------------PLSVLHIQYPEWPDhgvPKDtrSVRELLKRLYGIPPSA-- 143

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387264124 2236 rdGPMIVHDEHGGVTAGTFCAL-TTLMHQLEKENS-MDVYQVAKMINLMRPGVFADIEQYQFLY 2297
Cdd:cd17658    144 --GPIVVHCSAGIGRTGAYCTIhNTIRRILEGDMSaVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 1762-1991 1.84e-12

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: 68.97  E-value: 1.84e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1762 NRYINIvaydHSRVKLAqlaekDGKLtdyINANYVDGYNRPKAyIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKG 1841
Cdd:cd14559      1 NRFTNI----QTRVSTP-----VGKN---LNANRVQIGNKNVA-IACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQ 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1842 RRKCDQYWpvDGSEEYGNFLVTQKSIQVLAYYTVRNFTLRNTKIKKGSQKgrpsgRVVTQYHYTQWPDMG-VPEYSLPVL 1920
Cdd:cd14559     68 RKGLPPYF--RQSGTYGSVTVKSKKTGKDELVDGLKADMYNLKITDGNKT-----ITIPVVHVTNWPDHTaISSEGLKEL 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1921 T-FVRKASHAKRHAVGPV-------------VVHCSAGVGRTGTYIvldSMLQQIQHEGTVNVFGFLKHIRSQRN-YLVQ 1985
Cdd:cd14559    141 AdLVNKSAEEKRNFYKSKgssaindknkllpVIHCRAGVGRTGQLA---AAMELNKSPNNLSVEDIVSDMRTSRNgKMVQ 217


                   ....*.
gi 1387264124 1986 TEEQYV 1991
Cdd:cd14559    218 KDEQLD 223
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 2085-2304 2.99e-12

catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein phosphatase non-receptor type 21 (PTPN21), also called protein-tyrosine phosphatase D1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN21 is a component of a multivalent scaffold complex nucleated by focal adhesion kinase (FAK) at specific intracellular sites. It promotes cytoskeleton events that induce cell adhesion and migration by modulating Src-FAK signaling. It can also selectively associate with and stimulate Tec family kinases and modulate Stat3 activation. Human PTPN21 may also play a pathologic role in gastrointestinal tract tumorigenesis. PTPN21 contains an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350446 [Multi-domain]  Cd Length: 220  Bit Score: 68.46  E-value: 2.99e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2085 YINASYIMGYYQSNE--FIITQHPLLHTIQDFWRMIWDHNAQLVVMLpdgqNMVSPSGHfwhflfraEDEFVYWP---NK 2159
Cdd:cd14598      1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMV----TAEEEGGR--------EKSFRYWPrlgSR 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2160 DEPINCESFKVTLMAEEHKCLSNEEKLIMQDFIL--EATqddyvleVRHFQCPKWPNPDSP------ISKTFELISIIKE 2231
Cdd:cd14598     69 HNTVTYGRFKITTRFRTDSGCYATTGLKIKHLLTgqERT-------VWHLQYTDWPEHGCPedlkgfLSYLEEIQSVRRH 141

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387264124 2232 EAATRD-----GPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAVLSLV 2304
Cdd:cd14598    142 TNSTIDpkspnPPVLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFL 219
fn3 pfam00041
Fibronectin type III domain;
313-401 5.89e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 55.11  E-value: 5.89e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124  313 SEPENVQADPENYTSLLVTWERPRVVYDTmIEKFAVLYQQLEGEDQtKHEFLTDGYQDlGAILNNLLPNMSYVLQIVAIC 392
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGP-ITGYEVEYRPKNSGEP-WNEITVPGTTT-SVTLTGLKPGTEYEVRVQAVN 77


                   ....*....
gi 1387264124  393 TNGlYGKYS 401
Cdd:pfam00041   78 GGG-EGPPS 85
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
1901-1995 3.57e-08

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 54.59  E-value: 3.57e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1901 QYHYTQWPDMGVPEYSLpVLTFVRKAsHAKRHAVGPVVVHCSAGVGRTGT----YIVLDSM-LQQIqhegtvnvfgfLKH 1975
Cdd:COG2453     49 EYLHLPIPDFGAPDDEQ-LQEAVDFI-DEALREGKKVLVHCRGGIGRTGTvaaaYLVLLGLsAEEA-----------LAR 115

                           90       100
                   ....*....|....*....|
gi 1387264124 1976 IRSQRNYLVQTEEQYVFIHD 1995
Cdd:COG2453    116 VRAARPGAVETPAQRAFLER 135
PLN02179 PLN02179
carbonic anhydrase
 49-253 8.76e-08

carbonic anhydrase


Pssm-ID: 177835  Cd Length: 235  Bit Score: 55.37  E-value: 8.76e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124   49 WGKKYP---TCNSPK-QSPInideDLTQVNVNLkkLKFQDWDKT-SLENTFIHNTGKTVEINLTNDyrlsGG---VSETV 120
Cdd:PLN02179    50 WGKLNPqwkVCSTGKyQSPI----DLTDERVSL--IHDQALSRHyKPAPAVIQSRGHDVMVSWKGD----AGkitIHQTD 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124  121 FKAskIAFHWgkcnmsSDGSEHSLEGQKFPLEMQIYCFDAdrfssfeeaikgKGKLRALSILFEVGiEENLDYKAIIDGV 200
Cdd:PLN02179   120 YKL--VQCHW------HSPSEHTINGTSYDLELHMVHTSA------------SGKTAVVGVLYKLG-EPDEFLTKLLNGI 178

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1387264124  201 ERVsrfGKQ----AALDPFTLlnllPNSTDKYYTYNGSLTSPPCTDTVDWIIFKDTV 253
Cdd:PLN02179   179 KGV---GKKeinlGIVDPRDI----RFETNNFYRYIGSLTIPPCTEGVIWTVVKRVV 228
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 1935-1995 7.33e-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: 50.04  E-value: 7.33e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387264124 1935 GPVVVHCSAGVGRTGTYIVLDSMLQQIqhegtVNVFGFLKHIRSQR-NYLVQTEEQYVFIHD 1995
Cdd:cd14494     57 EPVLVHCKAGVGRTGTLVACYLVLLGG-----MSAEEAVRIVRLIRpGGIPQTIEQLDFLIK 113
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 2053-2305 1.34e-06

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 52.66  E-value: 1.34e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2053 KQCNREKNRT---SSIIPVER---SRVGISSlsgeGADYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLV 2126
Cdd:PHA02740    44 KACAQAENKAkdeNLALHITRllhRRIKLFN----DEKVLDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQII 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2127 VM---LPDGQNMVSpsghfwhflfraedefvYWPNKDEP-INCESFKVTLMAEEHKCLSNEEKLIMQDfileatQDDYVL 2202
Cdd:PHA02740   120 VLisrHADKKCFNQ-----------------FWSLKEGCvITSDKFQIETLEIIIKPHFNLTLLSLTD------KFGQAQ 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 2203 EVRHFQCPKWP------NPDSPISKTFELISII----KEEAATRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDV 2272
Cdd:PHA02740   177 KISHFQYTAWPadgfshDPDAFIDFFCNIDDLCadleKHKADGKIAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSI 256

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1387264124 2273 YQVAKMINLMRPGVFADIEQYQFLYKAVLSLVS 2305
Cdd:PHA02740   257 ANALKKVRQKKYGCMNCLDDYVFCYHLIAAYLK 289
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 1900-1995 2.72e-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: 2.72e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1900 TQYHYTqWPDMGVP---EYSLPVLTFVRKASHAKRHavgpVVVHCSAGVGRTGTyiVLDSMLQQIQheGTVNVFGFLKHI 1976
Cdd:cd14505     74 TWHHLP-IPDGGVPsdiAQWQELLEELLSALENGKK----VLIHCKGGLGRTGL--IAACLLLELG--DTLDPEQAIAAV 144

                           90
                   ....*....|....*....
gi 1387264124 1977 RSQRNYLVQTEEQYVFIHD 1995
Cdd:cd14505    145 RALRPGAIQTPKQENFLHQ 163
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 1902-1995 2.73e-05

protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine phosphatase domain-containing protein 1 (PTPDC1) is an uncharacterized non-receptor class protein-tyrosine phosphatase (PTP). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Small interfering RNA (siRNA) knockdown of the ptpdc1 gene is associated with elongated cilia.


Pssm-ID: 350356 [Multi-domain]  Cd Length: 206  Bit Score: 47.34  E-value: 2.73e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1902 YHYT-QWPDMGVPEYSLpVLTFVRKASHAKRHAvGPVVVHCSAGVGRTG----TYIVldsMLQQIQHEGTVnvfgflKHI 1976
Cdd:cd14506     78 YFYNfGWKDYGVPSLTT-ILDIVKVMAFALQEG-GKVAVHCHAGLGRTGvliaCYLV---YALRMSADQAI------RLV 146

                           90
                   ....*....|....*....
gi 1387264124 1977 RSQRNYLVQTEEQYVFIHD 1995
Cdd:cd14506    147 RSKRPNSIQTRGQVLCVRE 165
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 313-406 3.39e-05

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: 44.41  E-value: 3.39e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124  313 SEPENVQADPENYTSLLVTWERPRvVYDTMIEKFAVLYQQLEGEDQTKHEflTDGYQDLGAILNNLLPNMSYVLQIVAIC 392
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPPE-DDGGPITGYVVEYREKGSGDWKEVE--VTPGSETSYTLTGLKPGTEYEFRVRAVN 78

                           90
                   ....*....|....
gi 1387264124  393 TNGlYGKYSDQLIV 406
Cdd:cd00063     79 GGG-ESPPSESVTV 91
PLN02202 PLN02202
carbonate dehydratase
 1-263 4.34e-05

carbonate dehydratase


Pssm-ID: 177853 [Multi-domain]  Cd Length: 284  Bit Score: 47.74  E-value: 4.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124    1 MLILKRFLACIQLLCVCRLDwiygyyrqqrKLVEEIGWSYTGALNQKNWGKKYP---TCNSPK-QSPINIDEDLTQVNVN 76
Cdd:PLN02202     4 MMMIKLCFFAIALICIAPAD----------AQTEGVVFGYKGKNGPNQWGHLNPhftKCAVGKlQSPIDIQRRQIFYNHK 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124   77 LKKLKfQDWdktslentfiHNTGKTVEINLTNDYRLSGGVSETVFKASK----IAFHWgkcnmsSDGSEHSLEGQKFPLE 152
Cdd:PLN02202    74 LESIH-RDY----------YFTNATLVNHVCNVAMFFGEGAGDVIIDNKnytlLQMHW------HTPSEHHLHGVQYAAE 136

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124  153 MQIYCFDADrfssfeeaikgkGKLRALSILFEVGIEE----NLDYKAIIDGVERVSrfGKQAALDPFTLLNL--LPNSTD 226
Cdd:PLN02202   137 LHMVHQAKD------------GSFAVVASLFKIGTEEpflsQMKDKLVKLKEERFK--GNHTAQVEVGKIDTrhIERKTR 202

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1387264124  227 KYYTYNGSLTSPPCTDTVDWIIFKDTVSISESQLAVF 263
Cdd:PLN02202   203 KYFRYIGSLTTPPCSENVSWTILGKVRSMSKEQVELL 239
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 313-395 5.51e-05

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: 43.76  E-value: 5.51e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124   313 SEPENVQADPENYTSLLVTWERPRvvyDTMIEKFAVLYQQLEGEDQTKHEFLTDGYQDLGAILNNLLPNMSYVLQIVAIC 392
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPP---DDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78


                    ...
gi 1387264124   393 TNG 395
Cdd:smart00060   79 GAG 81
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 1901-1993 7.52e-05

dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as VH1-like phosphatase Z (VHZ) or low molecular mass dual specificity phosphatase 3 (LDP-3), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. DUSP23 is an atypical DUSP; it contains the catalytic dual specificity phosphatase domain but lacks the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. It is able to enhance activation of JNK and p38 MAPK, and has been shown to dephosphorylate p44-ERK1 (MAPK3) in vitro. It has been associated with cell growth and human primary cancers. It has also been identified as a cell-cell adhesion regulatory protein; it promotes the dephosphorylation of beta-catenin at Tyr 142 and enhances the interaction between alpha- and beta-catenin.


Pssm-ID: 350354 [Multi-domain]  Cd Length: 142  Bit Score: 44.96  E-value: 7.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264124 1901 QYHYTQWPDMGVPEYSL--PVLTFVRKAShakrhAVG-PVVVHCSAGVGRTGT----YIVLDSMLQQIQHegtvnvfgfL 1973
Cdd:cd14504     51 RYHHIPIEDYTPPTLEQidEFLDIVEEAN-----AKNeAVLVHCLAGKGRTGTmlacYLVKTGKISAVDA---------I 116

                           90       100
                   ....*....|....*....|
gi 1387264124 1974 KHIRSQRNYLVQTEEQYVFI 1993
Cdd:cd14504    117 NEIRRIRPGSIETSEQEKFV 136
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
1935-1979 5.40e-03

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 39.57  E-value: 5.40e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 1387264124  1935 GPVVVHCSAGVGRTGTYIVldSMLQQIQHEGTVNVFGFLKHIRSQ 1979
Cdd:smart00195   79 GKVLVHCQAGVSRSATLII--AYLMKTRNMSLNDAYDFVKDRRPI 121
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 1908-1952 6.58e-03

C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division control protein 14 (CDC14) family is highly conserved in all eukaryotes, although the roles of its members seem to have diverged during evolution. Yeast Cdc14, the best characterized member of this family, is a dual-specificity phosphatase that plays key roles in cell cycle control. It preferentially dephosphorylates cyclin-dependent kinase (CDK) targets, which makes it the main antagonist of CDK in the cell. Cdc14 functions at the end of mitosis and it triggers the events that completely eliminates the activity of CDK and other mitotic kinases. It is also involved in coordinating the nuclear division cycle with cytokinesis through the cytokinesis checkpoint, and in chromosome segregation. Cdc14 phosphatases also function in DNA replication, DNA damage checkpoint, and DNA repair. Vertebrates may contain more than one Cdc14 homolog; humans have three (CDC14A, CDC14B, and CDC14C). CDC14 family proteins contain a highly conserved N-terminal pseudophosphatase domain that contributes to substrate specificity and a C-terminal catalytic dual-specificity phosphatase domain with the PTP signature motif.


Pssm-ID: 350349 [Multi-domain]  Cd Length: 174  Bit Score: 39.74  E-value: 6.58e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1387264124 1908 PDMGVPEYSLpVLTFVRKASHAKrhavGPVVVHCSAGVGRTGTYI 1952
Cdd:cd14499     88 PDGSTPSDDI-VKKFLDICENEK----GAIAVHCKAGLGRTGTLI 127
 
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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