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Conserved domains on  [gi|300795888|ref|NP_001179201|]
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receptor-type tyrosine-protein phosphatase zeta precursor [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 ...
 1726-2003 3.46e-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: 3.46e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1726 FTEEFEtlkefyqEVQSCTVDLGITADSSNHPDNKHKNRYINIVAYDHSRVKLAQLAEKDGKLTDYINANYVDGYNRPKA 1805
Cdd:cd17667     1 FSEDFE-------EVQRCTADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSKHSDYINANYVDGYNKAKA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1806 YIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPVDGSEEYGNFLVTQKSIQVLAYYTVRNFTLRNTK 1885
Cdd:cd17667    74 YIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTK 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1886 IKKGSQ---KGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQI 1962
Cdd:cd17667   154 VKKGQKgnpKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQI 233

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 300795888 1963 QHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDALVEAIL 2003
Cdd:cd17667   234 KDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 274
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 2086-2289 1.39e-152

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: 470.25  E-value: 1.39e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2086 YINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDGQNMAEDEFVYWPNKDEPINCESFKVTLMAEEH 2165
Cdd:cd17669     1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFVYWPNKDEPINCETFKVTLIAEEH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2166 KCLSNEEKLIMQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTFELISIIKEEAATRDGPMIVHDEHGGVTAGTFCAL 2245
Cdd:cd17669    81 KCLSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTFELISIIKEEAANRDGPMIVHDEHGGVTAGTFCAL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 300795888 2246 TTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAVL 2289
Cdd:cd17669   161 TTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
alpha_CARP_receptor_like cd03122
Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related ...
 45-298 7.38e-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: 356.28  E-value: 7.38e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888   45 NQKNWGKKYPTCNS-PKQSPINIDEDlTQVNVN-LKKLKFQDWDKTSLEnTFIHNTGKTVEINLTN---DYRLSGGVSET 119
Cdd:cd03122     1 NPKHWAKKYPACGEgRQQSPIDIVED-TQVQRQgLQPLHFDGYEELTAS-TTLENTGKTVILRLEGnssDPFVSGGPLLG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888  120 VFKASKIAFHWGKCNmsSDGSEHSLEGQKFPLEMQIYCFDADRFSSFEeAIKGKGKLRALSILFEVGIEENLDYKAIIDG 199
Cdd:cd03122    79 RYKFSEITFHWGTCN--SDGSEHSIDGHKFPLEMQILHRNTDFFDSFE-AIKSPGGVLALAYLFELSHEDNPFLDPIIEG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888  200 VERVSRFGKQAALDPFTLLNLLPNSTDKYYTYNGSLTSPPCTDTVDWIIFKDTVSISESQLAVFCEVLTMQQSGyVMLMD 279
Cdd:cd03122   156 LRNVSRPGKEVELPPFPLSDLLPPFTDKYYSYEGSLTTPPCSETVEWIVFREPVPISSRQLEAFRELLTRRQDG-VMSGD 234

                         250
                  ....*....|....*....
gi 300795888  280 YLQNNFREQQYKFSRQVFS 298
Cdd:cd03122   235 YLPNNGRPQQPLGSRTVFS 253
fn3 pfam00041
Fibronectin type III domain;
313-401 5.98e-09

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 54.73  E-value: 5.98e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888   313 SEPENVQADPENYTSLLVTWERPRVVYDTmIEKFAVLYQQLEGEDQtKHEFLTDGYQDlGAILNNLLPNMSYVLQIVAIC 392
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGP-ITGYEVEYRPKNSGEP-WNEITVPGTTT-SVTLTGLKPGTEYEVRVQAVN 77


                   ....*....
gi 300795888   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 ...
 1726-2003 3.46e-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: 3.46e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1726 FTEEFEtlkefyqEVQSCTVDLGITADSSNHPDNKHKNRYINIVAYDHSRVKLAQLAEKDGKLTDYINANYVDGYNRPKA 1805
Cdd:cd17667     1 FSEDFE-------EVQRCTADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSKHSDYINANYVDGYNKAKA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1806 YIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPVDGSEEYGNFLVTQKSIQVLAYYTVRNFTLRNTK 1885
Cdd:cd17667    74 YIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTK 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1886 IKKGSQ---KGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQI 1962
Cdd:cd17667   154 VKKGQKgnpKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQI 233

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 300795888 1963 QHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDALVEAIL 2003
Cdd:cd17667   234 KDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 274
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 2086-2289 1.39e-152

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: 470.25  E-value: 1.39e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2086 YINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDGQNMAEDEFVYWPNKDEPINCESFKVTLMAEEH 2165
Cdd:cd17669     1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFVYWPNKDEPINCETFKVTLIAEEH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2166 KCLSNEEKLIMQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTFELISIIKEEAATRDGPMIVHDEHGGVTAGTFCAL 2245
Cdd:cd17669    81 KCLSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTFELISIIKEEAANRDGPMIVHDEHGGVTAGTFCAL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 300795888 2246 TTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAVL 2289
Cdd:cd17669   161 TTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1725-2000 2.71e-119

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 377.77  E-value: 2.71e-119
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888   1725 GFTEEFETLKEFYQEVQSCTVdlgitadsSNHPDNKHKNRYINIVAYDHSRVKLAQLaekDGKLTDYINANYVDGYNRPK 1804
Cdd:smart00194    1 GLEEEFEKLDRLKPDDESCTV--------AAFPENRDKNRYKDVLPYDHTRVKLKPP---PGEGSDYINASYIDGPNGPK 69

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888   1805 AYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPVDGSE--EYGNFLVTQKSIQVLAYYTVRNFTLR 1882
Cdd:smart00194   70 AYIATQGPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEplTYGDITVTLKSVEKVDDYTIRTLEVT 149

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888   1883 NTkikkgsqkGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQI 1962
Cdd:smart00194  150 NT--------GCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQL 221

                           250       260       270
                    ....*....|....*....|....*....|....*...
gi 300795888   1963 QHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDALVE 2000
Cdd:smart00194  222 EAGKEVDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1759-2000 2.75e-113

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 359.25  E-value: 2.75e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888  1759 NKHKNRYINIVAYDHSRVKLaqlaEKDGKLTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNL 1838
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKL----TGDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTEL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888  1839 VEKGRRKCDQYWP--VDGSEEYGNFLVTQKSI-QVLAYYTVRNFTLRNtkikkgsqKGRPSGRVVTQYHYTQWPDMGVPE 1915
Cdd:pfam00102   77 EEKGREKCAQYWPeeEGESLEYGDFTVTLKKEkEDEKDYTVRTLEVSN--------GGSEETRTVKHFHYTGWPDHGVPE 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888  1916 YSLPVLTFVRKASHAKRHA-VGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFI 1994
Cdd:pfam00102  149 SPNSLLDLLRKVRKSSLDGrSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFL 228


                   ....*.
gi 300795888  1995 HDALVE 2000
Cdd:pfam00102  229 YDAILE 234
alpha_CARP_receptor_like cd03122
Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related ...
 45-298 7.38e-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: 356.28  E-value: 7.38e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888   45 NQKNWGKKYPTCNS-PKQSPINIDEDlTQVNVN-LKKLKFQDWDKTSLEnTFIHNTGKTVEINLTN---DYRLSGGVSET 119
Cdd:cd03122     1 NPKHWAKKYPACGEgRQQSPIDIVED-TQVQRQgLQPLHFDGYEELTAS-TTLENTGKTVILRLEGnssDPFVSGGPLLG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888  120 VFKASKIAFHWGKCNmsSDGSEHSLEGQKFPLEMQIYCFDADRFSSFEeAIKGKGKLRALSILFEVGIEENLDYKAIIDG 199
Cdd:cd03122    79 RYKFSEITFHWGTCN--SDGSEHSIDGHKFPLEMQILHRNTDFFDSFE-AIKSPGGVLALAYLFELSHEDNPFLDPIIEG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888  200 VERVSRFGKQAALDPFTLLNLLPNSTDKYYTYNGSLTSPPCTDTVDWIIFKDTVSISESQLAVFCEVLTMQQSGyVMLMD 279
Cdd:cd03122   156 LRNVSRPGKEVELPPFPLSDLLPPFTDKYYSYEGSLTTPPCSETVEWIVFREPVPISSRQLEAFRELLTRRQDG-VMSGD 234

                         250
                  ....*....|....*....
gi 300795888  280 YLQNNFREQQYKFSRQVFS 298
Cdd:cd03122   235 YLPNNGRPQQPLGSRTVFS 253
Carb_anhydrase smart01057
Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse ...
 38-295 1.54e-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: 283.44  E-value: 1.54e-86
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888     38 WSYTGALNQKNWGKKYPT-CNSPKQSPINIDEDLTQVNVNLKKLKFqDWDKTSleNTFIHNTGKTVEINL-TNDYRLSGG 115
Cdd:smart01057    1 WGYEGKNGPEHWGKLDPPfCGGKRQSPIDIVTAEAQYDPSLKPLKL-SYDQPT--AKRILNNGHTVQVNFdDDGSTLSGG 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888    116 VSETVFKASKIAFHWGKCNmsSDGSEHSLEGQKFPLEMQIYCFDADrfSSFEEAIKGKGKLRALSILFEVGIEENLDYKA 195
Cdd:smart01057   78 PLPGRYRLKQFHFHWGGSD--SEGSEHTIDGKRFPLELHLVHYNSK--GSFSEAVSKPGGLAVVAVFFKVGAEENPALQA 153

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888    196 IIDGVERVSRFGKQAALDPFTLLNLLPNSTDKYYTYNGSLTSPPCTDTVDWIIFKDTVSISESQLAVFCEVLTMQQSgyv 275
Cdd:smart01057  154 ILDHLPLIKYKGQETELTPFDLSSLLPASTRHYYTYNGSLTTPPCSEGVTWIVFKEPITISTEQLEKFRTLLPMEGN--- 230

                           250       260
                    ....*....|....*....|
gi 300795888    276 mlmDYLQNNFREQQYKFSRQ 295
Cdd:smart01057  231 ---EPLVNNARPLQPLNGRV 247
Carb_anhydrase pfam00194
Eukaryotic-type carbonic anhydrase;
44-300 7.14e-85

Eukaryotic-type carbonic anhydrase;


Pssm-ID: 459707 [Multi-domain]  Cd Length: 252  Bit Score: 278.77  E-value: 7.14e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888    44 LNQKNWGKKYPTCNSPKQSPINIDEDLTQVNVNLKKLKFQDWDKTSLENTfIHNTGKTVEINLTNDYR--LSGGVSETVF 121
Cdd:pfam00194    1 LGPEHWGKVYPSCGGKRQSPINIDTRKVRYDPSLPPLTFQGYDVPPGKNT-LTNNGHTVQVSLDDGDPstISGGPLATRY 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888   122 KASKIAFHWGKCNmsSDGSEHSLEGQKFPLEMQIYCFDADRfSSFEEAIKGKGKLRALSILFEVGIEENLDYKAIIDGVE 201
Cdd:pfam00194   80 RLVQFHFHWGSTD--SRGSEHTIDGKRYPAELHIVHYNSKY-KSFDEAAKHPDGLAVLGVFFEVGDENNPYLQPIVSALD 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888   202 RVSRFGKQAALDPFTLLNLLPNSTDKYYTYNGSLTSPPCTDTVDWIIFKDTVSISESQLAVFCEVLTMQQSGYvmlMDYL 281
Cdd:pfam00194  157 NIKYKGKSVLLPPFDLSDLLPEDLTSYYTYNGSLTTPPCSESVTWIVFKEPISISEEQLEAFRTLLFSDGGEE---PRPL 233

                          250
                   ....*....|....*....
gi 300795888   282 QNNFREQQYKFSRQVFSSY 300
Cdd:pfam00194  234 VNNFRPTQPLNGRVVFASF 252
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
2031-2289 3.91e-77

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 256.82  E-value: 3.91e-77
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888   2031 KLEKQFKLLSQSNIQQSDYSTALKQCNREKNRTSSIIPVERSRVGISSLSGEGADYINASYIMGYYQSNEFIITQHPLLH 2110
Cdd:smart00194    1 GLEEEFEKLDRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGPLPS 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888   2111 TIQDFWRMIWDHNAQLVVML-PDGQNMAEDEFVYWPNK-DEPINCESFKVTLMAEEHKclsneEKLIMQDFILEATQDDY 2188
Cdd:smart00194   81 TVEDFWRMVWEQKVTVIVMLtELVEKGREKCAQYWPDEeGEPLTYGDITVTLKSVEKV-----DDYTIRTLEVTNTGCSE 155

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888   2189 VLEVRHFQCPKWP---NPDSPISkTFELISIIKEEAATRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAK 2265
Cdd:smart00194  156 TRTVTHYHYTNWPdhgVPESPES-ILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVK 234

                           250       260
                    ....*....|....*....|....
gi 300795888   2266 MINLMRPGVFADIEQYQFLYKAVL 2289
Cdd:smart00194  235 ELRSQRPGMVQTEEQYIFLYRAIL 258
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
2057-2289 5.95e-75

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 249.47  E-value: 5.95e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888  2057 NREKNRTSSIIPVERSRVGISSLSGeGADYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDGQNM 2136
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPG-PSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888  2137 A-EDEFVYWPNK-DEPINCESFKVTLMAEEhkclSNEEKLIMQDFILEATQDDYVLEVRHFQCPKWPN---PDSPISkTF 2211
Cdd:pfam00102   80 GrEKCAQYWPEEeGESLEYGDFTVTLKKEK----EDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDhgvPESPNS-LL 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300795888  2212 ELISIIKE-EAATRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAVL 2289
Cdd:pfam00102  155 DLLRKVRKsSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233
PHA02738 PHA02738
hypothetical protein; Provisional
 1731-2009 5.90e-54

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 192.45  E-value: 5.90e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1731 ETLKEFYQEVQSCTVDLGITADSSNhpdnKHKNRYINIVAYDHSRVKLAqlAEKDgkLTDYINANYVDGYNRPKAYIAAQ 1810
Cdd:PHA02738   25 EVITREHQKVISEKVDGTFNAEKKN----RKLNRYLDAVCFDHSRVILP--AERN--RGDYINANYVDGFEYKKKFICGQ 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1811 GPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWP-VDGSE-EYGNFLVTQKSIQVLAYYTVRNFTLRNtkikk 1888
Cdd:PHA02738   97 APTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSdVEQGSiRFGKFKITTTQVETHPHYVKSTLLLTD----- 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1889 gsqkGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFV------RKASHAKRHAVG-------PVVVHCSAGVGRTGTYIVL 1955
Cdd:PHA02738  172 ----GTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVlevrqcQKELAQESLQIGhnrlqppPIVVHCNAGLGRTPCYCVV 247

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 300795888 1956 DSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDALVEAILSKETEV 2009
Cdd:PHA02738  248 DISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAVKRYVNLTVNKV 301
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
1734-1994 5.69e-40

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 150.63  E-value: 5.69e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1734 KEFYQEVQSCTVDLGITADSSNHPDN---KHKNRYINIVAYDHSRVklaqlaEKDGKltdYINANYVDGYNrPKAYIAAQ 1810
Cdd:COG5599    14 EKINSRLSTLTNELAPSHNDPQYLQNingSPLNRFRDIQPYKETAL------RANLG---YLNANYIQVIG-NHRYIATQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1811 GPLKSTAEDFWRMIWEHNVEVIVMITNLVE--KGRRKCDQYWPVDGseEYGNFLVTQKSIQVlaYYTVRNFTLRNTKIK- 1887
Cdd:COG5599    84 YPLEEQLEDFFQMLFDNNTPVLVVLASDDEisKPKVKMPVYFRQDG--EYGKYEVSSELTES--IQLRDGIEARTYVLTi 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1888 KGS-QKGRPsgrvVTQYHYTQWPDMGVP--EYSLPVLTFVRKASHAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQ- 1963
Cdd:COG5599   160 KGTgQKKIE----IPVLHVKNWPDHGAIsaEALKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINa 235

                         250       260       270
                  ....*....|....*....|....*....|...
gi 300795888 1964 -HEGTVNVFGFLKHIRSQRNY-LVQTEEQYVFI 1994
Cdd:COG5599   236 lVQITLSVEEIVIDMRTSRNGgMVQTSEQLDVL 268
Cah COG3338
Carbonic anhydrase [Inorganic ion transport and metabolism];
38-263 1.01e-31

Carbonic anhydrase [Inorganic ion transport and metabolism];


Pssm-ID: 442567 [Multi-domain]  Cd Length: 247  Bit Score: 125.77  E-value: 1.01e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888   38 WSYTGALNQKNWGK---KYPTCNS-PKQSPINIDedlTQVNVNLKKLKFqDWDKTSLEntfIHNTGKTVEINLTNDYRLS 113
Cdd:COG3338    28 WSYEGETGPEHWGElspEFATCATgKNQSPIDIR---TAIKADLPPLKF-DYKPTPLE---IVNNGHTIQVNVDPGSTLT 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888  114 ggVSETVFKASKIAFHwgkcnmssDGSEHSLEGQKFPLEMQiycF---DADrfssfeeaikgkGKLRALSILFEVGiEEN 190
Cdd:COG3338   101 --VDGKRYELKQFHFH--------TPSEHTINGKSYPMEAH---LvhkDAD------------GELAVVGVLFEEG-AEN 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300795888  191 ldykAIIDGVERV--SRFGKQAALD-PFTLLNLLPNSTDkYYTYNGSLTSPPCTDTVDWIIFKDTVSISESQLAVF 263
Cdd:COG3338   155 ----PALAKLWANlpLEAGEEVALDaTIDLNDLLPEDRS-YYRYSGSLTTPPCSEGVLWIVLKQPITVSAEQIEAF 225
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 2050-2288 2.25e-28

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 118.21  E-value: 2.25e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2050 STALKQCNREKNRTSSIIPVERSRVGISS------------------LSGEGAD--YINASYIMGYYQSNEFIITQHPLL 2109
Cdd:PHA02746   44 NHFLKKENLKKNRFHDIPCWDHSRVVINAheslkmfdvgdsdgkkieVTSEDNAenYIHANFVDGFKEANKFICAQGPKE 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2110 HTIQDFWRMIWDHNAQLVVMLPDGQNMAEDEFVYWPN-KDEPINCESFKVTLMAEEHKCLSNEEKLIMQDFILEATQddy 2188
Cdd:PHA02746  124 DTSEDFFKLISEHESQVIVSLTDIDDDDEKCFELWTKeEDSELAFGRFVAKILDIIEELSFTKTRLMITDKISDTSR--- 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2189 vlEVRHFQCPKWP---NPDSPiSKTFELISIIKEEAA----------TRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKE 2255
Cdd:PHA02746  201 --EIHHFWFPDWPdngIPTGM-AEFLELINKVNEEQAelikqadndpQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKE 277

                         250       260       270
                  ....*....|....*....|....*....|...
gi 300795888 2256 NSMDVYQVAKMINLMRPGVFADIEQYQFLYKAV 2288
Cdd:PHA02746  278 KEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
fn3 pfam00041
Fibronectin type III domain;
313-401 5.98e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 54.73  E-value: 5.98e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888   313 SEPENVQADPENYTSLLVTWERPRVVYDTmIEKFAVLYQQLEGEDQtKHEFLTDGYQDlGAILNNLLPNMSYVLQIVAIC 392
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGP-ITGYEVEYRPKNSGEP-WNEITVPGTTT-SVTLTGLKPGTEYEVRVQAVN 77


                   ....*....
gi 300795888   393 TNGlYGKYS 401
Cdd:pfam00041   78 GGG-EGPPS 85
PLN02179 PLN02179
carbonic anhydrase
 49-253 7.24e-08

carbonic anhydrase


Pssm-ID: 177835  Cd Length: 235  Bit Score: 55.76  E-value: 7.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888   49 WGKKYP---TCNSPK-QSPInideDLTQVNVNLkkLKFQDWDKT-SLENTFIHNTGKTVEINLTNDyrlsGG---VSETV 120
Cdd:PLN02179   50 WGKLNPqwkVCSTGKyQSPI----DLTDERVSL--IHDQALSRHyKPAPAVIQSRGHDVMVSWKGD----AGkitIHQTD 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888  121 FKAskIAFHWgkcnmsSDGSEHSLEGQKFPLEMQIYCFDAdrfssfeeaikgKGKLRALSILFEVGiEENLDYKAIIDGV 200
Cdd:PLN02179  120 YKL--VQCHW------HSPSEHTINGTSYDLELHMVHTSA------------SGKTAVVGVLYKLG-EPDEFLTKLLNGI 178

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 300795888  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 3.44e-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: 3.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888  313 SEPENVQADPENYTSLLVTWERPRvVYDTMIEKFAVLYQQLEGEDQTKHEflTDGYQDLGAILNNLLPNMSYVLQIVAIC 392
Cdd:cd00063     2 SPPTNLRVTDVTSTSVTLSWTPPE-DDGGPITGYVVEYREKGSGDWKEVE--VTPGSETSYTLTGLKPGTEYEFRVRAVN 78

                          90
                  ....*....|....
gi 300795888  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 5.49e-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: 5.49e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888    313 SEPENVQADPENYTSLLVTWERPRvvyDTMIEKFAVLYQQLEGEDQTKHEFLTDGYQDLGAILNNLLPNMSYVLQIVAIC 392
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPP---DDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78


                    ...
gi 300795888    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 ...
 1726-2003 3.46e-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: 3.46e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1726 FTEEFEtlkefyqEVQSCTVDLGITADSSNHPDNKHKNRYINIVAYDHSRVKLAQLAEKDGKLTDYINANYVDGYNRPKA 1805
Cdd:cd17667     1 FSEDFE-------EVQRCTADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSKHSDYINANYVDGYNKAKA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1806 YIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPVDGSEEYGNFLVTQKSIQVLAYYTVRNFTLRNTK 1885
Cdd:cd17667    74 YIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTK 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1886 IKKGSQ---KGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQI 1962
Cdd:cd17667   154 VKKGQKgnpKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQI 233

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 300795888 1963 QHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDALVEAIL 2003
Cdd:cd17667   234 KDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 274
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 1791-1999 6.60e-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: 6.60e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1791 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPVDGSEEYGNFLVTQKSIQV 1870
Cdd:cd17668     1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1871 LAYYTVRNFTLRNTKIKKGSQKGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAKRHAVGPVVVHCSAGVGRTG 1950
Cdd:cd17668    81 LAYYTVRNFTLRNTKIKKGSQKGRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVGPVVVHCSAGVGRTG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 300795888 1951 TYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDALV 1999
Cdd:cd17668   161 TYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 2086-2289 1.39e-152

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: 470.25  E-value: 1.39e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2086 YINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDGQNMAEDEFVYWPNKDEPINCESFKVTLMAEEH 2165
Cdd:cd17669     1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFVYWPNKDEPINCETFKVTLIAEEH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2166 KCLSNEEKLIMQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTFELISIIKEEAATRDGPMIVHDEHGGVTAGTFCAL 2245
Cdd:cd17669    81 KCLSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTFELISIIKEEAANRDGPMIVHDEHGGVTAGTFCAL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 300795888 2246 TTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAVL 2289
Cdd:cd17669   161 TTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 1791-1996 2.83e-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: 2.83e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1791 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPVDGSEEYGNFLVTQKSIQV 1870
Cdd:cd14549     1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTETYGNIQVTLLSTEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1871 LAYYTVRNFTLRNTKIKKGsqKGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAKRHAVGPVVVHCSAGVGRTG 1950
Cdd:cd14549    81 LATYTVRTFSLKNLKLKKV--KGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAGVGRTG 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 300795888 1951 TYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHD 1996
Cdd:cd14549   159 TYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 2086-2290 2.15e-127

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: 398.67  E-value: 2.15e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2086 YINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDGQNMAEDEFVYWPNKDEPINCESFKVTLMAEEH 2165
Cdd:cd17670     1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQGLAEDEFVYWPSREESMNCEAFTVTLISKDR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2166 KCLSNEEKLIMQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTFELISIIKEEAATRDGPMIVHDEHGGVTAGTFCAL 2245
Cdd:cd17670    81 LCLSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISSTFELINVIKEEALTRDGPTIVHDEFGAVSAGTLCAL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 300795888 2246 TTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAVLS 2290
Cdd:cd17670   161 TTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAMLS 205
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 2086-2286 4.09e-125

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: 391.68  E-value: 4.09e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2086 YINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDGQnMAEDEFVYWPNKDEPINCESFKVTLMAEEH 2165
Cdd:cd14550     1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNE-LNEDEPIYWPTKEKPLECETFKVTLSGEDH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2166 KCLSNEEKLIMQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTFELISIIKEEAATRDGPMIVHDEHGGVTAGTFCAL 2245
Cdd:cd14550    80 SCLSNEIRLIVRDFILESTQDDYVLEVRQFQCPSWPNPCSPIHTVFELINTVQEWAQQRDGPIVVHDRYGGVQAATFCAL 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 300795888 2246 TTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYK 2286
Cdd:cd14550   160 TTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1725-2000 2.71e-119

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 377.77  E-value: 2.71e-119
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888   1725 GFTEEFETLKEFYQEVQSCTVdlgitadsSNHPDNKHKNRYINIVAYDHSRVKLAQLaekDGKLTDYINANYVDGYNRPK 1804
Cdd:smart00194    1 GLEEEFEKLDRLKPDDESCTV--------AAFPENRDKNRYKDVLPYDHTRVKLKPP---PGEGSDYINASYIDGPNGPK 69

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888   1805 AYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPVDGSE--EYGNFLVTQKSIQVLAYYTVRNFTLR 1882
Cdd:smart00194   70 AYIATQGPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEplTYGDITVTLKSVEKVDDYTIRTLEVT 149

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888   1883 NTkikkgsqkGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQI 1962
Cdd:smart00194  150 NT--------GCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQL 221

                           250       260       270
                    ....*....|....*....|....*....|....*...
gi 300795888   1963 QHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDALVE 2000
Cdd:smart00194  222 EAGKEVDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1759-2000 2.75e-113

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 359.25  E-value: 2.75e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888  1759 NKHKNRYINIVAYDHSRVKLaqlaEKDGKLTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNL 1838
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKL----TGDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTEL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888  1839 VEKGRRKCDQYWP--VDGSEEYGNFLVTQKSI-QVLAYYTVRNFTLRNtkikkgsqKGRPSGRVVTQYHYTQWPDMGVPE 1915
Cdd:pfam00102   77 EEKGREKCAQYWPeeEGESLEYGDFTVTLKKEkEDEKDYTVRTLEVSN--------GGSEETRTVKHFHYTGWPDHGVPE 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888  1916 YSLPVLTFVRKASHAKRHA-VGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFI 1994
Cdd:pfam00102  149 SPNSLLDLLRKVRKSSLDGrSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFL 228


                   ....*.
gi 300795888  1995 HDALVE 2000
Cdd:pfam00102  229 YDAILE 234
alpha_CARP_receptor_like cd03122
Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related ...
 45-298 7.38e-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: 356.28  E-value: 7.38e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888   45 NQKNWGKKYPTCNS-PKQSPINIDEDlTQVNVN-LKKLKFQDWDKTSLEnTFIHNTGKTVEINLTN---DYRLSGGVSET 119
Cdd:cd03122     1 NPKHWAKKYPACGEgRQQSPIDIVED-TQVQRQgLQPLHFDGYEELTAS-TTLENTGKTVILRLEGnssDPFVSGGPLLG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888  120 VFKASKIAFHWGKCNmsSDGSEHSLEGQKFPLEMQIYCFDADRFSSFEeAIKGKGKLRALSILFEVGIEENLDYKAIIDG 199
Cdd:cd03122    79 RYKFSEITFHWGTCN--SDGSEHSIDGHKFPLEMQILHRNTDFFDSFE-AIKSPGGVLALAYLFELSHEDNPFLDPIIEG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888  200 VERVSRFGKQAALDPFTLLNLLPNSTDKYYTYNGSLTSPPCTDTVDWIIFKDTVSISESQLAVFCEVLTMQQSGyVMLMD 279
Cdd:cd03122   156 LRNVSRPGKEVELPPFPLSDLLPPFTDKYYSYEGSLTTPPCSETVEWIVFREPVPISSRQLEAFRELLTRRQDG-VMSGD 234

                         250
                  ....*....|....*....
gi 300795888  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 ...
 1759-2004 1.38e-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: 1.38e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1759 NKHKNRYINIVAYDHSRVKLAQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNL 1838
Cdd:cd14553     3 NKPKNRYANVIAYDHSRVILQPIEGVPG--SDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1839 VEKGRRKCDQYWPVDGSEEYGNFLVTQKSIQVLAYYTVRNFTLRNTkikkgsqkGRPSGRVVTQYHYTQWPDMGVPEYSL 1918
Cdd:cd14553    81 EERSRVKCDQYWPTRGTETYGLIQVTLLDTVELATYTVRTFALHKN--------GSSEKREVRQFQFTAWPDHGVPEHPT 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1919 PVLTFVRKASHAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDAL 1998
Cdd:cd14553   153 PFLAFLRRVKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDAL 232


                  ....*.
gi 300795888 1999 VEAILS 2004
Cdd:cd14553   233 LEAVTC 238
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 1791-1996 2.92e-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: 2.92e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1791 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPVDGSE--EYGNFLVTQKSI 1868
Cdd:cd00047     1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKplEYGDITVTLVSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1869 QVLAYYTVRNFTLRNTKIKKGsqkgrpsgRVVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAKRHAVGPVVVHCSAGVGR 1948
Cdd:cd00047    81 EELSDYTIRTLELSPKGCSES--------REVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCSAGVGR 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 300795888 1949 TGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHD 1996
Cdd:cd00047   153 TGTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 1724-2002 3.73e-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: 3.73e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1724 SGFTEEFETLK-----EFYQEVQSCTVDLGITADSSNHPDNKHKNRYINIVAYDHSRVKLAQLAEKDGklTDYINANYVD 1798
Cdd:cd14626     1 SDLADNIERLKandglKFSQEYESIDPGQQFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPG--SDYINANYID 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1799 GYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPVDGSEEYGNFLVTQKSIQVLAYYTVRN 1878
Cdd:cd14626    79 GYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIRGTETYGMIQVTLLDTVELATYSVRT 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1879 FTLRntkiKKGSQKGRPsgrvVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAKRHAVGPVVVHCSAGVGRTGTYIVLDSM 1958
Cdd:cd14626   159 FALY----KNGSSEKRE----VRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVIDAM 230

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 300795888 1959 LQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDALVEAI 2002
Cdd:cd14626   231 LERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLEAA 274
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 1764-1995 5.87e-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: 5.87e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1764 RYINIVAYDHSRVKLAQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGR 1843
Cdd:cd14548     1 RYTNILPYDHSRVKLIPINEEEG--SDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1844 RKCDQYWPVDGSE-EYGNFLVTQKSIQVLAYYTVRNFTLrntkikkgsqKGRPSGRVVTQYHYTQWPDMGVPEYSLPVLT 1922
Cdd:cd14548    79 VKCDHYWPFDQDPvYYGDITVTMLSESVLPDWTIREFKL----------ERGDEVRSVRQFHFTAWPDHGVPEAPDSLLR 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300795888 1923 FVRKASHAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIH 1995
Cdd:cd14548   149 FVRLVRDYIKQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLH 221
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 1750-1995 6.91e-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: 6.91e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1750 TADSSNHPDNKHKNRYINIVAYDHSRVKLAQLAEKDgkLTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNV 1829
Cdd:cd14543    20 TFLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDE--RTDYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1830 EVIVMITNLVEKGRRKCDQYWPVDG--SEEYGNFLVTQKSIQVLAYYTVRNFTLRNTKIKkgsqkgrpSGRVVTQYHYTQ 1907
Cdd:cd14543    98 LVIVMTTRVVERGRVKCGQYWPLEEgsSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETD--------ESRQVTHFQFTS 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1908 WPDMGVPEYSLPVLTFVRKASHAKRHAVG-------------PVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFL 1974
Cdd:cd14543   170 WPDFGVPSSAAALLDFLGEVRQQQALAVKamgdrwkghppgpPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQTV 249

                         250       260
                  ....*....|....*....|.
gi 300795888 1975 KHIRSQRNYLVQTEEQYVFIH 1995
Cdd:cd14543   250 RRMRTQRAFSIQTPDQYYFCY 270
Carb_anhydrase smart01057
Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse ...
 38-295 1.54e-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: 283.44  E-value: 1.54e-86
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888     38 WSYTGALNQKNWGKKYPT-CNSPKQSPINIDEDLTQVNVNLKKLKFqDWDKTSleNTFIHNTGKTVEINL-TNDYRLSGG 115
Cdd:smart01057    1 WGYEGKNGPEHWGKLDPPfCGGKRQSPIDIVTAEAQYDPSLKPLKL-SYDQPT--AKRILNNGHTVQVNFdDDGSTLSGG 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888    116 VSETVFKASKIAFHWGKCNmsSDGSEHSLEGQKFPLEMQIYCFDADrfSSFEEAIKGKGKLRALSILFEVGIEENLDYKA 195
Cdd:smart01057   78 PLPGRYRLKQFHFHWGGSD--SEGSEHTIDGKRFPLELHLVHYNSK--GSFSEAVSKPGGLAVVAVFFKVGAEENPALQA 153

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888    196 IIDGVERVSRFGKQAALDPFTLLNLLPNSTDKYYTYNGSLTSPPCTDTVDWIIFKDTVSISESQLAVFCEVLTMQQSgyv 275
Cdd:smart01057  154 ILDHLPLIKYKGQETELTPFDLSSLLPASTRHYYTYNGSLTTPPCSEGVTWIVFKEPITISTEQLEKFRTLLPMEGN--- 230

                           250       260
                    ....*....|....*....|
gi 300795888    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 ...
 1708-2002 7.03e-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: 7.03e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1708 IPIKHFPKHVADLHASsgfteefETLKeFYQEVQSCTVDLGITADSSNHPDNKHKNRYINIVAYDHSRVKLAQLAEKDGk 1787
Cdd:cd14625     4 IPISELAEHTERLKAN-------DNLK-LSQEYESIDPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMG- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1788 lTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPVDGSEEYGNFLVTQKS 1867
Cdd:cd14625    75 -SDYINANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSRGTETYGMIQVTLLD 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1868 IQVLAYYTVRNFTLRntkiKKGSQKGRPsgrvVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAKRHAVGPVVVHCSAGVG 1947
Cdd:cd14625   154 TIELATFCVRTFSLH----KNGSSEKRE----VRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPPDAGPIVVHCSAGVG 225

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 300795888 1948 RTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDALVEAI 2002
Cdd:cd14625   226 RTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEAV 280
Carb_anhydrase pfam00194
Eukaryotic-type carbonic anhydrase;
44-300 7.14e-85

Eukaryotic-type carbonic anhydrase;


Pssm-ID: 459707 [Multi-domain]  Cd Length: 252  Bit Score: 278.77  E-value: 7.14e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888    44 LNQKNWGKKYPTCNSPKQSPINIDEDLTQVNVNLKKLKFQDWDKTSLENTfIHNTGKTVEINLTNDYR--LSGGVSETVF 121
Cdd:pfam00194    1 LGPEHWGKVYPSCGGKRQSPINIDTRKVRYDPSLPPLTFQGYDVPPGKNT-LTNNGHTVQVSLDDGDPstISGGPLATRY 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888   122 KASKIAFHWGKCNmsSDGSEHSLEGQKFPLEMQIYCFDADRfSSFEEAIKGKGKLRALSILFEVGIEENLDYKAIIDGVE 201
Cdd:pfam00194   80 RLVQFHFHWGSTD--SRGSEHTIDGKRYPAELHIVHYNSKY-KSFDEAAKHPDGLAVLGVFFEVGDENNPYLQPIVSALD 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888   202 RVSRFGKQAALDPFTLLNLLPNSTDKYYTYNGSLTSPPCTDTVDWIIFKDTVSISESQLAVFCEVLTMQQSGYvmlMDYL 281
Cdd:pfam00194  157 NIKYKGKSVLLPPFDLSDLLPEDLTSYYTYNGSLTTPPCSESVTWIVFKEPISISEEQLEAFRTLLFSDGGEE---PRPL 233

                          250
                   ....*....|....*....
gi 300795888   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 ...
 1694-2002 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 300795888 1694 PPTPIFPISDdvgaipikhfpkHVADLHASSGFteefetlkEFYQEVQSCTVDLGITADSSNHPDNKHKNRYINIVAYDH 1773
Cdd:cd14624     2 PPIPILELAD------------HIERLKANDNL--------KFSQEYESIDPGQQFTWEHSNLEVNKPKNRYANVIAYDH 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1774 SRVKLAQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPVD 1853
Cdd:cd14624    62 SRVLLSAIEGIPG--SDYINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSR 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1854 GSEEYGNFLVTQKSIQVLAYYTVRNFTLrntkIKKGSQKGRPsgrvVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAKRH 1933
Cdd:cd14624   140 GTETYGLIQVTLLDTVELATYCVRTFAL----YKNGSSEKRE----VRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPP 211

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300795888 1934 AVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDALVEAI 2002
Cdd:cd14624   212 DAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLEAV 280
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 1758-2003 4.93e-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: 4.93e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1758 DNKHKNRYINIVAYDHSRVKLAQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITN 1837
Cdd:cd14630     2 ENRNKNRYGNIISYDHSRVRLQLLDGDPH--SDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1838 LVEKGRRKCDQYWPvDGSEEYGNFLVTQKSIQVLAYYTVRNFTLRntkiKKGSQKGRPsgrvVTQYHYTQWPDMGVPEYS 1917
Cdd:cd14630    80 LVEVGRVKCVRYWP-DDTEVYGDIKVTLIETEPLAEYVIRTFTVQ----KKGYHEIRE----IRQFHFTSWPDHGVPCYA 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1918 LPVLTFVRKASHAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDA 1997
Cdd:cd14630   151 TGLLGFVRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDA 230


                  ....*.
gi 300795888 1998 LVEAIL 2003
Cdd:cd14630   231 ILEACL 236
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 1763-1994 2.84e-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: 2.84e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1763 NRYINIVAYDHSRVKLAQLAEKdgkLTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKG 1842
Cdd:cd14615     1 NRYNNVLPYDISRVKLSVQSHS---TDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1843 RRKCDQYWPVDGSEEYGNFLVTQKSIQVLAYYTVRNFTLRNtkiKKGSQKgrpsgRVVTQYHYTQWPDMGVPEYSLPVLT 1922
Cdd:cd14615    78 RTKCEEYWPSKQKKDYGDITVTMTSEIVLPEWTIRDFTVKN---AQTNES-----RTVRHFHFTSWPDHGVPETTDLLIN 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300795888 1923 F---VRKasHAKRHAV-GPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFI 1994
Cdd:cd14615   150 FrhlVRE--YMKQNPPnSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFL 223
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 1694-2009 8.14e-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: 8.14e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1694 PPTPIFPISDDVGaipikhfpKHVADlhASSGFTEEFETLKefyqevqSCTVDlgITADSSNHPDNKHKNRYINIVAYDH 1773
Cdd:cd14621     6 PPLPVDKLEEEIN--------RRMAD--DNKLFREEFNALP-------ACPIQ--ATCEAASKEENKEKNRYVNILPYDH 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1774 SRVKLAQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPVD 1853
Cdd:cd14621    67 SRVHLTPVEGVPD--SDYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQ 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1854 GSEEYGNFLVTQKSIQVLAYYTVRNFTLRNTkikkGSQKGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAKRH 1933
Cdd:cd14621   145 GCWTYGNIRVSVEDVTVLVDYTVRKFCIQQV----GDVTNKKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQ 220

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300795888 1934 AVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDALVEAILSKETEV 2009
Cdd:cd14621   221 YAGAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEHYLYGDTEL 296
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 1715-2003 2.30e-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: 2.30e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1715 KHVADLHASSG--FTEEFETlkefYQEVQSCTvdlgitADSSNHPDNKHKNRYINIVAYDHSRVKLAQLAEKDGklTDYI 1792
Cdd:cd14633     4 QHITQMKCAEGygFKEEYES----FFEGQSAP------WDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETS--SDYI 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1793 NANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPvDGSEEYGNFLVTQKSIQVLA 1872
Cdd:cd14633    72 NGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWP-DDTEIYKDIKVTLIETELLA 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1873 YYTVRNFTLRntkikkgsQKGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAKRHAVGPVVVHCSAGVGRTGTY 1952
Cdd:cd14633   151 EYVIRTFAVE--------KRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCF 222

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 300795888 1953 IVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDALVEAIL 2003
Cdd:cd14633   223 IVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILEACL 273
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
2031-2289 3.91e-77

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 256.82  E-value: 3.91e-77
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888   2031 KLEKQFKLLSQSNIQQSDYSTALKQCNREKNRTSSIIPVERSRVGISSLSGEGADYINASYIMGYYQSNEFIITQHPLLH 2110
Cdd:smart00194    1 GLEEEFEKLDRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGPLPS 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888   2111 TIQDFWRMIWDHNAQLVVML-PDGQNMAEDEFVYWPNK-DEPINCESFKVTLMAEEHKclsneEKLIMQDFILEATQDDY 2188
Cdd:smart00194   81 TVEDFWRMVWEQKVTVIVMLtELVEKGREKCAQYWPDEeGEPLTYGDITVTLKSVEKV-----DDYTIRTLEVTNTGCSE 155

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888   2189 VLEVRHFQCPKWP---NPDSPISkTFELISIIKEEAATRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAK 2265
Cdd:smart00194  156 TRTVTHYHYTNWPdhgVPESPES-ILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVK 234

                           250       260
                    ....*....|....*....|....
gi 300795888   2266 MINLMRPGVFADIEQYQFLYKAVL 2289
Cdd:smart00194  235 ELRSQRPGMVQTEEQYIFLYRAIL 258
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 1791-2003 6.14e-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: 6.14e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1791 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPvDGSEEYGNFLVTQKSIQV 1870
Cdd:cd14555     1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWP-DDTEVYGDIKVTLVETEP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1871 LAYYTVRNFTLRntkikkgsQKGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAKRHAVGPVVVHCSAGVGRTG 1950
Cdd:cd14555    80 LAEYVVRTFALE--------RRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAGPIVVHCSAGAGRTG 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 300795888 1951 TYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDALVEAIL 2003
Cdd:cd14555   152 CYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILEACL 204
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 1763-2002 6.41e-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: 255.20  E-value: 6.41e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1763 NRYINIVAYDHSRVKLAQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKG 1842
Cdd:cd14619     1 NRFRNVLPYDWSRVPLKPIHEEPG--SDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1843 RRKCDQYWPVDGSE-EYGNFLVTQKSIQVLAYYTVRNFTLRNTKIKKgsqkgrpsGRVVTQYHYTQWPDMGVPEYSLPVL 1921
Cdd:cd14619    79 RVKCEHYWPLDYTPcTYGHLRVTVVSEEVMENWTVREFLLKQVEEQK--------TLSVRHFHFTAWPDHGVPSSTDTLL 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1922 TF---VRKASHAKRHAvGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDAL 1998
Cdd:cd14619   151 AFrrlLRQWLDQTMSG-GPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCI 229


                  ....
gi 300795888 1999 VEAI 2002
Cdd:cd14619   230 LDFL 233
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 1765-2000 1.69e-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: 1.69e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1765 YINIVAYDHSRVKLAQLaekDGKL-TDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGR 1843
Cdd:cd14620     1 YPNILPYDHSRVILSQL---DGIPcSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1844 RKCDQYWPVDGSEEYGNFLVTQKSIQVLAYYTVRNFTLRntkiKKGSQKGRPSgRVVTQYHYTQWPDMGVPEYSLPVLTF 1923
Cdd:cd14620    78 EKCYQYWPDQGCWTYGNIRVAVEDCVVLVDYTIRKFCIQ----PQLPDGCKAP-RLVTQLHFTSWPDFGVPFTPIGMLKF 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300795888 1924 VRKASHAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDALVE 2000
Cdd:cd14620   153 LKKVKSVNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 1763-1995 3.49e-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: 3.49e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1763 NRYINIVAYDHSRVKLAQLaeKDGKLTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKG 1842
Cdd:cd14617     1 NRYNNILPYDSTRVKLSNV--DDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1843 RRKCDQYWPVD-GSEEYGNFLVTQKSIQVLAYYTVRNFtlrntKIKKGSQKGRPsgRVVTQYHYTQWPDMGVPEYSLPVL 1921
Cdd:cd14617    79 RVKCDHYWPADqDSLYYGDLIVQMLSESVLPEWTIREF-----KICSEEQLDAP--RLVRHFHYTVWPDHGVPETTQSLI 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300795888 1922 TFVRKASH--AKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIH 1995
Cdd:cd14617   152 QFVRTVRDyiNRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 227
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
2057-2289 5.95e-75

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 249.47  E-value: 5.95e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888  2057 NREKNRTSSIIPVERSRVGISSLSGeGADYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDGQNM 2136
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPG-PSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888  2137 A-EDEFVYWPNK-DEPINCESFKVTLMAEEhkclSNEEKLIMQDFILEATQDDYVLEVRHFQCPKWPN---PDSPISkTF 2211
Cdd:pfam00102   80 GrEKCAQYWPEEeGESLEYGDFTVTLKKEK----EDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDhgvPESPNS-LL 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300795888  2212 ELISIIKE-EAATRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAVL 2289
Cdd:pfam00102  155 DLLRKVRKsSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 1754-1997 1.51e-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: 1.51e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1754 SNHPDNKHKNRYINIVAYDHSRVKLAQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIV 1833
Cdd:cd14554     1 ANLPCNKFKNRLVNILPYESTRVCLQPIRGVEG--SDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1834 MITNLVEKGRRKCDQYWPVDGSEEYGNFLVtqksiQVLAYYTVRNFTLRNTKIKKGSQKgrpSGRVVTQYHYTQWPDMGV 1913
Cdd:cd14554    79 MLTKLREMGREKCHQYWPAERSARYQYFVV-----DPMAEYNMPQYILREFKVTDARDG---QSRTVRQFQFTDWPEQGV 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1914 PEYSLPVLTFVRKASHAKRH--AVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQY 1991
Cdd:cd14554   151 PKSGEGFIDFIGQVHKTKEQfgQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQY 230


                  ....*.
gi 300795888 1992 VFIHDA 1997
Cdd:cd14554   231 QFCYRA 236
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 1784-2003 1.71e-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: 1.71e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1784 KDGKLTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPvDGSEEYGNFLV 1863
Cdd:cd14631     8 EDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWP-DDTEVYGDFKV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1864 TQKSIQVLAYYTVRNFTLrntkikkgSQKGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAKRHAVGPVVVHCS 1943
Cdd:cd14631    87 TCVEMEPLAEYVVRTFTL--------ERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVHCS 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1944 AGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDALVEAIL 2003
Cdd:cd14631   159 AGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACL 218
alpha_CA cd00326
Carbonic anhydrase alpha (vertebrate-like) group. Carbonic anhydrases (CAs) are ...
 60-297 2.89e-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: 244.50  E-value: 2.89e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888   60 KQSPINIDEDLTQVNVNLKKLKFQDWDKTSLEntfIHNTGKTVEINL-TNDYRLSGGVSETVFKASKIAFHWGKCNmsSD 138
Cdd:cd00326     3 RQSPINIVTSAVVYDPSLPPLNFDYYPTTSLT---LVNNGHTVQVNFdDDGGTLSGGGLPGRYKLVQFHFHWGSEN--SP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888  139 GSEHSLEGQKFPLEMQIYCFDADRFSSfeEAIKGKGKLRALSILFEVGIEENLDYKAIIDGVERVSRFGKQAALDPFTLL 218
Cdd:cd00326    78 GSEHTIDGKRYPLELHLVHYNSDYYSS--EAAKKPGGLAVLGVFFEVGEKENPFLKKILDALPKIKYKGKETTLPPFDLS 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300795888  219 NLLPNSTDKYYTYNGSLTSPPCTDTVDWIIFKDTVSISESQLAVFCEVLTMQqsgyvmlMDYLQNNFREQQYKFSRQVF 297
Cdd:cd00326   156 DLLPSSLRDYYTYEGSLTTPPCSEGVTWIVFKEPITISKEQLEAFRSLLDRE-------GKPLVNNYRPVQPLNGRVVY 227
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 1791-1995 2.10e-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: 2.10e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1791 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPVDGSEEYGNFLVTQKSIQV 1870
Cdd:cd14551     1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCWTYGNLRVRVEDTVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1871 LAYYTVRNFTLRntkiKKGSQKGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAKRHAVGPVVVHCSAGVGRTG 1950
Cdd:cd14551    81 LVDYTTRKFCIQ----KVNRGIGEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAGPIVVHCSAGVGRTG 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 300795888 1951 TYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIH 1995
Cdd:cd14551   157 TFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 1763-1995 1.91e-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: 1.91e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1763 NRYINIVAYDHSRVKLAQlaEKDGKLTDYINANYVDGYN-RPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEK 1841
Cdd:cd14547     1 NRYKTILPNEHSRVCLPS--VDDDPLSSYINANYIRGYDgEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1842 gRRKCDQYWPVDGSEEYGNFLVTQKSIQVLAYYTVRNFTLRNtkikkGSQKgrpsgRVVTQYHYTQWPDMGVPEYSLPVL 1921
Cdd:cd14547    79 -KEKCAQYWPEEENETYGDFEVTVQSVKETDGYTVRKLTLKY-----GGEK-----RYLKHYWYTSWPDHKTPEAAQPLL 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300795888 1922 TFVRKASHAKRHAV--GPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIH 1995
Cdd:cd14547   148 SLVQEVEEARQTEPhrGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVH 223
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 1791-2003 4.62e-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: 4.62e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1791 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPvDGSEEYGNFLVTQKSIQV 1870
Cdd:cd14632     1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWP-DDSDTYGDIKITLLKTET 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1871 LAYYTVRNFTLRntkikkgsQKGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAKRHAVGPVVVHCSAGVGRTG 1950
Cdd:cd14632    80 LAEYSVRTFALE--------RRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTG 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 300795888 1951 TYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDALVEAIL 2003
Cdd:cd14632   152 CYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILEACL 204
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 1759-2002 4.70e-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: 4.70e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1759 NKHKNRYINIVAYDHSRVKLaQLAEKDGKLTDYINANYVDGYN-------RPKAYIAAQGPLKSTAEDFWRMIWEHNVEV 1831
Cdd:cd14544     1 NKGKNRYKNILPFDHTRVIL-KDRDPNVPGSDYINANYIRNENegpttdeNAKTYIATQGCLENTVSDFWSMVWQENSRV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1832 IVMITNLVEKGRRKCDQYWPVDG-SEEYGNFlvtqkSIQVLAYYTVRNFTLRNTKIKKGSQKGRPsgRVVTQYHYTQWPD 1910
Cdd:cd14544    80 IVMTTKEVERGKNKCVRYWPDEGmQKQYGPY-----RVQNVSEHDTTDYTLRELQVSKLDQGDPI--REIWHYQYLSWPD 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1911 MGVPEYSLPVLTFVRKASHAKRH--AVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEG---TVNVFGFLKHIRSQRNYLV 1985
Cdd:cd14544   153 HGVPSDPGGVLNFLEDVNQRQESlpHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGldcDIDIQKTIQMVRSQRSGMV 232

                         250
                  ....*....|....*..
gi 300795888 1986 QTEEQYVFIHDALVEAI 2002
Cdd:cd14544   233 QTEAQYKFIYVAVAQYI 249
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 1749-1995 1.06e-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: 1.06e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1749 ITADSSNHPDNKHKNRYINIVAYDHSRVKLAQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHN 1828
Cdd:cd14614     2 IPHFAADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEG--SDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1829 VEVIVMITNLVEKGRRKCDQYWPVdgSEE---YGNFLVTQKSIQVLAYYTVRNFtlrntKIKKGSQKGRpsgrvVTQYHY 1905
Cdd:cd14614    80 SQIIVMLTQCNEKRRVKCDHYWPF--TEEpvaYGDITVEMLSEEEQPDWAIREF-----RVSYADEVQD-----VMHFNY 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1906 TQWPDMGVPEYSL--PVLTFVRKASHAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNY 1983
Cdd:cd14614   148 TAWPDHGVPTANAaeSILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMS 227

                         250
                  ....*....|..
gi 300795888 1984 LVQTEEQYVFIH 1995
Cdd:cd14614   228 MVQTEEQYIFIH 239
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 1763-1999 1.61e-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: 1.61e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1763 NRYINIVAYDHSRVKLAQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKG 1842
Cdd:cd14618     1 NRYPHVLPYDHSRVRLSQLGGEPH--SDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1843 RRKCDQYWPVDGSE-EYGnflvtQKSIQVLAYYTVRNFTLRNTKIKKGSQKGRpsgRVVTQYHYTQWPDMGVPEYSLPVL 1921
Cdd:cd14618    79 RVLCDHYWPSESTPvSYG-----HITVHLLAQSSEDEWTRREFKLWHEDLRKE---RRVKHLHYTAWPDHGIPESTSSLM 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1922 TF---VRKASHAKRHAvGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDAL 1998
Cdd:cd14618   151 AFrelVREHVQATKGK-GPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCI 229


                  .
gi 300795888 1999 V 1999
Cdd:cd14618   230 L 230
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 1791-1996 2.42e-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: 2.42e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1791 YINANYVD-GYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPVDGSE-EYGNFLVTQKSI 1868
Cdd:cd18533     1 YINASYITlPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEgEYGDLTVELVSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1869 QVL--AYYTVRNFTLRNTKIKKgsqkgrpsgRVVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAKRHA--VGPVVVHCSA 1944
Cdd:cd18533    81 EENddGGFIVREFELSKEDGKV---------KKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRELNDSAslDPPIIVHCSA 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 300795888 1945 GVGRTGTYIVLDSMLQQIQ--HEGTVN-------VFGFLKHIRSQRNYLVQTEEQYVFIHD 1996
Cdd:cd18533   152 GVGRTGTFIALDSLLDELKrgLSDSQDledsedpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 1753-2004 1.10e-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: 1.10e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1753 SSNHPDNKHKNRYINIVAYDHSRVKLAQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVI 1832
Cdd:cd14628    46 SANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEG--SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIV 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1833 VMITNLVEKGRRKCDQYWPVDGSEEYGNFLVTQksiqvLAYYTVRNFTLRNTKIKKgSQKGRpsGRVVTQYHYTQWPDMG 1912
Cdd:cd14628   124 VMLTKLREMGREKCHQYWPAERSARYQYFVVDP-----MAEYNMPQYILREFKVTD-ARDGQ--SRTVRQFQFTDWPEQG 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1913 VPEYSLPVLTFVRKASHAKRH--AVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQ 1990
Cdd:cd14628   196 VPKSGEGFIDFIGQVHKTKEQfgQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQ 275

                         250
                  ....*....|....
gi 300795888 1991 YVFIHDALVEAILS 2004
Cdd:cd14628   276 YQFCYRAALEYLGS 289
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 1791-1995 4.98e-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: 4.98e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1791 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPV--DGSEEYGNFLVTQKSI 1868
Cdd:cd14557     1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSmeEGSRAFGDVVVKINEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1869 QVLAYYTVRNFTLRNTKIKKgsqkgrpSGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAKRHAVGPVVVHCSAGVGR 1948
Cdd:cd14557    81 KICPDYIIRKLNINNKKEKG-------SGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGR 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 300795888 1949 TGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIH 1995
Cdd:cd14557   154 TGTYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIH 200
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 1753-2004 1.30e-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: 1.30e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1753 SSNHPDNKHKNRYINIVAYDHSRVKLAQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVI 1832
Cdd:cd14627    47 SANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEG--SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIV 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1833 VMITNLVEKGRRKCDQYWPVDGSEEYGNFLVTQksiqvLAYYTVRNFTLRNTKIKKgSQKGRpsGRVVTQYHYTQWPDMG 1912
Cdd:cd14627   125 VMLTKLREMGREKCHQYWPAERSARYQYFVVDP-----MAEYNMPQYILREFKVTD-ARDGQ--SRTVRQFQFTDWPEQG 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1913 VPEYSLPVLTFVRKASHAKRH--AVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQ 1990
Cdd:cd14627   197 VPKSGEGFIDFIGQVHKTKEQfgQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDE 276

                         250
                  ....*....|....
gi 300795888 1991 YVFIHDALVEAILS 2004
Cdd:cd14627   277 YQFCYQAALEYLGS 290
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 1753-2004 6.36e-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: 6.36e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1753 SSNHPDNKHKNRYINIVAYDHSRVKLAQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVI 1832
Cdd:cd14629    47 SANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEG--SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIV 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1833 VMITNLVEKGRRKCDQYWPVDGSEEYGNFLVTQksiqvLAYYTVRNFTLRNTKIKKgSQKGRpsGRVVTQYHYTQWPDMG 1912
Cdd:cd14629   125 VMLTKLREMGREKCHQYWPAERSARYQYFVVDP-----MAEYNMPQYILREFKVTD-ARDGQ--SRTIRQFQFTDWPEQG 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1913 VPEYSLPVLTFVRKASHAKRH--AVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQ 1990
Cdd:cd14629   197 VPKTGEGFIDFIGQVHKTKEQfgQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQ 276

                         250
                  ....*....|....
gi 300795888 1991 YVFIHDALVEAILS 2004
Cdd:cd14629   277 YQLCYRAALEYLGS 290
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 1734-2000 5.38e-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: 5.38e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1734 KEFyQEVQSCTV----DLGITADSSNHPDNKHKNRYINIVAYDHSRVKLAQLAEKDGklTDYINANYVDGYNRPKAYIAA 1809
Cdd:cd14603     2 GEF-SEIRACSAafkaDYVCSTVAGGRKENVKKNRYKDILPYDQTRVILSLLQEEGH--SDYINANFIKGVDGSRAYIAT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1810 QGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPV-DGSEEYGNFLVTQ-KSIQVLAYYTVRNFTLrntKIK 1887
Cdd:cd14603    79 QGPLSHTVLDFWRMIWQYGVKVILMACREIEMGKKKCERYWAQeQEPLQTGPFTITLvKEKRLNEEVILRTLKV---TFQ 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1888 KGSqkgrpsgRVVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAKRHAVGPVVVHCSAGVGRTGTYIVLDS-----MLQQI 1962
Cdd:cd14603   156 KES-------RSVSHFQYMAWPDHGIPDSPDCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYvrqllLTQRI 228

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 300795888 1963 QHEgtVNVFGFLKHIRSQRNYLVQTEEQYVFIHDALVE 2000
Cdd:cd14603   229 PPD--FSIFDVVLEMRKQRPAAVQTEEQYEFLYHTVAQ 264
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 1752-2004 6.34e-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: 6.34e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1752 DSSNHPDNKHKNRYINIVAYDHSRVKLaQLAEKDGKLTDYINANYVDGY-----NRPKAYIAAQGPLKSTAEDFWRMIWE 1826
Cdd:cd14606    11 LEGQRPENKSKNRYKNILPFDHSRVIL-QGRDSNIPGSDYINANYVKNQllgpdENAKTYIASQGCLEATVNDFWQMAWQ 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1827 HNVEVIVMITNLVEKGRRKCDQYWP-VDGSEEYGNFLVTQKSIQVLAYYTVRnfTLRNTKIKKGSQKgrpsgRVVTQYHY 1905
Cdd:cd14606    90 ENSRVIVMTTREVEKGRNKCVPYWPeVGMQRAYGPYSVTNCGEHDTTEYKLR--TLQVSPLDNGELI-----REIWHYQY 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1906 TQWPDMGVPEYSLPVLTF---VRKASHAKRHAvGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGT---VNVFGFLKHIRS 1979
Cdd:cd14606   163 LSWPDHGVPSEPGGVLSFldqINQRQESLPHA-GPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVRA 241

                         250       260
                  ....*....|....*....|....*
gi 300795888 1980 QRNYLVQTEEQYVFIHDALVEAILS 2004
Cdd:cd14606   242 QRSGMVQTEAQYKFIYVAIAQFIET 266
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 1791-2002 1.56e-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: 1.56e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1791 YINANYV--DGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPvDGSEE----YGNFLVT 1864
Cdd:cd14538     1 YINASHIriPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWP-DSLNKplicGGRLEVS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1865 QKSIQVLAYYTVRNFTLRNTKIKKGsqkgrpsgRVVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAkrHAVGPVVVHCSA 1944
Cdd:cd14538    80 LEKYQSLQDFVIRRISLRDKETGEV--------HHITHLNFTTWPDHGTPQSADPLLRFIRYMRRI--HNSGPIVVHCSA 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 300795888 1945 GVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDALVEAI 2002
Cdd:cd14538   150 GIGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEVL 207
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 1791-1999 4.49e-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: 4.49e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1791 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPVDGSEEYGNFLVTQKSIQV 1870
Cdd:cd14552     1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGSVSSGDITVELKDQTD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1871 LAYYTVRNFTLRNTKIKKgsqkgrpsGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAKRHA-VGPVVVHCSAGVGRT 1949
Cdd:cd14552    81 YEDYTLRDFLVTKGKGGS--------TRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQSgNHPITVHCSAGAGRT 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 300795888 1950 GTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDALV 1999
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; ...
 1791-1995 2.33e-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: 2.33e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1791 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPVDGSEE--YGNFLVTQKSI 1868
Cdd:cd14542     1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQlqFGPFKISLEKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1869 QVLAyytvRNFTLRNTKIKKGSQKgrpsgRVVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAKRHAVGPVVVHCSAGVGR 1948
Cdd:cd14542    81 KRVG----PDFLIRTLKVTFQKES-----RTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDVPICVHCSAGCGR 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 300795888 1949 TGTYIVLDSMLQQIQHEG---TVNVFGFLKHIRSQRNYLVQTEEQYVFIH 1995
Cdd:cd14542   152 TGTICAIDYVWNLLKTGKipeEFSLFDLVREMRKQRPAMVQTKEQYELVY 201
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 1763-1995 2.71e-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: 2.71e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1763 NRYINIVAYDHSRVKLAQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKG 1842
Cdd:cd14616     1 NRFPNIKPYNNNRVKLIADAGVPG--SDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1843 RRKCDQYWPVDGS--EEYGNFLVTQksiqvLAYYTVRNFTLRNTKIKKGSQKgrpsgRVVTQYHYTQWPDMGVPEYSLPV 1920
Cdd:cd14616    79 RIRCHQYWPEDNKpvTVFGDIVITK-----LMEDVQIDWTIRDLKIERHGDY-----MMVRQCNFTSWPEHGVPESSAPL 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 300795888 1921 LTFVRKASHAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIH 1995
Cdd:cd14616   149 IHFVKLVRASRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLH 223
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 1758-2000 2.93e-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: 2.93e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1758 DNKHKNRYINIVAYDHSRVKLA-QLAEKDgklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMIT 1836
Cdd:cd14604    56 ENVKKNRYKDILPFDHSRVKLTlKTSSQD---SDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMAC 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1837 NLVEKGRRKCDQYWPVDGSE--EYGNFLVTQKSIQVLAYYTVRNFTLrntkikkgsqKGRPSGRVVTQYHYTQWPDMGVP 1914
Cdd:cd14604   133 REFEMGRKKCERYWPLYGEEpmTFGPFRISCEAEQARTDYFIRTLLL----------EFQNETRRLYQFHYVNWPDHDVP 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1915 EYSLPVLTFVRKASHAKRHAVGPVVVHCSAGVGRTGTYIVLD---SMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQY 1991
Cdd:cd14604   203 SSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQY 282


                  ....*....
gi 300795888 1992 VFIHDALVE 2000
Cdd:cd14604   283 ELVHRAIAQ 291
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 1760-1993 7.01e-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: 7.01e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1760 KHKNRYINIVAYDHSRVKLaqlaeKDGKlTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLV 1839
Cdd:cd14545     1 LNRYRDRDPYDHDRSRVKL-----KQGD-NDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLM 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1840 EKGRRKCDQYWPVDGSE----EYGNFLVTQKSIQVLAYYTVRNFTLRNTKIkkgsqkgrPSGRVVTQYHYTQWPDMGVPE 1915
Cdd:cd14545    75 EKGQIKCAQYWPQGEGNamifEDTGLKVTLLSEEDKSYYTVRTLELENLKT--------QETREVLHFHYTTWPDFGVPE 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1916 YSLPVLTF---VRKASHAKRHaVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGT--VNVFGFLKHIRSQRNYLVQTEEQ 1990
Cdd:cd14545   147 SPAAFLNFlqkVRESGSLSSD-VGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYRMGLIQTPDQ 225


                  ...
gi 300795888 1991 YVF 1993
Cdd:cd14545   226 LRF 228
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1790-2004 7.49e-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: 7.49e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1790 DYINANYVDgYNRPKA-----YIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWP-VDGSEEYGNFLV 1863
Cdd:cd14541     1 DYINANYVN-MEIPGSgivnrYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPdLGETMQFGNLQI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1864 TQKSIQVLAYYTVRNFTLRNTKIKKGsqkgrpsgRVVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAKRHAVGPVVVHCS 1943
Cdd:cd14541    80 TCVSEEVTPSFAFREFILTNTNTGEE--------RHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVEPTVVHCS 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 300795888 1944 AGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIhdalVEAILS 2004
Cdd:cd14541   152 AGIGRTGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFV----CEAILR 208
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 1728-2002 4.81e-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: 4.81e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1728 EEFETLKEFYQEVQSCtvdlgitaDSSNHPDNKHKNRYINIVAYDHSRVKLAqlAEKDGKLTDYINAN-YVDGYNRPKAY 1806
Cdd:cd14609    19 KEWQALCAYQAEPNTC--------STAQGEANVKKNRNPDFVPYDHARIKLK--AESNPSRSDYINASpIIEHDPRMPAY 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1807 IAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPVDGSEEYGNFLVTQKSIQVLAY-YTVRNFTLRNTK 1885
Cdd:cd14609    89 IATQGPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHIYEVNLVSEHIWCEdFLVRSFYLKNVQ 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1886 IKKgsqkgrpsGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQhE 1965
Cdd:cd14609   169 TQE--------TRTLTQFHFLSWPAEGIPSSTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMA-K 239

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 300795888 1966 GT--VNVFGFLKHIRSQRNYLVQTEEQYVFIHDALVEAI 2002
Cdd:cd14609   240 GVkeIDIAATLEHVRDQRPGMVRTKDQFEFALTAVAEEV 278
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 1758-1998 5.30e-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: 5.30e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1758 DNKHKNRYINIVAYDHSRVKLAQlAEKDGKLTDYINANYVDGYN-------RPK-AYIAAQGPLKSTAEDFWRMIWEHNV 1829
Cdd:cd14605     1 ENKNKNRYKNILPFDHTRVVLHD-GDPNEPVSDYINANIIMPEFetkcnnsKPKkSYIATQGCLQNTVNDFWRMVFQENS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1830 EVIVMITNLVEKGRRKCDQYWPVDGS-EEYGNFLVTQKSIQVLAYYTVRNFTLrnTKIKKGSQKgrpsgRVVTQYHYTQW 1908
Cdd:cd14605    80 RVIVMTTKEVERGKSKCVKYWPDEYAlKEYGVMRVRNVKESAAHDYILRELKL--SKVGQGNTE-----RTVWQYHFRTW 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1909 PDMGVPEYSLPVLTFVRKASHaKRHAV---GPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGT---VNVFGFLKHIRSQRN 1982
Cdd:cd14605   153 PDHGVPSDPGGVLDFLEEVHH-KQESImdaGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRS 231

                         250
                  ....*....|....*.
gi 300795888 1983 YLVQTEEQYVFIHDAL 1998
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 6.92e-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: 204.08  E-value: 6.92e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888   46 QKNWGKKYPTCNSPKQSPINIDEDLTQVNVNLKKLKFQDWDKTSLENTFIHNTGKTVEINLTNDYRLSGGVSeTVFKASK 125
Cdd:cd03123     2 EDHWPKKYPACGGKRQSPIDIQTDIVQFDPSLPPLELVGYDLPGTEEFTLTNNGHTVQLSLPPTMHIRGGPG-TEYTAAQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888  126 IAFHWGKCNMSSdGSEHSLEGQKFPLEMQIYCFDADRFSSFEEAIKGKGKLRALSILFEVGIEENLDYKAIIDGVERVSR 205
Cdd:cd03123    81 LHLHWGGRGSLS-GSEHTIDGIRFAAELHIVHYNSDKYSSFDEAADKPDGLAVLAILIEVGYPENTYYEKIISHLHEIKY 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888  206 FGKQAALDPFTLLNLLPNSTDKYYTYNGSLTSPPCTDTVDWIIFKDTVSISESQLavfcevLTMQQSgyvmLMDY----L 281
Cdd:cd03123   160 KGQETTVPGFNVRELLPEDLSHYYRYEGSLTTPPCYESVLWTVFRDPVTLSKEQL------ETLENT----LMDThnktL 229

                         250
                  ....*....|....*....
gi 300795888  282 QNNFREQQYKFSRQVFSSY 300
Cdd:cd03123   230 QNNYRATQPLNGRVVEASF 248
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 1728-2002 1.85e-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: 1.85e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1728 EEFETLKEFYQEVQSCTVDLgitadssnHPDNKHKNRYINIVAYDHSRVKLAqlAEKDGKLTDYINANYV-DGYNRPKAY 1806
Cdd:cd14610    21 KEWEALCAYQAEPNATNVAQ--------REENVQKNRSLAVLPYDHSRIILK--AENSHSHSDYINASPImDHDPRNPAY 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1807 IAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPVDGSEEYGNFLVTQKSIQVLAY-YTVRNFTLRNTK 1885
Cdd:cd14610    91 IATQGPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEGSNLYHIYEVNLVSEHIWCEdFLVRSFYLKNLQ 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1886 IKKgsqkgrpsGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQI-QH 1964
Cdd:cd14610   171 TNE--------TRTVTQFHFLSWNDQGVPASTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLNKMaKG 242

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 300795888 1965 EGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDALVEAI 2002
Cdd:cd14610   243 AKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAEEV 280
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 1749-1998 2.26e-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: 2.26e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1749 ITADSSNHPDNKHKNRYINIVAYDHSRVKLAQLAEKDgKLTDYINANYVDGYN-RPKAYIAAQGPLKSTAEDFWRMIWEH 1827
Cdd:cd14612     5 VSPEELDIPGHASKDRYKTILPNPQSRVCLRRAGSQE-EEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1828 NVEVIVMITNLVEKgRRKCDQYWPvDGSEEYGNFLVTQKSIQVLAYYTVRNFTlrntkIKKGSQKgrpsgRVVTQYHYTQ 1907
Cdd:cd14612    84 ECPIIVMITKLKEK-KEKCVHYWP-EKEGTYGRFEIRVQDMKECDGYTIRDLT-----IQLEEES-----RSVKHYWFSS 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1908 WPDMGVPEYSLPVLTFVRKASHAKRHAV--GPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLV 1985
Cdd:cd14612   152 WPDHQTPESAGPLLRLVAEVEESRQTAAspGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMI 231

                         250
                  ....*....|...
gi 300795888 1986 QTEEQYVFIHDAL 1998
Cdd:cd14612   232 QTSEQYQFLHHTL 244
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 1764-2000 5.58e-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: 5.58e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1764 RYINIVAYDHSRVKLAqlAEKDGKLTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGR 1843
Cdd:cd14623     1 RVLQIIPYEFNRVIIP--VKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1844 RKCDQYWPVDGSEEYGNFLVTQKSIQVLAYYTVRNFTLRNTKIKKgsqkgrpsGRVVTQYHYTQWPDMGVPEYSLPVLTF 1923
Cdd:cd14623    79 EKCAQYWPSDGSVSYGDITIELKKEEECESYTVRDLLVTNTRENK--------SRQIRQFHFHGWPEVGIPSDGKGMINI 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 300795888 1924 VRKASHAKRHAVG-PVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDALVE 2000
Cdd:cd14623   151 IAAVQKQQQQSGNhPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 1762-2000 1.89e-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: 1.89e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1762 KNRYINIVAYDHSRVKLAQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEK 1841
Cdd:cd14602     1 KNRYKDILPYDHSRVELSLITSDED--SDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1842 GRRKCDQYWPVDGSE--EYGNFLVTQKSIQVLAYYTVRnfTLrntKIKKGSQKgrpsgRVVTQYHYTQWPDMGVPEYSLP 1919
Cdd:cd14602    79 GKKKCERYWAEPGEMqlEFGPFSVTCEAEKRKSDYIIR--TL---KVKFNSET-----RTIYQFHYKNWPDHDVPSSIDP 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1920 VLTFVRKASHAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQhEGTV----NVFGFLKHIRSQRNYLVQTEEQYVFIH 1995
Cdd:cd14602   149 ILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLK-DGIIpenfSVFSLIQEMRTQRPSLVQTKEQYELVY 227


                  ....*
gi 300795888 1996 DALVE 2000
Cdd:cd14602   228 NAVIE 232
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 2086-2286 2.05e-57

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: 197.89  E-value: 2.05e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2086 YINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPD----GQNMAEDefvYWPNK-DEPINCESFKVTL 2160
Cdd:cd00047     1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNlvekGREKCER---YWPEEgGKPLEYGDITVTL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2161 MAEEHKclsneEKLIMQDFILEATQDDYVLEVRHFQCPKWPN---PDSPISkTFELISIIKEEAATRDGPMIVHDEHGGV 2237
Cdd:cd00047    78 VSEEEL-----SDYTIRTLELSPKGCSESREVTHLHYTGWPDhgvPSSPED-LLALVRRVRKEARKPNGPIVVHCSAGVG 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 300795888 2238 TAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYK 2286
Cdd:cd00047   152 RTGTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 1791-2002 9.59e-57

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


Pssm-ID: 350394 [Multi-domain]  Cd Length: 208  Bit Score: 196.13  E-value: 9.59e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1791 YINANYVDGYN-RPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPVDGSEEYGNFLVTQKSIQ 1869
Cdd:cd14546     1 YINASTIYDHDpRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEVYHIYEVHLVSEH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1870 VL-AYYTVRNFTLRNTKIKKgsqkgrpsGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAKRHAVGPVVVHCSAGVGR 1948
Cdd:cd14546    81 IWcDDYLVRSFYLKNLQTSE--------TRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYRGRSCPIVVHCSDGAGR 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 300795888 1949 TGTYIVLDSMLQQIQhEGT--VNVFGFLKHIRSQRNYLVQTEEQYVFIHDALVEAI 2002
Cdd:cd14546   153 TGTYILIDMVLNRMA-KGAkeIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAEEV 207
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1791-2000 1.49e-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: 1.49e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1791 YINANYVDGY--NRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPVDGSEE----YGNFLVT 1864
Cdd:cd14540     1 YINASHITATvgGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGGEHdaltFGEYKVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1865 QKSIQVLAYYTVRNFTLRNTkikkgsqkgrPSGRVVTQYH--YTQWPDMGVPEYSLPVLTFVRKASHAKRHAVG------ 1936
Cdd:cd14540    81 TKFSVSSGCYTTTGLRVKHT----------LSGQSRTVWHlqYTDWPDHGCPEDVSGFLDFLEEINSVRRHTNQdvaghn 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300795888 1937 ---PVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDALVE 2000
Cdd:cd14540   151 rnpPTLVHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQ 217
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 1757-2003 1.54e-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: 1.54e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1757 PDNKHKNRYINIVAYDHSRVKLaqlaekDGKlTDYINANYVD----GYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVI 1832
Cdd:cd14600    38 PQNMDKNRYKDVLPYDATRVVL------QGN-EDYINASYVNmeipSANIVNKYIATQGPLPHTCAQFWQVVWEQKLSLI 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1833 VMITNLVEKGRRKCDQYWPvDGSE--EYGNFLVTQKSIQVLAYYTVRNFTLrnTKIKKGSQkgrpsgRVVTQYHYTQWPD 1910
Cdd:cd14600   111 VMLTTLTERGRTKCHQYWP-DPPDvmEYGGFRVQCHSEDCTIAYVFREMLL--TNTQTGEE------RTVTHLQYVAWPD 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1911 MGVPEYSLPVLTFVrKASHAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQ 1990
Cdd:cd14600   182 HGVPDDSSDFLEFV-NYVRSKRVENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQ 260

                         250
                  ....*....|...
gi 300795888 1991 YVFIhdalVEAIL 2003
Cdd:cd14600   261 YKFV----CEAIL 269
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 1762-1995 4.72e-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: 4.72e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1762 KNRYINIVAYDHSRVKLAQLAEKDgKLTDYINANYVDGY-NRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVE 1840
Cdd:cd14611     2 KNRYKTILPNPHSRVCLKPKNSND-SLSTYINANYIRGYgGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1841 KGRrKCDQYWPvDGSEEYGNFLVTQKSIQVLAYYTVRNFTLrntkiKKGSQKgrpsgRVVTQYHYTQWPDMGVPEYSLPV 1920
Cdd:cd14611    81 KNE-KCVLYWP-EKRGIYGKVEVLVNSVKECDNYTIRNLTL-----KQGSQS-----RSVKHYWYTSWPDHKTPDSAQPL 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1921 LTFV------RKASHAKrhavGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFI 1994
Cdd:cd14611   149 LQLMldveedRLASPGR----GPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFV 224


                  .
gi 300795888 1995 H 1995
Cdd:cd14611   225 H 225
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 1762-1998 3.25e-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: 3.25e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1762 KNRYINIVAYDHSRVKLAQlAEKDGKLTDYINANYVDGYN-RPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVE 1840
Cdd:cd14613    28 KNRYKTILPNPHSRVCLTS-PDQDDPLSSYINANYIRGYGgEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEE 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1841 KGRrKCDQYWPVDgSEEYGNFLVTQKSIQVLAYYTVRNFTLrntkiKKGSQKgrpsgRVVTQYHYTQWPDMGVPEYSLPV 1920
Cdd:cd14613   107 MNE-KCTEYWPEE-QVTYEGIEITVKQVIHADDYRLRLITL-----KSGGEE-----RGLKHYWYTSWPDQKTPDNAPPL 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1921 LTFVRKASHAKRHA---VGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDA 1997
Cdd:cd14613   175 LQLVQEVEEARQQAepnCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVHHV 254


                  .
gi 300795888 1998 L 1998
Cdd:cd14613   255 L 255
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 1790-1995 2.98e-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: 2.98e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1790 DYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPVDGSEEYGNFLVTQKSIQ 1869
Cdd:cd14622     1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEGSVTHGEITIEIKNDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1870 VLAYYTVRNFTLRNTKIKKgsqkgrpsGRVVTQYHYTQWPDMGVPEYSLPVLTFVrKASHAKRHAVG--PVVVHCSAGVG 1947
Cdd:cd14622    81 LLETISIRDFLVTYNQEKQ--------TRLVRQFHFHGWPEIGIPAEGKGMIDLI-AAVQKQQQQTGnhPIVVHCSAGAG 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 300795888 1948 RTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIH 1995
Cdd:cd14622   152 RTGTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCY 199
PHA02738 PHA02738
hypothetical protein; Provisional
 1731-2009 5.90e-54

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 192.45  E-value: 5.90e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1731 ETLKEFYQEVQSCTVDLGITADSSNhpdnKHKNRYINIVAYDHSRVKLAqlAEKDgkLTDYINANYVDGYNRPKAYIAAQ 1810
Cdd:PHA02738   25 EVITREHQKVISEKVDGTFNAEKKN----RKLNRYLDAVCFDHSRVILP--AERN--RGDYINANYVDGFEYKKKFICGQ 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1811 GPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWP-VDGSE-EYGNFLVTQKSIQVLAYYTVRNFTLRNtkikk 1888
Cdd:PHA02738   97 APTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSdVEQGSiRFGKFKITTTQVETHPHYVKSTLLLTD----- 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1889 gsqkGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFV------RKASHAKRHAVG-------PVVVHCSAGVGRTGTYIVL 1955
Cdd:PHA02738  172 ----GTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVlevrqcQKELAQESLQIGhnrlqppPIVVHCNAGLGRTPCYCVV 247

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 300795888 1956 DSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDALVEAILSKETEV 2009
Cdd:PHA02738  248 DISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAVKRYVNLTVNKV 301
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 1737-2000 3.83e-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: 3.83e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1737 YQEVQSCTVDLgiTADSSNHPDNKHKNRYINIVAYDHSRVKLAQlaekdgKLTDYINANYVDGYNRPKAYIAAQGPLKST 1816
Cdd:cd14608     5 YQDIRHEASDF--PCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQ------EDNDYINASLIKMEEAQRSYILTQGPLPNT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1817 AEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPVDGSEEY----GNFLVTQKSIQVLAYYTVRNFTLRNTKIKKgsqk 1892
Cdd:cd14608    77 CGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMifedTNLKLTLISEDIKSYYTVRQLELENLTTQE---- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1893 grpsGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKA--SHAKRHAVGPVVVHCSAGVGRTGTYIVLDS---MLQQIQHEGT 1967
Cdd:cd14608   153 ----TREILHFHYTTWPDFGVPESPASFLNFLFKVreSGSLSPEHGPVVVHCSAGIGRSGTFCLADTcllLMDKRKDPSS 228

                         250       260       270
                  ....*....|....*....|....*....|...
gi 300795888 1968 VNVFGFLKHIRSQRNYLVQTEEQYVFIHDALVE 2000
Cdd:cd14608   229 VDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIE 261
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 1758-1993 7.71e-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: 7.71e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1758 DNKHKNRYINIVAYDHSRVKLAQlaekDGkltDYINANYVD---GyNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVM 1834
Cdd:cd14597     2 ENRKKNRYKNILPYDTTRVPLGD----EG---GYINASFIKmpvG-DEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAM 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1835 ITNLVEKGRRKCDQYWPvdgsEEYGNFLVTQKSIQV--LAYYTVRNFTLRNTKIKKgSQKGRPsgRVVTQYHYTQWPDMG 1912
Cdd:cd14597    74 MTQEVEGGKIKCQRYWP----EILGKTTMVDNRLQLtlVRMQQLKNFVIRVLELED-IQTREV--RHITHLNFTAWPDHD 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1913 VPEYSLPVLTFVRKASHAkrHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYV 1992
Cdd:cd14597   147 TPSQPEQLLTFISYMRHI--HKSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYI 224


                  .
gi 300795888 1993 F 1993
Cdd:cd14597   225 F 225
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 1737-1998 1.08e-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: 1.08e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1737 YQEVQSCTVDLGITAdsSNHPDNKHKNRYINIVAYDHSRVKLaQLAEkdgklTDYINANYVDGYNRPKAYIAAQGPLKST 1816
Cdd:cd14607     4 YLEIRNESHDYPHRV--AKYPENRNRNRYRDVSPYDHSRVKL-QNTE-----NDYINASLVVIEEAQRSYILTQGPLPNT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1817 AEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPVDGSEEYG----NFLVTQKSIQVLAYYTVRNFTLRNtkIKKGSQk 1892
Cdd:cd14607    76 CCHFWLMVWQQKTKAVVMLNRIVEKDSVKCAQYWPTDEEEVLSfketGFSVKLLSEDVKSYYTVHLLQLEN--INSGET- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1893 grpsgRVVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAKRHAV--GPVVVHCSAGVGRTGTYIVLDS--MLQQIQHEGTV 1968
Cdd:cd14607   153 -----RTISHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSPehGPAVVHCSAGIGRSGTFSLVDTclVLMEKKDPDSV 227

                         250       260       270
                  ....*....|....*....|....*....|
gi 300795888 1969 NVFGFLKHIRSQRNYLVQTEEQYVFIHDAL 1998
Cdd:cd14607   228 DIKQVLLDMRKYRMGLIQTPDQLRFSYMAV 257
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 1791-1996 2.54e-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: 2.54e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1791 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPvDGSEEYGNFLVTQKSIQV 1870
Cdd:cd14558     1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWG-DEKKTYGDIEVELKDTEK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1871 LAYYTVRNFTLRNTKIKKgsqkgrpsGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKASH------AKRHAVGPVVVHCSA 1944
Cdd:cd14558    80 SPTYTVRVFEITHLKRKD--------SRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQklpyknSKHGRSVPIVVHCSD 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 300795888 1945 GVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHD 1996
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 1.35e-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: 1.35e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888   59 PKQSPINIDEDLTQVNVNLKKLKFQDWDKTSLeNTFIHNTGKTVEINLTNDYRLSGGVSETVFKASKIAFHWGkcNMSSD 138
Cdd:cd03117     2 KRQSPINIVTKKVQYDENLTPFTFTGYDDTTT-NWTITNNGHTVQVTLPDGAKISGGGLPGTYKALQFHFHWG--SNGSP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888  139 GSEHSLEGQKFPLEMQIYCFDADrFSSFEEAIKGKGKLRALSILFEVGIEENLDYKAIIDGVERVSRFGKQAALDPFTLL 218
Cdd:cd03117    79 GSEHTIDGERYPMELHIVHIKES-YNSLLEALKDSDGLAVLGFFIEEGEEENTNFDPLISALSNIPQKGGSTNLTPFSLR 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888  219 NLLP-NSTDKYYTYNGSLTSPPCTDTVDWIIFKDTVSISESQLAVFCEVLTMQQSGYVMLMdylqNNFREQQYKFSRQVF 297
Cdd:cd03117   158 SLLPsVLLTKYYRYNGSLTTPGCNEAVIWTVFEEPIPISRAQLDAFSTVLFFDTDNGQPMV----NNFRPVQPLNGRVVY 233


                  .
gi 300795888  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 2.14e-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: 2.14e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888   46 QKNWGKKYPTCNSPKQSPINIDEDLTQVNVNLKKLKFQDWDKTSLENTFIHNTGKTVEINLTNDYRLSGGVSEtvFKASK 125
Cdd:cd03126     2 ENSWPKKYPFCGGVAQSPIDIHTDILQYDSSLPPLEFHGYNVSGTEQFTLTNNGHTVQLSLPPTMHIGGLPFK--YTASQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888  126 IAFHWGKCNmSSDGSEHSLEGQKFPLEMQIYCFDADRFSSFEEAIKGKGKLRALSILFEVGiEENLDYKAIIDGVERVSR 205
Cdd:cd03126    80 LHLHWGQRG-SPEGSEHTISGKHFAAELHIVHYNSDKYPDISTAMNKSQGLAVLGILIEVG-PFNPSYEKIFSHLHEVKY 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888  206 FGKQAALDPFTLLNLLPNSTDKYYTYNGSLTSPPCTDTVDWIIFKDTVSISESQLavfcevLTMQQSGYVMLMD---YLQ 282
Cdd:cd03126   158 KDQKVSVPGFNVQELLPKRLDEYYRYEGSLTTPPCYPSVLWTVFRNPVQISQEQL------LALETALYSTEEDesrEMV 231

                         250
                  ....*....|....*...
gi 300795888  283 NNFREQQYKFSRQVFSSY 300
Cdd:cd03126   232 NNYRQVQPFNERLVFASF 249
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 1791-2002 2.51e-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: 2.51e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1791 YINANYVDGYNRPKA--YIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPVDGSE--EYGNFLVTQK 1866
Cdd:cd14596     1 YINASYITMPVGEEElfYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEpmELENYQLRLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1867 SIQVLAYYTVRNFTLrntkikkgSQKGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAkrHAVGPVVVHCSAGV 1946
Cdd:cd14596    81 NYQALQYFIIRIIKL--------VEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKV--HNTGPIVVHCSAGI 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 300795888 1947 GRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDALVEAI 2002
Cdd:cd14596   151 GRAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVL 206
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 2007-2294 4.15e-49

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: 177.62  E-value: 4.15e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2007 TEVPDSHIHAYVNGLL-IPGPTGKTKLEKQFKLLSQSNIQQSDYSTALKQCNREKNRTSSIIPVERSRVGISSLSG-EGA 2084
Cdd:cd14628     1 TEVPARNLYAYIQKLTqIETGENVTGMELEFKRLASSKAHTSRFISANLPCNKFKNRLVNIMPYESTRVCLQPIRGvEGS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2085 DYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDGQNMAEDE-FVYWPnKDEPINCESFKVTLMAE 2163
Cdd:cd14628    81 DYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKcHQYWP-AERSARYQYFVVDPMAE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2164 ehkclSNEEKLIMQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKT--FELISII--KEEAATRDGPMIVHDEHGGVTA 2239
Cdd:cd14628   160 -----YNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEgfIDFIGQVhkTKEQFGQDGPISVHCSAGVGRT 234

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 300795888 2240 GTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAVLSLVST 2294
Cdd:cd14628   235 GVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEYLGS 289
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 1790-2003 6.26e-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: 6.26e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1790 DYINANYVDG-------YNRpkaYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWP-VDGSEEYGNF 1861
Cdd:cd14601     1 DYINANYINMeipsssiINR---YIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPePSGSSSYGGF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1862 LVTQKSIQVLAYYTVRNFTLRNTKikkgSQKGRPsgrvVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAKRHAVGPVVVH 1941
Cdd:cd14601    78 QVTCHSEEGNPAYVFREMTLTNLE----KNESRP----LTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDEPVVVH 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 300795888 1942 CSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIhdalVEAIL 2003
Cdd:cd14601   150 CSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFV----CEAIL 207
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 1757-2000 9.17e-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: 9.17e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1757 PDNKHKNRYINIVAYDHSRVKLAQLAEKDgklTDYINANYVDGYNRPKA--YIAAQGPLKSTAEDFWRMIWEHNVEVIVM 1834
Cdd:cd14599    36 PENAERNRIREVVPYEENRVELVPTKENN---TGYINASHIKVTVGGEEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAM 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1835 ITNLVEKGRRKCDQYWPVDG----SEEYGNFLVTQKSIQVLAYYTVRNFTLRNtkIKKGSQkgrpsgRVVTQYHYTQWPD 1910
Cdd:cd14599   113 VTAEEEGGRSKSHRYWPKLGskhsSATYGKFKVTTKFRTDSGCYATTGLKVKH--LLSGQE------RTVWHLQYTDWPD 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1911 MGVPEYSLPVLTFVRKASHAKRHAVG----------PVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQ 1980
Cdd:cd14599   185 HGCPEEVQGFLSYLEEIQSVRRHTNSmldstkncnpPIVVHCSAGVGRTGVVILTELMIGCLEHNEKVEVPVMLRHLREQ 264

                         250       260
                  ....*....|....*....|
gi 300795888 1981 RNYLVQTEEQYVFIHDALVE 2000
Cdd:cd14599   265 RMFMIQTIAQYKFVYQVLIQ 284
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 2007-2294 1.64e-47

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: 173.00  E-value: 1.64e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2007 TEVPDSHIHAYVNGLLIPGPTGK-TKLEKQFKLLSQSNIQQSDYSTALKQCNREKNRTSSIIPVERSRVGISSLSG-EGA 2084
Cdd:cd14627     2 TEVPARNLYSYIQKLAQVEVGEHvTGMELEFKRLANSKAHTSRFISANLPCNKFKNRLVNIMPYETTRVCLQPIRGvEGS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2085 DYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDGQNMAEDE-FVYWPnKDEPINCESFKVTLMAE 2163
Cdd:cd14627    82 DYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGREKcHQYWP-AERSARYQYFVVDPMAE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2164 ehkclSNEEKLIMQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKT--FELISII--KEEAATRDGPMIVHDEHGGVTA 2239
Cdd:cd14627   161 -----YNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEgfIDFIGQVhkTKEQFGQDGPISVHCSAGVGRT 235

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 300795888 2240 GTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAVLSLVST 2294
Cdd:cd14627   236 GVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALEYLGS 290
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 2007-2294 1.76e-47

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: 172.60  E-value: 1.76e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2007 TEVPDSHIHAYVNGL-LIPGPTGKTKLEKQFKLLSQSNIQQSDYSTALKQCNREKNRTSSIIPVERSRVGISSLSG-EGA 2084
Cdd:cd14629     2 TEVPARNLYAHIQKLtQVPPGESVTAMELEFKLLANSKAHTSRFISANLPCNKFKNRLVNIMPYELTRVCLQPIRGvEGS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2085 DYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDGQNMAEDE-FVYWPnKDEPINCESFKVTLMAE 2163
Cdd:cd14629    82 DYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKcHQYWP-AERSARYQYFVVDPMAE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2164 ehkclSNEEKLIMQDFILEATQDDYVLEVRHFQCPKWPNPDSPisKTFE-LISIIKEEAATR-----DGPMIVHDEHGGV 2237
Cdd:cd14629   161 -----YNMPQYILREFKVTDARDGQSRTIRQFQFTDWPEQGVP--KTGEgFIDFIGQVHKTKeqfgqDGPITVHCSAGVG 233

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 300795888 2238 TAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAVLSLVST 2294
Cdd:cd14629   234 RTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALEYLGS 290
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 2056-2289 4.33e-47

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: 169.63  E-value: 4.33e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2056 CNREKNRTSSIIPVERSRVGISSLSG-EGADYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDGQ 2134
Cdd:cd14554     5 CNKFKNRLVNILPYESTRVCLQPIRGvEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTKLR 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2135 NMAEDE-FVYWPNkDEPINCESFKVTLMAEehkclSNEEKLIMQDFILEATQDDYVLEVRHFQCPKWPNPDSPisKTFE- 2212
Cdd:cd14554    85 EMGREKcHQYWPA-ERSARYQYFVVDPMAE-----YNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVP--KSGEg 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2213 LISIIKEEAATR-----DGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYKA 2287
Cdd:cd14554   157 FIDFIGQVHKTKeqfgqEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRA 236


                  ..
gi 300795888 2288 VL 2289
Cdd:cd14554   237 AL 238
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 1750-1995 1.94e-46

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 170.57  E-value: 1.94e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1750 TADSSNHPDNKHKNRYINIVAYDHSRVKLAQlaeKDGKLTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNV 1829
Cdd:PHA02747   42 LIANFEKPENQPKNRYWDIPCWDHNRVILDS---GGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHC 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1830 EVIVMIT-NLVEKGRRKCDQYWPV--DGSEEYGNFLVTQKSIQVLAYYTVRNFTLRNtKIKKGSQKgrpsgrvVTQYHYT 1906
Cdd:PHA02747  119 SIIVMLTpTKGTNGEEKCYQYWCLneDGNIDMEDFRIETLKTSVRAKYILTLIEITD-KILKDSRK-------ISHFQCS 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1907 QWPDMGVPEYSLPVLTF------VRKAS----HAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKH 1976
Cdd:PHA02747  191 EWFEDETPSDHPDFIKFikiidiNRKKSgklfNPKDALLCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEK 270

                         250
                  ....*....|....*....
gi 300795888 1977 IRSQRNYLVQTEEQYVFIH 1995
Cdd:PHA02747  271 IREQRHAGIMNFDDYLFIQ 289
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 1759-1993 1.98e-46

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 170.18  E-value: 1.98e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1759 NKHKNRYINIVAYDHSRVKLAQlaeKDGkLTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNL 1838
Cdd:PHA02742   52 NMKKCRYPDAPCFDRNRVILKI---EDG-GDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKI 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1839 VEKGRRKCDQYWPVD--GSEEYGNFLVTQKSIQVLAYYTVRNFTLRNTKikkgsqkgrpSGRV--VTQYHYTQWPDMGVP 1914
Cdd:PHA02742  128 MEDGKEACYPYWMPHerGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTN----------TGASldIKHFAYEDWPHGGLP 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1915 EYSLPVLTFVRKASHAK-----------RHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNY 1983
Cdd:PHA02742  198 RDPNKFLDFVLAVREADlkadvdikgenIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHN 277

                         250
                  ....*....|
gi 300795888 1984 LVQTEEQYVF 1993
Cdd:PHA02742  278 CLSLPQQYIF 287
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 1791-1996 2.11e-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: 2.11e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1791 YINANYVDGY-NRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPVD-GSE-EYGNFLVTQKS 1867
Cdd:cd14539     1 YINASLIEDLtPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTErGQAlVYGAITVSLQS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1868 IQVLAYYTVRNFTlrntkIKKGSQKGRpsgRVVTQYHYTQWPDMGVPEYSLPVLTFVRKA-SH--AKRHAVGPVVVHCSA 1944
Cdd:cd14539    81 VRTTPTHVERIIS-----IQHKDTRLS---RSVVHLQFTTWPELGLPDSPNPLLRFIEEVhSHylQQRSLQTPIVVHCSS 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 300795888 1945 GVGRTGTYIVLDSMLQQIQHE-GTVNVFGFLKHIRSQRNYLVQTEEQYVFIHD 1996
Cdd:cd14539   153 GVGRTGAFCLLYAAVQEIEAGnGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 1791-1995 1.17e-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: 1.17e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1791 YINANYV---DGYNRPKaYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRR-KCDQYWPVD--GSEEYGNFLVT 1864
Cdd:cd17658     1 YINASLVetpASESLPK-FIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTaKCADYFPAEenESREFGRISVT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1865 QKSIQvlayYTVRNFTLRNTKIKKGSQKGRPsgRVVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAKRHAvGPVVVHCSA 1944
Cdd:cd17658    80 NKKLK----HSQHSITLRVLEVQYIESEEPP--LSVLHIQYPEWPDHGVPKDTRSVRELLKRLYGIPPSA-GPIVVHCSA 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 300795888 1945 GVGRTGTYIVLDSMLQQIQhEG---TVNVFGFLKHIRSQRNYLVQTEEQYVFIH 1995
Cdd:cd17658   153 GIGRTGAYCTIHNTIRRIL-EGdmsAVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 1750-2003 1.90e-45

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 167.90  E-value: 1.90e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1750 TADSSNHPDNKHKNRYINIVAYDHSRV--------KLAQLAEKDGKL---------TDYINANYVDGYNRPKAYIAAQGP 1812
Cdd:PHA02746   42 TTNHFLKKENLKKNRFHDIPCWDHSRVvinaheslKMFDVGDSDGKKievtsednaENYIHANFVDGFKEANKFICAQGP 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1813 LKSTAEDFWRMIWEHNVEVIVMITNlVEKGRRKCDQYW--PVDGSEEYGNFLVtqKSIQVLAYYTVRNFTLRNTkikkgs 1890
Cdd:PHA02746  122 KEDTSEDFFKLISEHESQVIVSLTD-IDDDDEKCFELWtkEEDSELAFGRFVA--KILDIIEELSFTKTRLMIT------ 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1891 QKGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAKR----------HAVGPVVVHCSAGVGRTGTYIVLDSMLQ 1960
Cdd:PHA02746  193 DKISDTSREIHHFWFPDWPDNGIPTGMAEFLELINKVNEEQAelikqadndpQTLGPIVVHCSAGIGRAGTFCAIDNALE 272

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 300795888 1961 QIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDALVEAIL 2003
Cdd:PHA02746  273 QLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKALKYAII 315
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 1791-1996 2.32e-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: 163.35  E-value: 2.32e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1791 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMItNLVEKGRRKCDQYWPVDGSEEYGNFLVTQKSIQV 1870
Cdd:cd14556     1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVML-NQLDPKDQSCPQYWPDEGSGTYGPIQVEFVSTTI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1871 LAYYTVRNFTLRNTKikkgsqkgRPS--GRVVTQYHYTQWPDMG----VPEYSLPVLTFVRKAShaKRHAVGPVVVHCSA 1944
Cdd:cd14556    80 DEDVISRIFRLQNTT--------RPQegYRMVQQFQFLGWPRDRdtppSKRALLKLLSEVEKWQ--EQSGEGPIVVHCLN 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 300795888 1945 GVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHD 1996
Cdd:cd14556   150 GVGRSGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 2062-2286 3.07e-42

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


Pssm-ID: 350396 [Multi-domain]  Cd Length: 222  Bit Score: 155.20  E-value: 3.07e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2062 RTSSIIPVERSRVGISSLSG-EGADYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLpdgQNMAEDE 2140
Cdd:cd14548     1 RYTNILPYDHSRVKLIPINEeEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVML---TQCMEKG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2141 FV----YWPNKDEPINCESFKVTLMAEEHkclsnEEKLIMQDFILEatQDDYVLEVRHFQCPKWPN---PDSPISktfeL 2213
Cdd:cd14548    78 RVkcdhYWPFDQDPVYYGDITVTMLSESV-----LPDWTIREFKLE--RGDEVRSVRQFHFTAWPDhgvPEAPDS----L 146

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300795888 2214 ISIIKEEAATRD---GPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYK 2286
Cdd:cd14548   147 LRFVRLVRDYIKqekGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLHQ 222
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 2086-2285 6.34e-42

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


Pssm-ID: 350404 [Multi-domain]  Cd Length: 201  Bit Score: 153.33  E-value: 6.34e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2086 YINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDGQNMAEDEFVYWPNKdepincESFKVTLMAEEH 2165
Cdd:cd14556     1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDQSCPQYWPDE------GSGTYGPIQVEF 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2166 KCLSNEEKLIMQDFILEAT---QDDYVLeVRHFQCPKWP-NPDSPISKT--FELISII-KEEAATRDGPMIVHDEHGGVT 2238
Cdd:cd14556    75 VSTTIDEDVISRIFRLQNTtrpQEGYRM-VQQFQFLGWPrDRDTPPSKRalLKLLSEVeKWQEQSGEGPIVVHCLNGVGR 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 300795888 2239 AGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLY 2285
Cdd:cd14556   154 SGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCY 200
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 2086-2288 9.46e-42

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


Pssm-ID: 350400 [Multi-domain]  Cd Length: 202  Bit Score: 152.81  E-value: 9.46e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2086 YINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDGQNMAEDE-FVYWPNkDEPINCESFKVTLMAEE 2164
Cdd:cd14552     1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKcAQYWPE-DGSVSSGDITVELKDQT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2165 hkclsNEEKLIMQDFILEATQDDYVLEVRHFQCPKWPNPDSPiSKTFELISII----KEEAATRDGPMIVHDEHGGVTAG 2240
Cdd:cd14552    80 -----DYEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIP-DNGKGMIDLIaavqKQQQQSGNHPITVHCSAGAGRTG 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 300795888 2241 TFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAV 2288
Cdd:cd14552   154 TFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 2062-2288 1.53e-41

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: 153.28  E-value: 1.53e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2062 RTSSIIPVERSRVGISSLSGE-GADYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDGQNMAEDE 2140
Cdd:cd14623     1 RVLQIIPYEFNRVIIPVKRGEeNTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2141 FV-YWPNkDEPINCESFKVTLMAEEhKClsneEKLIMQDFILEATQDDYVLEVRHFQCPKWPNPDSPiSKTFELISII-- 2217
Cdd:cd14623    81 CAqYWPS-DGSVSYGDITIELKKEE-EC----ESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIP-SDGKGMINIIaa 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300795888 2218 --KEEAATRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAV 2288
Cdd:cd14623   154 vqKQQQQSGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVV 226
alpha_CA_VI cd03125
Carbonic anhydrase alpha, isozyme VI. Carbonic anhydrases (CAs) are zinc-containing enzymes ...
 45-300 6.15e-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: 6.15e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888   45 NQKNWGKKYPTCNSPKQSPINIDEDLTQVNVNLKKLKFQDWDKTSLENTFIHNtGKTVEINLTNDYRLSGGVSeTVFKAS 124
Cdd:cd03125     1 DESHWPEKYPACGGKRQSPIDIQRREVRFNPSLLQLELVGYEKEQGEFTMTNN-GHTVQIDLPPTMSITTGDG-TVYTAV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888  125 KIAFHWGKCNMSSDGSEHSLEGQKFPLEMQIYCFDADrFSSFEEAIKGKGKLRALSILFEVG-IEENLDYKAIIDGVERV 203
Cdd:cd03125    79 QMHFHWGGRDSEISGSEHTIDGMRYVAELHIVHYNSK-YKSYEEAKDKPDGLAVLAFLYKVGhYAENTYYSDFISKLAKI 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888  204 SRFGKQAALDPFTLLNLLPNSTDKYYTYNGSLTSPPCTDTVDWIIFKDTVSISESQlavfceVLTMQQSgyvmLMDY--- 280
Cdd:cd03125   158 KYAGQTTTLTSLDVRDMLPENLHHYYTYQGSLTTPPCTENVLWFVFDDPVTLSKTQ------IVKLENT----LMDHhnk 227

                         250       260
                  ....*....|....*....|.
gi 300795888  281 -LQNNFREQQYKFSRQVFSSY 300
Cdd:cd03125   228 tIRNDYRRTQPLNHRVVEANF 248
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 2086-2285 2.80e-40

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: 148.69  E-value: 2.80e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2086 YINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPD-GQNMAEDEFVYWPNKDEpiNCESFKVTLMAEE 2164
Cdd:cd14558     1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTElKEGDQEQCAQYWGDEKK--TYGDIEVELKDTE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2165 hkclsNEEKLIMQDFILEATQDDYVLEVRHFQCPKWpNPDSPISKTFELISIIKE---------EAATRDGPMIVHDEHG 2235
Cdd:cd14558    79 -----KSPTYTVRVFEITHLKRKDSRTVYQYQYHKW-KGEELPEKPKDLVDMIKSikqklpyknSKHGRSVPIVVHCSDG 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 300795888 2236 GVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLY 2285
Cdd:cd14558   153 SSRTGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
1734-1994 5.69e-40

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 150.63  E-value: 5.69e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1734 KEFYQEVQSCTVDLGITADSSNHPDN---KHKNRYINIVAYDHSRVklaqlaEKDGKltdYINANYVDGYNrPKAYIAAQ 1810
Cdd:COG5599    14 EKINSRLSTLTNELAPSHNDPQYLQNingSPLNRFRDIQPYKETAL------RANLG---YLNANYIQVIG-NHRYIATQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1811 GPLKSTAEDFWRMIWEHNVEVIVMITNLVE--KGRRKCDQYWPVDGseEYGNFLVTQKSIQVlaYYTVRNFTLRNTKIK- 1887
Cdd:COG5599    84 YPLEEQLEDFFQMLFDNNTPVLVVLASDDEisKPKVKMPVYFRQDG--EYGKYEVSSELTES--IQLRDGIEARTYVLTi 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1888 KGS-QKGRPsgrvVTQYHYTQWPDMGVP--EYSLPVLTFVRKASHAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQ- 1963
Cdd:COG5599   160 KGTgQKKIE----IPVLHVKNWPDHGAIsaEALKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINa 235

                         250       260       270
                  ....*....|....*....|....*....|...
gi 300795888 1964 -HEGTVNVFGFLKHIRSQRNY-LVQTEEQYVFI 1994
Cdd:COG5599   236 lVQITLSVEEIVIDMRTSRNGgMVQTSEQLDVL 268
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 1900-2000 6.61e-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: 6.61e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888   1900 VTQYHYTQWPDMGVPEYSLPVLTFVR--KASHAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHE-GTVNVFGFLKH 1976
Cdd:smart00012    2 VKHYHYTGWPDHGVPESPDSILELLRavKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVKE 81

                            90       100
                    ....*....|....*....|....
gi 300795888   1977 IRSQRNYLVQTEEQYVFIHDALVE 2000
Cdd:smart00012   82 LRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1900-2000 6.61e-40

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 144.04  E-value: 6.61e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888   1900 VTQYHYTQWPDMGVPEYSLPVLTFVR--KASHAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHE-GTVNVFGFLKH 1976
Cdd:smart00404    2 VKHYHYTGWPDHGVPESPDSILELLRavKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVKE 81

                            90       100
                    ....*....|....*....|....
gi 300795888   1977 IRSQRNYLVQTEEQYVFIHDALVE 2000
Cdd:smart00404   82 LRSQRPGMVQTEEQYLFLYRALLE 105
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 1791-2000 7.86e-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: 7.86e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1791 YINANYVDGYNRPKA--YIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPVDGSEE----YGNFLVT 1864
Cdd:cd14598     1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRLGSRHntvtYGRFKIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1865 QKSIQVLAYYTVRNFTLRNtkIKKGSQkgrpsgRVVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAKRHAVG-------- 1936
Cdd:cd14598    81 TRFRTDSGCYATTGLKIKH--LLTGQE------RTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHTNStidpkspn 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 300795888 1937 -PVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDALVE 2000
Cdd:cd14598   153 pPVLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQ 217
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 2061-2289 2.49e-39

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: 147.01  E-value: 2.49e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2061 NRTSSIIPVERSRVGISSLSGE-GADYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLP----DGQN 2135
Cdd:cd14618     1 NRYPHVLPYDHSRVRLSQLGGEpHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTvgmeNGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2136 MAEDefvYWPNKDEPINCESFKVTLMAEEhkclsNEEKLIMQDFILEATQDDYVLEVRHFQCPKWPN---PDSPISkTFE 2212
Cdd:cd14618    81 LCDH---YWPSESTPVSYGHITVHLLAQS-----SEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDhgiPESTSS-LMA 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300795888 2213 LISIIKEEA-ATRD-GPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAVL 2289
Cdd:cd14618   152 FRELVREHVqATKGkGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
alpha_CA_IX cd03150
Carbonic anhydrase alpha, isozyme IX. Carbonic anhydrases (CAs) are zinc-containing enzymes ...
 45-300 5.27e-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: 5.27e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888   45 NQKNWGKKYPTCNSPKQSPINIDEDLTQVNVNLKKLKFQDWDKTSLENTFIHNTGKTVEINLTNDYRLSGGVSEtVFKAS 124
Cdd:cd03150     1 GQPPWPSVSPACAGRFQSPVDIRPHLVAFCPALRPLELLGFDLPPSPSLRLLNNGHTVQLSLPSGLRMALGPGQ-EYRAL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888  125 KIAFHWGKCNMSsdGSEHSLEGQKFPLEMQIYCFDAdRFSSFEEAIKGKGKLRALSILFEVGIEENLDYKAIIDGVERVS 204
Cdd:cd03150    80 QLHLHWGAAGRP--GSEHTVDGHRFPAEIHVVHLST-AFANLDEALGRPGGLAVLAAFLAEGLHENSAYEQLLSRLSEIS 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888  205 RFGKQAALDPFTLLNLLPNSTDKYYTYNGSLTSPPCTDTVDWIIFKDTVSISESQLAVFCEVLTMQQSgyvmlmDYLQNN 284
Cdd:cd03150   157 EEESETVVPGLDVSALLPSDLSRYFRYEGSLTTPPCAQGVIWTVFNQTVRLSAKQLHTLSDSLWGPHD------SRLQLN 230

                         250
                  ....*....|....*.
gi 300795888  285 FREQQYKFSRQVFSSY 300
Cdd:cd03150   231 FRATQPLNGRKIEASF 246
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 2085-2288 4.43e-37

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


Pssm-ID: 350470 [Multi-domain]  Cd Length: 205  Bit Score: 139.76  E-value: 4.43e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2085 DYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDGQNMAEDE-FVYWPNKDEPINCEsfkVTLmae 2163
Cdd:cd14622     1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKcVQYWPSEGSVTHGE---ITI--- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2164 EHKCLSNEEKLIMQDFILEATQDDYVLEVRHFQCPKWPNPDSPiSKTFELISII----KEEAATRDGPMIVHDEHGGVTA 2239
Cdd:cd14622    75 EIKNDTLLETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIP-AEGKGMIDLIaavqKQQQQTGNHPIVVHCSAGAGRT 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 300795888 2240 GTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAV 2288
Cdd:cd14622   154 GTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 2061-2289 8.62e-37

catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type tyrosine-protein phosphatase J (PTPRJ or R-PTP-J), also known as receptor-type tyrosine-protein phosphatase eta (R-PTP-eta) or density-enhanced phosphatase 1 (DEP-1) OR CD148, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRJ is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats (eight in PTPRJ) and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is expressed in various cell types including epithelial, hematopoietic, and endothelial cells. It plays a role in cell adhesion, migration, proliferation and differentiation. It dephosphorylates or contributes to the dephosphorylation of various substrates including protein kinases such as FLT3, PDGFRB, MET, RET (variant MEN2A), VEGFR-2, LYN, SRC, MAPK1, MAPK3, and EGFR, as well as PIK3R1 and PIK3R2.


Pssm-ID: 350463 [Multi-domain]  Cd Length: 229  Bit Score: 139.57  E-value: 8.62e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2061 NRTSSIIPVERSRVGISSLSGEGADYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPD----GQNM 2136
Cdd:cd14615     1 NRYNNVLPYDISRVKLSVQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKcveqGRTK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2137 AEDefvYWPNKdEPINCESFKVTLMAEehkclSNEEKLIMQDFILEATQDDYVLEVRHFQCPKWpnPDSPISKTFELI-- 2214
Cdd:cd14615    81 CEE---YWPSK-QKKDYGDITVTMTSE-----IVLPEWTIRDFTVKNAQTNESRTVRHFHFTSW--PDHGVPETTDLLin 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300795888 2215 --SIIKE--EAATRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAVL 2289
Cdd:cd14615   150 frHLVREymKQNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCAL 228
alpha_CA_I_II_III_XIII cd03119
Carbonic anhydrase alpha, isozymes I, II, and III and XIII. Carbonic anhydrases (CAs) are ...
 38-300 3.34e-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: 139.11  E-value: 3.34e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888   38 WSYTGALNQKNWGKKYPTCNSPKQSPINIDEDLTQVNVNLKKLKFqDWDKTSLENtfIHNTGKTVEINLTNDYR---LSG 114
Cdd:cd03119     5 WGYDSHNGPEHWHELFPIAKGDRQSPIDIKTKDAKHDPSLKPLSV-SYDPATAKT--ILNNGHSFNVEFDDTDDrsvLRG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888  115 GVSETVFKASKIAFHWGKCNmsSDGSEHSLEGQKFPLEMQIYCFDAdRFSSFEEAIKGKGKLRALSILFEVGiEENLDYK 194
Cdd:cd03119    82 GPLTGSYRLRQFHFHWGSSD--DHGSEHTVDGVKYAAELHLVHWNS-KYGSFGEAAKQPDGLAVVGVFLKVG-EANPELQ 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888  195 AIIDGVERVSRFGKQAALDPFTLLNLLPNSTDkYYTYNGSLTSPPCTDTVDWIIFKDTVSISESQLAVFCEVLTMQQSGY 274
Cdd:cd03119   158 KVLDALDSIKTKGKQAPFTNFDPSCLLPASLD-YWTYPGSLTTPPLLECVTWIVLKEPISVSSEQMAKFRSLLFNAEGEP 236

                         250       260
                  ....*....|....*....|....*.
gi 300795888  275 VMLMdylQNNFREQQYKFSRQVFSSY 300
Cdd:cd03119   237 PCPM---VDNWRPPQPLKGRKVRASF 259
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 2055-2293 9.70e-36

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: 137.14  E-value: 9.70e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2055 QCNREKNRTSSIIPVERSRVGISSLSG-EGADYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLpdg 2133
Cdd:cd14553     1 EVNKPKNRYANVIAYDHSRVILQPIEGvPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMM--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2134 QNMAEDEFV----YWPNKDEPiNCESFKVTLMAEEHkcLSNeekLIMQDFILEATQDDYVLEVRHFQCPKWPN---PDSP 2206
Cdd:cd14553    78 TKLEERSRVkcdqYWPTRGTE-TYGLIQVTLLDTVE--LAT---YTVRTFALHKNGSSEKREVRQFQFTAWPDhgvPEHP 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2207 ISkTFELISIIKEEAATRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYK 2286
Cdd:cd14553   152 TP-FLAFLRRVKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHD 230


                  ....*..
gi 300795888 2287 AVLSLVS 2293
Cdd:cd14553   231 ALLEAVT 237
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 2057-2289 1.48e-35

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


Pssm-ID: 350462 [Multi-domain]  Cd Length: 245  Bit Score: 136.56  E-value: 1.48e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2057 NREKNRTSSIIPVERSRVGISSLSG-EGADYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLP---D 2132
Cdd:cd14614    12 NRCKNRYTNILPYDFSRVKLVSMHEeEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTqcnE 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2133 GQNMAEDEfvYWPNKDEPINCESFKVTLMAEEhkclsNEEKLIMQDFILeaTQDDYVLEVRHFQCPKWPNPDSPISKTFE 2212
Cdd:cd14614    92 KRRVKCDH--YWPFTEEPVAYGDITVEMLSEE-----EQPDWAIREFRV--SYADEVQDVMHFNYTAWPDHGVPTANAAE 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2213 ----LISIIKEEAATRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAV 2288
Cdd:cd14614   163 silqFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 242


                  .
gi 300795888 2289 L 2289
Cdd:cd14614   243 Q 243
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 1791-1994 4.86e-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: 4.86e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1791 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGrrKCDQYWPVDGSE-EYGNFLVTQ--KS 1867
Cdd:cd14550     1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNE--DEPIYWPTKEKPlECETFKVTLsgED 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1868 IQVLAY---YTVRNFTLRNTKikkgsqkgrpSGRVVT--QYHYTQWPDMGVPEYSlpVLTFVRKASHAKRHAVGPVVVHC 1942
Cdd:cd14550    79 HSCLSNeirLIVRDFILESTQ----------DDYVLEvrQFQCPSWPNPCSPIHT--VFELINTVQEWAQQRDGPIVVHD 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 300795888 1943 SAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFI 1994
Cdd:cd14550   147 RYGGVQAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFL 198
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 2061-2292 1.23e-34

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: 133.48  E-value: 1.23e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2061 NRTSSIIPVERSRVGISSLSGE-GADYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLpdgQNMAED 2139
Cdd:cd14619     1 NRFRNVLPYDWSRVPLKPIHEEpGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVML---TNCMEA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2140 EFV----YWPNKDEPINCESFKVTLMAEEhkclsNEEKLIMQDFILEATQDDYVLEVRHFQCPKWPNPDSPiSKTFELIS 2215
Cdd:cd14619    78 GRVkcehYWPLDYTPCTYGHLRVTVVSEE-----VMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVP-SSTDTLLA 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2216 ---IIKE--EAATRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAVLS 2290
Cdd:cd14619   152 frrLLRQwlDQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILD 231


                  ..
gi 300795888 2291 LV 2292
Cdd:cd14619   232 FL 233
alpha_CA_V cd03118
Carbonic anhydrase alpha, CA isozyme V_like subgroup. Carbonic anhydrases (CAs) are ...
 60-300 2.43e-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: 133.05  E-value: 2.43e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888   60 KQSPINIDEDLTQVNVNLKKLKFQDWDKTSLentFIHNTGKTVEINL---TNDYRLSGGVSETVFKASKIAFHWGKCNms 136
Cdd:cd03118     3 RQSPINIQWRDSVYDPQLAPLRVSYDPATCL---YIWNNGYSFQVEFddsTDKSGISGGPLENHYRLKQFHFHWGANN-- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888  137 SDGSEHSLEGQKFPLEMQIYCFDADRFSSFEEAIKGKGKLRALSILFEVGIE-ENLdyKAIIDGVERVSRFGKQAALDPF 215
Cdd:cd03118    78 EWGSEHTVDGHTYPAELHLVHWNSVKYENFEEAVMEENGLAVIGVFLKLGAHhEGL--QKLVDALPEVRHKDTVVEFNPF 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888  216 TLLNLLPNSTDkYYTYNGSLTSPPCTDTVDWIIFKDTVSISESQLAVFCEVLTmqqSGYVMLMDYLQNNFREQQYKFSRQ 295
Cdd:cd03118   156 DPSCLLPACRD-YWTYPGSLTTPPLTESVTWIIQKQPIEVSPSQLSVFRTLLF---TSRGEEEKVMVNNFRPLQPLMNRK 231


                  ....*
gi 300795888  296 VFSSY 300
Cdd:cd03118   232 VRSSF 236
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 2045-2289 2.75e-34

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: 134.01  E-value: 2.75e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2045 QQSDYSTALKQCNREKNRTSSIIPVERSRVGISSLSGE-GADYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHN 2123
Cdd:cd14633    28 QSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGEtSSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHEN 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2124 AQLVVMLpdgQNMAEDEFV----YWPNKDEPIncESFKVTLMaeEHKCLSneeKLIMQDFILEATQDDYVLEVRHFQCPK 2199
Cdd:cd14633   108 TASIIMV---TNLVEVGRVkcckYWPDDTEIY--KDIKVTLI--ETELLA---EYVIRTFAVEKRGVHEIREIRQFHFTG 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2200 WPNPDSPISKT--FELISIIKEEAATRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFAD 2277
Cdd:cd14633   178 WPDHGVPYHATglLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQT 257

                         250
                  ....*....|..
gi 300795888 2278 IEQYQFLYKAVL 2289
Cdd:cd14633   258 EEQYVFIHDAIL 269
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 2046-2288 3.20e-34

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: 133.41  E-value: 3.20e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2046 QSDYSTAL----KQCNREKNRTSSIIPVERSRVGISSLSGEG-ADYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIW 2120
Cdd:cd14603    15 KADYVCSTvaggRKENVKKNRYKDILPYDQTRVILSLLQEEGhSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIW 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2121 DHNAQLVVM----LPDGQNMAEdefVYWPNKDEPINCESFKVTLMAEEHkclSNEEKLIMQdfiLEATQDDYVLEVRHFQ 2196
Cdd:cd14603    95 QYGVKVILMacreIEMGKKKCE---RYWAQEQEPLQTGPFTITLVKEKR---LNEEVILRT---LKVTFQKESRSVSHFQ 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2197 CPKWPN---PDSPiSKTFELISIIKEEAATRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLM--- 2270
Cdd:cd14603   166 YMAWPDhgiPDSP-DCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPDFSIFDVVLEMrkq 244

                         250
                  ....*....|....*...
gi 300795888 2271 RPGVFADIEQYQFLYKAV 2288
Cdd:cd14603   245 RPAAVQTEEQYEFLYHTV 262
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 2052-2286 1.89e-33

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: 131.33  E-value: 1.89e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2052 ALKQCNREKNRTSSIIPVERSRVGISSLSG-EGADYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVML 2130
Cdd:cd14543    24 SLAPANQEKNRYGDVLCLDQSRVKLPKRNGdERTDYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKVLVIVMT 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2131 PD---------GQnmaedefvYWPNKDEpiNCESF-KVTLmaeEHKCLSNEEKLIMQDFILEATQDDYVLEVRHFQCPKW 2200
Cdd:cd14543   104 TRvvergrvkcGQ--------YWPLEEG--SSLRYgDLTV---TNLSVENKEHYKKTTLEIHNTETDESRQVTHFQFTSW 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2201 PN---PDSPISKTFELISIIKEEAA------------TRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAK 2265
Cdd:cd14543   171 PDfgvPSSAAALLDFLGEVRQQQALavkamgdrwkghPPGPPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQTVR 250

                         250       260
                  ....*....|....*....|.
gi 300795888 2266 MINLMRPGVFADIEQYQFLYK 2286
Cdd:cd14543   251 RMRTQRAFSIQTPDQYYFCYK 271
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 2061-2285 1.53e-32

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


Pssm-ID: 350395 [Multi-domain]  Cd Length: 224  Bit Score: 127.13  E-value: 1.53e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2061 NRTSSIIPVERSRVGISSL-SGEGADYINASYIMGY-YQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDGQNMAE 2138
Cdd:cd14547     1 NRYKTILPNEHSRVCLPSVdDDPLSSYINANYIRGYdGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEAKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2139 DEFVYWPNKdEPINCESFKVTLMAEEHKclsneEKLIMQDFILEatqddYVLEVR---HFQCPKWPNPDSPiSKTFELIS 2215
Cdd:cd14547    81 KCAQYWPEE-ENETYGDFEVTVQSVKET-----DGYTVRKLTLK-----YGGEKRylkHYWYTSWPDHKTP-EAAQPLLS 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300795888 2216 IIKE-----EAATRDGPMIVHDEHG-GVTaGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLY 2285
Cdd:cd14547   149 LVQEveearQTEPHRGPIVVHCSAGiGRT-GCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVH 223
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 2060-2291 1.92e-32

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: 127.26  E-value: 1.92e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2060 KNRTSSIIPVERSRVGISSL-SGEGADYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVM----LPDGQ 2134
Cdd:cd14602     1 KNRYKDILPYDHSRVELSLItSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMacmeFEMGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2135 NMAEDefvYWPN-KDEPINCESFKVTLMAEEHKclsnEEKLIMqdfILEATQDDYVLEVRHFQCPKWPNPDSP--ISKTF 2211
Cdd:cd14602    81 KKCER---YWAEpGEMQLEFGPFSVTCEAEKRK----SDYIIR---TLKVKFNSETRTIYQFHYKNWPDHDVPssIDPIL 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2212 ELISIIKEEAATRDGPMIVHDEHGGVTAGTFCALTTLMHQLEK----ENsMDVYQVAKMINLMRPGVFADIEQYQFLYKA 2287
Cdd:cd14602   151 ELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDgiipEN-FSVFSLIQEMRTQRPSLVQTKEQYELVYNA 229


                  ....
gi 300795888 2288 VLSL 2291
Cdd:cd14602   230 VIEL 233
alpha_CA_prokaryotic_like cd03124
Carbonic anhydrase alpha, prokaryotic-like subfamily. Carbonic anhydrases (CAs) are ...
 45-263 4.14e-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: 125.85  E-value: 4.14e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888   45 NQKNWG---KKYPTCNS-PKQSPINIDEDLTQVNVnLKKLKFQdWDKTSLEntfIHNTGKTVEINLTNDyrlsGGVSE-- 118
Cdd:cd03124     1 GPEHWGnldPEFALCATgKNQSPIDITTKAVVSDK-LPPLNYN-YKPTSAT---LVNNGHTIQVNFEGN----GGTLTid 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888  119 -TVFKASKIAFHwgkcnmssDGSEHSLEGQKFPLEMQIycfdadrfsSFEEAikgKGKLRALSILFEVGiEENLDYKAII 197
Cdd:cd03124    72 gETYQLLQFHFH--------SPSEHLINGKRYPLEAHL---------VHKSK---DGQLAVVAVLFEEG-KENPFLKKIL 130

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300795888  198 DGVErvSRFGKQAALDPFTLLN-LLPNSTDkYYTYNGSLTSPPCTDTVDWIIFKDTVSISESQLAVF 263
Cdd:cd03124   131 DNMP--KKEGTEVNLPAILDPNeLLPESRS-YYRYEGSLTTPPCSEGVRWIVLKQPITISKEQLAKF 194
Cah COG3338
Carbonic anhydrase [Inorganic ion transport and metabolism];
38-263 1.01e-31

Carbonic anhydrase [Inorganic ion transport and metabolism];


Pssm-ID: 442567 [Multi-domain]  Cd Length: 247  Bit Score: 125.77  E-value: 1.01e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888   38 WSYTGALNQKNWGK---KYPTCNS-PKQSPINIDedlTQVNVNLKKLKFqDWDKTSLEntfIHNTGKTVEINLTNDYRLS 113
Cdd:COG3338    28 WSYEGETGPEHWGElspEFATCATgKNQSPIDIR---TAIKADLPPLKF-DYKPTPLE---IVNNGHTIQVNVDPGSTLT 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888  114 ggVSETVFKASKIAFHwgkcnmssDGSEHSLEGQKFPLEMQiycF---DADrfssfeeaikgkGKLRALSILFEVGiEEN 190
Cdd:COG3338   101 --VDGKRYELKQFHFH--------TPSEHTINGKSYPMEAH---LvhkDAD------------GELAVVGVLFEEG-AEN 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300795888  191 ldykAIIDGVERV--SRFGKQAALD-PFTLLNLLPNSTDkYYTYNGSLTSPPCTDTVDWIIFKDTVSISESQLAVF 263
Cdd:COG3338   155 ----PALAKLWANlpLEAGEEVALDaTIDLNDLLPEDRS-YYRYSGSLTTPPCSEGVLWIVLKQPITVSAEQIEAF 225
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 2057-2289 3.14e-31

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: 123.98  E-value: 3.14e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2057 NREKNRTSSIIPVERSRVGISSLSGE-GADYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDGQN 2135
Cdd:cd14630     3 NRNKNRYGNIISYDHSRVRLQLLDGDpHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2136 MAEDEFV-YWPNKDEPINceSFKVTLMAEEHKClsneeKLIMQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKT--FE 2212
Cdd:cd14630    83 VGRVKCVrYWPDDTEVYG--DIKVTLIETEPLA-----EYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATglLG 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300795888 2213 LISIIKEEAATRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAVL 2289
Cdd:cd14630   156 FVRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAIL 232
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 2086-2285 4.06e-31

fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae protein-tyrosine phosphatases 1 (PTP1) and 2 (PTP2), Schizosaccharomyces pombe PTP1, PTP2, and PTP3, and similar fungal proteins. PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. PTP2, together with PTP3, is the major phosphatase that dephosphorylates and inactivates the MAP kinase HOG1 and also modulates its subcellular localization.


Pssm-ID: 350509 [Multi-domain]  Cd Length: 212  Bit Score: 122.74  E-value: 4.06e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2086 YINASYI-MGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVML-PDGQNMAEDEFVYWPNKDEPINCESFKVTLMae 2163
Cdd:cd18533     1 YINASYItLPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLtPLVENGREKCDQYWPSGEYEGEYGDLTVELV-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2164 ehkclsNEEKLIMQDFI---LEATQDDYVL-EVRHFQCPKWPN---PDSPISkTFELISIIKE--EAATRDGPMIVHDEH 2234
Cdd:cd18533    79 ------SEEENDDGGFIvreFELSKEDGKVkKVYHIQYKSWPDfgvPDSPED-LLTLIKLKRElnDSASLDPPIIVHCSA 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 300795888 2235 G-GVTaGTFCALTTLMHQLEKENSMDVYQ------VAKMINLM---RPGVFADIEQYQFLY 2285
Cdd:cd18533   152 GvGRT-GTFIALDSLLDELKRGLSDSQDLedsedpVYEIVNQLrkqRMSMVQTLRQYIFLY 211
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 2060-2285 1.01e-30

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


Pssm-ID: 350460 [Multi-domain]  Cd Length: 247  Bit Score: 122.64  E-value: 1.01e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2060 KNRTSSIIPVERSRVGISSL--SGEGADYINASYIMGYY-QSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDGQNM 2136
Cdd:cd14612    18 KDRYKTILPNPQSRVCLRRAgsQEEEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMITKLKEK 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2137 AEDEFVYWPNKDEPINCESFKVTLMAEehkClsneEKLIMQDFILEATQDDYvlEVRHFQCPKWPNPDSPISKT--FELI 2214
Cdd:cd14612    98 KEKCVHYWPEKEGTYGRFEIRVQDMKE---C----DGYTIRDLTIQLEEESR--SVKHYWFSSWPDHQTPESAGplLRLV 168

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300795888 2215 SIIKE--EAATRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLY 2285
Cdd:cd14612   169 AEVEEsrQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLH 241
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 2060-2291 1.57e-30

catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein phosphatase non-receptor type 5 (PTPN5), also called striatum-enriched protein-tyrosine phosphatase (STEP) or neural-specific PTP, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN5/STEP is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. It is a CNS-enriched protein that regulates key signaling proteins required for synaptic strengthening, as well as NMDA and AMPA receptor trafficking. PTPN5 is implicated in multiple neurologic and neuropsychiatric disorders, such as Alzheimer's disease, Parkinson's disease, schizophrenia, and fragile X syndrome.


Pssm-ID: 350461 [Multi-domain]  Cd Length: 258  Bit Score: 122.66  E-value: 1.57e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2060 KNRTSSIIPVERSRVGISSLSGEG--ADYINASYIMGY-YQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDGQNM 2136
Cdd:cd14613    28 KNRYKTILPNPHSRVCLTSPDQDDplSSYINANYIRGYgGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEM 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2137 AEDEFVYWPnkDEPINCESFKVTLMAEEHkclsnEEKLIMQDFILEATQDDYVLevRHFQCPKWPNPDSPiSKTFELISI 2216
Cdd:cd14613   108 NEKCTEYWP--EEQVTYEGIEITVKQVIH-----ADDYRLRLITLKSGGEERGL--KHYWYTSWPDQKTP-DNAPPLLQL 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2217 IKE------EAATRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYKaVLS 2290
Cdd:cd14613   178 VQEveearqQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVHH-VLS 256


                  .
gi 300795888 2291 L 2291
Cdd:cd14613   257 L 257
alpha_CA_VII cd03149
Carbonic anhydrase alpha, CA isozyme VII_like subgroup. Carbonic anhydrases (CAs) are ...
 60-300 1.76e-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: 1.76e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888   60 KQSPINIDEDLTQVNVNLKKLKFQDWDKTSLEntfIHNTGKTVEINLtNDYR----LSGGVSETVFKASKIAFHWGKcnM 135
Cdd:cd03149     3 RQSPIDIVSSEAVYDPKLKPLSLSYDPCTSLS---ISNNGHSVMVEF-DDSDdktvITGGPLENPYRLKQFHFHWGA--K 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888  136 SSDGSEHSLEGQKFPLEMQIYCFDADRFSSFEEAIKGKGKLRALSILFEVGiEENLDYKAIIDGVERVSRFGKQAALDPF 215
Cdd:cd03149    77 HGSGSEHTVDGKTFPSELHLVHWNAKKYKSFGEAAAAPDGLAVLGVFLETG-DEHPGLNRLTDALYMVRFKGTKAQFLDF 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888  216 TLLNLLPNSTDkYYTYNGSLTSPPCTDTVDWIIFKDTVSISESQLAVFCEVLTMQQSGYVMLMdylQNNFREQQYKFSRQ 295
Cdd:cd03149   156 NPKCLLPKSLD-YWTYPGSLTTPPLNESVTWIVLKEPIPVSEKQMGKFRELLFTSEEDQRNHM---VNNFRPPQPLKGRT 231


                  ....*
gi 300795888  296 VFSSY 300
Cdd:cd03149   232 VRASF 236
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 2045-2293 4.02e-30

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: 122.07  E-value: 4.02e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2045 QQSDYSTALKQCNREKNRTSSIIPVERSRVGISSLSG-EGADYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHN 2123
Cdd:cd14626    29 QQFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGvPGSDYINANYIDGYRKQNAYIATQGPLPETLSDFWRMVWEQR 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2124 AQLVVM---LPDGQNMAEDEfvYWPNKDEPiNCESFKVTLM-AEEHKCLSneekliMQDFILEATQDDYVLEVRHFQCPK 2199
Cdd:cd14626   109 TATIVMmtrLEEKSRVKCDQ--YWPIRGTE-TYGMIQVTLLdTVELATYS------VRTFALYKNGSSEKREVRQFQFMA 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2200 WPN---PDSPiSKTFELISIIKEEAATRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFA 2276
Cdd:cd14626   180 WPDhgvPEYP-TPILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQ 258

                         250
                  ....*....|....*..
gi 300795888 2277 DIEQYQFLYKAVLSLVS 2293
Cdd:cd14626   259 TEDQYIFIHEALLEAAT 275
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 2086-2289 9.29e-30

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: 118.86  E-value: 9.29e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2086 YINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLP--DGQNMAEDEFVYWPnkdEPINCesfKVTLMAE 2163
Cdd:cd14637     1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNqlNQSNSAWPCLQYWP---EPGLQ---QYGPMEV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2164 EHKCLSNEEKLIMQDFILE--ATQDDYVLEVRHFQCPKWP----NPDSPISKTFELISIIKEEAATRDGPMIVHDEHGGV 2237
Cdd:cd14637    75 EFVSGSADEDIVTRLFRVQniTRLQEGHLMVRHFQFLRWSayrdTPDSKKAFLHLLASVEKWQRESGEGRTVVHCLNGGG 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 300795888 2238 TAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAVL 2289
Cdd:cd14637   155 RSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIAL 206
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 2065-2289 1.22e-29

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: 119.28  E-value: 1.22e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2065 SIIPVERSRVGISSLSG-EGADYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDGQNMAEDE-FV 2142
Cdd:cd14620     3 NILPYDHSRVILSQLDGiPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKcYQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2143 YWPNKdepiNCESF-KVTLMAEEHKCLSNeekLIMQDFILEATQDDYVLEVR-----HFQcpKWPN---PDSPISkTFEL 2213
Cdd:cd14620    83 YWPDQ----GCWTYgNIRVAVEDCVVLVD---YTIRKFCIQPQLPDGCKAPRlvtqlHFT--SWPDfgvPFTPIG-MLKF 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300795888 2214 ISIIKEEAATRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAVL 2289
Cdd:cd14620   153 LKKVKSVNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALL 228
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 1791-2000 1.49e-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: 1.49e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1791 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLveKGRRKCDQYWPVDGSEEYGNFLVTQKSIQV 1870
Cdd:cd14634     1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEM--DAAQLCMQYWPEKTSCCYGPIQVEFVSADI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1871 LAYYTVRNFTLRNTkikkgsqkGRPSG--RVVTQYHYTQWPDM-GVPEYSLPVLTFVRKASHAKRH---AVGPVVVHCSA 1944
Cdd:cd14634    79 DEDIISRIFRICNM--------ARPQDgyRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLEKWQEQydgREGRTVVHCLN 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 300795888 1945 GVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDALVE 2000
Cdd:cd14634   151 GGGRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
alpha_CARP_VIII cd03120
Carbonic anhydrase alpha related protein, group VIII. Carbonic anhydrase related proteins ...
 49-289 3.02e-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: 3.02e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888   49 WGKKYPTCNSPKQSPINI-------DEDLTQVNVNLKKLKFQDWDKTslentfihNTGKTVEINLTNDYRLSGGV--SET 119
Cdd:cd03120     4 WGLLFPEANGEYQSPINLnsrearyDPSLLEVRLSPNYVVCRDCEVI--------NDGHTIQIILKSKSVLSGGPlpQGH 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888  120 VFKASKIAFHWGKCNMSsdGSEHSLEGQKFPLEMQIYCFDADRFSSFEEAIKGKGKLRALSILFEVGiEENLDYKAIIDG 199
Cdd:cd03120    76 EFELAEVRFHWGRENQR--GSEHTVNFKAFPMELHLIHWNSTLYSSLEEAMGKPHGIAIIALFVQIG-KEHVGLKAVTEI 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888  200 VERVSRFGKQAALDPFTLLNLLPNSTDK-YYTYNGSLTSPPCTDTVDWIIFKDTVSISESQLAVFCEvLTMQQSGYVMLM 278
Cdd:cd03120   153 LQDIQYKGKSKTIPCFNPNTLLPDPLLRdYWVYEGSLTTPPCSEGVTWILFRYPLTISQSQIEEFRR-LRTHVKGAELVE 231

                         250
                  ....*....|....
gi 300795888  279 --DY-LQNNFREQQ 289
Cdd:cd03120   232 gcDGlLGDNFRPTQ 245
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 2049-2291 5.69e-29

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


Pssm-ID: 350452 [Multi-domain]  Cd Length: 297  Bit Score: 119.27  E-value: 5.69e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2049 YSTAL--KQCNREKNRTSSIIPVERSRVGIS-SLSGEGADYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQ 2125
Cdd:cd14604    47 YPTATgeKEENVKKNRYKDILPFDHSRVKLTlKTSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVA 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2126 LVVM----LPDGQNMAEDefvYWPN-KDEPINCESFKVTLMAEEHKclsneEKLIMQDFILEATQDDYVLEVRHFQcpKW 2200
Cdd:cd14604   127 IIVMacreFEMGRKKCER---YWPLyGEEPMTFGPFRISCEAEQAR-----TDYFIRTLLLEFQNETRRLYQFHYV--NW 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2201 PNPDSPIS--KTFELISIIKEEAATRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADI 2278
Cdd:cd14604   197 PDHDVPSSfdSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAV 276

                         250
                  ....*....|....*.
gi 300795888 2279 ---EQYQFLYKAVLSL 2291
Cdd:cd14604   277 qtkEQYELVHRAIAQL 292
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 2061-2286 1.59e-28

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: 115.77  E-value: 1.59e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2061 NRTSSIIPVERSRVGISSLSG-EGADYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPD----GQN 2135
Cdd:cd14616     1 NRFPNIKPYNNNRVKLIADAGvPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQcfekGRI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2136 MAEDefvYWPNKDEPINCES-FKVTLMAEEhkclsNEEKLIMQDFILEaTQDDYVLeVRHFQCPKWPNPDSPISkTFELI 2214
Cdd:cd14616    81 RCHQ---YWPEDNKPVTVFGdIVITKLMED-----VQIDWTIRDLKIE-RHGDYMM-VRQCNFTSWPEHGVPES-SAPLI 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 300795888 2215 SIIKEEAATRDG---PMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYK 2286
Cdd:cd14616   150 HFVKLVRASRAHdntPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLHQ 224
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 2086-2289 1.91e-28

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: 114.73  E-value: 1.91e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2086 YINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDgQNMAEDEFVYWPNKDE----PINCESFKVTLm 2161
Cdd:cd14634     1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNE-MDAAQLCMQYWPEKTSccygPIQVEFVSADI- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2162 aeehkclsnEEKLIMQDFI---LEATQDDYVLeVRHFQCPKWPN-PDSPISKTfELISIIK------EEAATRDGPMIVH 2231
Cdd:cd14634    79 ---------DEDIISRIFRicnMARPQDGYRI-VQHLQYIGWPAyRDTPPSKR-SILKVVRrlekwqEQYDGREGRTVVH 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 300795888 2232 DEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAVL 2289
Cdd:cd14634   148 CLNGGGRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVAL 205
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 2050-2288 2.25e-28

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 118.21  E-value: 2.25e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2050 STALKQCNREKNRTSSIIPVERSRVGISS------------------LSGEGAD--YINASYIMGYYQSNEFIITQHPLL 2109
Cdd:PHA02746   44 NHFLKKENLKKNRFHDIPCWDHSRVVINAheslkmfdvgdsdgkkieVTSEDNAenYIHANFVDGFKEANKFICAQGPKE 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2110 HTIQDFWRMIWDHNAQLVVMLPDGQNMAEDEFVYWPN-KDEPINCESFKVTLMAEEHKCLSNEEKLIMQDFILEATQddy 2188
Cdd:PHA02746  124 DTSEDFFKLISEHESQVIVSLTDIDDDDEKCFELWTKeEDSELAFGRFVAKILDIIEELSFTKTRLMITDKISDTSR--- 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2189 vlEVRHFQCPKWP---NPDSPiSKTFELISIIKEEAA----------TRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKE 2255
Cdd:PHA02746  201 --EIHHFWFPDWPdngIPTGM-AEFLELINKVNEEQAelikqadndpQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKE 277

                         250       260       270
                  ....*....|....*....|....*....|...
gi 300795888 2256 NSMDVYQVAKMINLMRPGVFADIEQYQFLYKAV 2288
Cdd:PHA02746  278 KEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 2061-2286 2.83e-28

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: 115.02  E-value: 2.83e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2061 NRTSSIIPVERSRVGISSLSGEG-ADYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLpdgQNMAED 2139
Cdd:cd14617     1 NRYNNILPYDSTRVKLSNVDDDPcSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMV---TQCVEK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2140 EFV----YWPNKDEPINCESFKVTLMAEehkclSNEEKLIMQDF-ILEATQDDYVLEVRHFQCPKWPNPDSPiSKTFELI 2214
Cdd:cd14617    78 GRVkcdhYWPADQDSLYYGDLIVQMLSE-----SVLPEWTIREFkICSEEQLDAPRLVRHFHYTVWPDHGVP-ETTQSLI 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2215 SIIKeeaATRD--------GPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYK 2286
Cdd:cd14617   152 QFVR---TVRDyinrtpgsGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228
alpha_CARP_X_XI_like cd03121
Carbonic anhydrase alpha related protein: groups X, XI and related proteins. This subgroup ...
 49-296 3.59e-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: 3.59e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888   49 WGKKYPT---CNSPK-QSPINIDEDLTQVNVNLKKLKFQDWDKTSLEntfIHNTGKTVEINLTNDY--RLSGGVSETVFK 122
Cdd:cd03121     5 WGLVNSAwnlCSKGRrQSPVDIEPSRLLFDPFLTPLRIDTGRKVSGT---FYNTGRHVSFRPDKDPvvNISGGPLSYRYR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888  123 ASKIAFHWGKCNmsSDGSEHSLEGQKFPLEMQIYCFDADRFSSFEEAIKGKGKLRALSILFEVGIEENLDYKAII--DGV 200
Cdd:cd03121    82 LEEIRLHFGRED--EQGSEHTVNGQAFPGEVQLIHYNSELYPNFSEASKSPNGLVIVSLFVKIGETSNPELRRLTnrDTI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888  201 ERVSRFGKQAALDPFTLLNLLPNsTDKYYTYNGSLTSPPCTDTVDWIIFKDTVSISESQLAvfcEVLTMQQSGYVMLMDY 280
Cdd:cd03121   160 TSIRYKGDAYFLQDLSIELLLPE-TDHYITYEGSLTSPGCHETVTWIILNKPIYITKEQMH---SLRLLSQNSPSQEKAP 235

                         250
                  ....*....|....*.
gi 300795888  281 LQNNFREQQYKFSRQV 296
Cdd:cd03121   236 MSPNFRPVQPLNNRPV 251
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 2057-2288 5.18e-28

catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; Tyrosine-protein phosphatase non-receptor type 11 (PTPN11) and type 6 (PTPN6) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN11 and PTPN6, are also called SH2 domain-containing tyrosine phosphatase 2 (SHP2) and 1 (SHP1), respectively. They contain two tandem SH2 domains: a catalytic PTP domain, and a C-terminal tail with regulatory properties. Although structurally similar, they have different localization and different roles in signal transduction. PTPN11/SHP2 is expressed ubiquitously and plays a positive role in cell signaling, leading to cell activation, while PTPN6/SHP1 expression is restricted mainly to hematopoietic and epithelial cells and functions as a negative regulator of signaling events.


Pssm-ID: 350392 [Multi-domain]  Cd Length: 251  Bit Score: 115.25  E-value: 5.18e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2057 NREKNRTSSIIPVERSRVGISSL--SGEGADYINASYIM-------GYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLV 2127
Cdd:cd14544     1 NKGKNRYKNILPFDHTRVILKDRdpNVPGSDYINANYIRnenegptTDENAKTYIATQGCLENTVSDFWSMVWQENSRVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2128 VMLPDGQNMAEDEFV-YWPnkDEpincesfkVTLMAEEHKCLSNEEKLIMQDFIL------EATQDDYVLEVRHFQCPKW 2200
Cdd:cd14544    81 VMTTKEVERGKNKCVrYWP--DE--------GMQKQYGPYRVQNVSEHDTTDYTLrelqvsKLDQGDPIREIWHYQYLSW 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2201 PNPDSPiSKTFELISII-----KEEAATRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKEN---SMDVYQVAKMINLMRP 2272
Cdd:cd14544   151 PDHGVP-SDPGGVLNFLedvnqRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGldcDIDIQKTIQMVRSQRS 229

                         250
                  ....*....|....*.
gi 300795888 2273 GVFADIEQYQFLYKAV 2288
Cdd:cd14544   230 GMVQTEAQYKFIYVAV 245
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 2032-2289 7.24e-28

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


Pssm-ID: 350469 [Multi-domain]  Cd Length: 296  Bit Score: 115.89  E-value: 7.24e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2032 LEKQFKLLSQSNIQQSdYSTALKQCNREKNRTSSIIPVERSRVGISSLSG-EGADYINASYIMGYYQSNEFIITQHPLLH 2110
Cdd:cd14621    28 FREEFNALPACPIQAT-CEAASKEENKEKNRYVNILPYDHSRVHLTPVEGvPDSDYINASFINGYQEKNKFIAAQGPKEE 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2111 TIQDFWRMIWDHNAQLVVMLPDGQNMAEDEFV-YWPNKdepiNCESF-KVTLMAEEHKCLSNE--EKLIMQDfILEATQD 2186
Cdd:cd14621   107 TVNDFWRMIWEQNTATIVMVTNLKERKECKCAqYWPDQ----GCWTYgNIRVSVEDVTVLVDYtvRKFCIQQ-VGDVTNK 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2187 DYVLEVRHFQCPKWPN---PDSPISkTFELISIIKEEAATRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQV 2263
Cdd:cd14621   182 KPQRLITQFHFTSWPDfgvPFTPIG-MLKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGF 260

                         250       260
                  ....*....|....*....|....*.
gi 300795888 2264 AKMINLMRPGVFADIEQYQFLYKAVL 2289
Cdd:cd14621   261 VSRIRAQRCQMVQTDMQYVFIYQALL 286
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 2086-2285 1.24e-27

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


Pssm-ID: 350397 [Multi-domain]  Cd Length: 204  Bit Score: 112.44  E-value: 1.24e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2086 YINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLpdgQNMAE------DEfvYWPNKDEPiNCESFKVT 2159
Cdd:cd14549     1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMI---TNLVErgrrkcDQ--YWPKEGTE-TYGNIQVT 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2160 LMAEEHK--------CLSNEEklimqdfILEATQDDYVLEVRHFQCPKWPN---PDSPISktfeLISIIKEEAATRD--- 2225
Cdd:cd14549    75 LLSTEVLatytvrtfSLKNLK-------LKKVKGRSSERVVYQYHYTQWPDhgvPDYTLP----VLSFVRKSSAANPpga 143

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2226 GPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLY 2285
Cdd:cd14549   144 GPIVVHCSAGVGRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 2049-2293 1.35e-27

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 115.87  E-value: 1.35e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2049 YSTALKQCNREKNRTSSIIPVERSRVGISSLSGEGADYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVV 2128
Cdd:PHA02747   43 IANFEKPENQPKNRYWDIPCWDHNRVILDSGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIV 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2129 ML--PDGQNMAEDEFVYW-PNKDEPINCESFKVTLMAEEHKCLSNEEKLIMQDFILEATQddyvlEVRHFQCPKWPNPDS 2205
Cdd:PHA02747  123 MLtpTKGTNGEEKCYQYWcLNEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILKDSR-----KISHFQCSEWFEDET 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2206 PIS-----KTFELISIIKEEAAT----RDG---PMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPG 2273
Cdd:PHA02747  198 PSDhpdfiKFIKIIDINRKKSGKlfnpKDAllcPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHA 277

                         250       260
                  ....*....|....*....|...
gi 300795888 2274 VFADIEQYQFL---YKAVLSLVS 2293
Cdd:PHA02747  278 GIMNFDDYLFIqpgYEVLHYFLS 300
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 2045-2289 3.29e-27

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: 113.58  E-value: 3.29e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2045 QQSDY--STALKQCNREKNRTSSIIPVERSRVgisSLSGEGADYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDH 2122
Cdd:cd14608    11 EASDFpcRVAKLPKNKNRNRYRDVSPFDHSRI---KLHQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQ 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2123 NAQLVVMLpdgQNMAEDEFV----YWPNKDEP---INCESFKVTLMAEEHKCLSNEEKLIMQDFILEATQddyvlEVRHF 2195
Cdd:cd14608    88 KSRGVVML---NRVMEKGSLkcaqYWPQKEEKemiFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETR-----EILHF 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2196 QCPKWPN---PDSPISkTFELISIIKEEAA--TRDGPMIVHDEHGGVTAGTFCALTT---LMHQLEKENSMDVYQVAKMI 2267
Cdd:cd14608   160 HYTTWPDfgvPESPAS-FLNFLFKVRESGSlsPEHGPVVVHCSAGIGRSGTFCLADTcllLMDKRKDPSSVDIKKVLLEM 238

                         250       260
                  ....*....|....*....|..
gi 300795888 2268 NLMRPGVFADIEQYQFLYKAVL 2289
Cdd:cd14608   239 RKFRMGLIQTADQLRFSYLAVI 260
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 2029-2288 5.78e-27

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: 113.23  E-value: 5.78e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2029 KTKLEKQFKLLSQSNIQQSDYSTALKQCNREKNRTSSIIPVERSRVGISSL-SGEGADYINASYIMGYYQSN-EFIITQH 2106
Cdd:cd14610    16 KNRLEKEWEALCAYQAEPNATNVAQREENVQKNRSLAVLPYDHSRIILKAEnSHSHSDYINASPIMDHDPRNpAYIATQG 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2107 PLLHTIQDFWRMIWDHNAQLVVML-PDGQNMAEDEFVYWPnkDEPINC-ESFKVTLMAEEHKClsneEKLIMQDFILEAT 2184
Cdd:cd14610    96 PLPATVADFWQMVWESGCVVIVMLtPLAENGVKQCYHYWP--DEGSNLyHIYEVNLVSEHIWC----EDFLVRSFYLKNL 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2185 QDDYVLEVRHFQCPKWPNPDSPIS--KTFELISIIKEEAATRDGPMIVHDEHGGVTAGTFCALTTLMHQLEK-ENSMDVY 2261
Cdd:cd14610   170 QTNETRTVTQFHFLSWNDQGVPAStrSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLNKMAKgAKEIDIA 249

                         250       260
                  ....*....|....*....|....*..
gi 300795888 2262 QVAKMINLMRPGVFADIEQYQFLYKAV 2288
Cdd:cd14610   250 ATLEHLRDQRPGMVQTKEQFEFALTAV 276
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 2086-2289 6.04e-27

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


Pssm-ID: 350403 [Multi-domain]  Cd Length: 204  Bit Score: 110.39  E-value: 6.04e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2086 YINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLpdgQNMAEDEFV----YWPNKDEPINceSFKVTLM 2161
Cdd:cd14555     1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMV---TNLVEVGRVkcsrYWPDDTEVYG--DIKVTLV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2162 AEEHKClsneeKLIMQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKT--FELISIIKEEAATRDGPMIVHDEHGGVTA 2239
Cdd:cd14555    76 ETEPLA-----EYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATglLGFIRRVKASNPPSAGPIVVHCSAGAGRT 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 300795888 2240 GTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAVL 2289
Cdd:cd14555   151 GCYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAIL 200
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 2086-2286 6.32e-27

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: 110.21  E-value: 6.32e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2086 YINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDGQNMAEDEFV-YWPNK-DEPINCESFKVTLMAE 2163
Cdd:cd14542     1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCErYWPEEgEEQLQFGPFKISLEKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2164 EHKClsneeklimQDFI---LEATQDDYVLEVRHFQCPKWPNPDSPISKT--FELISIIKEEAATRDGPMIVHDEHGGVT 2238
Cdd:cd14542    81 KRVG---------PDFLirtLKVTFQKESRTVYQFHYTAWPDHGVPSSVDpiLDLVRLVRDYQGSEDVPICVHCSAGCGR 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 300795888 2239 AGTFCALT---TLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYK 2286
Cdd:cd14542   152 TGTICAIDyvwNLLKTGKIPEEFSLFDLVREMRKQRPAMVQTKEQYELVYR 202
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 2045-2293 9.75e-27

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: 112.52  E-value: 9.75e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2045 QQSDYSTALKQCNREKNRTSSIIPVERSRVGISSLSG-EGADYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHN 2123
Cdd:cd14624    35 QQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGiPGSDYINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQR 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2124 AQLVVMLPDGQNMAE---DEfvYWPNKDEPINcESFKVTLMAEEHKClsneeKLIMQDFILEATQDDYVLEVRHFQCPKW 2200
Cdd:cd14624   115 SATVVMMTKLEERSRvkcDQ--YWPSRGTETY-GLIQVTLLDTVELA-----TYCVRTFALYKNGSSEKREVRQFQFTAW 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2201 PNPDSPISKT--FELISIIKEEAATRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADI 2278
Cdd:cd14624   187 PDHGVPEHPTpfLAFLRRVKTCNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTE 266

                         250
                  ....*....|....*
gi 300795888 2279 EQYQFLYKAVLSLVS 2293
Cdd:cd14624   267 DQYIFIHDALLEAVT 281
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 2057-2292 1.12e-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: 112.05  E-value: 1.12e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2057 NREKNRTSSIIPVERSRVGISSLSGEGA---DYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLpdg 2133
Cdd:cd17667    27 NKHKNRYINILAYDHSRVKLRPLPGKDSkhsDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMI--- 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2134 QNMAE------DEfvYWPNKdepiNCESFK---VTLMAEE-HKCLSneekliMQDFILEATQDDYVLE-----------V 2192
Cdd:cd17667   104 TNLVEkgrrkcDQ--YWPTE----NSEEYGniiVTLKSTKiHACYT------VRRFSIRNTKVKKGQKgnpkgrqnertV 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2193 RHFQCPKWPNPDSPiSKTFELISIIKEEAATRD---GPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINL 2269
Cdd:cd17667   172 IQYHYTQWPDMGVP-EYALPVLTFVRRSSAARTpemGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRT 250

                         250       260
                  ....*....|....*....|...
gi 300795888 2270 MRPGVFADIEQYQFLYKAVLSLV 2292
Cdd:cd17667   251 QRNYLVQTEEQYIFIHDALLEAI 273
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 2084-2289 1.42e-26

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


Pssm-ID: 350479 [Multi-domain]  Cd Length: 218  Bit Score: 109.72  E-value: 1.42e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2084 ADYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLpdgQNMAE----DEFVYWPNKDEPINceSFKVT 2159
Cdd:cd14631    13 SDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMV---TNLVEvgrvKCYKYWPDDTEVYG--DFKVT 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2160 LMAEEHKClsneeKLIMQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKT--FELISIIKEEAATRDGPMIVHDEHGGV 2237
Cdd:cd14631    88 CVEMEPLA-----EYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATglLSFIRRVKLSNPPSAGPIVVHCSAGAG 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 300795888 2238 TAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAVL 2289
Cdd:cd14631   163 RTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAIL 214
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 2045-2293 2.17e-26

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: 111.34  E-value: 2.17e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2045 QQSDYSTALKQCNREKNRTSSIIPVERSRVGISSLSG-EGADYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHN 2123
Cdd:cd14625    35 QQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGiMGSDYINANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQR 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2124 AQLVVM---LPDGQNMAEDEfvYWPNKdepiNCESF---KVTLMAEEHKClsneeKLIMQDFILEATQDDYVLEVRHFQC 2197
Cdd:cd14625   115 SATVVMmtkLEEKSRIKCDQ--YWPSR----GTETYgmiQVTLLDTIELA-----TFCVRTFSLHKNGSSEKREVRQFQF 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2198 PKWPNPDSPISKT--FELISIIKEEAATRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVF 2275
Cdd:cd14625   184 TAWPDHGVPEYPTpfLAFLRRVKTCNPPDAGPIVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMV 263

                         250
                  ....*....|....*...
gi 300795888 2276 ADIEQYQFLYKAVLSLVS 2293
Cdd:cd14625   264 QTEDQYSFIHDALLEAVA 281
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 1791-2000 3.31e-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: 3.31e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1791 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRR-KCDQYWPVDGSEEYGNFLVTQKSIQ 1869
Cdd:cd14637     1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWPEPGLQQYGPMEVEFVSGS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1870 VLAYYTVRNFTLRN-TKIKKGSqkgrpsgRVVTQYHYTQW-PDMGVPEYS---LPVLTFVRKASHAKRHavGPVVVHCSA 1944
Cdd:cd14637    81 ADEDIVTRLFRVQNiTRLQEGH-------LMVRHFQFLRWsAYRDTPDSKkafLHLLASVEKWQRESGE--GRTVVHCLN 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 300795888 1945 GVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDALVE 2000
Cdd:cd14637   152 GGGRSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 2086-2289 5.53e-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: 107.85  E-value: 5.53e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2086 YINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDgQNMAEDEFVYWP----NKDEPINCESFKVTLm 2161
Cdd:cd14635     1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLND-VDPAQLCPQYWPengvHRHGPIQVEFVSADL- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2162 aeehkclsnEEKLIMQDF-ILEAT--QDDYVLeVRHFQCPKWP-NPDSPISKT--FELISII---KEEAATRDGPMIVHD 2232
Cdd:cd14635    79 ---------EEDIISRIFrIYNAArpQDGYRM-VQQFQFLGWPmYRDTPVSKRsfLKLIRQVdkwQEEYNGGEGRTVVHC 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 300795888 2233 EHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAVL 2289
Cdd:cd14635   149 LNGGGRSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVAL 205
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 1791-2000 6.45e-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: 6.45e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1791 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLveKGRRKCDQYWPVDGSEEYGNFLVTQKSIQV 1870
Cdd:cd14635     1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDV--DPAQLCPQYWPENGVHRHGPIQVEFVSADL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1871 LAYYTVRNFTLRNTkikkgsqkGRPSG--RVVTQYHYTQWPDM-GVPEYSLPVLTFVRKASHAKRH---AVGPVVVHCSA 1944
Cdd:cd14635    79 EEDIISRIFRIYNA--------ARPQDgyRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEyngGEGRTVVHCLN 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 300795888 1945 GVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDALVE 2000
Cdd:cd14635   151 GGGRSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 2058-2286 2.01e-25

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


Pssm-ID: 350393 [Multi-domain]  Cd Length: 231  Bit Score: 107.09  E-value: 2.01e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2058 REKNRTSSIIPVERSRVgisSLSGEGADYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLpdgQNMA 2137
Cdd:cd14545     1 LNRYRDRDPYDHDRSRV---KLKQGDNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIML---NKLM 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2138 EDE----FVYWPNKDEPINC---ESFKVTLMAEEHKclsneEKLIMQDFILEATQDDYVLEVRHFQCPKWPN---PDSPI 2207
Cdd:cd14545    75 EKGqikcAQYWPQGEGNAMIfedTGLKVTLLSEEDK-----SYYTVRTLELENLKTQETREVLHFHYTTWPDfgvPESPA 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2208 SKTFELISIIKEEAATRD-GPMIVHDEHGGVTAGTFCALTTLMHQLEKEN--SMDVYQVAKMINLMRPGVFADIEQYQFL 2284
Cdd:cd14545   150 AFLNFLQKVRESGSLSSDvGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNpsSVDVKKVLLEMRKYRMGLIQTPDQLRFS 229


                  ..
gi 300795888 2285 YK 2286
Cdd:cd14545   230 YL 231
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 1791-2000 2.01e-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: 2.01e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1791 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNL-VEKGrrkCDQYWPVDGSEEYGNFLVTQKSIQ 1869
Cdd:cd14636     1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVdLAQG---CPQYWPEEGMLRYGPIQVECMSCS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1870 VLAYYTVRNFTLRN-TKIKKGSQkgrpsgrVVTQYHYTQWPD-MGVPEYS---LPVLTFVRKASHAKRHAVGPVVVHCSA 1944
Cdd:cd14636    78 MDCDVISRIFRICNlTRPQEGYL-------MVQQFQYLGWAShREVPGSKrsfLKLILQVEKWQEECDEGEGRTIIHCLN 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 300795888 1945 GVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDALVE 2000
Cdd:cd14636   151 GGGRSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 2029-2288 4.06e-25

PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type tyrosine-protein phosphatase-like N (PTPRN or R-PTP-N), also called islet cell antigen 512 (ICA512) or PTP IA-2, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). It consists of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. PTPRN is located in secretory granules of neuroendocrine cells and is involved in the generation, cargo storage, traffic, exocytosis and recycling of insulin secretory granules, as well as in beta-cell proliferation. It is a major autoantigen in type 1 diabetes and is involved in the regulation of insulin secretion.


Pssm-ID: 350457 [Multi-domain]  Cd Length: 281  Bit Score: 107.43  E-value: 4.06e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2029 KTKLEKQFKLLSQSNIQQSDYSTALKQCNREKNRTSSIIPVERSRVGI-SSLSGEGADYINASYIMGY-YQSNEFIITQH 2106
Cdd:cd14609    14 RDRLAKEWQALCAYQAEPNTCSTAQGEANVKKNRNPDFVPYDHARIKLkAESNPSRSDYINASPIIEHdPRMPAYIATQG 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2107 PLLHTIQDFWRMIWDHNAQLVVMLP----DGQNMAEDefvYWPNKDEPINcESFKVTLMAEEHKClsneEKLIMQDFILE 2182
Cdd:cd14609    94 PLSHTIADFWQMVWENGCTVIVMLTplveDGVKQCDR---YWPDEGSSLY-HIYEVNLVSEHIWC----EDFLVRSFYLK 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2183 ATQDDYVLEVRHFQCPKWPNPDSPiSKTFELISI---IKEEAATRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKE-NSM 2258
Cdd:cd14609   166 NVQTQETRTLTQFHFLSWPAEGIP-SSTRPLLDFrrkVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKGvKEI 244

                         250       260       270
                  ....*....|....*....|....*....|
gi 300795888 2259 DVYQVAKMINLMRPGVFADIEQYQFLYKAV 2288
Cdd:cd14609   245 DIAATLEHVRDQRPGMVRTKDQFEFALTAV 274
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 2086-2289 1.07e-24

catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type tyrosine-protein phosphatase U (PTPRU), also known as pancreatic carcinoma phosphatase 2 (PCP-2), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRU/PCP-2 is the most distant member of the type IIb subfamily and may have a distinct biological function other than cell-cell aggregation. It localizes to the adherens junctions and directly binds and dephosphorylates beta-catenin, and regulates the balance between signaling and adhesive beta-catenin. It plays an important role in the maintenance of epithelial integrity. PTPRU contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350480 [Multi-domain]  Cd Length: 205  Bit Score: 103.98  E-value: 1.07e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2086 YINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLpdgQNMAEDEFV----YWPNKDEPINceSFKVTLM 2161
Cdd:cd14632     1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMI---TKLVEVGRVkcskYWPDDSDTYG--DIKITLL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2162 AEEhkclsNEEKLIMQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKT--FELISIIKEEAATRDGPMIVHDEHGGVTA 2239
Cdd:cd14632    76 KTE-----TLAEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATglLAFIRRVKASTPPDAGPVVVHCSAGAGRT 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 300795888 2240 GTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAVL 2289
Cdd:cd14632   151 GCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAIL 200
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 2060-2285 1.80e-24

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


Pssm-ID: 350459 [Multi-domain]  Cd Length: 226  Bit Score: 104.23  E-value: 1.80e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2060 KNRTSSIIPVERSRVGI--SSLSGEGADYINASYIMGYY-QSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDGQNM 2136
Cdd:cd14611     2 KNRYKTILPNPHSRVCLkpKNSNDSLSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2137 AEDEFVYWPNKDEPINcesfKVTLMAeehKCLSNEEKLIMQDFILEatQDDYVLEVRHFQCPKWPNPDSPISKT--FELI 2214
Cdd:cd14611    82 NEKCVLYWPEKRGIYG----KVEVLV---NSVKECDNYTIRNLTLK--QGSQSRSVKHYWYTSWPDHKTPDSAQplLQLM 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300795888 2215 SIIKEE--AATRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLY 2285
Cdd:cd14611   153 LDVEEDrlASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 2086-2289 1.02e-23

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: 101.30  E-value: 1.02e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2086 YINASYIMGYYQSNEF--IITQHPLLHTIQDFWRMIWDHNAQLVVMLPdgQNMaEDEFV----YWPnkdepincESFKVT 2159
Cdd:cd14538     1 YINASHIRIPVGGDTYhyIACQGPLPNTTGDFWQMVWEQKSEVIAMVT--QDV-EGGKVkchrYWP--------DSLNKP 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2160 LMAEEHKCLSNEEKLIMQDFI-----LEATQDDYVLEVRHFQCPKWPNPDSPISKtfelISIIKEEAATR----DGPMIV 2230
Cdd:cd14538    70 LICGGRLEVSLEKYQSLQDFVirrisLRDKETGEVHHITHLNFTTWPDHGTPQSA----DPLLRFIRYMRrihnSGPIVV 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 300795888 2231 HDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAVL 2289
Cdd:cd14538   146 HCSAGIGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACL 204
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 2057-2289 1.11e-23

catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein phosphatase non-receptor type 13 (PTPN13, also known as PTPL1) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN13 is an important regulator of tumor aggressiveness. It regulates breast cancer cell aggressiveness through direct inactivation of Src kinase. In hepatocellular carcinoma, PTPN13 is a tumor suppressor. PTPN13 contains a FERM domain, five PDZ domains, and a C-terminal catalytic PTP domain. With its PDZ domains, PTPN13 has numerous interacting partners that can actively participate in the regulation of its phosphatase activity or can permit direct or indirect recruitment of tyrosine phosphorylated substrates. Its FERM domain is necessary for localization to the membrane.


Pssm-ID: 350445 [Multi-domain]  Cd Length: 234  Bit Score: 102.22  E-value: 1.11e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2057 NREKNRTSSIIPVERSRVgissLSGEGADYINASYIMGYYQSNEF--IITQHPLLHTIQDFWRMIWDHNAQLVVMLpdgQ 2134
Cdd:cd14597     3 NRKKNRYKNILPYDTTRV----PLGDEGGYINASFIKMPVGDEEFvyIACQGPLPTTVADFWQMVWEQKSTVIAMM---T 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2135 NMAEDEFV----YWP---NKDEPINcESFKVTLMAEEHkclsnEEKLIMQDFILEATQDDYVLEVRHFQCPKWPNPDSPi 2207
Cdd:cd14597    76 QEVEGGKIkcqrYWPeilGKTTMVD-NRLQLTLVRMQQ-----LKNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTP- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2208 SKTFELISIIK-EEAATRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYK 2286
Cdd:cd14597   149 SQPEQLLTFISyMRHIHKSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQ 228


                  ...
gi 300795888 2287 AVL 2289
Cdd:cd14597   229 VIL 231
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 2086-2286 1.25e-23

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


Pssm-ID: 350399 [Multi-domain]  Cd Length: 202  Bit Score: 100.76  E-value: 1.25e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2086 YINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDGQNMAEDEFV-YWPNKdepiNCESFKVTLMaee 2164
Cdd:cd14551     1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSqYWPDQ----GCWTYGNLRV--- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2165 hkCLSNEEKLI---MQDFILEATQDDY----VLEVRHFQCPKWPN---PDSPISkTFELISIIKEEAATRDGPMIVHDEH 2234
Cdd:cd14551    74 --RVEDTVVLVdytTRKFCIQKVNRGIgekrVRLVTQFHFTSWPDfgvPFTPIG-MLKFLKKVKSANPPRAGPIVVHCSA 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 300795888 2235 GGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYK 2286
Cdd:cd14551   151 GVGRTGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 1791-1999 1.80e-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: 1.80e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1791 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITN---LVEkgrrkcDQ--YWPvdGSEEYGN---FL 1862
Cdd:cd17670     1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDnqgLAE------DEfvYWP--SREESMNceaFT 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1863 VTQKSIQVLAYYT-----VRNFTLRNTKIKKGSQkgrpsgrvVTQYHYTQWPDMGVPEYSLPVLTFVRKASHAKRHavGP 1937
Cdd:cd17670    73 VTLISKDRLCLSNeeqiiIHDFILEATQDDYVLE--------VRHFQCPKWPNPDAPISSTFELINVIKEEALTRD--GP 142

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 300795888 1938 VVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDALV 1999
Cdd:cd17670   143 TIVHDEFGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 2086-2289 2.39e-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: 100.10  E-value: 2.39e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2086 YINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDgQNMAEDEFVYWPNKDE----PINCESFKVTLM 2161
Cdd:cd14636     1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNE-VDLAQGCPQYWPEEGMlrygPIQVECMSCSMD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2162 AEehkCLSNeeklIMQDFILEATQDDYVLeVRHFQCPKWP-NPDSPISKTFELISII-----KEEAATRDGPMIVHDEHG 2235
Cdd:cd14636    80 CD---VISR----IFRICNLTRPQEGYLM-VQQFQYLGWAsHREVPGSKRSFLKLILqvekwQEECDEGEGRTIIHCLNG 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 300795888 2236 GVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAVL 2289
Cdd:cd14636   152 GGRSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVAL 205
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 1791-1999 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 300795888 1791 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCdQYWPvdGSEEYGN---FLVT--- 1864
Cdd:cd17669     1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEF-VYWP--NKDEPINcetFKVTlia 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1865 --QKSIQVLAYYTVRNFTLRNTKikkgsqkgrpSGRVVTQYHYT--QWPDMGVPEYSLPVLTFVRKASHAKRHavGPVVV 1940
Cdd:cd17669    78 eeHKCLSNEEKLIIQDFILEATQ----------DDYVLEVRHFQcpKWPNPDSPISKTFELISIIKEEAANRD--GPMIV 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 300795888 1941 HCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIRSQRNYLVQTEEQYVFIHDALV 1999
Cdd:cd17669   146 HDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 2086-2289 1.32e-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: 98.13  E-value: 1.32e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2086 YINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLpdgQNMAE------DEfvYWPNKDEPiNCESFKVT 2159
Cdd:cd17668     1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMI---TNLVEkgrrkcDQ--YWPADGSE-EYGNFLVT 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2160 LMAEEHKCLSNEEKLIMQDF-ILEATQDDYVLE--VRHFQCPKWPNPDSPiSKTFELISIIKEEAATRD---GPMIVHDE 2233
Cdd:cd17668    75 QKSVQVLAYYTVRNFTLRNTkIKKGSQKGRPSGrvVTQYHYTQWPDMGVP-EYTLPVLTFVRKASYAKRhavGPVVVHCS 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 300795888 2234 HGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAVL 2289
Cdd:cd17668   154 AGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 2086-2289 2.43e-22

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: 97.13  E-value: 2.43e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2086 YINASYIMGYYQSNE--FIITQHPLLHTIQDFWRMIWDHNAQLVVMLPD----GQNMAEDefvYWPNK-DEPINCESFKV 2158
Cdd:cd14596     1 YINASYITMPVGEEElfYIATQGPLPSTIDDFWQMVWENRSDVIAMMTReverGKVKCHR---YWPETlQEPMELENYQL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2159 TLmaeehkclsnEEKLIMQDFILEATQddyVLE--------VRHFQCPKWPNPDSPISKTFELISIIKEEAATRDGPMIV 2230
Cdd:cd14596    78 RL----------ENYQALQYFIIRIIK---LVEketgenrlIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHNTGPIVV 144

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 300795888 2231 HDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAVL 2289
Cdd:cd14596   145 HCSAGIGRAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVL 203
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 2191-2290 2.91e-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: 2.91e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888   2191 EVRHFQCPKWPNPDSPISKT--FELISIIKEE--AATRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKE-NSMDVYQVAK 2265
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDsiLELLRAVKKNlnQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 300795888   2266 MINLMRPGVFADIEQYQFLYKAVLS 2290
Cdd:smart00012   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
2191-2290 2.91e-22

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 93.58  E-value: 2.91e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888   2191 EVRHFQCPKWPNPDSPISKT--FELISIIKEE--AATRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKE-NSMDVYQVAK 2265
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDsiLELLRAVKKNlnQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 300795888   2266 MINLMRPGVFADIEQYQFLYKAVLS 2290
Cdd:smart00404   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PHA02738 PHA02738
hypothetical protein; Provisional
 2057-2288 7.14e-22

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 99.23  E-value: 7.14e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2057 NREKNRTSSIIPVERSRVGISSLSGEGaDYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVML-PDGQN 2135
Cdd:PHA02738   49 NRKLNRYLDAVCFDHSRVILPAERNRG-DYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLcKKKEN 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2136 MAEDEFVYWPNKDE-PINCESFKVTLMAEEHKCLSNEEKLIMQDFIlEATQddyvlEVRHFQCPKWPNPDSPiSKTFELI 2214
Cdd:PHA02738  128 GREKCFPYWSDVEQgSIRFGKFKITTTQVETHPHYVKSTLLLTDGT-SATQ-----TVTHFNFTAWPDHDVP-KNTSEFL 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2215 SII-------KEEAATR---------DGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADI 2278
Cdd:PHA02738  201 NFVlevrqcqKELAQESlqighnrlqPPPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIP 280

                         250
                  ....*....|
gi 300795888 2279 EQYQFLYKAV 2288
Cdd:PHA02738  281 FQYFFCYRAV 290
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 1753-2004 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 300795888 1753 SSNHPDNKHK--NRYINIVAYDHSRVKLaqlaEKDGKLTDyinANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVE 1830
Cdd:PHA02740   45 ACAQAENKAKdeNLALHITRLLHRRIKL----FNDEKVLD---ARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQ 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1831 VIVMITNLVEKgrrKC-DQYWpvdgSEEYGNFLVTQK-SIQVLAYYTVRNFTLrnTKIKKGSQKGRpsGRVVTQYHYTQW 1908
Cdd:PHA02740  118 IIVLISRHADK---KCfNQFW----SLKEGCVITSDKfQIETLEIIIKPHFNL--TLLSLTDKFGQ--AQKISHFQYTAW 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1909 PDMGVPEYSLPVLTF----------VRKASHAKRhaVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNVFGFLKHIR 1978
Cdd:PHA02740  187 PADGFSHDPDAFIDFfcniddlcadLEKHKADGK--IAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVR 264

                         250       260
                  ....*....|....*....|....*.
gi 300795888 1979 SQRNYLVQTEEQYVFIHDaLVEAILS 2004
Cdd:PHA02740  265 QKKYGCMNCLDDYVFCYH-LIAAYLK 289
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 2057-2288 1.74e-21

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


Pssm-ID: 350455 [Multi-domain]  Cd Length: 257  Bit Score: 96.19  E-value: 1.74e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2057 NREKNRTSSIIPVERSRVGISSLSGegaDYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLpdgQNM 2136
Cdd:cd14607    24 NRNRNRYRDVSPYDHSRVKLQNTEN---DYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVML---NRI 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2137 AEDEFV----YWPNKDEPINCES---FKVTLMAEEHKCLSNEEKLIMQDFILEATQDdyvleVRHFQCPKWPN---PDSP 2206
Cdd:cd14607    98 VEKDSVkcaqYWPTDEEEVLSFKetgFSVKLLSEDVKSYYTVHLLQLENINSGETRT-----ISHFHYTTWPDfgvPESP 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2207 ISKTFELISIIKEEAATRD-GPMIVHDEHGGVTAGTFCALTTLMHQLEKEN--SMDVYQVAKMINLMRPGVFADIEQYQF 2283
Cdd:cd14607   173 ASFLNFLFKVRESGSLSPEhGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDIKQVLLDMRKYRMGLIQTPDQLRF 252


                  ....*
gi 300795888 2284 LYKAV 2288
Cdd:cd14607   253 SYMAV 257
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 2057-2289 6.49e-21

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: 94.92  E-value: 6.49e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2057 NREKNRTSSIIPVERSRVgissLSGEGADYINASY----IMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPD 2132
Cdd:cd14600    40 NMDKNRYKDVLPYDATRV----VLQGNEDYINASYvnmeIPSANIVNKYIATQGPLPHTCAQFWQVVWEQKLSLIVMLTT 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2133 ----GQNMAEDefvYWPNKDEPINCESFKVTLMAEEHKClsneeKLIMQDFILEATQDDYVLEVRHFQCPKWPN---PDS 2205
Cdd:cd14600   116 lterGRTKCHQ---YWPDPPDVMEYGGFRVQCHSEDCTI-----AYVFREMLLTNTQTGEERTVTHLQYVAWPDhgvPDD 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2206 PiSKTFELISIIKEEAATRDgPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLY 2285
Cdd:cd14600   188 S-SDFLEFVNYVRSKRVENE-PVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKFVC 265


                  ....
gi 300795888 2286 KAVL 2289
Cdd:cd14600   266 EAIL 269
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 2086-2286 7.16e-21

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: 92.97  E-value: 7.16e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2086 YINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDGQNMAEDE-FVYWPNKDEPINC-ESFKVTLMAE 2163
Cdd:cd14557     1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKcAQYWPSMEEGSRAfGDVVVKINEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2164 EHkClsnEEKLIMQDFILEATQDDYVLEVRHFQCPKWPN---PDSPiSKTFELISIIKEEAATRDGPMIVHDEHGGVTAG 2240
Cdd:cd14557    81 KI-C---PDYIIRKLNINNKKEKGSGREVTHIQFTSWPDhgvPEDP-HLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRTG 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 300795888 2241 TFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYK 2286
Cdd:cd14557   156 TYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 2086-2288 1.34e-20

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


Pssm-ID: 350394 [Multi-domain]  Cd Length: 208  Bit Score: 92.12  E-value: 1.34e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2086 YINASYIMGYYQSNE-FIITQHPLLHTIQDFWRMIWDHNAQLVVML-PDGQNMAEDEFVYWPNKDEPINcESFKVTLMAE 2163
Cdd:cd14546     1 YINASTIYDHDPRNPaYIATQGPLPHTIADFWQMIWEQGCVVIVMLtRLQENGVKQCARYWPEEGSEVY-HIYEVHLVSE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2164 EHKClsneEKLIMQDFILEATQDDYVLEVRHFQCPKWPNPDSPIS-KTF-ELISIIKEEAATRDGPMIVHDEHGGVTAGT 2241
Cdd:cd14546    80 HIWC----DDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASaKPLlEFRRKVNKSYRGRSCPIVVHCSDGAGRTGT 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 300795888 2242 FCALTTLMHQLEK-ENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAV 2288
Cdd:cd14546   156 YILIDMVLNRMAKgAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAV 203
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 2057-2294 1.73e-20

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: 93.16  E-value: 1.73e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2057 NREKNRTSSIIPVERSRVGISS--LSGEGADYINASYIMGYYQSN--------EFIITQHPLLHTIQDFWRMIWDHNAQL 2126
Cdd:cd14605     2 NKNKNRYKNILPFDHTRVVLHDgdPNEPVSDYINANIIMPEFETKcnnskpkkSYIATQGCLQNTVNDFWRMVFQENSRV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2127 VVMLPDGQNMAEDEFV-YWPNKDEPINCESFKVTLMAEE--HKCLSNEEKLImqdfilEATQDDYVLEVRHFQCPKWPN- 2202
Cdd:cd14605    82 IVMTTKEVERGKSKCVkYWPDEYALKEYGVMRVRNVKESaaHDYILRELKLS------KVGQGNTERTVWQYHFRTWPDh 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2203 --PDSP--ISKTFELISiIKEEAATRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKEN---SMDVYQVAKMINLMRPGVF 2275
Cdd:cd14605   156 gvPSDPggVLDFLEEVH-HKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGvdcDIDVPKTIQMVRSQRSGMV 234

                         250
                  ....*....|....*....
gi 300795888 2276 ADIEQYQFLYKAVLSLVST 2294
Cdd:cd14605   235 QTEAQYRFIYMAVQHYIET 253
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 2057-2294 4.42e-19

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


Pssm-ID: 350454 [Multi-domain]  Cd Length: 266  Bit Score: 89.55  E-value: 4.42e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2057 NREKNRTSSIIPVERSRVGISSLSGE--GADYINASYIMGYYQSNE-----FIITQHPLLHTIQDFWRMIWDHNAQLVVM 2129
Cdd:cd14606    18 NKSKNRYKNILPFDHSRVILQGRDSNipGSDYINANYVKNQLLGPDenaktYIASQGCLEATVNDFWQMAWQENSRVIVM 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2130 LPDGQNMAEDEFV-YWPNKDEPINCESFKVTLMAEEHkclSNEEKL-IMQDFILEATqdDYVLEVRHFQCPKWPNPDSPi 2207
Cdd:cd14606    98 TTREVEKGRNKCVpYWPEVGMQRAYGPYSVTNCGEHD---TTEYKLrTLQVSPLDNG--ELIREIWHYQYLSWPDHGVP- 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2208 SKTFELISII-----KEEAATRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKEN---SMDVYQVAKMINLMRPGVFADIE 2279
Cdd:cd14606   172 SEPGGVLSFLdqinqRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGldcDIDIQKTIQMVRAQRSGMVQTEA 251

                         250
                  ....*....|....*
gi 300795888 2280 QYQFLYKAVLSLVST 2294
Cdd:cd14606   252 QYKFIYVAIAQFIET 266
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 2032-2295 9.10e-19

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 89.29  E-value: 9.10e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2032 LEKQFKLLSQSNIQQSDYsTALKQCNREKNRTSSIIPVERSRVGISSLSGeGADYINASYIMGYYQSNEFIITQHPLLHT 2111
Cdd:PHA02742   28 LKEEHEHIMQEIVAFSCN-ESLELKNMKKCRYPDAPCFDRNRVILKIEDG-GDDFINASYVDGHNAKGRFICTQAPLEET 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2112 IQDFWRMIWDHNAQLVVMLP----DGQnmaEDEFVYWpNKDEPINCESFKVTLMAEEHKCLSNEEKLIMQdfiLEATQDD 2187
Cdd:PHA02742  106 ALDFWQAIFQDQVRVIVMITkimeDGK---EACYPYW-MPHERGKATHGEFKIKTKKIKSFRNYAVTNLC---LTDTNTG 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2188 YVLEVRHFQCPKWPNPDSP--ISKTFELISIIKEEAATRD-----------GPMIVHDEHGGVTAGTFCALTTLMHQLEK 2254
Cdd:PHA02742  179 ASLDIKHFAYEDWPHGGLPrdPNKFLDFVLAVREADLKADvdikgenivkePPILVHCSAGLDRAGAFCAIDICISKYNE 258

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 300795888 2255 ENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAVL---SLVSTR 2295
Cdd:PHA02742  259 RAIIPLLSIVRDLRKQRHNCLSLPQQYIFCYFIVLifaKLMADK 302
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 2086-2286 9.69e-19

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: 86.67  E-value: 9.69e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2086 YINASYIMGYYQ-SNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDGQNMAEDEFV-YWP-NKDEPINCESFKVTLMA 2162
Cdd:cd14539     1 YINASLIEDLTPyCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHrYWPtERGQALVYGAITVSLQS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2163 EEHKCLSNEEklimqdfILEATQDDYVLE--VRHFQCPKWPNPDSPISKTfELISIIKE------EAATRDGPMIVHDEH 2234
Cdd:cd14539    81 VRTTPTHVER-------IISIQHKDTRLSrsVVHLQFTTWPELGLPDSPN-PLLRFIEEvhshylQQRSLQTPIVVHCSS 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 300795888 2235 GGVTAGTFCALTTLMHQLEKENSM-DVYQVAKMINLMRPGVFADIEQYQFLYK 2286
Cdd:cd14539   153 GVGRTGAFCLLYAAVQEIEAGNGIpDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 2085-2290 2.29e-18

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: 85.84  E-value: 2.29e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2085 DYINASY----IMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLpdgQNMAEDEFV----YWPNKDEPINCESF 2156
Cdd:cd14541     1 DYINANYvnmeIPGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVML---TTLVERGRVkchqYWPDLGETMQFGNL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2157 KVTLMAEEhkclsNEEKLIMQDFILEATQDDYVLEVRHFQCPKWPN---PDSPiSKTFELISIIKEEAATRDGPMIVHDE 2233
Cdd:cd14541    78 QITCVSEE-----VTPSFAFREFILTNTNTGEERHITQMQYLAWPDhgvPDDS-SDFLDFVKRVRQNRVGMVEPTVVHCS 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 300795888 2234 HG-GVTaGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAVLS 2290
Cdd:cd14541   152 AGiGRT-GVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAILR 208
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 2085-2289 1.65e-17

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: 83.46  E-value: 1.65e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2085 DYINASYIMGYYQS----NEFIITQHPLLHTIQDFWRMIWDHNAQLVVMLpdgQNMAEDEFV----YWPNKDEPINCESF 2156
Cdd:cd14601     1 DYINANYINMEIPSssiiNRYIACQGPLPNTCSDFWQMTWEQGSSMVVML---TTQVERGRVkchqYWPEPSGSSSYGGF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2157 KVTLMAEEhkclsNEEKLIMQDFILEATQDDYVLEVRHFQCPKWPN---PDSPiSKTFELISIIKEEAATRDGPMIVHDE 2233
Cdd:cd14601    78 QVTCHSEE-----GNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDhgvPDDS-SDFLDFVCLVRNKRAGKDEPVVVHCS 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 300795888 2234 HGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAVL 2289
Cdd:cd14601   152 AGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAIL 207
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 2049-2292 3.17e-16

catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein phosphatase non-receptor type 14 (PTPN14), also called protein-tyrosine phosphatase pez, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN14 is a potential tumor suppressor and plays a regulatory role in the Hippo and Wnt/beta-catenin signaling pathways. It contains an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350447 [Multi-domain]  Cd Length: 287  Bit Score: 81.58  E-value: 3.17e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2049 YSTALKQCNREKNRTSSIIPVERSRVGISSLSGEGADYINASYIMGYYQSNE--FIITQHPLLHTIQDFWRMIWDHNAQL 2126
Cdd:cd14599    30 FTTATLPENAERNRIREVVPYEENRVELVPTKENNTGYINASHIKVTVGGEEwhYIATQGPLPHTCHDFWQMVWEQGVNV 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2127 VVMLpdgqnMAEDE------FVYWPNKDEPINCES---FKVTL-MAEEHKC-----------LSNEEKlimqdfileatq 2185
Cdd:cd14599   110 IAMV-----TAEEEggrsksHRYWPKLGSKHSSATygkFKVTTkFRTDSGCyattglkvkhlLSGQER------------ 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2186 ddyvlEVRHFQCPKWPNPDSP------ISKTFELISIIKEEAATRDG------PMIVHDEHGGVTAGTFCALTTLMHQLE 2253
Cdd:cd14599   173 -----TVWHLQYTDWPDHGCPeevqgfLSYLEEIQSVRRHTNSMLDStkncnpPIVVHCSAGVGRTGVVILTELMIGCLE 247

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 300795888 2254 KENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAVLSLV 2292
Cdd:cd14599   248 HNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQFL 286
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 2086-2289 7.06e-16

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


Pssm-ID: 350388 [Multi-domain]  Cd Length: 219  Bit Score: 79.04  E-value: 7.06e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2086 YINASYIMGYYQSNE--FIITQHPLLHTIQDFWRMIWDHNAQLVVMLPDGQ-NMAEDEFVYWPNkdepincesfkvtlMA 2162
Cdd:cd14540     1 YINASHITATVGGKQrfYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEeGGREKCFRYWPT--------------LG 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2163 EEHKCLSNEEKLIMQDF------------ILEATQDDYVLEVRHFQCPKWPN---PDSPisKTF-----ELISI---IKE 2219
Cdd:cd14540    67 GEHDALTFGEYKVSTKFsvssgcytttglRVKHTLSGQSRTVWHLQYTDWPDhgcPEDV--SGFldfleEINSVrrhTNQ 144

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 300795888 2220 EAAT--RDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAVL 2289
Cdd:cd14540   145 DVAGhnRNPPTLVHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLI 216
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 2086-2285 1.59e-15

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


Pssm-ID: 350496 [Multi-domain]  Cd Length: 206  Bit Score: 77.50  E-value: 1.59e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2086 YINASYIMGYYQSN--EFIITQHPLLHTIQDFWRMIWDHNAQLVVMLP---DGQNMAEDEFVYWPNKDEPINCESFKVTl 2160
Cdd:cd17658     1 YINASLVETPASESlpKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTrlvDNYSTAKCADYFPAEENESREFGRISVT- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2161 maeeHKCLSNEEKLIMQDFiLEATQ---DDYVLEVRHFQCPKWPN---PDS--PISKTFELISIIKEEAatrdGPMIVHD 2232
Cdd:cd17658    80 ----NKKLKHSQHSITLRV-LEVQYiesEEPPLSVLHIQYPEWPDhgvPKDtrSVRELLKRLYGIPPSA----GPIVVHC 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 300795888 2233 EHGGVTAGTFCAL-TTLMHQLEKENS-MDVYQVAKMINLMRPGVFADIEQYQFLY 2285
Cdd:cd17658   151 SAGIGRTGAYCTIhNTIRRILEGDMSaVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 2086-2292 2.97e-13

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: 71.16  E-value: 2.97e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2086 YINASYIMGYYQSNE--FIITQHPLLHTIQDFWRMIWDHNAQLVVMLP-DGQNMAEDEFVYWP---NKDEPINCESFKVT 2159
Cdd:cd14598     1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTaEEEGGREKSFRYWPrlgSRHNTVTYGRFKIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2160 LMAEEHKCLSNEEKLIMQDFIL--EATqddyvleVRHFQCPKWPNPDSP------ISKTFELISIIKEEAATRD-----G 2226
Cdd:cd14598    81 TRFRTDSGCYATTGLKIKHLLTgqERT-------VWHLQYTDWPEHGCPedlkgfLSYLEEIQSVRRHTNSTIDpkspnP 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300795888 2227 PMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPGVFADIEQYQFLYKAVLSLV 2292
Cdd:cd14598   154 PVLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFL 219
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 1763-1992 2.02e-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: 2.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1763 NRYINIvaydHSRVKLAqlaekDGKLtdyINANYVDGYNRPKAyIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKG 1842
Cdd:cd14559     1 NRFTNI----QTRVSTP-----VGKN---LNANRVQIGNKNVA-IACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQ 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1843 RRKCDQYWpvDGSEEYGNFLVTQKSIQVLAYYTVRNFTLRNTKIKKGSQKgrpsgRVVTQYHYTQWPDMG-VPEYSLPVL 1921
Cdd:cd14559    68 RKGLPPYF--RQSGTYGSVTVKSKKTGKDELVDGLKADMYNLKITDGNKT-----ITIPVVHVTNWPDHTaISSEGLKEL 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1922 T-FVRKASHAKRHAVGPV-------------VVHCSAGVGRTGTYIvldSMLQQIQHEGTVNVFGFLKHIRSQRN-YLVQ 1986
Cdd:cd14559   141 AdLVNKSAEEKRNFYKSKgssaindknkllpVIHCRAGVGRTGQLA---AAMELNKSPNNLSVEDIVSDMRTSRNgKMVQ 217


                  ....*.
gi 300795888 1987 TEEQYV 1992
Cdd:cd14559   218 KDEQLD 223
fn3 pfam00041
Fibronectin type III domain;
313-401 5.98e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 54.73  E-value: 5.98e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888   313 SEPENVQADPENYTSLLVTWERPRVVYDTmIEKFAVLYQQLEGEDQtKHEFLTDGYQDlGAILNNLLPNMSYVLQIVAIC 392
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGP-ITGYEVEYRPKNSGEP-WNEITVPGTTT-SVTLTGLKPGTEYEVRVQAVN 77


                   ....*....
gi 300795888   393 TNGlYGKYS 401
Cdd:pfam00041   78 GGG-EGPPS 85
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 2054-2293 1.67e-08

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 58.44  E-value: 1.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2054 KQCNREKNRT---SSIIPVER---SRVGISSlsgeGADYINASYIMGYYQSNEFIITQHPLLHTIQDFWRMIWDHNAQLV 2127
Cdd:PHA02740   44 KACAQAENKAkdeNLALHITRllhRRIKLFN----DEKVLDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQII 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2128 VM---LPDGQNMAEdefvYWPNKDEP-INCESFKVTLMAEEHKCLSNEEKLIMQDfileatQDDYVLEVRHFQCPKWP-- 2201
Cdd:PHA02740  120 VLisrHADKKCFNQ----FWSLKEGCvITSDKFQIETLEIIIKPHFNLTLLSLTD------KFGQAQKISHFQYTAWPad 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 2202 ----NPDSPISKTFELISII----KEEAATRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSMDVYQVAKMINLMRPG 2273
Cdd:PHA02740  190 gfshDPDAFIDFFCNIDDLCadleKHKADGKIAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYG 269

                         250       260
                  ....*....|....*....|
gi 300795888 2274 VFADIEQYQFLYKAVLSLVS 2293
Cdd:PHA02740  270 CMNCLDDYVFCYHLIAAYLK 289
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
1902-1996 3.55e-08

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 54.59  E-value: 3.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1902 QYHYTQWPDMGVPEYSLpVLTFVRKAsHAKRHAVGPVVVHCSAGVGRTGT----YIVLDSM-LQQIqhegtvnvfgfLKH 1976
Cdd:COG2453    49 EYLHLPIPDFGAPDDEQ-LQEAVDFI-DEALREGKKVLVHCRGGIGRTGTvaaaYLVLLGLsAEEA-----------LAR 115

                          90       100
                  ....*....|....*....|
gi 300795888 1977 IRSQRNYLVQTEEQYVFIHD 1996
Cdd:COG2453   116 VRAARPGAVETPAQRAFLER 135
PLN02179 PLN02179
carbonic anhydrase
 49-253 7.24e-08

carbonic anhydrase


Pssm-ID: 177835  Cd Length: 235  Bit Score: 55.76  E-value: 7.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888   49 WGKKYP---TCNSPK-QSPInideDLTQVNVNLkkLKFQDWDKT-SLENTFIHNTGKTVEINLTNDyrlsGG---VSETV 120
Cdd:PLN02179   50 WGKLNPqwkVCSTGKyQSPI----DLTDERVSL--IHDQALSRHyKPAPAVIQSRGHDVMVSWKGD----AGkitIHQTD 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888  121 FKAskIAFHWgkcnmsSDGSEHSLEGQKFPLEMQIYCFDAdrfssfeeaikgKGKLRALSILFEVGiEENLDYKAIIDGV 200
Cdd:PLN02179  120 YKL--VQCHW------HSPSEHTINGTSYDLELHMVHTSA------------SGKTAVVGVLYKLG-EPDEFLTKLLNGI 178

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 300795888  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 ...
 1936-1996 7.29e-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: 7.29e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 300795888 1936 GPVVVHCSAGVGRTGTYIVLDSMLQQIqhegtVNVFGFLKHIRSQR-NYLVQTEEQYVFIHD 1996
Cdd:cd14494    57 EPVLVHCKAGVGRTGTLVACYLVLLGG-----MSAEEAVRIVRLIRpGGIPQTIEQLDFLIK 113
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 1901-1996 2.70e-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: 2.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1901 TQYHYTqWPDMGVP---EYSLPVLTFVRKASHAKRHavgpVVVHCSAGVGRTGTyiVLDSMLQQIQheGTVNVFGFLKHI 1977
Cdd:cd14505    74 TWHHLP-IPDGGVPsdiAQWQELLEELLSALENGKK----VLIHCKGGLGRTGL--IAACLLLELG--DTLDPEQAIAAV 144

                          90
                  ....*....|....*....
gi 300795888 1978 RSQRNYLVQTEEQYVFIHD 1996
Cdd:cd14505   145 RALRPGAIQTPKQENFLHQ 163
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 1903-1996 2.72e-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: 2.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1903 YHYT-QWPDMGVPEYSLpVLTFVRKASHAKRHAvGPVVVHCSAGVGRTG----TYIVldsMLQQIQHEGTVnvfgflKHI 1977
Cdd:cd14506    78 YFYNfGWKDYGVPSLTT-ILDIVKVMAFALQEG-GKVAVHCHAGLGRTGvliaCYLV---YALRMSADQAI------RLV 146

                          90
                  ....*....|....*....
gi 300795888 1978 RSQRNYLVQTEEQYVFIHD 1996
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 3.44e-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: 3.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888  313 SEPENVQADPENYTSLLVTWERPRvVYDTMIEKFAVLYQQLEGEDQTKHEflTDGYQDLGAILNNLLPNMSYVLQIVAIC 392
Cdd:cd00063     2 SPPTNLRVTDVTSTSVTLSWTPPE-DDGGPITGYVVEYREKGSGDWKEVE--VTPGSETSYTLTGLKPGTEYEFRVRAVN 78

                          90
                  ....*....|....
gi 300795888  393 TNGlYGKYSDQLIV 406
Cdd:cd00063    79 GGG-ESPPSESVTV 91
PLN02202 PLN02202
carbonate dehydratase
 1-263 4.35e-05

carbonate dehydratase


Pssm-ID: 177853 [Multi-domain]  Cd Length: 284  Bit Score: 47.74  E-value: 4.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888    1 MLILKRFLACIQLLCVCRLDwiygyyrqqrKLVEEIGWSYTGALNQKNWGKKYP---TCNSPK-QSPINIDEDLTQVNVN 76
Cdd:PLN02202    4 MMMIKLCFFAIALICIAPAD----------AQTEGVVFGYKGKNGPNQWGHLNPhftKCAVGKlQSPIDIQRRQIFYNHK 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888   77 LKKLKfQDWdktslentfiHNTGKTVEINLTNDYRLSGGVSETVFKASK----IAFHWgkcnmsSDGSEHSLEGQKFPLE 152
Cdd:PLN02202   74 LESIH-RDY----------YFTNATLVNHVCNVAMFFGEGAGDVIIDNKnytlLQMHW------HTPSEHHLHGVQYAAE 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888  153 MQIYCFDADrfssfeeaikgkGKLRALSILFEVGIEE----NLDYKAIIDGVERVSrfGKQAALDPFTLLNL--LPNSTD 226
Cdd:PLN02202  137 LHMVHQAKD------------GSFAVVASLFKIGTEEpflsQMKDKLVKLKEERFK--GNHTAQVEVGKIDTrhIERKTR 202

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 300795888  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 5.49e-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: 5.49e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888    313 SEPENVQADPENYTSLLVTWERPRvvyDTMIEKFAVLYQQLEGEDQTKHEFLTDGYQDLGAILNNLLPNMSYVLQIVAIC 392
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPP---DDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78


                    ...
gi 300795888    393 TNG 395
Cdd:smart00060   79 GAG 81
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 1902-1994 7.48e-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: 7.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795888 1902 QYHYTQWPDMGVPEYSL--PVLTFVRKAShakrhAVG-PVVVHCSAGVGRTGT----YIVLDSMLQQIQHegtvnvfgfL 1974
Cdd:cd14504    51 RYHHIPIEDYTPPTLEQidEFLDIVEEAN-----AKNeAVLVHCLAGKGRTGTmlacYLVKTGKISAVDA---------I 116

                          90       100
                  ....*....|....*....|
gi 300795888 1975 KHIRSQRNYLVQTEEQYVFI 1994
Cdd:cd14504   117 NEIRRIRPGSIETSEQEKFV 136
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
1936-1980 5.37e-03

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 39.57  E-value: 5.37e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 300795888   1936 GPVVVHCSAGVGRTGTYIVldSMLQQIQHEGTVNVFGFLKHIRSQ 1980
Cdd:smart00195   79 GKVLVHCQAGVSRSATLII--AYLMKTRNMSLNDAYDFVKDRRPI 121
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 1909-1953 6.55e-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: 6.55e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 300795888 1909 PDMGVPEYSLpVLTFVRKASHAKrhavGPVVVHCSAGVGRTGTYI 1953
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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