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Conserved domains on  [gi|124486807|ref|NP_001074775|]
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receptor-type tyrosine-protein phosphatase zeta isoform 3 precursor [Mus musculus]

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 ...
1714-1991 4.92e-159

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: 491.47  E-value: 4.92e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1714 FTEEFEtlkefyqEVQSCTADLGITADSSNHPDNKHKNRYVNIVAYDHSRVKLTQLAEKDGKLTDYINANYVDGYNRPKA 1793
Cdd:cd17667     1 FSEDFE-------EVQRCTADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSKHSDYINANYVDGYNKAKA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1794 YIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPTDGSEEYGSFLVNQKSVQVLAYYTVRNFTLRNTK 1873
Cdd:cd17667    74 YIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTK 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1874 LKKGSQ---KGRSSGRLVTQYHYTQWPDMGVPEYSLPVLAFVRKAAQAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQI 1950
Cdd:cd17667   154 VKKGQKgnpKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQI 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 124486807 1951 QHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAIL 1991
Cdd:cd17667   234 KDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 274
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
2074-2277 4.18e-153

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: 471.40  E-value: 4.18e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2074 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAEDEFVYWPNKDEPINCESFKVTLMSEEH 2153
Cdd:cd17669     1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFVYWPNKDEPINCETFKVTLIAEEH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2154 KCLSNEEKLIVQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTFELISIIKEEAANRDGPMIVHDEHGGVTAGTFCAL 2233
Cdd:cd17669    81 KCLSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTFELISIIKEEAANRDGPMIVHDEHGGVTAGTFCAL 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 124486807 2234 TTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVVL 2277
Cdd:cd17669   161 TTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
alpha_CARP_receptor_like cd03122
Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related ...
45-298 5.91e-110

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: 350.50  E-value: 5.91e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807   45 NQKNWGKKYPICNS-PKQSPINIDEDlTQVNVN-LKKLKFQGWEKASLEnTFIHNTGKTVEINLTN---DYYLSGGLSEK 119
Cdd:cd03122     1 NPKHWAKKYPACGEgRQQSPIDIVED-TQVQRQgLQPLHFDGYEELTAS-TTLENTGKTVILRLEGnssDPFVSGGPLLG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807  120 VFKASKITFHWGKCNvsSEGSEHSLEGQKFPLEMQVYCFDADRFSSFEeAVKGKGRLRALSILFEVGVEENLDYKAIIDG 199
Cdd:cd03122    79 RYKFSEITFHWGTCN--SDGSEHSIDGHKFPLEMQILHRNTDFFDSFE-AIKSPGGVLALAYLFELSHEDNPFLDPIIEG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807  200 TESVSRFGKQAALDPFVLQNLLPNSTDKYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLAVFCEVLTMQQSGyVMLMD 279
Cdd:cd03122   156 LRNVSRPGKEVELPPFPLSDLLPPFTDKYYSYEGSLTTPPCSETVEWIVFREPVPISSRQLEAFRELLTRRQDG-VMSGD 234
                         250
                  ....*....|....*....
gi 124486807  280 YLQNNFREQQYKFSRQVFS 298
Cdd:cd03122   235 YLPNNGRPQQPLGSRTVFS 253
fn3 pfam00041
Fibronectin type III domain;
313-401 9.77e-10

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 57.04  E-value: 9.77e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807   313 SEPENVQADPENYTSLLVTWERPRVVyDAMIEKFAVLYQPLaGNDQAKHEFLTDGYQDlGAILNNLLPNMSYVLQIVAVC 392
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDG-NGPITGYEVEYRPK-NSGEPWNEITVPGTTT-SVTLTGLKPGTEYEVRVQAVN 77

                   ....*....
gi 124486807   393 SNGlYGKYS 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 ...
1714-1991 4.92e-159

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: 491.47  E-value: 4.92e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1714 FTEEFEtlkefyqEVQSCTADLGITADSSNHPDNKHKNRYVNIVAYDHSRVKLTQLAEKDGKLTDYINANYVDGYNRPKA 1793
Cdd:cd17667     1 FSEDFE-------EVQRCTADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSKHSDYINANYVDGYNKAKA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1794 YIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPTDGSEEYGSFLVNQKSVQVLAYYTVRNFTLRNTK 1873
Cdd:cd17667    74 YIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTK 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1874 LKKGSQ---KGRSSGRLVTQYHYTQWPDMGVPEYSLPVLAFVRKAAQAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQI 1950
Cdd:cd17667   154 VKKGQKgnpKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQI 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 124486807 1951 QHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAIL 1991
Cdd:cd17667   234 KDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 274
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
2074-2277 4.18e-153

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: 471.40  E-value: 4.18e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2074 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAEDEFVYWPNKDEPINCESFKVTLMSEEH 2153
Cdd:cd17669     1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFVYWPNKDEPINCETFKVTLIAEEH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2154 KCLSNEEKLIVQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTFELISIIKEEAANRDGPMIVHDEHGGVTAGTFCAL 2233
Cdd:cd17669    81 KCLSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTFELISIIKEEAANRDGPMIVHDEHGGVTAGTFCAL 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 124486807 2234 TTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVVL 2277
Cdd:cd17669   161 TTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1713-1988 2.27e-121

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 383.55  E-value: 2.27e-121
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807   1713 GFTEEFETLKEFYQEVQSCTadlgitadSSNHPDNKHKNRYVNIVAYDHSRVKLTQLaekDGKLTDYINANYVDGYNRPK 1792
Cdd:smart00194    1 GLEEEFEKLDRLKPDDESCT--------VAAFPENRDKNRYKDVLPYDHTRVKLKPP---PGEGSDYINASYIDGPNGPK 69
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807   1793 AYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPTDGSE--EYGSFLVNQKSVQVLAYYTVRNFTLR 1870
Cdd:smart00194   70 AYIATQGPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEplTYGDITVTLKSVEKVDDYTIRTLEVT 149
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807   1871 NTklkkgsqkGRSSGRLVTQYHYTQWPDMGVPEYSLPVLAFVRKAAQAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQI 1950
Cdd:smart00194  150 NT--------GCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQL 221
                           250       260       270
                    ....*....|....*....|....*....|....*...
gi 124486807   1951 QHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVE 1988
Cdd:smart00194  222 EAGKEVDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1747-1988 1.54e-113

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 360.02  E-value: 1.54e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807  1747 NKHKNRYVNIVAYDHSRVKLTqlaeKDGKLTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNL 1826
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLT----GDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTEL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807  1827 VEKGRRKCDQYWPT--DGSEEYGSFLVN-QKSVQVLAYYTVRNFTLRNtklkkgsqKGRSSGRLVTQYHYTQWPDMGVPE 1903
Cdd:pfam00102   77 EEKGREKCAQYWPEeeGESLEYGDFTVTlKKEKEDEKDYTVRTLEVSN--------GGSEETRTVKHFHYTGWPDHGVPE 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807  1904 YSLPVLAFVRKAAQAKRHA-VGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFI 1982
Cdd:pfam00102  149 SPNSLLDLLRKVRKSSLDGrSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFL 228

                   ....*.
gi 124486807  1983 HDTLVE 1988
Cdd:pfam00102  229 YDAILE 234
alpha_CARP_receptor_like cd03122
Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related ...
45-298 5.91e-110

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: 350.50  E-value: 5.91e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807   45 NQKNWGKKYPICNS-PKQSPINIDEDlTQVNVN-LKKLKFQGWEKASLEnTFIHNTGKTVEINLTN---DYYLSGGLSEK 119
Cdd:cd03122     1 NPKHWAKKYPACGEgRQQSPIDIVED-TQVQRQgLQPLHFDGYEELTAS-TTLENTGKTVILRLEGnssDPFVSGGPLLG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807  120 VFKASKITFHWGKCNvsSEGSEHSLEGQKFPLEMQVYCFDADRFSSFEeAVKGKGRLRALSILFEVGVEENLDYKAIIDG 199
Cdd:cd03122    79 RYKFSEITFHWGTCN--SDGSEHSIDGHKFPLEMQILHRNTDFFDSFE-AIKSPGGVLALAYLFELSHEDNPFLDPIIEG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807  200 TESVSRFGKQAALDPFVLQNLLPNSTDKYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLAVFCEVLTMQQSGyVMLMD 279
Cdd:cd03122   156 LRNVSRPGKEVELPPFPLSDLLPPFTDKYYSYEGSLTTPPCSETVEWIVFREPVPISSRQLEAFRELLTRRQDG-VMSGD 234
                         250
                  ....*....|....*....
gi 124486807  280 YLQNNFREQQYKFSRQVFS 298
Cdd:cd03122   235 YLPNNGRPQQPLGSRTVFS 253
Carb_anhydrase smart01057
Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse ...
38-295 4.74e-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: 281.90  E-value: 4.74e-86
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807     38 WSYTGALNQKNWGKKYP-ICNSPKQSPINIDEDLTQVNVNLKKLKFQgWEKASleNTFIHNTGKTVEINL-TNDYYLSGG 115
Cdd:smart01057    1 WGYEGKNGPEHWGKLDPpFCGGKRQSPIDIVTAEAQYDPSLKPLKLS-YDQPT--AKRILNNGHTVQVNFdDDGSTLSGG 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807    116 LSEKVFKASKITFHWGKCNvsSEGSEHSLEGQKFPLEMQVYCFDADrfSSFEEAVKGKGRLRALSILFEVGVEENLDYKA 195
Cdd:smart01057   78 PLPGRYRLKQFHFHWGGSD--SEGSEHTIDGKRFPLELHLVHYNSK--GSFSEAVSKPGGLAVVAVFFKVGAEENPALQA 153
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807    196 IIDGTESVSRFGKQAALDPFVLQNLLPNSTDKYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLAVFCEVLTMQQSgyv 275
Cdd:smart01057  154 ILDHLPLIKYKGQETELTPFDLSSLLPASTRHYYTYNGSLTTPPCSEGVTWIVFKEPITISTEQLEKFRTLLPMEGN--- 230
                           250       260
                    ....*....|....*....|
gi 124486807    276 mlmDYLQNNFREQQYKFSRQ 295
Cdd:smart01057  231 ---EPLVNNARPLQPLNGRV 247
Carb_anhydrase pfam00194
Eukaryotic-type carbonic anhydrase;
44-300 1.31e-82

Eukaryotic-type carbonic anhydrase;


Pssm-ID: 459707 [Multi-domain]  Cd Length: 252  Bit Score: 272.22  E-value: 1.31e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807    44 LNQKNWGKKYPICNSPKQSPINIDEDLTQVNVNLKKLKFQGWEKASLENTfIHNTGKTVEINLTNDY--YLSGGLSEKVF 121
Cdd:pfam00194    1 LGPEHWGKVYPSCGGKRQSPINIDTRKVRYDPSLPPLTFQGYDVPPGKNT-LTNNGHTVQVSLDDGDpsTISGGPLATRY 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807   122 KASKITFHWGKCNvsSEGSEHSLEGQKFPLEMQVYCFDADRfSSFEEAVKGKGRLRALSILFEVGVEENLDYKAIIDGTE 201
Cdd:pfam00194   80 RLVQFHFHWGSTD--SRGSEHTIDGKRYPAELHIVHYNSKY-KSFDEAAKHPDGLAVLGVFFEVGDENNPYLQPIVSALD 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807   202 SVSRFGKQAALDPFVLQNLLPNSTDKYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLAVFCEVLTMQQSGYvmlMDYL 281
Cdd:pfam00194  157 NIKYKGKSVLLPPFDLSDLLPEDLTSYYTYNGSLTTPPCSESVTWIVFKEPISISEEQLEAFRTLLFSDGGEE---PRPL 233
                          250
                   ....*....|....*....
gi 124486807   282 QNNFREQQYKFSRQVFSSY 300
Cdd:pfam00194  234 VNNFRPTQPLNGRVVFASF 252
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
2019-2277 1.67e-78

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 260.67  E-value: 1.67e-78
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807   2019 KLEKQFQLLSQSNILQSDYSTALKQCNREKNRTSSIIPVERSRVGISSLSGEGTDYINASYIMGYYQSNEFIITQHPLLH 2098
Cdd:smart00194    1 GLEEEFEKLDRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGPLPS 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807   2099 TIKDFWRMIWDHNAQLVVMI-PDGQNMAEDEFVYWPNK-DEPINCESFKVTLMSEEHKclsneEKLIVQDFILEATQDDY 2176
Cdd:smart00194   81 TVEDFWRMVWEQKVTVIVMLtELVEKGREKCAQYWPDEeGEPLTYGDITVTLKSVEKV-----DDYTIRTLEVTNTGCSE 155
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807   2177 VLEVRHFQCPKWP---NPDSPISkTFELISIIKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAK 2253
Cdd:smart00194  156 TRTVTHYHYTNWPdhgVPESPES-ILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVK 234
                           250       260
                    ....*....|....*....|....
gi 124486807   2254 MINLMRPGVFTDIEQYQFLYKVVL 2277
Cdd:smart00194  235 ELRSQRPGMVQTEEQYIFLYRAIL 258
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
2045-2277 9.01e-77

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 254.86  E-value: 9.01e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807  2045 NREKNRTSSIIPVERSRVGISSLSGeGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNM 2124
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPG-PSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEK 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807  2125 A-EDEFVYWPNK-DEPINCESFKVTLMSEEhkclSNEEKLIVQDFILEATQDDYVLEVRHFQCPKWPN---PDSPISkTF 2199
Cdd:pfam00102   80 GrEKCAQYWPEEeGESLEYGDFTVTLKKEK----EDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDhgvPESPNS-LL 154
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124486807  2200 ELISIIKE-EAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVVL 2277
Cdd:pfam00102  155 DLLRKVRKsSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233
PHA02738 PHA02738
hypothetical protein; Provisional
1747-1981 1.15e-52

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 188.60  E-value: 1.15e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1747 NKHKNRYVNIVAYDHSRVKLTqlAEKDgkLTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNL 1826
Cdd:PHA02738   49 NRKLNRYLDAVCFDHSRVILP--AERN--RGDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKK 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1827 VEKGRRKCDQYWPT--DGSEEYGSFLVNQKSVQVLAYYTVRNFTLRNtklkkgsqkGRSSGRLVTQYHYTQWPDMGVPEY 1904
Cdd:PHA02738  125 KENGREKCFPYWSDveQGSIRFGKFKITTTQVETHPHYVKSTLLLTD---------GTSATQTVTHFNFTAWPDHDVPKN 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1905 SLPVLAFVRKAAQA-------------KRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNY 1971
Cdd:PHA02738  196 TSEFLNFVLEVRQCqkelaqeslqighNRLQPPPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYY 275
                         250
                  ....*....|
gi 124486807 1972 LVQTEEQYVF 1981
Cdd:PHA02738  276 SLFIPFQYFF 285
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
1722-1982 3.22e-43

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 160.26  E-value: 3.22e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1722 KEFYQEVQSCTADLGITADSSNHPDN---KHKNRYVNIVAYDHsrvklTQLAEKDGkltdYINANYVDGYNrPKAYIAAQ 1798
Cdd:COG5599    14 EKINSRLSTLTNELAPSHNDPQYLQNingSPLNRFRDIQPYKE-----TALRANLG----YLNANYIQVIG-NHRYIATQ 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1799 GPLKSTAEDFWRMIWEHNVEVIVMITNLVE--KGRRKCDQYWPTDGseEYGSFLVNQKSVQVlaYYTVRNFTLRNTKLK- 1875
Cdd:COG5599    84 YPLEEQLEDFFQMLFDNNTPVLVVLASDDEisKPKVKMPVYFRQDG--EYGKYEVSSELTES--IQLRDGIEARTYVLTi 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1876 KGS-QKGRSsgrlVTQYHYTQWPDMGVP--EYSLPVLAFVRKAAQAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQ- 1951
Cdd:COG5599   160 KGTgQKKIE----IPVLHVKNWPDHGAIsaEALKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINa 235
                         250       260       270
                  ....*....|....*....|....*....|...
gi 124486807 1952 -HEGTVNIFGFLKHIRSQRNY-LVQTEEQYVFI 1982
Cdd:COG5599   236 lVQITLSVEEIVIDMRTSRNGgMVQTSEQLDVL 268
Cah COG3338
Carbonic anhydrase [Inorganic ion transport and metabolism];
38-263 1.56e-32

Carbonic anhydrase [Inorganic ion transport and metabolism];


Pssm-ID: 442567 [Multi-domain]  Cd Length: 247  Bit Score: 128.08  E-value: 1.56e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807   38 WSYTGALNQKNWGK---KYPICNS-PKQSPINIDedlTQVNVNLKKLKFQgWEKASLEntfIHNTGKTVEINLTNDYYLS 113
Cdd:COG3338    28 WSYEGETGPEHWGElspEFATCATgKNQSPIDIR---TAIKADLPPLKFD-YKPTPLE---IVNNGHTIQVNVDPGSTLT 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807  114 ggLSEKVFKASKITFHwgkcnvssEGSEHSLEGQKFPLEMQ-VYcfdadrfssfeeaVKGKGRLRALSILFEVGvEENLD 192
Cdd:COG3338   101 --VDGKRYELKQFHFH--------TPSEHTINGKSYPMEAHlVH-------------KDADGELAVVGVLFEEG-AENPA 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124486807  193 YKAIID------GTESVSrfgkQAALDPfvlQNLLPNSTDkYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLAVF 263
Cdd:COG3338   157 LAKLWAnlpleaGEEVAL----DATIDL---NDLLPEDRS-YYRYSGSLTTPPCSEGVLWIVLKQPITVSAEQIEAF 225
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
2037-2281 8.68e-29

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 119.34  E-value: 8.68e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2037 YSTALKQCNREKNRTSSIIPVERSRVGISSLSGEGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVV 2116
Cdd:PHA02747   43 IANFEKPENQPKNRYWDIPCWDHNRVILDSGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIV 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2117 MI--PDGQNMAEDEFVYW-PNKDEPINCESFKVTLMSEEHKCLSNEEKLIVQDFILEATQddyvlEVRHFQCPKWPNPDS 2193
Cdd:PHA02747  123 MLtpTKGTNGEEKCYQYWcLNEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILKDSR-----KISHFQCSEWFEDET 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2194 PiSKTFELISIIKEEAANRD-------------GPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRP 2260
Cdd:PHA02747  198 P-SDHPDFIKFIKIIDINRKksgklfnpkdallCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRH 276
                         250       260
                  ....*....|....*....|....
gi 124486807 2261 GVFTDIEQYQFL---YKVVLSLVS 2281
Cdd:PHA02747  277 AGIMNFDDYLFIqpgYEVLHYFLS 300
fn3 pfam00041
Fibronectin type III domain;
313-401 9.77e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 57.04  E-value: 9.77e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807   313 SEPENVQADPENYTSLLVTWERPRVVyDAMIEKFAVLYQPLaGNDQAKHEFLTDGYQDlGAILNNLLPNMSYVLQIVAVC 392
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDG-NGPITGYEVEYRPK-NSGEPWNEITVPGTTT-SVTLTGLKPGTEYEVRVQAVN 77

                   ....*....
gi 124486807   393 SNGlYGKYS 401
Cdd:pfam00041   78 GGG-EGPPS 85
PLN02179 PLN02179
carbonic anhydrase
49-253 1.83e-08

carbonic anhydrase


Pssm-ID: 177835  Cd Length: 235  Bit Score: 57.30  E-value: 1.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807   49 WGKKYP---ICNSPK-QSPInideDLTQVNVNLkkLKFQGWEKA-SLENTFIHNTGKTVEINLTNDyylsgglsekvfkA 123
Cdd:PLN02179   50 WGKLNPqwkVCSTGKyQSPI----DLTDERVSL--IHDQALSRHyKPAPAVIQSRGHDVMVSWKGD-------------A 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807  124 SKITFHWG-----KCNVSSEgSEHSLEGQKFPLEMQVYCFDAdrfssfeeavkgKGRLRALSILFEVGvEENLDYKAIID 198
Cdd:PLN02179  111 GKITIHQTdyklvQCHWHSP-SEHTINGTSYDLELHMVHTSA------------SGKTAVVGVLYKLG-EPDEFLTKLLN 176
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 124486807  199 GTESVsrfGKQ----AALDPFVLQNllpnSTDKYYIYNGSLTSPPCTDTVEWIVFKDTV 253
Cdd:PLN02179  177 GIKGV---GKKeinlGIVDPRDIRF----ETNNFYRYIGSLTIPPCTEGVIWTVVKRVV 228
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
313-406 6.20e-06

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: 46.72  E-value: 6.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807  313 SEPENVQADPENYTSLLVTWERPRvVYDAMIEKFAVLYQPLAGNDQakHEFLTDGYQDLGAILNNLLPNMSYVLQIVAVC 392
Cdd:cd00063     2 SPPTNLRVTDVTSTSVTLSWTPPE-DDGGPITGYVVEYREKGSGDW--KEVEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78
                          90
                  ....*....|....
gi 124486807  393 SNGlYGKYSDQLIV 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 2.57e-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: 44.53  E-value: 2.57e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807    313 SEPENVQADPENYTSLLVTWERPRvvyDAMIEKFAVLYQPLAGNDQAKHEFLTDGYQDLGAILNNLLPNMSYVLQIVAVC 392
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPP---DDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                    ...
gi 124486807    393 SNG 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 ...
1714-1991 4.92e-159

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: 491.47  E-value: 4.92e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1714 FTEEFEtlkefyqEVQSCTADLGITADSSNHPDNKHKNRYVNIVAYDHSRVKLTQLAEKDGKLTDYINANYVDGYNRPKA 1793
Cdd:cd17667     1 FSEDFE-------EVQRCTADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSKHSDYINANYVDGYNKAKA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1794 YIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPTDGSEEYGSFLVNQKSVQVLAYYTVRNFTLRNTK 1873
Cdd:cd17667    74 YIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTK 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1874 LKKGSQ---KGRSSGRLVTQYHYTQWPDMGVPEYSLPVLAFVRKAAQAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQI 1950
Cdd:cd17667   154 VKKGQKgnpKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQI 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 124486807 1951 QHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAIL 1991
Cdd:cd17667   234 KDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 274
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
2074-2277 4.18e-153

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: 471.40  E-value: 4.18e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2074 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAEDEFVYWPNKDEPINCESFKVTLMSEEH 2153
Cdd:cd17669     1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFVYWPNKDEPINCETFKVTLIAEEH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2154 KCLSNEEKLIVQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTFELISIIKEEAANRDGPMIVHDEHGGVTAGTFCAL 2233
Cdd:cd17669    81 KCLSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTFELISIIKEEAANRDGPMIVHDEHGGVTAGTFCAL 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 124486807 2234 TTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVVL 2277
Cdd:cd17669   161 TTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
1779-1987 7.83e-152

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: 468.30  E-value: 7.83e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1779 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPTDGSEEYGSFLVNQKSVQV 1858
Cdd:cd17668     1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1859 LAYYTVRNFTLRNTKLKKGSQKGRSSGRLVTQYHYTQWPDMGVPEYSLPVLAFVRKAAQAKRHAVGPVVVHCSAGVGRTG 1938
Cdd:cd17668    81 LAYYTVRNFTLRNTKIKKGSQKGRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVGPVVVHCSAGVGRTG 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 124486807 1939 TYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLV 1987
Cdd:cd17668   161 TYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
1779-1984 3.14e-140

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: 435.24  E-value: 3.14e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1779 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPTDGSEEYGSFLVNQKSVQV 1858
Cdd:cd14549     1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTETYGNIQVTLLSTEV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1859 LAYYTVRNFTLRNTKLKKGsqKGRSSGRLVTQYHYTQWPDMGVPEYSLPVLAFVRKAAQAKRHAVGPVVVHCSAGVGRTG 1938
Cdd:cd14549    81 LATYTVRTFSLKNLKLKKV--KGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAGVGRTG 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 124486807 1939 TYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHD 1984
Cdd:cd14549   159 TYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
2074-2278 2.10e-128

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: 401.36  E-value: 2.10e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2074 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAEDEFVYWPNKDEPINCESFKVTLMSEEH 2153
Cdd:cd17670     1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQGLAEDEFVYWPSREESMNCEAFTVTLISKDR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2154 KCLSNEEKLIVQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTFELISIIKEEAANRDGPMIVHDEHGGVTAGTFCAL 2233
Cdd:cd17670    81 LCLSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISSTFELINVIKEEALTRDGPTIVHDEFGAVSAGTLCAL 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 124486807 2234 TTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVVLS 2278
Cdd:cd17670   161 TTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAMLS 205
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
2074-2274 7.35e-127

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: 396.69  E-value: 7.35e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2074 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQnMAEDEFVYWPNKDEPINCESFKVTLMSEEH 2153
Cdd:cd14550     1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNE-LNEDEPIYWPTKEKPLECETFKVTLSGEDH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2154 KCLSNEEKLIVQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTFELISIIKEEAANRDGPMIVHDEHGGVTAGTFCAL 2233
Cdd:cd14550    80 SCLSNEIRLIVRDFILESTQDDYVLEVRQFQCPSWPNPCSPIHTVFELINTVQEWAQQRDGPIVVHDRYGGVQAATFCAL 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 124486807 2234 TTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYK 2274
Cdd:cd14550   160 TTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1713-1988 2.27e-121

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 383.55  E-value: 2.27e-121
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807   1713 GFTEEFETLKEFYQEVQSCTadlgitadSSNHPDNKHKNRYVNIVAYDHSRVKLTQLaekDGKLTDYINANYVDGYNRPK 1792
Cdd:smart00194    1 GLEEEFEKLDRLKPDDESCT--------VAAFPENRDKNRYKDVLPYDHTRVKLKPP---PGEGSDYINASYIDGPNGPK 69
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807   1793 AYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPTDGSE--EYGSFLVNQKSVQVLAYYTVRNFTLR 1870
Cdd:smart00194   70 AYIATQGPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEplTYGDITVTLKSVEKVDDYTIRTLEVT 149
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807   1871 NTklkkgsqkGRSSGRLVTQYHYTQWPDMGVPEYSLPVLAFVRKAAQAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQI 1950
Cdd:smart00194  150 NT--------GCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQL 221
                           250       260       270
                    ....*....|....*....|....*....|....*...
gi 124486807   1951 QHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVE 1988
Cdd:smart00194  222 EAGKEVDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1747-1988 1.54e-113

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 360.02  E-value: 1.54e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807  1747 NKHKNRYVNIVAYDHSRVKLTqlaeKDGKLTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNL 1826
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLT----GDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTEL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807  1827 VEKGRRKCDQYWPT--DGSEEYGSFLVN-QKSVQVLAYYTVRNFTLRNtklkkgsqKGRSSGRLVTQYHYTQWPDMGVPE 1903
Cdd:pfam00102   77 EEKGREKCAQYWPEeeGESLEYGDFTVTlKKEKEDEKDYTVRTLEVSN--------GGSEETRTVKHFHYTGWPDHGVPE 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807  1904 YSLPVLAFVRKAAQAKRHA-VGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFI 1982
Cdd:pfam00102  149 SPNSLLDLLRKVRKSSLDGrSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFL 228

                   ....*.
gi 124486807  1983 HDTLVE 1988
Cdd:pfam00102  229 YDAILE 234
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
1747-1992 3.49e-110

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: 350.54  E-value: 3.49e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1747 NKHKNRYVNIVAYDHSRVKLTQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNL 1826
Cdd:cd14553     3 NKPKNRYANVIAYDHSRVILQPIEGVPG--SDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1827 VEKGRRKCDQYWPTDGSEEYGSFLVNQKSVQVLAYYTVRNFTLRNTklkkgsqkGRSSGRLVTQYHYTQWPDMGVPEYSL 1906
Cdd:cd14553    81 EERSRVKCDQYWPTRGTETYGLIQVTLLDTVELATYTVRTFALHKN--------GSSEKREVRQFQFTAWPDHGVPEHPT 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1907 PVLAFVRKAAQAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTL 1986
Cdd:cd14553   153 PFLAFLRRVKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDAL 232

                  ....*.
gi 124486807 1987 VEAILS 1992
Cdd:cd14553   233 LEAVTC 238
alpha_CARP_receptor_like cd03122
Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related ...
45-298 5.91e-110

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: 350.50  E-value: 5.91e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807   45 NQKNWGKKYPICNS-PKQSPINIDEDlTQVNVN-LKKLKFQGWEKASLEnTFIHNTGKTVEINLTN---DYYLSGGLSEK 119
Cdd:cd03122     1 NPKHWAKKYPACGEgRQQSPIDIVED-TQVQRQgLQPLHFDGYEELTAS-TTLENTGKTVILRLEGnssDPFVSGGPLLG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807  120 VFKASKITFHWGKCNvsSEGSEHSLEGQKFPLEMQVYCFDADRFSSFEeAVKGKGRLRALSILFEVGVEENLDYKAIIDG 199
Cdd:cd03122    79 RYKFSEITFHWGTCN--SDGSEHSIDGHKFPLEMQILHRNTDFFDSFE-AIKSPGGVLALAYLFELSHEDNPFLDPIIEG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807  200 TESVSRFGKQAALDPFVLQNLLPNSTDKYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLAVFCEVLTMQQSGyVMLMD 279
Cdd:cd03122   156 LRNVSRPGKEVELPPFPLSDLLPPFTDKYYSYEGSLTTPPCSETVEWIVFREPVPISSRQLEAFRELLTRRQDG-VMSGD 234
                         250
                  ....*....|....*....
gi 124486807  280 YLQNNFREQQYKFSRQVFS 298
Cdd:cd03122   235 YLPNNGRPQQPLGSRTVFS 253
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
1779-1984 1.54e-97

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: 312.68  E-value: 1.54e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1779 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPTDGSE--EYGSFLVNQKSV 1856
Cdd:cd00047     1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKplEYGDITVTLVSE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1857 QVLAYYTVRNFTLRNtklkkgsqKGRSSGRLVTQYHYTQWPDMGVPEYSLPVLAFVRKAAQAKRHAVGPVVVHCSAGVGR 1936
Cdd:cd00047    81 EELSDYTIRTLELSP--------KGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCSAGVGR 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 124486807 1937 TGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHD 1984
Cdd:cd00047   153 TGTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
1704-1990 2.13e-94

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


Pssm-ID: 350474 [Multi-domain]  Cd Length: 276  Bit Score: 306.96  E-value: 2.13e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1704 HVADLHASNGFteefetlkEFYQEVQSCTADLGITADSSNHPDNKHKNRYVNIVAYDHSRVKLTQLAEKDGklTDYINAN 1783
Cdd:cd14626     6 NIERLKANDGL--------KFSQEYESIDPGQQFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPG--SDYINAN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1784 YVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPTDGSEEYGSFLVNQKSVQVLAYYT 1863
Cdd:cd14626    76 YIDGYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIRGTETYGMIQVTLLDTVELATYS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1864 VRNFTLRntklkkgsQKGRSSGRLVTQYHYTQWPDMGVPEYSLPVLAFVRKAAQAKRHAVGPVVVHCSAGVGRTGTYIVL 1943
Cdd:cd14626   156 VRTFALY--------KNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVI 227
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 124486807 1944 DSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAI 1990
Cdd:cd14626   228 DAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLEAA 274
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
1752-1983 5.73e-93

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: 300.81  E-value: 5.73e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1752 RYVNIVAYDHSRVKLTQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGR 1831
Cdd:cd14548     1 RYTNILPYDHSRVKLIPINEEEG--SDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1832 RKCDQYWPTDGSE-EYGSFLVNQKSVQVLAYYTVRNFTLrntklkkgsqKGRSSGRLVTQYHYTQWPDMGVPEYSLPVLA 1910
Cdd:cd14548    79 VKCDHYWPFDQDPvYYGDITVTMLSESVLPDWTIREFKL----------ERGDEVRSVRQFHFTAWPDHGVPEAPDSLLR 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124486807 1911 FVRKAAQAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIH 1983
Cdd:cd14548   149 FVRLVRDYIKQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLH 221
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
1738-1983 1.62e-90

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: 295.81  E-value: 1.62e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1738 TADSSNHPDNKHKNRYVNIVAYDHSRVKLTQLAEKDgkLTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNV 1817
Cdd:cd14543    20 TFLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDE--RTDYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKV 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1818 EVIVMITNLVEKGRRKCDQYWPTDG--SEEYGSFLVNQKSVQVLAYYTVRNFTLRNTKlkkgsqkgRSSGRLVTQYHYTQ 1895
Cdd:cd14543    98 LVIVMTTRVVERGRVKCGQYWPLEEgsSLRYGDLTVTNLSVENKEHYKKTTLEIHNTE--------TDESRQVTHFQFTS 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1896 WPDMGVPEYSLPVLAFVRKAAQAKRHAVG-------------PVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFL 1962
Cdd:cd14543   170 WPDFGVPSSAAALLDFLGEVRQQQALAVKamgdrwkghppgpPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQTV 249
                         250       260
                  ....*....|....*....|.
gi 124486807 1963 KHIRSQRNYLVQTEEQYVFIH 1983
Cdd:cd14543   250 RRMRTQRAFSIQTPDQYYFCY 270
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
1696-1990 3.12e-87

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: 286.60  E-value: 3.12e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1696 IPIKHFPKHVADLHASNGFteefetlkEFYQEVQSCTADLGITADSSNHPDNKHKNRYVNIVAYDHSRVKLTQLAEKDGk 1775
Cdd:cd14625     4 IPISELAEHTERLKANDNL--------KLSQEYESIDPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMG- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1776 lTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPTDGSEEYGSFLVNQKS 1855
Cdd:cd14625    75 -SDYINANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSRGTETYGMIQVTLLD 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1856 VQVLAYYTVRNFTLRntklkkgsQKGRSSGRLVTQYHYTQWPDMGVPEYSLPVLAFVRKAAQAKRHAVGPVVVHCSAGVG 1935
Cdd:cd14625   154 TIELATFCVRTFSLH--------KNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPPDAGPIVVHCSAGVG 225
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 124486807 1936 RTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAI 1990
Cdd:cd14625   226 RTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEAV 280
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
1682-1990 3.06e-86

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


Pssm-ID: 350472 [Multi-domain]  Cd Length: 284  Bit Score: 283.93  E-value: 3.06e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1682 PPTPIFPISDdigaipikhfpkHVADLHASNGFteefetlkEFYQEVQSCTADLGITADSSNHPDNKHKNRYVNIVAYDH 1761
Cdd:cd14624     2 PPIPILELAD------------HIERLKANDNL--------KFSQEYESIDPGQQFTWEHSNLEVNKPKNRYANVIAYDH 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1762 SRVKLTQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPTD 1841
Cdd:cd14624    62 SRVLLSAIEGIPG--SDYINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSR 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1842 GSEEYGSFLVNQKSVQVLAYYTVRNFTLRntklkkgsQKGRSSGRLVTQYHYTQWPDMGVPEYSLPVLAFVRKAAQAKRH 1921
Cdd:cd14624   140 GTETYGLIQVTLLDTVELATYCVRTFALY--------KNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPP 211
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124486807 1922 AVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAI 1990
Cdd:cd14624   212 DAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLEAV 280
Carb_anhydrase smart01057
Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse ...
38-295 4.74e-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: 281.90  E-value: 4.74e-86
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807     38 WSYTGALNQKNWGKKYP-ICNSPKQSPINIDEDLTQVNVNLKKLKFQgWEKASleNTFIHNTGKTVEINL-TNDYYLSGG 115
Cdd:smart01057    1 WGYEGKNGPEHWGKLDPpFCGGKRQSPIDIVTAEAQYDPSLKPLKLS-YDQPT--AKRILNNGHTVQVNFdDDGSTLSGG 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807    116 LSEKVFKASKITFHWGKCNvsSEGSEHSLEGQKFPLEMQVYCFDADrfSSFEEAVKGKGRLRALSILFEVGVEENLDYKA 195
Cdd:smart01057   78 PLPGRYRLKQFHFHWGGSD--SEGSEHTIDGKRFPLELHLVHYNSK--GSFSEAVSKPGGLAVVAVFFKVGAEENPALQA 153
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807    196 IIDGTESVSRFGKQAALDPFVLQNLLPNSTDKYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLAVFCEVLTMQQSgyv 275
Cdd:smart01057  154 ILDHLPLIKYKGQETELTPFDLSSLLPASTRHYYTYNGSLTTPPCSEGVTWIVFKEPITISTEQLEKFRTLLPMEGN--- 230
                           250       260
                    ....*....|....*....|
gi 124486807    276 mlmDYLQNNFREQQYKFSRQ 295
Cdd:smart01057  231 ---EPLVNNARPLQPLNGRV 247
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
1746-1991 2.09e-83

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: 273.82  E-value: 2.09e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1746 DNKHKNRYVNIVAYDHSRVKLTQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITN 1825
Cdd:cd14630     2 ENRNKNRYGNIISYDHSRVRLQLLDGDPH--SDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1826 LVEKGRRKCDQYWPtDGSEEYGSFLVNQKSVQVLAYYTVRNFTLRntklKKGSQKGRSsgrlVTQYHYTQWPDMGVPEYS 1905
Cdd:cd14630    80 LVEVGRVKCVRYWP-DDTEVYGDIKVTLIETEPLAEYVIRTFTVQ----KKGYHEIRE----IRQFHFTSWPDHGVPCYA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1906 LPVLAFVRKAAQAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDT 1985
Cdd:cd14630   151 TGLLGFVRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDA 230

                  ....*.
gi 124486807 1986 LVEAIL 1991
Cdd:cd14630   231 ILEACL 236
Carb_anhydrase pfam00194
Eukaryotic-type carbonic anhydrase;
44-300 1.31e-82

Eukaryotic-type carbonic anhydrase;


Pssm-ID: 459707 [Multi-domain]  Cd Length: 252  Bit Score: 272.22  E-value: 1.31e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807    44 LNQKNWGKKYPICNSPKQSPINIDEDLTQVNVNLKKLKFQGWEKASLENTfIHNTGKTVEINLTNDY--YLSGGLSEKVF 121
Cdd:pfam00194    1 LGPEHWGKVYPSCGGKRQSPINIDTRKVRYDPSLPPLTFQGYDVPPGKNT-LTNNGHTVQVSLDDGDpsTISGGPLATRY 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807   122 KASKITFHWGKCNvsSEGSEHSLEGQKFPLEMQVYCFDADRfSSFEEAVKGKGRLRALSILFEVGVEENLDYKAIIDGTE 201
Cdd:pfam00194   80 RLVQFHFHWGSTD--SRGSEHTIDGKRYPAELHIVHYNSKY-KSFDEAAKHPDGLAVLGVFFEVGDENNPYLQPIVSALD 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807   202 SVSRFGKQAALDPFVLQNLLPNSTDKYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLAVFCEVLTMQQSGYvmlMDYL 281
Cdd:pfam00194  157 NIKYKGKSVLLPPFDLSDLLPEDLTSYYTYNGSLTTPPCSESVTWIVFKEPISISEEQLEAFRTLLFSDGGEE---PRPL 233
                          250
                   ....*....|....*....
gi 124486807   282 QNNFREQQYKFSRQVFSSY 300
Cdd:pfam00194  234 VNNFRPTQPLNGRVVFASF 252
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
1682-1997 1.78e-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: 268.05  E-value: 1.78e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1682 PPTPIFPISDDIGaipikhfpKHVADlhASNGFTEEFETLKefyqevqscTADLGITADSSNHPDNKHKNRYVNIVAYDH 1761
Cdd:cd14621     6 PPLPVDKLEEEIN--------RRMAD--DNKLFREEFNALP---------ACPIQATCEAASKEENKEKNRYVNILPYDH 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1762 SRVKLTQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPTD 1841
Cdd:cd14621    67 SRVHLTPVEGVPD--SDYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQ 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1842 GSEEYGSFLVNQKSVQVLAYYTVRNFTLRNTklkkGSQKGRSSGRLVTQYHYTQWPDMGVPEYSLPVLAFVRKAAQAKRH 1921
Cdd:cd14621   145 GCWTYGNIRVSVEDVTVLVDYTVRKFCIQQV----GDVTNKKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQ 220
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124486807 1922 AVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAILSKETEV 1997
Cdd:cd14621   221 YAGAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEHYLYGDTEL 296
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
1751-1982 5.24e-79

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: 260.90  E-value: 5.24e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1751 NRYVNIVAYDHSRVKLTQLAEKdgkLTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKG 1830
Cdd:cd14615     1 NRYNNVLPYDISRVKLSVQSHS---TDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1831 RRKCDQYWPTDGSEEYGSFLVNQKSVQVLAYYTVRNFTLRNTKlkkgsqkgRSSGRLVTQYHYTQWPDMGVPEYSLPVLA 1910
Cdd:cd14615    78 RTKCEEYWPSKQKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQ--------TNESRTVRHFHFTSWPDHGVPETTDLLIN 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124486807 1911 F---VRK-AAQAKRHavGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFI 1982
Cdd:cd14615   150 FrhlVREyMKQNPPN--SPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFL 223
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
1703-1991 9.62e-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: 261.90  E-value: 9.62e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1703 KHVADLHASNG--FTEEFETlkefYQEVQSCTADlgitadSSNHPDNKHKNRYVNIVAYDHSRVKLTQLAEKDGklTDYI 1780
Cdd:cd14633     4 QHITQMKCAEGygFKEEYES----FFEGQSAPWD------SAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETS--SDYI 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1781 NANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPTDgSEEYGSFLVNQKSVQVLA 1860
Cdd:cd14633    72 NGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDD-TEIYKDIKVTLIETELLA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1861 YYTVRNFTLRntklKKGSQKGRSsgrlVTQYHYTQWPDMGVPEYSLPVLAFVRKAAQAKRHAVGPVVVHCSAGVGRTGTY 1940
Cdd:cd14633   151 EYVIRTFAVE----KRGVHEIRE----IRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCF 222
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 124486807 1941 IVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAIL 1991
Cdd:cd14633   223 IVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILEACL 273
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
2019-2277 1.67e-78

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 260.67  E-value: 1.67e-78
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807   2019 KLEKQFQLLSQSNILQSDYSTALKQCNREKNRTSSIIPVERSRVGISSLSGEGTDYINASYIMGYYQSNEFIITQHPLLH 2098
Cdd:smart00194    1 GLEEEFEKLDRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGPLPS 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807   2099 TIKDFWRMIWDHNAQLVVMI-PDGQNMAEDEFVYWPNK-DEPINCESFKVTLMSEEHKclsneEKLIVQDFILEATQDDY 2176
Cdd:smart00194   81 TVEDFWRMVWEQKVTVIVMLtELVEKGREKCAQYWPDEeGEPLTYGDITVTLKSVEKV-----DDYTIRTLEVTNTGCSE 155
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807   2177 VLEVRHFQCPKWP---NPDSPISkTFELISIIKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAK 2253
Cdd:smart00194  156 TRTVTHYHYTNWPdhgVPESPES-ILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVK 234
                           250       260
                    ....*....|....*....|....
gi 124486807   2254 MINLMRPGVFTDIEQYQFLYKVVL 2277
Cdd:smart00194  235 ELRSQRPGMVQTEEQYIFLYRAIL 258
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
1751-1990 7.58e-77

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


Pssm-ID: 350467 [Multi-domain]  Cd Length: 233  Bit Score: 254.81  E-value: 7.58e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1751 NRYVNIVAYDHSRVKLTQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKG 1830
Cdd:cd14619     1 NRFRNVLPYDWSRVPLKPIHEEPG--SDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1831 RRKCDQYWPTDGSE-EYGSFLVNQKSVQVLAYYTVRNFTLRNTKlkkgSQKGRSsgrlVTQYHYTQWPDMGVPEYSLPVL 1909
Cdd:cd14619    79 RVKCEHYWPLDYTPcTYGHLRVTVVSEEVMENWTVREFLLKQVE----EQKTLS----VRHFHFTAWPDHGVPSSTDTLL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1910 AF---VRKAAQAKRHAvGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTL 1986
Cdd:cd14619   151 AFrrlLRQWLDQTMSG-GPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCI 229

                  ....
gi 124486807 1987 VEAI 1990
Cdd:cd14619   230 LDFL 233
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
1751-1983 8.55e-77

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: 254.46  E-value: 8.55e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1751 NRYVNIVAYDHSRVKLTQLaeKDGKLTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKG 1830
Cdd:cd14617     1 NRYNNILPYDSTRVKLSNV--DDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1831 RRKCDQYWPTD-GSEEYGSFLVNQKSVQVLAYYTVRNFtlrntklKKGSQKGRSSGRLVTQYHYTQWPDMGVPEYSLPVL 1909
Cdd:cd14617    79 RVKCDHYWPADqDSLYYGDLIVQMLSESVLPEWTIREF-------KICSEEQLDAPRLVRHFHYTVWPDHGVPETTQSLI 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124486807 1910 AFVRKAAQ--AKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIH 1983
Cdd:cd14617   152 QFVRTVRDyiNRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 227
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
2045-2277 9.01e-77

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 254.86  E-value: 9.01e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807  2045 NREKNRTSSIIPVERSRVGISSLSGeGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNM 2124
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPG-PSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEK 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807  2125 A-EDEFVYWPNK-DEPINCESFKVTLMSEEhkclSNEEKLIVQDFILEATQDDYVLEVRHFQCPKWPN---PDSPISkTF 2199
Cdd:pfam00102   80 GrEKCAQYWPEEeGESLEYGDFTVTLKKEK----EDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDhgvPESPNS-LL 154
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124486807  2200 ELISIIKE-EAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVVL 2277
Cdd:pfam00102  155 DLLRKVRKsSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
1779-1991 1.19e-76

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


Pssm-ID: 350403 [Multi-domain]  Cd Length: 204  Bit Score: 253.30  E-value: 1.19e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1779 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPTDgSEEYGSFLVNQKSVQV 1858
Cdd:cd14555     1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDD-TEVYGDIKVTLVETEP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1859 LAYYTVRNFTLRntklkkgsQKGRSSGRLVTQYHYTQWPDMGVPEYSLPVLAFVRKAAQAKRHAVGPVVVHCSAGVGRTG 1938
Cdd:cd14555    80 LAEYVVRTFALE--------RRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAGPIVVHCSAGAGRTG 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 124486807 1939 TYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAIL 1991
Cdd:cd14555   152 CYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILEACL 204
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
1753-1988 8.78e-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: 251.78  E-value: 8.78e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1753 YVNIVAYDHSRVKLTQLaekDGKL-TDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGR 1831
Cdd:cd14620     1 YPNILPYDHSRVILSQL---DGIPcSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1832 RKCDQYWPTDGSEEYGSFLVNQKSVQVLAYYTVRNFTLRNTklkkgSQKGRSSGRLVTQYHYTQWPDMGVPEYSLPVLAF 1911
Cdd:cd14620    78 EKCYQYWPDQGCWTYGNIRVAVEDCVVLVDYTIRKFCIQPQ-----LPDGCKAPRLVTQLHFTSWPDFGVPFTPIGMLKF 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124486807 1912 VRKAAQAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVE 1988
Cdd:cd14620   153 LKKVKSVNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
1742-1983 4.84e-74

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: 247.05  E-value: 4.84e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1742 SNHPDNKHKNRYVNIVAYDHSRVKLTQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIV 1821
Cdd:cd14554     1 ANLPCNKFKNRLVNILPYESTRVCLQPIRGVEG--SDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1822 MITNLVEKGRRKCDQYWPTDGSEEYGSFLVNQksvqvLAYYTVRNFTLRNTKLKKgSQKGRSsgRLVTQYHYTQWPDMGV 1901
Cdd:cd14554    79 MLTKLREMGREKCHQYWPAERSARYQYFVVDP-----MAEYNMPQYILREFKVTD-ARDGQS--RTVRQFQFTDWPEQGV 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1902 PEYSLPVLAFVRKAAQAKRH--AVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQY 1979
Cdd:cd14554   151 PKSGEGFIDFIGQVHKTKEQfgQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQY 230

                  ....
gi 124486807 1980 VFIH 1983
Cdd:cd14554   231 QFCY 234
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
1772-1991 2.69e-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: 244.16  E-value: 2.69e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1772 KDGKLTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPTDgSEEYGSFLV 1851
Cdd:cd14631     8 EDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDD-TEVYGDFKV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1852 NQKSVQVLAYYTVRNFTLrntklkkgSQKGRSSGRLVTQYHYTQWPDMGVPEYSLPVLAFVRKAAQAKRHAVGPVVVHCS 1931
Cdd:cd14631    87 TCVEMEPLAEYVVRTFTL--------ERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVHCS 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1932 AGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAIL 1991
Cdd:cd14631   159 AGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACL 218
alpha_CA cd00326
Carbonic anhydrase alpha (vertebrate-like) group. Carbonic anhydrases (CAs) are ...
60-297 1.17e-72

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: 242.57  E-value: 1.17e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807   60 KQSPINIDEDLTQVNVNLKKLKFQGWEKASLEntfIHNTGKTVEINL-TNDYYLSGGLSEKVFKASKITFHWGKCNvsSE 138
Cdd:cd00326     3 RQSPINIVTSAVVYDPSLPPLNFDYYPTTSLT---LVNNGHTVQVNFdDDGGTLSGGGLPGRYKLVQFHFHWGSEN--SP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807  139 GSEHSLEGQKFPLEMQVYCFDADRFSSfeEAVKGKGRLRALSILFEVGVEENLDYKAIIDGTESVSRFGKQAALDPFVLQ 218
Cdd:cd00326    78 GSEHTIDGKRYPLELHLVHYNSDYYSS--EAAKKPGGLAVLGVFFEVGEKENPFLKKILDALPKIKYKGKETTLPPFDLS 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124486807  219 NLLPNSTDKYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLAVFCEVLTMQqsgyvmlMDYLQNNFREQQYKFSRQVF 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; ...
1779-1983 1.69e-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: 1.69e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1779 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPTDGSEEYGSFLVNQKSVQV 1858
Cdd:cd14551     1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCWTYGNLRVRVEDTVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1859 LAYYTVRNFTLRntklKKGSQKGRSSGRLVTQYHYTQWPDMGVPEYSLPVLAFVRKAAQAKRHAVGPVVVHCSAGVGRTG 1938
Cdd:cd14551    81 LVDYTTRKFCIQ----KVNRGIGEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAGPIVVHCSAGVGRTG 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 124486807 1939 TYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIH 1983
Cdd:cd14551   157 TFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
1751-1983 6.68e-72

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: 240.38  E-value: 6.68e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1751 NRYVNIVAYDHSRVKLTQlaEKDGKLTDYINANYVDGYN-RPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEK 1829
Cdd:cd14547     1 NRYKTILPNEHSRVCLPS--VDDDPLSSYINANYIRGYDgEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1830 gRRKCDQYWPTDGSEEYGSFLVNQKSVQVLAYYTVRNFTLRNtklkkGSQKgrssgRLVTQYHYTQWPDMGVPEYSLPVL 1909
Cdd:cd14547    79 -KEKCAQYWPEEENETYGDFEVTVQSVKETDGYTVRKLTLKY-----GGEK-----RYLKHYWYTSWPDHKTPEAAQPLL 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124486807 1910 AFVRKAAQAKRHAV--GPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIH 1983
Cdd:cd14547   148 SLVQEVEEARQTEPhrGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVH 223
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
1737-1983 1.35e-71

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


Pssm-ID: 350462 [Multi-domain]  Cd Length: 245  Bit Score: 240.18  E-value: 1.35e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1737 ITADSSNHPDNKHKNRYVNIVAYDHSRVKLTQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHN 1816
Cdd:cd14614     2 IPHFAADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEG--SDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1817 VEVIVMITNLVEKGRRKCDQYWP-TDGSEEYGSFLVNQKSVQVLAYYTVRNFtlrNTKLKKGSQKgrssgrlVTQYHYTQ 1895
Cdd:cd14614    80 SQIIVMLTQCNEKRRVKCDHYWPfTEEPVAYGDITVEMLSEEEQPDWAIREF---RVSYADEVQD-------VMHFNYTA 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1896 WPDMGVPEYSL--PVLAFVRKAAQAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLV 1973
Cdd:cd14614   150 WPDHGVPTANAaeSILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMV 229
                         250
                  ....*....|
gi 124486807 1974 QTEEQYVFIH 1983
Cdd:cd14614   230 QTEEQYIFIH 239
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
1779-1991 3.24e-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: 237.64  E-value: 3.24e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1779 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPtDGSEEYGSFLVNQKSVQV 1858
Cdd:cd14632     1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWP-DDSDTYGDIKITLLKTET 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1859 LAYYTVRNFTLRntklkkgsQKGRSSGRLVTQYHYTQWPDMGVPEYSLPVLAFVRKAAQAKRHAVGPVVVHCSAGVGRTG 1938
Cdd:cd14632    80 LAEYSVRTFALE--------RRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTG 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 124486807 1939 TYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAIL 1991
Cdd:cd14632   152 CYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILEACL 204
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
1747-1983 8.18e-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: 235.43  E-value: 8.18e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1747 NKHKNRYVNIVAYDHSRVKLTQlAEKDGKLTDYINANYVDGYN-------RPKAYIAAQGPLKSTAEDFWRMIWEHNVEV 1819
Cdd:cd14544     1 NKGKNRYKNILPFDHTRVILKD-RDPNVPGSDYINANYIRNENegpttdeNAKTYIATQGCLENTVSDFWSMVWQENSRV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1820 IVMITNLVEKGRRKCDQYWPTDG-SEEYGSFlvnqkSVQVLAYYTVRNFTLRNTKLKKGSQkgRSSGRLVTQYHYTQWPD 1898
Cdd:cd14544    80 IVMTTKEVERGKNKCVRYWPDEGmQKQYGPY-----RVQNVSEHDTTDYTLRELQVSKLDQ--GDPIREIWHYQYLSWPD 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1899 MGVPEYSLPVLAFVRKAAQAKRH--AVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEG---TVNIFGFLKHIRSQRNYLV 1973
Cdd:cd14544   153 HGVPSDPGGVLNFLEDVNQRQESlpHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGldcDIDIQKTIQMVRSQRSGMV 232
                         250
                  ....*....|
gi 124486807 1974 QTEEQYVFIH 1983
Cdd:cd14544   233 QTEAQYKFIY 242
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
1751-1987 2.99e-69

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: 232.91  E-value: 2.99e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1751 NRYVNIVAYDHSRVKLTQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKG 1830
Cdd:cd14618     1 NRYPHVLPYDHSRVRLSQLGGEPH--SDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1831 RRKCDQYWPTDGSE-EYGsflvnQKSVQVLAYYTVRNFTLRNTKLKKGSQKGRssgRLVTQYHYTQWPDMGVPEYSLPVL 1909
Cdd:cd14618    79 RVLCDHYWPSESTPvSYG-----HITVHLLAQSSEDEWTRREFKLWHEDLRKE---RRVKHLHYTAWPDHGIPESTSSLM 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1910 AF---VRKAAQAKRHAvGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTL 1986
Cdd:cd14618   151 AFrelVREHVQATKGK-GPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCI 229

                  .
gi 124486807 1987 V 1987
Cdd:cd14618   230 L 230
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
1741-1992 3.19e-67

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: 229.62  E-value: 3.19e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1741 SSNHPDNKHKNRYVNIVAYDHSRVKLTQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVI 1820
Cdd:cd14628    46 SANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEG--SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIV 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1821 VMITNLVEKGRRKCDQYWPTDGSEEYGSFLVNQksvqvLAYYTVRNFTLRNTKLKKgSQKGRSsgRLVTQYHYTQWPDMG 1900
Cdd:cd14628   124 VMLTKLREMGREKCHQYWPAERSARYQYFVVDP-----MAEYNMPQYILREFKVTD-ARDGQS--RTVRQFQFTDWPEQG 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1901 VPEYSLPVLAFVRKAAQAKRH--AVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQ 1978
Cdd:cd14628   196 VPKSGEGFIDFIGQVHKTKEQfgQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQ 275
                         250
                  ....*....|....
gi 124486807 1979 YVFIHDTLVEAILS 1992
Cdd:cd14628   276 YQFCYRAALEYLGS 289
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
1779-1984 1.07e-66

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: 224.82  E-value: 1.07e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1779 YINANYVD-GYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPTDGSE-EYGSFLVNQKSV 1856
Cdd:cd18533     1 YINASYITlPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEgEYGDLTVELVSE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1857 QVL--AYYTVRNFTLRNTKLKKgsqkgrssgRLVTQYHYTQWPDMGVPEYSLPVLAFVR--KAAQAKRHAVGPVVVHCSA 1932
Cdd:cd18533    81 EENddGGFIVREFELSKEDGKV---------KKVYHIQYKSWPDFGVPDSPEDLLTLIKlkRELNDSASLDPPIIVHCSA 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124486807 1933 GVGRTGTYIVLDSMLQQIQ--HEGTVN-------IFGFLKHIRSQRNYLVQTEEQYVFIHD 1984
Cdd:cd18533   152 GVGRTGTFIALDSLLDELKrgLSDSQDledsedpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
1741-1992 3.42e-66

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: 226.54  E-value: 3.42e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1741 SSNHPDNKHKNRYVNIVAYDHSRVKLTQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVI 1820
Cdd:cd14627    47 SANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEG--SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIV 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1821 VMITNLVEKGRRKCDQYWPTDGSEEYGSFLVNQksvqvLAYYTVRNFTLRNTKLKKgSQKGRSsgRLVTQYHYTQWPDMG 1900
Cdd:cd14627   125 VMLTKLREMGREKCHQYWPAERSARYQYFVVDP-----MAEYNMPQYILREFKVTD-ARDGQS--RTVRQFQFTDWPEQG 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1901 VPEYSLPVLAFVRKAAQAKRH--AVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQ 1978
Cdd:cd14627   197 VPKSGEGFIDFIGQVHKTKEQfgQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDE 276
                         250
                  ....*....|....
gi 124486807 1979 YVFIHDTLVEAILS 1992
Cdd:cd14627   277 YQFCYQAALEYLGS 290
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
1779-1983 7.08e-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: 222.01  E-value: 7.08e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1779 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPT--DGSEEYGSFLVNQKSV 1856
Cdd:cd14557     1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSmeEGSRAFGDVVVKINEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1857 QVLAYYTVRNFTLRNTKLKkgsqkgrSSGRLVTQYHYTQWPDMGVPEYSLPVLAFVRKAAQAKRHAVGPVVVHCSAGVGR 1936
Cdd:cd14557    81 KICPDYIIRKLNINNKKEK-------GSGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGR 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 124486807 1937 TGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIH 1983
Cdd:cd14557   154 TGTYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIH 200
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
1741-1992 2.53e-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: 224.22  E-value: 2.53e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1741 SSNHPDNKHKNRYVNIVAYDHSRVKLTQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVI 1820
Cdd:cd14629    47 SANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEG--SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIV 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1821 VMITNLVEKGRRKCDQYWPTDGSEEYGSFLVNQksvqvLAYYTVRNFTLRNTKLKKgSQKGRSsgRLVTQYHYTQWPDMG 1900
Cdd:cd14629   125 VMLTKLREMGREKCHQYWPAERSARYQYFVVDP-----MAEYNMPQYILREFKVTD-ARDGQS--RTIRQFQFTDWPEQG 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1901 VPEYSLPVLAFVRKAAQAKRH--AVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQ 1978
Cdd:cd14629   197 VPKTGEGFIDFIGQVHKTKEQfgQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQ 276
                         250
                  ....*....|....
gi 124486807 1979 YVFIHDTLVEAILS 1992
Cdd:cd14629   277 YQLCYRAALEYLGS 290
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
1722-1988 5.59e-64

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: 219.31  E-value: 5.59e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1722 KEFyQEVQSCTA----DLGITADSSNHPDNKHKNRYVNIVAYDHSRVKLTQLAEKDGklTDYINANYVDGYNRPKAYIAA 1797
Cdd:cd14603     2 GEF-SEIRACSAafkaDYVCSTVAGGRKENVKKNRYKDILPYDQTRVILSLLQEEGH--SDYINANFIKGVDGSRAYIAT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1798 QGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWP-TDGSEEYGSFLVNQ-KSVQVLAYYTVRNFTLrntKLK 1875
Cdd:cd14603    79 QGPLSHTVLDFWRMIWQYGVKVILMACREIEMGKKKCERYWAqEQEPLQTGPFTITLvKEKRLNEEVILRTLKV---TFQ 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1876 KGSqkgrssgRLVTQYHYTQWPDMGVPEYSLPVLAFVRKAAQAKRHAVGPVVVHCSAGVGRTGTYIVLDS-----MLQQI 1950
Cdd:cd14603   156 KES-------RSVSHFQYMAWPDHGIPDSPDCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYvrqllLTQRI 228
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 124486807 1951 QHEgtVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVE 1988
Cdd:cd14603   229 PPD--FSIFDVVLEMRKQRPAAVQTEEQYEFLYHTVAQ 264
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
1740-1992 4.72e-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: 4.72e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1740 DSSNHPDNKHKNRYVNIVAYDHSRVKLtQLAEKDGKLTDYINANYVDGY-----NRPKAYIAAQGPLKSTAEDFWRMIWE 1814
Cdd:cd14606    11 LEGQRPENKSKNRYKNILPFDHSRVIL-QGRDSNIPGSDYINANYVKNQllgpdENAKTYIASQGCLEATVNDFWQMAWQ 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1815 HNVEVIVMITNLVEKGRRKCDQYWPTDGSE-EYGSFLVNQKSVQVLAYYTVRnfTLRNTKLKKGSQKgrssgRLVTQYHY 1893
Cdd:cd14606    90 ENSRVIVMTTREVEKGRNKCVPYWPEVGMQrAYGPYSVTNCGEHDTTEYKLR--TLQVSPLDNGELI-----REIWHYQY 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1894 TQWPDMGVPEYSLPVLAFVRKAAQAK---RHAvGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGT---VNIFGFLKHIRS 1967
Cdd:cd14606   163 LSWPDHGVPSEPGGVLSFLDQINQRQeslPHA-GPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVRA 241
                         250       260
                  ....*....|....*....|....*
gi 124486807 1968 QRNYLVQTEEQYVFIHDTLVEAILS 1992
Cdd:cd14606   242 QRSGMVQTEAQYKFIYVAIAQFIET 266
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
1779-1987 2.57e-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: 209.05  E-value: 2.57e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1779 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPTDGSEEYGSFLVNQKSVQV 1858
Cdd:cd14552     1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGSVSSGDITVELKDQTD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1859 LAYYTVRNFTLRNTKlkkgsqkgRSSGRLVTQYHYTQWPDMGVPEYS---LPVLAFVRKaaQAKRHAVGPVVVHCSAGVG 1935
Cdd:cd14552    81 YEDYTLRDFLVTKGK--------GGSTRTVRQFHFHGWPEVGIPDNGkgmIDLIAAVQK--QQQQSGNHPITVHCSAGAG 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 124486807 1936 RTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLV 1987
Cdd:cd14552   151 RTGTFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVVQ 202
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
1779-1990 4.25e-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: 208.77  E-value: 4.25e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1779 YINANYV--DGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPtDGSEE----YGSFLVN 1852
Cdd:cd14538     1 YINASHIriPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWP-DSLNKplicGGRLEVS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1853 QKSVQVLAYYTVRNFTLRNTklkkgsQKGRSsgRLVTQYHYTQWPDMGVPEYSLPVLAFVRKAAqaKRHAVGPVVVHCSA 1932
Cdd:cd14538    80 LEKYQSLQDFVIRRISLRDK------ETGEV--HHITHLNFTTWPDHGTPQSADPLLRFIRYMR--RIHNSGPIVVHCSA 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 124486807 1933 GVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAI 1990
Cdd:cd14538   150 GIGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEVL 207
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
1716-1990 2.96e-60

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


Pssm-ID: 350457 [Multi-domain]  Cd Length: 281  Bit Score: 209.12  E-value: 2.96e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1716 EEFETLKEFYQEVQSCtadlgitaDSSNHPDNKHKNRYVNIVAYDHSRVKLTqlAEKDGKLTDYINAN-YVDGYNRPKAY 1794
Cdd:cd14609    19 KEWQALCAYQAEPNTC--------STAQGEANVKKNRNPDFVPYDHARIKLK--AESNPSRSDYINASpIIEHDPRMPAY 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1795 IAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPTDGSEEYGSFLVNQKSVQVLAY-YTVRNFTLRNTK 1873
Cdd:cd14609    89 IATQGPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHIYEVNLVSEHIWCEdFLVRSFYLKNVQ 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1874 lkkgSQKGRSsgrlVTQYHYTQWPDMGVPEYSLPVLAFVRKAAQAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQhE 1953
Cdd:cd14609   169 ----TQETRT----LTQFHFLSWPAEGIPSSTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMA-K 239
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 124486807 1954 GT--VNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAI 1990
Cdd:cd14609   240 GVkeIDIAATLEHVRDQRPGMVRTKDQFEFALTAVAEEV 278
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
1751-1983 3.34e-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: 206.68  E-value: 3.34e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1751 NRYVNIVAYDHSRVKLTQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKG 1830
Cdd:cd14616     1 NRFPNIKPYNNNRVKLIADAGVPG--SDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1831 RRKCDQYWPTDGS--EEYGSFLVNQksvqvLAYYTVRNFTLRNTKLKKgsqkgRSSGRLVTQYHYTQWPDMGVPEYSLPV 1908
Cdd:cd14616    79 RIRCHQYWPEDNKpvTVFGDIVITK-----LMEDVQIDWTIRDLKIER-----HGDYMMVRQCNFTSWPEHGVPESSAPL 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124486807 1909 LAFVrKAAQAKR-HAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIH 1983
Cdd:cd14616   149 IHFV-KLVRASRaHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLH 223
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
1737-1986 5.17e-60

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: 207.00  E-value: 5.17e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1737 ITADSSNHPDNKHKNRYVNIVAYDHSRVKLTQLAEKDgKLTDYINANYVDGYN-RPKAYIAAQGPLKSTAEDFWRMIWEH 1815
Cdd:cd14612     5 VSPEELDIPGHASKDRYKTILPNPQSRVCLRRAGSQE-EEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1816 NVEVIVMITNLVEKgRRKCDQYWPTDgSEEYGSFLVNQKSVQVLAYYTVRNFTLrntklkkgsqKGRSSGRLVTQYHYTQ 1895
Cdd:cd14612    84 ECPIIVMITKLKEK-KEKCVHYWPEK-EGTYGRFEIRVQDMKECDGYTIRDLTI----------QLEEESRSVKHYWFSS 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1896 WPDMGVPEYSLPVLAFVRKAAQAKRHAV--GPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLV 1973
Cdd:cd14612   152 WPDHQTPESAGPLLRLVAEVEESRQTAAspGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMI 231
                         250
                  ....*....|...
gi 124486807 1974 QTEEQYVFIHDTL 1986
Cdd:cd14612   232 QTSEQYQFLHHTL 244
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
1779-1983 6.53e-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: 204.96  E-value: 6.53e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1779 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPTDGSEE--YGSFLVNQKSV 1856
Cdd:cd14542     1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQlqFGPFKISLEKE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1857 QVLAyytvRNFTLRNTKLKKGSQKgrssgRLVTQYHYTQWPDMGVPEYSLPVLAFVRKAAQAKRHAVGPVVVHCSAGVGR 1936
Cdd:cd14542    81 KRVG----PDFLIRTLKVTFQKES-----RTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDVPICVHCSAGCGR 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 124486807 1937 TGTYIVLDSMLQQIQHEG---TVNIFGFLKHIRSQRNYLVQTEEQYVFIH 1983
Cdd:cd14542   152 TGTICAIDYVWNLLKTGKipeEFSLFDLVREMRKQRPAMVQTKEQYELVY 201
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
1748-1981 7.17e-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: 7.17e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1748 KHKNRYVNIVAYDHSRVKLTQlaekdgKLTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLV 1827
Cdd:cd14545     1 LNRYRDRDPYDHDRSRVKLKQ------GDNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLM 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1828 EKGRRKCDQYWPTDGSE----EYGSFLVNQKSVQVLAYYTVRNFTLRNtklKKGSQKgrssgRLVTQYHYTQWPDMGVPE 1903
Cdd:cd14545    75 EKGQIKCAQYWPQGEGNamifEDTGLKVTLLSEEDKSYYTVRTLELEN---LKTQET-----REVLHFHYTTWPDFGVPE 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1904 ---YSLPVLAFVRKAAQAKRHaVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGT--VNIFGFLKHIRSQRNYLVQTEEQ 1978
Cdd:cd14545   147 spaAFLNFLQKVRESGSLSSD-VGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYRMGLIQTPDQ 225

                  ...
gi 124486807 1979 YVF 1981
Cdd:cd14545   226 LRF 228
alpha_CA_VI_IX_XII_XIV cd03123
Carbonic anhydrase alpha, isozymes VI, IX, XII and XIV. Carbonic anhydrases (CAs) are ...
46-300 7.77e-60

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: 206.77  E-value: 7.77e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807   46 QKNWGKKYPICNSPKQSPINIDEDLTQVNVNLKKLKFQGWEKASLENTFIHNTGKTVEINLTNDYYLSGGLSEKvFKASK 125
Cdd:cd03123     2 EDHWPKKYPACGGKRQSPIDIQTDIVQFDPSLPPLELVGYDLPGTEEFTLTNNGHTVQLSLPPTMHIRGGPGTE-YTAAQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807  126 ITFHWGKCNvSSEGSEHSLEGQKFPLEMQVYCFDADRFSSFEEAVKGKGRLRALSILFEVGVEENLDYKAIIDGTESVSR 205
Cdd:cd03123    81 LHLHWGGRG-SLSGSEHTIDGIRFAAELHIVHYNSDKYSSFDEAADKPDGLAVLAILIEVGYPENTYYEKIISHLHEIKY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807  206 FGKQAALDPFVLQNLLPNSTDKYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLavfcevLTMQQSgyvmLMDY----L 281
Cdd:cd03123   160 KGQETTVPGFNVRELLPEDLSHYYRYEGSLTTPPCYESVLWTVFRDPVTLSKEQL------ETLENT----LMDThnktL 229
                         250
                  ....*....|....*....
gi 124486807  282 QNNFREQQYKFSRQVFSSY 300
Cdd:cd03123   230 QNNYRATQPLNGRVVEASF 248
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
1752-1988 2.65e-59

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: 204.51  E-value: 2.65e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1752 RYVNIVAYDHSRVKLTqlAEKDGKLTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGR 1831
Cdd:cd14623     1 RVLQIIPYEFNRVIIP--VKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1832 RKCDQYWPTDGSEEYGSFLVNQKSVQVLAYYTVRNFTLRNTKLKKgsqkgrssGRLVTQYHYTQWPDMGVPEYS---LPV 1908
Cdd:cd14623    79 EKCAQYWPSDGSVSYGDITIELKKEEECESYTVRDLLVTNTRENK--------SRQIRQFHFHGWPEVGIPSDGkgmINI 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1909 LAFVRKaaQAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVE 1988
Cdd:cd14623   151 IAAVQK--QQQQSGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
1746-1983 3.36e-59

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


Pssm-ID: 350452 [Multi-domain]  Cd Length: 297  Bit Score: 206.71  E-value: 3.36e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1746 DNKHKNRYVNIVAYDHSRVKLT-QLAEKDgklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMIT 1824
Cdd:cd14604    56 ENVKKNRYKDILPFDHSRVKLTlKTSSQD---SDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMAC 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1825 NLVEKGRRKCDQYWPTDGSE--EYGSFLVNQKSVQVLAYYTVRNFTLrntklkkgsqKGRSSGRLVTQYHYTQWPDMGVP 1902
Cdd:cd14604   133 REFEMGRKKCERYWPLYGEEpmTFGPFRISCEAEQARTDYFIRTLLL----------EFQNETRRLYQFHYVNWPDHDVP 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1903 EYSLPVLAFVRKAAQAKRHAVGPVVVHCSAGVGRTGTYIVLD---SMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQY 1979
Cdd:cd14604   203 SSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQY 282

                  ....
gi 124486807 1980 VFIH 1983
Cdd:cd14604   283 ELVH 286
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
1708-1990 4.69e-59

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: 205.68  E-value: 4.69e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1708 LHASNGFTEEFETLKEFYQEVQSCTADLgitadssnHPDNKHKNRYVNIVAYDHSRVKLTqlAEKDGKLTDYINANYV-D 1786
Cdd:cd14610    13 LKNKNRLEKEWEALCAYQAEPNATNVAQ--------REENVQKNRSLAVLPYDHSRIILK--AENSHSHSDYINASPImD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1787 GYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPTDGSEEYGSFLVNQKSVQVLAY-YTVR 1865
Cdd:cd14610    83 HDPRNPAYIATQGPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEGSNLYHIYEVNLVSEHIWCEdFLVR 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1866 NFTLRNTKLKKgsqkgrssGRLVTQYHYTQWPDMGVPEYSLPVLAFVRKAAQAKRHAVGPVVVHCSAGVGRTGTYIVLDS 1945
Cdd:cd14610   163 SFYLKNLQTNE--------TRTVTQFHFLSWNDQGVPASTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILIDM 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 124486807 1946 MLQQI-QHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAI 1990
Cdd:cd14610   235 VLNKMaKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAEEV 280
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
1746-1983 6.39e-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: 204.10  E-value: 6.39e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1746 DNKHKNRYVNIVAYDHSRVKLTQlAEKDGKLTDYINANYVDGYN-------RPK-AYIAAQGPLKSTAEDFWRMIWEHNV 1817
Cdd:cd14605     1 ENKNKNRYKNILPFDHTRVVLHD-GDPNEPVSDYINANIIMPEFetkcnnsKPKkSYIATQGCLQNTVNDFWRMVFQENS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1818 EVIVMITNLVEKGRRKCDQYWPTDGS-EEYGSFLVnqKSVQVLAYYtvrNFTLRNTKLKKGSQKgrSSGRLVTQYHYTQW 1896
Cdd:cd14605    80 RVIVMTTKEVERGKSKCVKYWPDEYAlKEYGVMRV--RNVKESAAH---DYILRELKLSKVGQG--NTERTVWQYHFRTW 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1897 PDMGVPEYSLPVLAFVRKA--AQAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGT---VNIFGFLKHIRSQRNY 1971
Cdd:cd14605   153 PDHGVPSDPGGVLDFLEEVhhKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRSG 232
                         250
                  ....*....|..
gi 124486807 1972 LVQTEEQYVFIH 1983
Cdd:cd14605   233 MVQTEAQYRFIY 244
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
2074-2274 2.39e-58

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: 200.59  E-value: 2.39e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2074 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPD----GQNMAEDefvYWPNK-DEPINCESFKVTL 2148
Cdd:cd00047     1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNlvekGREKCER---YWPEEgGKPLEYGDITVTL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2149 MSEEHKclsneEKLIVQDFILEATQDDYVLEVRHFQCPKWPN---PDSPISkTFELISIIKEEAANRDGPMIVHDEHGGV 2225
Cdd:cd00047    78 VSEEEL-----SDYTIRTLELSPKGCSESREVTHLHYTGWPDhgvPSSPED-LLALVRRVRKEARKPNGPIVVHCSAGVG 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 124486807 2226 TAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYK 2274
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 ...
1779-1990 6.62e-58

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: 199.59  E-value: 6.62e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1779 YINANYVDGYN-RPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPTDGSEEYGSFLVNQKSVQ 1857
Cdd:cd14546     1 YINASTIYDHDpRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEVYHIYEVHLVSEH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1858 VL-AYYTVRNFTLRNTKlkkgsqkgRSSGRLVTQYHYTQWPDMGVPEYSLPVLAFVRKAAQAKRHAVGPVVVHCSAGVGR 1936
Cdd:cd14546    81 IWcDDYLVRSFYLKNLQ--------TSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYRGRSCPIVVHCSDGAGR 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 124486807 1937 TGTYIVLDSMLQQIQhEGT--VNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAI 1990
Cdd:cd14546   153 TGTYILIDMVLNRMA-KGAkeIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAEEV 207
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
1750-1988 2.22e-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: 198.91  E-value: 2.22e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1750 KNRYVNIVAYDHSRVKLTQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEK 1829
Cdd:cd14602     1 KNRYKDILPYDHSRVELSLITSDED--SDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1830 GRRKCDQYWPTDGSE--EYGSFLVNQKSVQVLAYYTVRnfTLRNTKLkkgsqkgrSSGRLVTQYHYTQWPDMGVPEYSLP 1907
Cdd:cd14602    79 GKKKCERYWAEPGEMqlEFGPFSVTCEAEKRKSDYIIR--TLKVKFN--------SETRTIYQFHYKNWPDHDVPSSIDP 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1908 VLAFVRKAAQAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQhEGTV----NIFGFLKHIRSQRNYLVQTEEQYVFIH 1983
Cdd:cd14602   149 ILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLK-DGIIpenfSVFSLIQEMRTQRPSLVQTKEQYELVY 227

                  ....*
gi 124486807 1984 DTLVE 1988
Cdd:cd14602   228 NAVIE 232
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
1778-1992 2.68e-57

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: 197.94  E-value: 2.68e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1778 DYINANYVDgYNRPKA-----YIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWP-TDGSEEYGSFLV 1851
Cdd:cd14541     1 DYINANYVN-MEIPGSgivnrYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPdLGETMQFGNLQI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1852 NQKSVQVLAYYTVRNFTLRNTKLKKgsqkgrssGRLVTQYHYTQWPDMGVPEYSLPVLAFVRKAAQAKRHAVGPVVVHCS 1931
Cdd:cd14541    80 TCVSEEVTPSFAFREFILTNTNTGE--------ERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVEPTVVHCS 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124486807 1932 AGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIhdtlVEAILS 1992
Cdd:cd14541   152 AGIGRTGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFV----CEAILR 208
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
1779-1988 5.23e-57

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: 197.29  E-value: 5.23e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1779 YINANYVDGY--NRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPTDGSEE----YGSFLVN 1852
Cdd:cd14540     1 YINASHITATvgGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGGEHdaltFGEYKVS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1853 QKSVQVLAYYTVRNFTLRNTklkkgsqkgrSSGRLVTQYH--YTQWPDMGVPEYSLPVLAFVRKAAQAKRHAVG------ 1924
Cdd:cd14540    81 TKFSVSSGCYTTTGLRVKHT----------LSGQSRTVWHlqYTDWPDHGCPEDVSGFLDFLEEINSVRRHTNQdvaghn 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124486807 1925 ---PVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVE 1988
Cdd:cd14540   151 rnpPTLVHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQ 217
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
1750-1983 2.95e-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: 195.52  E-value: 2.95e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1750 KNRYVNIVAYDHSRVKLTQLAEKDgKLTDYINANYVDGY-NRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVE 1828
Cdd:cd14611     2 KNRYKTILPNPHSRVCLKPKNSND-SLSTYINANYIRGYgGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1829 KGRrKCDQYWPtDGSEEYGSFLVNQKSVQVLAYYTVRNFTLrntklKKGSQKgrssgRLVTQYHYTQWPDMGVPEYSLPV 1908
Cdd:cd14611    81 KNE-KCVLYWP-EKRGIYGKVEVLVNSVKECDNYTIRNLTL-----KQGSQS-----RSVKHYWYTSWPDHKTPDSAQPL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1909 LAFV------RKAAQAKrhavGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFI 1982
Cdd:cd14611   149 LQLMldveedRLASPGR----GPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFV 224

                  .
gi 124486807 1983 H 1983
Cdd:cd14611   225 H 225
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
1778-1983 6.90e-56

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: 193.68  E-value: 6.90e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1778 DYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPTDGSEEYGSFLVNQKSVQ 1857
Cdd:cd14622     1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEGSVTHGEITIEIKNDT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1858 VLAYYTVRNFTLRNTKLKKgsqkgrssGRLVTQYHYTQWPDMGVPEYS---LPVLAFVRKaaQAKRHAVGPVVVHCSAGV 1934
Cdd:cd14622    81 LLETISIRDFLVTYNQEKQ--------TRLVRQFHFHGWPEIGIPAEGkgmIDLIAAVQK--QQQQTGNHPIVVHCSAGA 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 124486807 1935 GRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIH 1983
Cdd:cd14622   151 GRTGTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCY 199
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
1745-1991 7.03e-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: 196.22  E-value: 7.03e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1745 PDNKHKNRYVNIVAYDHSRVKLTqlaEKDgkltDYINANYVD----GYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVI 1820
Cdd:cd14600    38 PQNMDKNRYKDVLPYDATRVVLQ---GNE----DYINASYVNmeipSANIVNKYIATQGPLPHTCAQFWQVVWEQKLSLI 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1821 VMITNLVEKGRRKCDQYWPtDGSE--EYGSFLVNQKSVQVLAYYTVRNFTLrnTKLKKGSQkgrssgRLVTQYHYTQWPD 1898
Cdd:cd14600   111 VMLTTLTERGRTKCHQYWP-DPPDvmEYGGFRVQCHSEDCTIAYVFREMLL--TNTQTGEE------RTVTHLQYVAWPD 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1899 MGVPEYSLPVLAFVRKAAQaKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQ 1978
Cdd:cd14600   182 HGVPDDSSDFLEFVNYVRS-KRVENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQ 260
                         250
                  ....*....|...
gi 124486807 1979 YVFIhdtlVEAIL 1991
Cdd:cd14600   261 YKFV----CEAIL 269
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
1750-1986 7.32e-56

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


Pssm-ID: 350461 [Multi-domain]  Cd Length: 258  Bit Score: 195.85  E-value: 7.32e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1750 KNRYVNIVAYDHSRVKLTQlAEKDGKLTDYINANYVDGYN-RPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVE 1828
Cdd:cd14613    28 KNRYKTILPNPHSRVCLTS-PDQDDPLSSYINANYIRGYGgEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEE 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1829 KGRrKCDQYWPTDgSEEYGSFLVNQKSVQVLAYYTVRNFTLrntklKKGSQKgrssgRLVTQYHYTQWPDMGVPEYSLPV 1908
Cdd:cd14613   107 MNE-KCTEYWPEE-QVTYEGIEITVKQVIHADDYRLRLITL-----KSGGEE-----RGLKHYWYTSWPDQKTPDNAPPL 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1909 LAFVRKAAQAKRHA---VGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDT 1985
Cdd:cd14613   175 LQLVQEVEEARQQAepnCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVHHV 254

                  .
gi 124486807 1986 L 1986
Cdd:cd14613   255 L 255
alpha_CA_XII_XIV cd03126
Carbonic anhydrase alpha, isozymes XII and XIV. Carbonic anhydrases (CAs) are zinc-containing ...
46-300 5.50e-53

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: 186.97  E-value: 5.50e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807   46 QKNWGKKYPICNSPKQSPINIDEDLTQVNVNLKKLKFQGWEKASLENTFIHNTGKTVEINLTNDYYLsGGLSEKvFKASK 125
Cdd:cd03126     2 ENSWPKKYPFCGGVAQSPIDIHTDILQYDSSLPPLEFHGYNVSGTEQFTLTNNGHTVQLSLPPTMHI-GGLPFK-YTASQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807  126 ITFHWGKCNvSSEGSEHSLEGQKFPLEMQVYCFDADRFSSFEEAVKGKGRLRALSILFEVGvEENLDYKAIIDGTESVSR 205
Cdd:cd03126    80 LHLHWGQRG-SPEGSEHTISGKHFAAELHIVHYNSDKYPDISTAMNKSQGLAVLGILIEVG-PFNPSYEKIFSHLHEVKY 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807  206 FGKQAALDPFVLQNLLPNSTDKYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLavfcevLTMQQSGYVMLMD---YLQ 282
Cdd:cd03126   158 KDQKVSVPGFNVQELLPKRLDEYYRYEGSLTTPPCYPSVLWTVFRNPVQISQEQL------LALETALYSTEEDesrEMV 231
                         250
                  ....*....|....*...
gi 124486807  283 NNFREQQYKFSRQVFSSY 300
Cdd:cd03126   232 NNYRQVQPFNERLVFASF 249
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
1725-1981 1.05e-52

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: 186.71  E-value: 1.05e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1725 YQEVQSCTADLGITAdsSNHPDNKHKNRYVNIVAYDHSRVKLtQLAEkdgklTDYINANYVDGYNRPKAYIAAQGPLKST 1804
Cdd:cd14607     4 YLEIRNESHDYPHRV--AKYPENRNRNRYRDVSPYDHSRVKL-QNTE-----NDYINASLVVIEEAQRSYILTQGPLPNT 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1805 AEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPTDGSEEYG----SFLVNQKSVQVLAYYTVRNFTLRNTKlkkgsqK 1880
Cdd:cd14607    76 CCHFWLMVWQQKTKAVVMLNRIVEKDSVKCAQYWPTDEEEVLSfketGFSVKLLSEDVKSYYTVHLLQLENIN------S 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1881 GRSsgRLVTQYHYTQWPDMGVPEYSLPVLAFVRKAAQAKRHAV--GPVVVHCSAGVGRTGTYIVLDS--MLQQIQHEGTV 1956
Cdd:cd14607   150 GET--RTISHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSPehGPAVVHCSAGIGRSGTFSLVDTclVLMEKKDPDSV 227
                         250       260
                  ....*....|....*....|....*
gi 124486807 1957 NIFGFLKHIRSQRNYLVQTEEQYVF 1981
Cdd:cd14607   228 DIKQVLLDMRKYRMGLIQTPDQLRF 252
PHA02738 PHA02738
hypothetical protein; Provisional
1747-1981 1.15e-52

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 188.60  E-value: 1.15e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1747 NKHKNRYVNIVAYDHSRVKLTqlAEKDgkLTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNL 1826
Cdd:PHA02738   49 NRKLNRYLDAVCFDHSRVILP--AERN--RGDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKK 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1827 VEKGRRKCDQYWPT--DGSEEYGSFLVNQKSVQVLAYYTVRNFTLRNtklkkgsqkGRSSGRLVTQYHYTQWPDMGVPEY 1904
Cdd:PHA02738  125 KENGREKCFPYWSDveQGSIRFGKFKITTTQVETHPHYVKSTLLLTD---------GTSATQTVTHFNFTAWPDHDVPKN 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1905 SLPVLAFVRKAAQA-------------KRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNY 1971
Cdd:PHA02738  196 TSEFLNFVLEVRQCqkelaqeslqighNRLQPPPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYY 275
                         250
                  ....*....|
gi 124486807 1972 LVQTEEQYVF 1981
Cdd:PHA02738  276 SLFIPFQYFF 285
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
1746-1981 1.22e-52

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


Pssm-ID: 350445 [Multi-domain]  Cd Length: 234  Bit Score: 185.42  E-value: 1.22e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1746 DNKHKNRYVNIVAYDHSRVKLtqlaekdGKLTDYINANYVD---GyNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVM 1822
Cdd:cd14597     2 ENRKKNRYKNILPYDTTRVPL-------GDEGGYINASFIKmpvG-DEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAM 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1823 ITNLVEKGRRKCDQYWPtdgsEEYGSFLV--NQKSVQVLAYYTVRNFTLRNTKLKKgSQKGRSsgRLVTQYHYTQWPDMG 1900
Cdd:cd14597    74 MTQEVEGGKIKCQRYWP----EILGKTTMvdNRLQLTLVRMQQLKNFVIRVLELED-IQTREV--RHITHLNFTAWPDHD 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1901 V---PEYSLPVLAFVRKAaqakrHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEE 1977
Cdd:cd14597   147 TpsqPEQLLTFISYMRHI-----HKSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTED 221

                  ....
gi 124486807 1978 QYVF 1981
Cdd:cd14597   222 QYIF 225
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
1725-1988 1.52e-51

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: 184.07  E-value: 1.52e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1725 YQEVQSCTADLgiTADSSNHPDNKHKNRYVNIVAYDHSRVKLTQlaekdgKLTDYINANYVDGYNRPKAYIAAQGPLKST 1804
Cdd:cd14608     5 YQDIRHEASDF--PCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQ------EDNDYINASLIKMEEAQRSYILTQGPLPNT 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1805 AEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPTDGSEEY----GSFLVNQKSVQVLAYYTVRNFTLRNTKlkkgSQK 1880
Cdd:cd14608    77 CGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMifedTNLKLTLISEDIKSYYTVRQLELENLT----TQE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1881 GRSsgrlVTQYHYTQWPDMGVPEYSLPVLAFVRKAAQAK--RHAVGPVVVHCSAGVGRTGTYIVLDS---MLQQIQHEGT 1955
Cdd:cd14608   153 TRE----ILHFHYTTWPDFGVPESPASFLNFLFKVRESGslSPEHGPVVVHCSAGIGRSGTFCLADTcllLMDKRKDPSS 228
                         250       260       270
                  ....*....|....*....|....*....|...
gi 124486807 1956 VNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVE 1988
Cdd:cd14608   229 VDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIE 261
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
1779-1984 2.68e-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: 2.68e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1779 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPtDGSEEYGSFLVNQKSVQV 1858
Cdd:cd14558     1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWG-DEKKTYGDIEVELKDTEK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1859 LAYYTVRNFTLRNTKLKKGSQkgrssgrlVTQYHYTQWPDMGVPEYSLPVLAFVRKAAQ------AKRHAVGPVVVHCSA 1932
Cdd:cd14558    80 SPTYTVRVFEITHLKRKDSRT--------VYQYQYHKWKGEELPEKPKDLVDMIKSIKQklpyknSKHGRSVPIVVHCSD 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 124486807 1933 GVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHD 1984
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 5.27e-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: 177.85  E-value: 5.27e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807   59 PKQSPINIDEDLTQVNVNLKKLKFQGWEKASLeNTFIHNTGKTVEINLTNDYYLSGG-LSEKvFKASKITFHWGkcNVSS 137
Cdd:cd03117     2 KRQSPINIVTKKVQYDENLTPFTFTGYDDTTT-NWTITNNGHTVQVTLPDGAKISGGgLPGT-YKALQFHFHWG--SNGS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807  138 EGSEHSLEGQKFPLEMQVYCFDADrFSSFEEAVKGKGRLRALSILFEVGVEENLDYKAIIDGTESVSRFGKQAALDPFVL 217
Cdd:cd03117    78 PGSEHTIDGERYPMELHIVHIKES-YNSLLEALKDSDGLAVLGFFIEEGEEENTNFDPLISALSNIPQKGGSTNLTPFSL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807  218 QNLLP-NSTDKYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLAVFCEVLTMQQSGYVMLMdylqNNFREQQYKFSRQV 296
Cdd:cd03117   157 RSLLPsVLLTKYYRYNGSLTTPGCNEAVIWTVFEEPIPISRAQLDAFSTVLFFDTDNGQPMV----NNFRPVQPLNGRVV 232

                  ..
gi 124486807  297 FS 298
Cdd:cd03117   233 YA 234
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
1779-1990 1.38e-49

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: 175.71  E-value: 1.38e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1779 YINANYVDGYNRPKA--YIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWP-----TDGSEEYGSFLV 1851
Cdd:cd14596     1 YINASYITMPVGEEElfYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPetlqePMELENYQLRLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1852 NqksVQVLAYYTVRNFTLrntklkkgSQKGRSSGRLVTQYHYTQWPDMGVPEYSLPVLAFVRKAaqAKRHAVGPVVVHCS 1931
Cdd:cd14596    81 N---YQALQYFIIRIIKL--------VEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYM--RKVHNTGPIVVHCS 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 124486807 1932 AGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAI 1990
Cdd:cd14596   148 AGIGRAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVL 206
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
1745-1988 1.84e-48

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


Pssm-ID: 350447 [Multi-domain]  Cd Length: 287  Bit Score: 175.57  E-value: 1.84e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1745 PDNKHKNRYVNIVAYDHSRVKLTQLAEKDgklTDYINANYVDGYNRPKA--YIAAQGPLKSTAEDFWRMIWEHNVEVIVM 1822
Cdd:cd14599    36 PENAERNRIREVVPYEENRVELVPTKENN---TGYINASHIKVTVGGEEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAM 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1823 ITNLVEKGRRKCDQYWPTDG----SEEYGSFLVNQKSVQVLAYYTVRNFTLRNtkLKKGSQkgrssgRLVTQYHYTQWPD 1898
Cdd:cd14599   113 VTAEEEGGRSKSHRYWPKLGskhsSATYGKFKVTTKFRTDSGCYATTGLKVKH--LLSGQE------RTVWHLQYTDWPD 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1899 MGVPEYSLPVLAFVRKAAQAKRHAVG----------PVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQ 1968
Cdd:cd14599   185 HGCPEEVQGFLSYLEEIQSVRRHTNSmldstkncnpPIVVHCSAGVGRTGVVILTELMIGCLEHNEKVEVPVMLRHLREQ 264
                         250       260
                  ....*....|....*....|
gi 124486807 1969 RNYLVQTEEQYVFIHDTLVE 1988
Cdd:cd14599   265 RMFMIQTIAQYKFVYQVLIQ 284
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
1778-1991 2.02e-48

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


Pssm-ID: 350449 [Multi-domain]  Cd Length: 212  Bit Score: 172.44  E-value: 2.02e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1778 DYINANYVDG-------YNRpkaYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWP-TDGSEEYGSF 1849
Cdd:cd14601     1 DYINANYINMeipsssiINR---YIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPePSGSSSYGGF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1850 LVNQKSVQVLAYYTVRNFTLRNTklkkgsQKGRSsgRLVTQYHYTQWPDMGVPEYSLPVLAFVRKAAQAKRHAVGPVVVH 1929
Cdd:cd14601    78 QVTCHSEEGNPAYVFREMTLTNL------EKNES--RPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDEPVVVH 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124486807 1930 CSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIhdtlVEAIL 1991
Cdd:cd14601   150 CSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFV----CEAIL 207
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
1779-1984 2.65e-47

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: 169.10  E-value: 2.65e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1779 YINANYVDGY-NRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPTD-GSE-EYGSFLVNQKS 1855
Cdd:cd14539     1 YINASLIEDLtPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTErGQAlVYGAITVSLQS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1856 VQVLAYYTVRNFTL--RNTKLKkgsqkgrssgRLVTQYHYTQWPDMGVPEYSLPVLAF---VRKAAQAKRHAVGPVVVHC 1930
Cdd:cd14539    81 VRTTPTHVERIISIqhKDTRLS----------RSVVHLQFTTWPELGLPDSPNPLLRFieeVHSHYLQQRSLQTPIVVHC 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 124486807 1931 SAGVGRTGTYIVLDSMLQQIQHE-GTVNIFGFLKHIRSQRNYLVQTEEQYVFIHD 1984
Cdd:cd14539   151 SSGVGRTGAFCLLYAAVQEIEAGnGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
1995-2282 1.19e-46

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: 170.30  E-value: 1.19e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1995 TEVPDSHIHSYVNTLL-IPGPTGKTKLEKQFQLLSQSNILQSDYSTALKQCNREKNRTSSIIPVERSRVGISSLSG-EGT 2072
Cdd:cd14628     1 TEVPARNLYAYIQKLTqIETGENVTGMELEFKRLASSKAHTSRFISANLPCNKFKNRLVNIMPYESTRVCLQPIRGvEGS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2073 DYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAEDE-FVYWPnKDEPINCESFKVTLMSE 2151
Cdd:cd14628    81 DYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKcHQYWP-AERSARYQYFVVDPMAE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2152 ehkclSNEEKLIVQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKT--FELISII--KEEAANRDGPMIVHDEHGGVTA 2227
Cdd:cd14628   160 -----YNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEgfIDFIGQVhkTKEQFGQDGPISVHCSAGVGRT 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 124486807 2228 GTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVVLSLVST 2282
Cdd:cd14628   235 GVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEYLGS 289
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
1723-1983 2.80e-46

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 170.18  E-value: 2.80e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1723 EFYQEVqscTADLGITADSSNHPDNKHKNRYVNIVAYDHSRVKLTQlaeKDGKLTDYINANYVDGYNRPKAYIAAQGPLK 1802
Cdd:PHA02747   30 EHHQII---LKPFDGLIANFEKPENQPKNRYWDIPCWDHNRVILDS---GGGSTSDYIHANWIDGFEDDKKFIATQGPFA 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1803 STAEDFWRMIWEHNVEVIVMIT-NLVEKGRRKCDQYW--PTDGSEEYGSFLVNQKSVQVLAYYTVRNFTLRNTKLKkgsq 1879
Cdd:PHA02747  104 ETCADFWKAVWQEHCSIIVMLTpTKGTNGEEKCYQYWclNEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILK---- 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1880 kgrsSGRLVTQYHYTQWPDMGVPEYSLPVLAFVR----------KAAQAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQ 1949
Cdd:PHA02747  180 ----DSRKISHFQCSEWFEDETPSDHPDFIKFIKiidinrkksgKLFNPKDALLCPIVVHCSDGVGKTGIFCAVDICLNQ 255
                         250       260       270
                  ....*....|....*....|....*....|....
gi 124486807 1950 IQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIH 1983
Cdd:PHA02747  256 LVKRKAICLAKTAEKIREQRHAGIMNFDDYLFIQ 289
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
1738-1991 6.33e-46

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 169.44  E-value: 6.33e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1738 TADSSNHPDNKHKNRYVNIVAYDHSRV--------KLTQLAEKDGKL---------TDYINANYVDGYNRPKAYIAAQGP 1800
Cdd:PHA02746   42 TTNHFLKKENLKKNRFHDIPCWDHSRVvinaheslKMFDVGDSDGKKievtsednaENYIHANFVDGFKEANKFICAQGP 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1801 LKSTAEDFWRMIWEHNVEVIVMITNlVEKGRRKCDQYW--PTDGSEEYGSFLVNQKSVQVLAYYTVRNFTLRNtklkkgs 1878
Cdd:PHA02746  122 KEDTSEDFFKLISEHESQVIVSLTD-IDDDDEKCFELWtkEEDSELAFGRFVAKILDIIEELSFTKTRLMITD------- 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1879 qKGRSSGRLVTQYHYTQWPDMGVPEYSLPVL----------AFVRKAAQAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQ 1948
Cdd:PHA02746  194 -KISDTSREIHHFWFPDWPDNGIPTGMAEFLelinkvneeqAELIKQADNDPQTLGPIVVHCSAGIGRAGTFCAIDNALE 272
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 124486807 1949 QIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAIL 1991
Cdd:PHA02746  273 QLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKALKYAII 315
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
2044-2277 1.01e-45

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


Pssm-ID: 350402 [Multi-domain]  Cd Length: 238  Bit Score: 165.78  E-value: 1.01e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2044 CNREKNRTSSIIPVERSRVGISSLSG-EGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQ 2122
Cdd:cd14554     5 CNKFKNRLVNILPYESTRVCLQPIRGvEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTKLR 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2123 NMAEDE-FVYWPNkDEPINCESFKVTLMSEehkclSNEEKLIVQDFILEATQDDYVLEVRHFQCPKWPNPDSPisKTFE- 2200
Cdd:cd14554    85 EMGREKcHQYWPA-ERSARYQYFVVDPMAE-----YNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVP--KSGEg 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2201 LISIIKE-----EAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKV 2275
Cdd:cd14554   157 FIDFIGQvhktkEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRA 236

                  ..
gi 124486807 2276 VL 2277
Cdd:cd14554   237 AL 238
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
1747-1988 1.10e-45

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 167.87  E-value: 1.10e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1747 NKHKNRYVNIVAYDHSRVKLTQlaeKDGkLTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNL 1826
Cdd:PHA02742   52 NMKKCRYPDAPCFDRNRVILKI---EDG-GDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKI 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1827 VEKGRRKCDQYWPTD--GSEEYGSFLVNQKSVQVLAYYTVRNFTLRNTklkkgsQKGRSSGrlVTQYHYTQWPDMGVPEY 1904
Cdd:PHA02742  128 MEDGKEACYPYWMPHerGKATHGEFKIKTKKIKSFRNYAVTNLCLTDT------NTGASLD--IKHFAYEDWPHGGLPRD 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1905 SLPVLAFVRKAAQAK-----------RHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLV 1973
Cdd:PHA02742  200 PNKFLDFVLAVREADlkadvdikgenIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCL 279
                         250
                  ....*....|....*
gi 124486807 1974 QTEEQYVFIHDTLVE 1988
Cdd:PHA02742  280 SLPQQYIFCYFIVLI 294
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
1995-2282 4.52e-45

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: 165.68  E-value: 4.52e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1995 TEVPDSHIHSYVNTLLIPGPTGK-TKLEKQFQLLSQSNILQSDYSTALKQCNREKNRTSSIIPVERSRVGISSLSG-EGT 2072
Cdd:cd14627     2 TEVPARNLYSYIQKLAQVEVGEHvTGMELEFKRLANSKAHTSRFISANLPCNKFKNRLVNIMPYETTRVCLQPIRGvEGS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2073 DYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAEDE-FVYWPnKDEPINCESFKVTLMSE 2151
Cdd:cd14627    82 DYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGREKcHQYWP-AERSARYQYFVVDPMAE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2152 ehkclSNEEKLIVQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKT--FELISII--KEEAANRDGPMIVHDEHGGVTA 2227
Cdd:cd14627   161 -----YNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEgfIDFIGQVhkTKEQFGQDGPISVHCSAGVGRT 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 124486807 2228 GTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVVLSLVST 2282
Cdd:cd14627   236 GVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALEYLGS 290
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
1779-1984 5.96e-45

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


Pssm-ID: 350404 [Multi-domain]  Cd Length: 201  Bit Score: 162.19  E-value: 5.96e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1779 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMItNLVEKGRRKCDQYWPTDGSEEYGSFLVNQKSVQV 1858
Cdd:cd14556     1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVML-NQLDPKDQSCPQYWPDEGSGTYGPIQVEFVSTTI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1859 LAYYTVRNFTLRNTKlkkgsqKGRSSGRLVTQYHYTQWPDMG----VPEYSLPVLAFVRKAAQakRHAVGPVVVHCSAGV 1934
Cdd:cd14556    80 DEDVISRIFRLQNTT------RPQEGYRMVQQFQFLGWPRDRdtppSKRALLKLLSEVEKWQE--QSGEGPIVVHCLNGV 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 124486807 1935 GRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHD 1984
Cdd:cd14556   152 GRSGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
1995-2282 6.35e-45

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: 165.28  E-value: 6.35e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1995 TEVPDSHIHSYVNTL-LIPGPTGKTKLEKQFQLLSQSNILQSDYSTALKQCNREKNRTSSIIPVERSRVGISSLSG-EGT 2072
Cdd:cd14629     2 TEVPARNLYAHIQKLtQVPPGESVTAMELEFKLLANSKAHTSRFISANLPCNKFKNRLVNIMPYELTRVCLQPIRGvEGS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2073 DYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAEDE-FVYWPnKDEPINCESFKVTLMSE 2151
Cdd:cd14629    82 DYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKcHQYWP-AERSARYQYFVVDPMAE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2152 ehkclSNEEKLIVQDFILEATQDDYVLEVRHFQCPKWPNPDSPisKTFE-LISIIKE-----EAANRDGPMIVHDEHGGV 2225
Cdd:cd14629   161 -----YNMPQYILREFKVTDARDGQSRTIRQFQFTDWPEQGVP--KTGEgFIDFIGQvhktkEQFGQDGPITVHCSAGVG 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 124486807 2226 TAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVVLSLVST 2282
Cdd:cd14629   234 RTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALEYLGS 290
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
1779-1983 2.86e-43

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: 157.63  E-value: 2.86e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1779 YINANYV---DGYNRPKaYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRR-KCDQYWPTD--GSEEYGSFLVN 1852
Cdd:cd17658     1 YINASLVetpASESLPK-FIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTaKCADYFPAEenESREFGRISVT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1853 QKSVQvlayYTVRNFTLRNTKLKKgsQKGRSSGRLVTQYHYTQWPDMGVPEYSLPVLAFVRKAAQAKRHAvGPVVVHCSA 1932
Cdd:cd17658    80 NKKLK----HSQHSITLRVLEVQY--IESEEPPLSVLHIQYPEWPDHGVPKDTRSVRELLKRLYGIPPSA-GPIVVHCSA 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 124486807 1933 GVGRTGTYIVLDSMLQQIQhEG---TVNIFGFLKHIRSQRNYLVQTEEQYVFIH 1983
Cdd:cd17658   153 GIGRTGAYCTIHNTIRRIL-EGdmsAVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
1722-1982 3.22e-43

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 160.26  E-value: 3.22e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1722 KEFYQEVQSCTADLGITADSSNHPDN---KHKNRYVNIVAYDHsrvklTQLAEKDGkltdYINANYVDGYNrPKAYIAAQ 1798
Cdd:COG5599    14 EKINSRLSTLTNELAPSHNDPQYLQNingSPLNRFRDIQPYKE-----TALRANLG----YLNANYIQVIG-NHRYIATQ 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1799 GPLKSTAEDFWRMIWEHNVEVIVMITNLVE--KGRRKCDQYWPTDGseEYGSFLVNQKSVQVlaYYTVRNFTLRNTKLK- 1875
Cdd:COG5599    84 YPLEEQLEDFFQMLFDNNTPVLVVLASDDEisKPKVKMPVYFRQDG--EYGKYEVSSELTES--IQLRDGIEARTYVLTi 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1876 KGS-QKGRSsgrlVTQYHYTQWPDMGVP--EYSLPVLAFVRKAAQAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQ- 1951
Cdd:COG5599   160 KGTgQKKIE----IPVLHVKNWPDHGAIsaEALKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINa 235
                         250       260       270
                  ....*....|....*....|....*....|...
gi 124486807 1952 -HEGTVNIFGFLKHIRSQRNY-LVQTEEQYVFI 1982
Cdd:COG5599   236 lVQITLSVEEIVIDMRTSRNGgMVQTSEQLDVL 268
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
2050-2276 4.88e-43

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: 157.51  E-value: 4.88e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2050 RTSSIIPVERSRVGISSLSGE-GTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAEDE 2128
Cdd:cd14623     1 RVLQIIPYEFNRVIIPVKRGEeNTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2129 FV-YWPNkDEPINCESFKVTLMSEEhKClsneEKLIVQDFILEATQDDYVLEVRHFQCPKWPNPDSPiSKTFELISII-- 2205
Cdd:cd14623    81 CAqYWPS-DGSVSYGDITIELKKEE-EC----ESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIP-SDGKGMINIIaa 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124486807 2206 --KEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVV 2276
Cdd:cd14623   154 vqKQQQQSGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVV 226
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
2050-2274 6.27e-43

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: 157.13  E-value: 6.27e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2050 RTSSIIPVERSRVGISSLSG-EGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIpdgQNMAEDE 2128
Cdd:cd14548     1 RYTNILPYDHSRVKLIPINEeEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVML---TQCMEKG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2129 FV----YWPNKDEPINCESFKVTLMSEEHkclsnEEKLIVQDFILEatQDDYVLEVRHFQCPKWPN---PDSPISktfeL 2201
Cdd:cd14548    78 RVkcdhYWPFDQDPVYYGDITVTMLSESV-----LPDWTIREFKLE--RGDEVRSVRQFHFTAWPDhgvPEAPDS----L 146
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124486807 2202 ISIIK---EEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYK 2274
Cdd:cd14548   147 LRFVRlvrDYIKQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLHQ 222
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
2074-2273 8.93e-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: 152.95  E-value: 8.93e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2074 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAEDEFVYWPNKdepincESFKVTLMSEEH 2153
Cdd:cd14556     1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDQSCPQYWPDE------GSGTYGPIQVEF 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2154 KCLSNEEKLIVQDFILEAT---QDDYVLeVRHFQCPKWP-NPDSPISKT--FELISII-KEEAANRDGPMIVHDEHGGVT 2226
Cdd:cd14556    75 VSTTIDEDVISRIFRLQNTtrpQEGYRM-VQQFQFLGWPrDRDTPPSKRalLKLLSEVeKWQEQSGEGPIVVHCLNGVGR 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 124486807 2227 AGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLY 2273
Cdd:cd14556   154 SGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCY 200
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
2074-2276 1.55e-41

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: 152.42  E-value: 1.55e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2074 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAEDE-FVYWPNkDEPINCESFKVTLMSEE 2152
Cdd:cd14552     1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKcAQYWPE-DGSVSSGDITVELKDQT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2153 hkclsNEEKLIVQDFILEATQDDYVLEVRHFQCPKWPNPDSPiSKTFELISII----KEEAANRDGPMIVHDEHGGVTAG 2228
Cdd:cd14552    80 -----DYEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIP-DNGKGMIDLIaavqKQQQQSGNHPITVHCSAGAGRTG 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 124486807 2229 TFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVV 2276
Cdd:cd14552   154 TFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
2074-2273 4.41e-41

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: 151.01  E-value: 4.41e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2074 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPD-GQNMAEDEFVYWPNKDEpiNCESFKVTLMSEE 2152
Cdd:cd14558     1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTElKEGDQEQCAQYWGDEKK--TYGDIEVELKDTE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2153 hkclsNEEKLIVQDFILEATQDDYVLEVRHFQCPKWpNPDSPISKTFELISIIKE---------EAANRDGPMIVHDEHG 2223
Cdd:cd14558    79 -----KSPTYTVRVFEITHLKRKDSRTVYQYQYHKW-KGEELPEKPKDLVDMIKSikqklpyknSKHGRSVPIVVHCSDG 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 124486807 2224 GVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLY 2273
Cdd:cd14558   153 SSRTGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202
alpha_CA_VI cd03125
Carbonic anhydrase alpha, isozyme VI. Carbonic anhydrases (CAs) are zinc-containing enzymes ...
45-300 1.88e-40

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: 151.09  E-value: 1.88e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807   45 NQKNWGKKYPICNSPKQSPINIDEDLTQVNVNLKKLKFQGWEKASLENTFIHNtGKTVEINLTNDYYLSGGLSeKVFKAS 124
Cdd:cd03125     1 DESHWPEKYPACGGKRQSPIDIQRREVRFNPSLLQLELVGYEKEQGEFTMTNN-GHTVQIDLPPTMSITTGDG-TVYTAV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807  125 KITFHWGKCNVSSEGSEHSLEGQKFPLEMQVYCFDADrFSSFEEAVKGKGRLRALSILFEVG-VEENLDYKAIIDGTESV 203
Cdd:cd03125    79 QMHFHWGGRDSEISGSEHTIDGMRYVAELHIVHYNSK-YKSYEEAKDKPDGLAVLAFLYKVGhYAENTYYSDFISKLAKI 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807  204 SRFGKQAALDPFVLQNLLPNSTDKYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQlavfceVLTMQQSgyvmLMDY--- 280
Cdd:cd03125   158 KYAGQTTTLTSLDVRDMLPENLHHYYTYQGSLTTPPCTENVLWFVFDDPVTLSKTQ------IVKLENT----LMDHhnk 227
                         250       260
                  ....*....|....*....|.
gi 124486807  281 -LQNNFREQQYKFSRQVFSSY 300
Cdd:cd03125   228 tIRNDYRRTQPLNHRVVEANF 248
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
1779-1988 9.04e-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: 147.81  E-value: 9.04e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1779 YINANYVDGYNRPKA--YIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPTDGSEE----YGSFLVN 1852
Cdd:cd14598     1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRLGSRHntvtYGRFKIT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1853 QKSVQVLAYYTVRNFTLRNtkLKKGSQkgrssgRLVTQYHYTQWPDMGVPEYSLPVLAFVRKAAQAKRHAVG-------- 1924
Cdd:cd14598    81 TRFRTDSGCYATTGLKIKH--LLTGQE------RTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHTNStidpkspn 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124486807 1925 -PVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVE 1988
Cdd:cd14598   153 pPVLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQ 217
alpha_CA_IX cd03150
Carbonic anhydrase alpha, isozyme IX. Carbonic anhydrases (CAs) are zinc-containing enzymes ...
45-300 5.39e-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: 5.39e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807   45 NQKNWGKKYPICNSPKQSPINIDEDLTQVNVNLKKLKFQGWEKASLENTFIHNTGKTVEINLTNDYYLSGGLsEKVFKAS 124
Cdd:cd03150     1 GQPPWPSVSPACAGRFQSPVDIRPHLVAFCPALRPLELLGFDLPPSPSLRLLNNGHTVQLSLPSGLRMALGP-GQEYRAL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807  125 KITFHWGKCNVSseGSEHSLEGQKFPLEMQVYCFDAdRFSSFEEAVKGKGRLRALSILFEVGVEENLDYKAIIDGTESVS 204
Cdd:cd03150    80 QLHLHWGAAGRP--GSEHTVDGHRFPAEIHVVHLST-AFANLDEALGRPGGLAVLAAFLAEGLHENSAYEQLLSRLSEIS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807  205 RFGKQAALDPFVLQNLLPNSTDKYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLAVFCEVLTMQQSgyvmlmDYLQNN 284
Cdd:cd03150   157 EEESETVVPGLDVSALLPSDLSRYFRYEGSLTTPPCAQGVIWTVFNQTVRLSAKQLHTLSDSLWGPHD------SRLQLN 230
                         250
                  ....*....|....*.
gi 124486807  285 FREQQYKFSRQVFSSY 300
Cdd:cd03150   231 FRATQPLNGRKIEASF 246
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1888-1988 8.28e-39

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 140.57  E-value: 8.28e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807   1888 VTQYHYTQWPDMGVPEYSLPVLAFVR--KAAQAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHE-GTVNIFGFLKH 1964
Cdd:smart00404    2 VKHYHYTGWPDHGVPESPDSILELLRavKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVKE 81
                            90       100
                    ....*....|....*....|....
gi 124486807   1965 IRSQRNYLVQTEEQYVFIHDTLVE 1988
Cdd:smart00404   82 LRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
1888-1988 8.28e-39

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


Pssm-ID: 214469 [Multi-domain]  Cd Length: 105  Bit Score: 140.57  E-value: 8.28e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807   1888 VTQYHYTQWPDMGVPEYSLPVLAFVR--KAAQAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHE-GTVNIFGFLKH 1964
Cdd:smart00012    2 VKHYHYTGWPDHGVPESPDSILELLRavKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVKE 81
                            90       100
                    ....*....|....*....|....
gi 124486807   1965 IRSQRNYLVQTEEQYVFIHDTLVE 1988
Cdd:smart00012   82 LRSQRPGMVQTEEQYLFLYRALLE 105
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
2049-2277 2.50e-38

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


Pssm-ID: 350466 [Multi-domain]  Cd Length: 230  Bit Score: 144.32  E-value: 2.50e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2049 NRTSSIIPVERSRVGISSLSGE-GTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIP----DGQN 2123
Cdd:cd14618     1 NRYPHVLPYDHSRVRLSQLGGEpHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTvgmeNGRV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2124 MAEDefvYWPNKDEPINCESFKVTLMSEEhkclsNEEKLIVQDFILEATQDDYVLEVRHFQCPKWPN---PDSPiSKTFE 2200
Cdd:cd14618    81 LCDH---YWPSESTPVSYGHITVHLLAQS-----SEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDhgiPEST-SSLMA 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124486807 2201 LISIIKEE--AANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVVL 2277
Cdd:cd14618   152 FRELVREHvqATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
2049-2277 4.46e-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: 140.72  E-value: 4.46e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2049 NRTSSIIPVERSRVGISSLSGEGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVM----IPDGQNM 2124
Cdd:cd14615     1 NRYNNVLPYDISRVKLSVQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMltkcVEQGRTK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2125 AEDefvYWPNKdEPINCESFKVTLMSEehkclSNEEKLIVQDFILEATQDDYVLEVRHFQCPKWpnPDSPISKTFELI-- 2202
Cdd:cd14615    81 CEE---YWPSK-QKKDYGDITVTMTSE-----IVLPEWTIRDFTVKNAQTNESRTVRHFHFTSW--PDHGVPETTDLLin 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124486807 2203 --SIIKE--EAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVVL 2277
Cdd:cd14615   150 frHLVREymKQNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCAL 228
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
2073-2276 6.42e-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: 139.37  E-value: 6.42e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2073 DYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAEDE-FVYWPNKDEPINCEsfkvtlMSE 2151
Cdd:cd14622     1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKcVQYWPSEGSVTHGE------ITI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2152 EHKCLSNEEKLIVQDFILEATQDDYVLEVRHFQCPKWPNPDSPiSKTFELISII----KEEAANRDGPMIVHDEHGGVTA 2227
Cdd:cd14622    75 EIKNDTLLETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIP-AEGKGMIDLIaavqKQQQQTGNHPIVVHCSAGAGRT 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 124486807 2228 GTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVV 2276
Cdd:cd14622   154 GTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
2043-2281 4.69e-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: 137.91  E-value: 4.69e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2043 QCNREKNRTSSIIPVERSRVGISSLSG-EGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIpdg 2121
Cdd:cd14553     1 EVNKPKNRYANVIAYDHSRVILQPIEGvPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMM--- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2122 QNMAEDEFV----YWPNKDEPiNCESFKVTLMSEEHkcLSNeekLIVQDFILEATQDDYVLEVRHFQCPKWPN---PDSP 2194
Cdd:cd14553    78 TKLEERSRVkcdqYWPTRGTE-TYGLIQVTLLDTVE--LAT---YTVRTFALHKNGSSEKREVRQFQFTAWPDhgvPEHP 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2195 ISkTFELISIIKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVY-QVAKM---INLMrpgVFTDiEQYQ 2270
Cdd:cd14553   152 TP-FLAFLRRVKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYgHVTCLraqRNYM---VQTE-DQYI 226
                         250
                  ....*....|.
gi 124486807 2271 FLYKVVLSLVS 2281
Cdd:cd14553   227 FIHDALLEAVT 237
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
2022-2276 5.63e-36

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: 138.80  E-value: 5.63e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2022 KQFQLL-SQSNILQSDYSTAL----KQCNREKNRTSSIIPVERSRVGISSLSGEG-TDYINASYIMGYYQSNEFIITQHP 2095
Cdd:cd14603     2 GEFSEIrACSAAFKADYVCSTvaggRKENVKKNRYKDILPYDQTRVILSLLQEEGhSDYINANFIKGVDGSRAYIATQGP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2096 LLHTIKDFWRMIWDHNAQLVVM----IPDGQNMAEdefVYWPNKDEPINCESFKVTLMSEEHkclSNEEKLIVQdfiLEA 2171
Cdd:cd14603    82 LSHTVLDFWRMIWQYGVKVILMacreIEMGKKKCE---RYWAQEQEPLQTGPFTITLVKEKR---LNEEVILRT---LKV 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2172 TQDDYVLEVRHFQCPKWPN---PDSPiSKTFELISIIKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDV 2248
Cdd:cd14603   153 TFQKESRSVSHFQYMAWPDhgiPDSP-DCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPD 231
                         250       260       270
                  ....*....|....*....|....*....|.
gi 124486807 2249 YQVAKMINLM---RPGVFTDIEQYQFLYKVV 2276
Cdd:cd14603   232 FSIFDVVLEMrkqRPAAVQTEEQYEFLYHTV 262
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
2049-2280 8.12e-36

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


Pssm-ID: 350467 [Multi-domain]  Cd Length: 233  Bit Score: 136.94  E-value: 8.12e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2049 NRTSSIIPVERSRVGISSLSGEGT-DYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIpdgQNMAED 2127
Cdd:cd14619     1 NRFRNVLPYDWSRVPLKPIHEEPGsDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVML---TNCMEA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2128 EFV----YWPNKDEPINCESFKVTLMSEEhkclsNEEKLIVQDFILEATQDDYVLEVRHFQCPKWPNPDSPiSKTFELIS 2203
Cdd:cd14619    78 GRVkcehYWPLDYTPCTYGHLRVTVVSEE-----VMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVP-SSTDTLLA 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2204 ---IIKE--EAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVVLS 2278
Cdd:cd14619   152 frrLLRQwlDQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILD 231

                  ..
gi 124486807 2279 LV 2280
Cdd:cd14619   232 FL 233
alpha_CA_I_II_III_XIII cd03119
Carbonic anhydrase alpha, isozymes I, II, and III and XIII. Carbonic anhydrases (CAs) are ...
38-300 9.74e-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: 137.57  E-value: 9.74e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807   38 WSYTGALNQKNWGKKYPICNSPKQSPINIDEDLTQVNVNLKKLKFQgWEKASLENtfIHNTGKTVEINLTNDY---YLSG 114
Cdd:cd03119     5 WGYDSHNGPEHWHELFPIAKGDRQSPIDIKTKDAKHDPSLKPLSVS-YDPATAKT--ILNNGHSFNVEFDDTDdrsVLRG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807  115 GLSEKVFKASKITFHWGKCNvsSEGSEHSLEGQKFPLEMQVYCFDAdRFSSFEEAVKGKGRLRALSILFEVGvEENLDYK 194
Cdd:cd03119    82 GPLTGSYRLRQFHFHWGSSD--DHGSEHTVDGVKYAAELHLVHWNS-KYGSFGEAAKQPDGLAVVGVFLKVG-EANPELQ 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807  195 AIIDGTESVSRFGKQAALDPFVLQNLLPNSTDkYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLAVFCEVLTMQQSGY 274
Cdd:cd03119   158 KVLDALDSIKTKGKQAPFTNFDPSCLLPASLD-YWTYPGSLTTPPLLECVTWIVLKEPISVSSEQMAKFRSLLFNAEGEP 236
                         250       260
                  ....*....|....*....|....*.
gi 124486807  275 VMLMdylQNNFREQQYKFSRQVFSSY 300
Cdd:cd03119   237 PCPM---VDNWRPPQPLKGRKVRASF 259
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
2045-2277 2.08e-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: 136.17  E-value: 2.08e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2045 NREKNRTSSIIPVERSRVGISSLSG-EGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIP---D 2120
Cdd:cd14614    12 NRCKNRYTNILPYDFSRVKLVSMHEeEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTqcnE 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2121 GQNMAEDEfvYWPNKDEPINCESFKVTLMSEEhkclsNEEKLIVQDFilEATQDDYVLEVRHFQCPKWPNPDSPISKTFE 2200
Cdd:cd14614    92 KRRVKCDH--YWPFTEEPVAYGDITVEMLSEE-----EQPDWAIREF--RVSYADEVQDVMHFNYTAWPDHGVPTANAAE 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2201 ----LISIIKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVV 2276
Cdd:cd14614   163 silqFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 242

                  .
gi 124486807 2277 L 2277
Cdd:cd14614   243 Q 243
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
1779-1982 3.83e-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: 133.99  E-value: 3.83e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1779 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGrrKCDQYWPTDG----SEEYGSFLVNQK 1854
Cdd:cd14550     1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNE--DEPIYWPTKEkpleCETFKVTLSGED 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1855 SVQVLAY--YTVRNFTLRNTK----LKkgsqkgrssgrlVTQYHYTQWPDMGVPEYSlpVLAFVRKAAQAKRHAVGPVVV 1928
Cdd:cd14550    79 HSCLSNEirLIVRDFILESTQddyvLE------------VRQFQCPSWPNPCSPIHT--VFELINTVQEWAQQRDGPIVV 144
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 124486807 1929 HCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFI 1982
Cdd:cd14550   145 HDRYGGVQAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFL 198
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
2049-2273 1.80e-34

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: 132.91  E-value: 1.80e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2049 NRTSSIIPVERSRVGISSL-SGEGTDYINASYIMGY-YQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAE 2126
Cdd:cd14547     1 NRYKTILPNEHSRVCLPSVdDDPLSSYINANYIRGYdGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEAKE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2127 DEFVYWPNKdEPINCESFKVTLMSEEHKclsneEKLIVQDFILEatqddYVLEVR---HFQCPKWPNPDSPiSKTFELIS 2203
Cdd:cd14547    81 KCAQYWPEE-ENETYGDFEVTVQSVKET-----DGYTVRKLTLK-----YGGEKRylkHYWYTSWPDHKTP-EAAQPLLS 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124486807 2204 IIKE-----EAANRDGPMIVHDEHG-GVTaGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLY 2273
Cdd:cd14547   149 LVQEveearQTEPHRGPIVVHCSAGiGRT-GCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVH 223
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
2040-2274 5.22e-34

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: 133.26  E-value: 5.22e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2040 ALKQCNREKNRTSSIIPVERSRVGISSLSG-EGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMI 2118
Cdd:cd14543    24 SLAPANQEKNRYGDVLCLDQSRVKLPKRNGdERTDYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKVLVIVMT 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2119 PD---------GQnmaedefvYWPNKDEpiNCESF-KVTLmseEHKCLSNEEKLIVQDFILEATQDDYVLEVRHFQCPKW 2188
Cdd:cd14543   104 TRvvergrvkcGQ--------YWPLEEG--SSLRYgDLTV---TNLSVENKEHYKKTTLEIHNTETDESRQVTHFQFTSW 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2189 PN---PDSPISKTFELISIIKEEAAN------------RDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAK 2253
Cdd:cd14543   171 PDfgvPSSAAALLDFLGEVRQQQALAvkamgdrwkghpPGPPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQTVR 250
                         250       260
                  ....*....|....*....|.
gi 124486807 2254 MINLMRPGVFTDIEQYQFLYK 2274
Cdd:cd14543   251 RMRTQRAFSIQTPDQYYFCYK 271
alpha_CA_V cd03118
Carbonic anhydrase alpha, CA isozyme V_like subgroup. Carbonic anhydrases (CAs) are ...
60-300 1.50e-33

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: 130.73  E-value: 1.50e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807   60 KQSPINIDEDLTQVNVNLKKLKFQgWEKASLEntFIHNTGKTVEINL---TNDYYLSGGLSEKVFKASKITFHWGKCNvs 136
Cdd:cd03118     3 RQSPINIQWRDSVYDPQLAPLRVS-YDPATCL--YIWNNGYSFQVEFddsTDKSGISGGPLENHYRLKQFHFHWGANN-- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807  137 SEGSEHSLEGQKFPLEMQVYCFDADRFSSFEEAVKGKGRLRALSILFEVGVE-ENLdyKAIIDGTESVSRFGKQAALDPF 215
Cdd:cd03118    78 EWGSEHTVDGHTYPAELHLVHWNSVKYENFEEAVMEENGLAVIGVFLKLGAHhEGL--QKLVDALPEVRHKDTVVEFNPF 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807  216 VLQNLLPNSTDkYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLAVFCEVLTmqqSGYVMLMDYLQNNFREQQYKFSRQ 295
Cdd:cd03118   156 DPSCLLPACRD-YWTYPGSLTTPPLTESVTWIIQKQPIEVSPSQLSVFRTLLF---TSRGEEEKVMVNNFRPLQPLMNRK 231

                  ....*
gi 124486807  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 ...
2037-2277 1.69e-33

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: 131.70  E-value: 1.69e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2037 YSTALKQCNREKNRTSSIIPVERSRVGISSLSGE-GTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLV 2115
Cdd:cd14633    32 WDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGEtSSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASI 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2116 VMIpdgQNMAEDEFV----YWPNKDEPIncESFKVTLMseEHKCLSneeKLIVQDFILEATQDDYVLEVRHFQCPKWPNP 2191
Cdd:cd14633   112 IMV---TNLVEVGRVkcckYWPDDTEIY--KDIKVTLI--ETELLA---EYVIRTFAVEKRGVHEIREIRQFHFTGWPDH 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2192 DSPISKT--FELISIIKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQY 2269
Cdd:cd14633   182 GVPYHATglLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQY 261

                  ....*...
gi 124486807 2270 QFLYKVVL 2277
Cdd:cd14633   262 VFIHDAIL 269
Cah COG3338
Carbonic anhydrase [Inorganic ion transport and metabolism];
38-263 1.56e-32

Carbonic anhydrase [Inorganic ion transport and metabolism];


Pssm-ID: 442567 [Multi-domain]  Cd Length: 247  Bit Score: 128.08  E-value: 1.56e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807   38 WSYTGALNQKNWGK---KYPICNS-PKQSPINIDedlTQVNVNLKKLKFQgWEKASLEntfIHNTGKTVEINLTNDYYLS 113
Cdd:COG3338    28 WSYEGETGPEHWGElspEFATCATgKNQSPIDIR---TAIKADLPPLKFD-YKPTPLE---IVNNGHTIQVNVDPGSTLT 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807  114 ggLSEKVFKASKITFHwgkcnvssEGSEHSLEGQKFPLEMQ-VYcfdadrfssfeeaVKGKGRLRALSILFEVGvEENLD 192
Cdd:COG3338   101 --VDGKRYELKQFHFH--------TPSEHTINGKSYPMEAHlVH-------------KDADGELAVVGVLFEEG-AENPA 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124486807  193 YKAIID------GTESVSrfgkQAALDPfvlQNLLPNSTDkYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLAVF 263
Cdd:COG3338   157 LAKLWAnlpleaGEEVAL----DATIDL---NDLLPEDRS-YYRYSGSLTTPPCSEGVLWIVLKQPITVSAEQIEAF 225
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
2048-2279 3.14e-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: 126.88  E-value: 3.14e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2048 KNRTSSIIPVERSRVGISSL-SGEGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAE 2126
Cdd:cd14602     1 KNRYKDILPYDHSRVELSLItSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2127 DEFV-YWPN-KDEPINCESFKVTLMSEEHKclsneEKLIVQdfILEATQDDYVLEVRHFQCPKWPNPDSP--ISKTFELI 2202
Cdd:cd14602    81 KKCErYWAEpGEMQLEFGPFSVTCEAEKRK-----SDYIIR--TLKVKFNSETRTIYQFHYKNWPDHDVPssIDPILELI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2203 SIIKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEK----ENaMDVYQVAKMINLMRPGVFTDIEQYQFLYKVVLS 2278
Cdd:cd14602   154 WDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDgiipEN-FSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIE 232

                  .
gi 124486807 2279 L 2279
Cdd:cd14602   233 L 233
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
2048-2273 4.10e-32

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: 126.87  E-value: 4.10e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2048 KNRTSSIIPVERSRVGISSL--SGEGTDYINASYIMGYY-QSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNM 2124
Cdd:cd14612    18 KDRYKTILPNPQSRVCLRRAgsQEEEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMITKLKEK 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2125 AEDEFVYWPNKDEPINCESFKVTLMSEehkClsneEKLIVQDFILEATQDDYvlEVRHFQCPKWPNPDSPISKT--FELI 2202
Cdd:cd14612    98 KEKCVHYWPEKEGTYGRFEIRVQDMKE---C----DGYTIRDLTIQLEEESR--SVKHYWFSSWPDHQTPESAGplLRLV 168
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124486807 2203 SIIKE--EAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLY 2273
Cdd:cd14612   169 AEVEEsrQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLH 241
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
2045-2277 7.46e-32

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: 125.91  E-value: 7.46e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2045 NREKNRTSSIIPVERSRVGISSLSGE-GTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQN 2123
Cdd:cd14630     3 NRNKNRYGNIISYDHSRVRLQLLDGDpHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2124 MAEDEFV-YWPNKDEPINceSFKVTLMSEEHKClsneeKLIVQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKT--FE 2200
Cdd:cd14630    83 VGRVKCVrYWPDDTEVYG--DIKVTLIETEPLA-----EYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATglLG 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124486807 2201 LISIIKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVVL 2277
Cdd:cd14630   156 FVRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAIL 232
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
2048-2279 2.53e-31

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


Pssm-ID: 350461 [Multi-domain]  Cd Length: 258  Bit Score: 124.97  E-value: 2.53e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2048 KNRTSSIIPVERSRVGISSLSGEG--TDYINASYIMGY-YQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNM 2124
Cdd:cd14613    28 KNRYKTILPNPHSRVCLTSPDQDDplSSYINANYIRGYgGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEM 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2125 AEDEFVYWPnkDEPINCESFKVTLMSEEHkclsnEEKLIVQDFILEATQDDYVLevRHFQCPKWPNPDSPiSKTFELISI 2204
Cdd:cd14613   108 NEKCTEYWP--EEQVTYEGIEITVKQVIH-----ADDYRLRLITLKSGGEERGL--KHYWYTSWPDQKTP-DNAPPLLQL 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2205 IKE------EAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKvVLS 2278
Cdd:cd14613   178 VQEveearqQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVHH-VLS 256

                  .
gi 124486807 2279 L 2279
Cdd:cd14613   257 L 257
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
2074-2277 1.19e-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: 121.17  E-value: 1.19e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2074 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIP--DGQNMAEDEFVYWPnkdEPINCesfKVTLMSE 2151
Cdd:cd14637     1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNqlNQSNSAWPCLQYWP---EPGLQ---QYGPMEV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2152 EHKCLSNEEKLIVQDFILE--ATQDDYVLEVRHFQCPKWP----NPDSPISKTFELISIIKEEAANRDGPMIVHDEHGGV 2225
Cdd:cd14637    75 EFVSGSADEDIVTRLFRVQniTRLQEGHLMVRHFQFLRWSayrdTPDSKKAFLHLLASVEKWQRESGEGRTVVHCLNGGG 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 124486807 2226 TAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVVL 2277
Cdd:cd14637   155 RSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIAL 206
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
2074-2273 2.07e-30

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: 120.82  E-value: 2.07e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2074 YINASYI-MGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMI-PDGQNMAEDEFVYWPNKDEPINCESFKVTLMSE 2151
Cdd:cd18533     1 YINASYItLPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLtPLVENGREKCDQYWPSGEYEGEYGDLTVELVSE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2152 EHKclsNEEKLIVQDFILeATQDDYVLEVRHFQCPKWPN---PDSPISkTFELISIIKE--EAANRDGPMIVHDEHG-GV 2225
Cdd:cd18533    81 EEN---DDGGFIVREFEL-SKEDGKVKKVYHIQYKSWPDfgvPDSPED-LLTLIKLKRElnDSASLDPPIIVHCSAGvGR 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 124486807 2226 TaGTFCALTTLMHQLEK------ENAMDVYQVAKMINLM---RPGVFTDIEQYQFLY 2273
Cdd:cd18533   156 T-GTFIALDSLLDELKRglsdsqDLEDSEDPVYEIVNQLrkqRMSMVQTLRQYIFLY 211
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
1779-1988 3.74e-30

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: 119.74  E-value: 3.74e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1779 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLveKGRRKCDQYWPTDGSEEYGSFLVNQKSVQV 1858
Cdd:cd14634     1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEM--DAAQLCMQYWPEKTSCCYGPIQVEFVSADI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1859 LAYYTVRNFTLRNTKlkkgsqKGRSSGRLVTQYHYTQWPDM-GVPEYSLPVLAFVRKAAQAKRH---AVGPVVVHCSAGV 1934
Cdd:cd14634    79 DEDIISRIFRICNMA------RPQDGYRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLEKWQEQydgREGRTVVHCLNGG 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 124486807 1935 GRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVE 1988
Cdd:cd14634   153 GRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
2043-2281 1.89e-29

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: 120.14  E-value: 1.89e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2043 QCNREKNRTSSIIPVERSRVGISSLSG-EGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIpdg 2121
Cdd:cd14626    39 EVNKPKNRYANVIAYDHSRVILTSVDGvPGSDYINANYIDGYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMM--- 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2122 QNMAEDEFV----YWPNKDEPiNCESFKVTLMSEEHKCLSNeekliVQDFILEATQDDYVLEVRHFQCPKWPNPDSPISK 2197
Cdd:cd14626   116 TRLEEKSRVkcdqYWPIRGTE-TYGMIQVTLLDTVELATYS-----VRTFALYKNGSSEKREVRQFQFMAWPDHGVPEYP 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2198 TFELISIIKEEAAN--RDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKV 2275
Cdd:cd14626   190 TPILAFLRRVKACNppDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEA 269

                  ....*.
gi 124486807 2276 VLSLVS 2281
Cdd:cd14626   270 LLEAAT 275
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
2037-2279 1.99e-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: 120.81  E-value: 1.99e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2037 YSTAL--KQCNREKNRTSSIIPVERSRVGIS-SLSGEGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQ 2113
Cdd:cd14604    47 YPTATgeKEENVKKNRYKDILPFDHSRVKLTlKTSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVA 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2114 LVVMIPDGQNMAEDEFV-YWPN-KDEPINCESFKVTLMSEEHKclsneEKLIVQDFILEATQDDYVLEVRHFQcpKWPNP 2191
Cdd:cd14604   127 IIVMACREFEMGRKKCErYWPLyGEEPMTFGPFRISCEAEQAR-----TDYFIRTLLLEFQNETRRLYQFHYV--NWPDH 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2192 DSPIS--KTFELISIIKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDI--- 2266
Cdd:cd14604   200 DVPSSfdSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVqtk 279
                         250
                  ....*....|...
gi 124486807 2267 EQYQFLYKVVLSL 2279
Cdd:cd14604   280 EQYELVHRAIAQL 292
alpha_CA_VII cd03149
Carbonic anhydrase alpha, CA isozyme VII_like subgroup. Carbonic anhydrases (CAs) are ...
60-300 2.21e-29

Carbonic anhydrase alpha, CA isozyme VII_like subgroup. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. Most alpha CAs are monomeric enzymes. The zinc ion is complexed by three histidines. This vertebrate subgroup comprises isozyme VII. CA VII is the most active cytosolic enzyme after CA II, and may be highly expressed in the brain. Human CA VII may be a target of antiepileptic sulfonamides/sulfamates.


Pssm-ID: 239402  Cd Length: 236  Bit Score: 118.40  E-value: 2.21e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807   60 KQSPINIDEDLTQVNVNLKKLKFQgWEKASLENtfIHNTGKTVEINLtNDY----YLSGGLSEKVFKASKITFHWGKCNv 135
Cdd:cd03149     3 RQSPIDIVSSEAVYDPKLKPLSLS-YDPCTSLS--ISNNGHSVMVEF-DDSddktVITGGPLENPYRLKQFHFHWGAKH- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807  136 sSEGSEHSLEGQKFPLEMQVYCFDADRFSSFEEAVKGKGRLRALSILFEVGvEENLDYKAIIDGTESVSRFGKQAALDPF 215
Cdd:cd03149    78 -GSGSEHTVDGKTFPSELHLVHWNAKKYKSFGEAAAAPDGLAVLGVFLETG-DEHPGLNRLTDALYMVRFKGTKAQFLDF 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807  216 VLQNLLPNSTDkYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLAVFCEVLTMQQSGYVMLMdylQNNFREQQYKFSRQ 295
Cdd:cd03149   156 NPKCLLPKSLD-YWTYPGSLTTPPLNESVTWIVLKEPIPVSEKQMGKFRELLFTSEEDQRNHM---VNNFRPPQPLKGRT 231

                  ....*
gi 124486807  296 VFSSY 300
Cdd:cd03149   232 VRASF 236
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
2049-2274 3.89e-29

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


Pssm-ID: 350465 [Multi-domain]  Cd Length: 228  Bit Score: 117.71  E-value: 3.89e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2049 NRTSSIIPVERSRVGISSLSGEG-TDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIpdgQNMAED 2127
Cdd:cd14617     1 NRYNNILPYDSTRVKLSNVDDDPcSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMV---TQCVEK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2128 EFV----YWPNKDEPINCESFKVTLMSEehkclSNEEKLIVQDF-ILEATQDDYVLEVRHFQCPKWPNPDSPiSKTFELI 2202
Cdd:cd14617    78 GRVkcdhYWPADQDSLYYGDLIVQMLSE-----SVLPEWTIREFkICSEEQLDAPRLVRHFHYTVWPDHGVP-ETTQSLI 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124486807 2203 SIIK--EEAANRD---GPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYK 2274
Cdd:cd14617   152 QFVRtvRDYINRTpgsGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228
alpha_CA_prokaryotic_like cd03124
Carbonic anhydrase alpha, prokaryotic-like subfamily. Carbonic anhydrases (CAs) are ...
45-263 4.12e-29

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: 116.99  E-value: 4.12e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807   45 NQKNWG---KKYPICNS-PKQSPINIDEDLTQVNVnLKKLKFQgWEKASLEntfIHNTGKTVEINLTNDyylSGGLS--E 118
Cdd:cd03124     1 GPEHWGnldPEFALCATgKNQSPIDITTKAVVSDK-LPPLNYN-YKPTSAT---LVNNGHTIQVNFEGN---GGTLTidG 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807  119 KVFKASKITFHwgkcnvssEGSEHSLEGQKFPLEMQ-VYcfdadrfssfeeaVKGKGRLRALSILFEVGvEENLDYKAII 197
Cdd:cd03124    73 ETYQLLQFHFH--------SPSEHLINGKRYPLEAHlVH-------------KSKDGQLAVVAVLFEEG-KENPFLKKIL 130
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124486807  198 DGTESvsRFGKQAALDPFV-LQNLLPNSTDkYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLAVF 263
Cdd:cd03124   131 DNMPK--KEGTEVNLPAILdPNELLPESRS-YYRYEGSLTTPPCSEGVRWIVLKQPITISKEQLAKF 194
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
2074-2277 5.23e-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: 116.66  E-value: 5.23e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2074 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDgQNMAEDEFVYWPNKDE----PINCESFKVTLm 2149
Cdd:cd14634     1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNE-MDAAQLCMQYWPEKTSccygPIQVEFVSADI- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2150 seehkclsnEEKLIVQDFI---LEATQDDYVLeVRHFQCPKWPN-PDSPISKTfELISIIK------EEAANRDGPMIVH 2219
Cdd:cd14634    79 ---------DEDIISRIFRicnMARPQDGYRI-VQHLQYIGWPAyRDTPPSKR-SILKVVRrlekwqEQYDGREGRTVVH 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 124486807 2220 DEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVVL 2277
Cdd:cd14634   148 CLNGGGRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVAL 205
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
2049-2274 5.54e-29

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


Pssm-ID: 350464 [Multi-domain]  Cd Length: 224  Bit Score: 116.93  E-value: 5.54e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2049 NRTSSIIPVERSRVGISSLSG-EGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPD----GQN 2123
Cdd:cd14616     1 NRFPNIKPYNNNRVKLIADAGvPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQcfekGRI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2124 MAEDefvYWPNKDEPINCES-FKVTLMSEEhkclsNEEKLIVQDFILEaTQDDYVLeVRHFQCPKWPNPDSPISkTFELI 2202
Cdd:cd14616    81 RCHQ---YWPEDNKPVTVFGdIVITKLMED-----VQIDWTIRDLKIE-RHGDYMM-VRQCNFTSWPEHGVPES-SAPLI 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124486807 2203 SIIKEEAANRDG---PMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYK 2274
Cdd:cd14616   150 HFVKLVRASRAHdntPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLHQ 224
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
2037-2281 8.68e-29

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 119.34  E-value: 8.68e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2037 YSTALKQCNREKNRTSSIIPVERSRVGISSLSGEGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVV 2116
Cdd:PHA02747   43 IANFEKPENQPKNRYWDIPCWDHNRVILDSGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIV 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2117 MI--PDGQNMAEDEFVYW-PNKDEPINCESFKVTLMSEEHKCLSNEEKLIVQDFILEATQddyvlEVRHFQCPKWPNPDS 2193
Cdd:PHA02747  123 MLtpTKGTNGEEKCYQYWcLNEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILKDSR-----KISHFQCSEWFEDET 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2194 PiSKTFELISIIKEEAANRD-------------GPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRP 2260
Cdd:PHA02747  198 P-SDHPDFIKFIKIIDINRKksgklfnpkdallCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRH 276
                         250       260
                  ....*....|....*....|....
gi 124486807 2261 GVFTDIEQYQFL---YKVVLSLVS 2281
Cdd:PHA02747  277 AGIMNFDDYLFIqpgYEVLHYFLS 300
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
2074-2273 1.17e-28

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: 115.53  E-value: 1.17e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2074 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIpdgQNMAE------DEfvYWPNKDEPiNCESFKVT 2147
Cdd:cd14549     1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMI---TNLVErgrrkcDQ--YWPKEGTE-TYGNIQVT 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2148 LMSEEHkcLSNeekLIVQDFILEATQ------DDYVLEVRHFQCPKWPN---PDSPISktfeLISII-KEEAANRD--GP 2215
Cdd:cd14549    75 LLSTEV--LAT---YTVRTFSLKNLKlkkvkgRSSERVVYQYHYTQWPDhgvPDYTLP----VLSFVrKSSAANPPgaGP 145
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124486807 2216 MIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMI----NLMrpgVFTDiEQYQFLY 2273
Cdd:cd14549   146 IVVHCSAGVGRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIrtqrNYL---VQTE-EQYIFIH 203
alpha_CARP_X_XI_like cd03121
Carbonic anhydrase alpha related protein: groups X, XI and related proteins. This subgroup ...
49-296 1.38e-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: 116.74  E-value: 1.38e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807   49 WGKKYP---ICNSPK-QSPINIDEDLTQVNVNLKKLKFQGWEKASLEntfIHNTGKTVEINLTNDY--YLSGGLSEKVFK 122
Cdd:cd03121     5 WGLVNSawnLCSKGRrQSPVDIEPSRLLFDPFLTPLRIDTGRKVSGT---FYNTGRHVSFRPDKDPvvNISGGPLSYRYR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807  123 ASKITFHWGKCNvsSEGSEHSLEGQKFPLEMQVYCFDADRFSSFEEAVKGKGRLRALSILFEVGVEENLDYKAIIDGTES 202
Cdd:cd03121    82 LEEIRLHFGRED--EQGSEHTVNGQAFPGEVQLIHYNSELYPNFSEASKSPNGLVIVSLFVKIGETSNPELRRLTNRDTI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807  203 VS-RFGKQAA-LDPFVLQNLLPNsTDKYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLAvfcEVLTMQQSGYVMLMDY 280
Cdd:cd03121   160 TSiRYKGDAYfLQDLSIELLLPE-TDHYITYEGSLTSPGCHETVTWIILNKPIYITKEQMH---SLRLLSQNSPSQEKAP 235
                         250
                  ....*....|....*.
gi 124486807  281 LQNNFREQQYKFSRQV 296
Cdd:cd03121   236 MSPNFRPVQPLNNRPV 251
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
2053-2277 2.51e-28

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: 115.42  E-value: 2.51e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2053 SIIPVERSRVGISSLSG-EGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAEDE-FV 2130
Cdd:cd14620     3 NILPYDHSRVILSQLDGiPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKcYQ 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2131 YWPNKdepiNCESF-KVTLMSEEHKCLSNeekLIVQDFILEATQDDYVLEVR-----HFQcpKWPN---PDSPISkTFEL 2201
Cdd:cd14620    83 YWPDQ----GCWTYgNIRVAVEDCVVLVD---YTIRKFCIQPQLPDGCKAPRlvtqlHFT--SWPDfgvPFTPIG-MLKF 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124486807 2202 ISIIKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVVL 2277
Cdd:cd14620   153 LKKVKSVNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALL 228
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
2038-2276 6.50e-28

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 117.05  E-value: 6.50e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2038 STALKQCNREKNRTSSIIPVERSRVGISS------------------LSGEGTD--YINASYIMGYYQSNEFIITQHPLL 2097
Cdd:PHA02746   44 NHFLKKENLKKNRFHDIPCWDHSRVVINAheslkmfdvgdsdgkkieVTSEDNAenYIHANFVDGFKEANKFICAQGPKE 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2098 HTIKDFWRMIWDHNAQLVVMIPDGQNMAEDEFVYWPN-KDEPINCESFKVTLMSEEHKCLSNEEKLIVQDFILEATQddy 2176
Cdd:PHA02746  124 DTSEDFFKLISEHESQVIVSLTDIDDDDEKCFELWTKeEDSELAFGRFVAKILDIIEELSFTKTRLMITDKISDTSR--- 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2177 vlEVRHFQCPKWP---NPDSPiSKTFELISIIKEEAA----------NRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKE 2243
Cdd:PHA02746  201 --EIHHFWFPDWPdngIPTGM-AEFLELINKVNEEQAelikqadndpQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKE 277
                         250       260       270
                  ....*....|....*....|....*....|...
gi 124486807 2244 NAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVV 2276
Cdd:PHA02746  278 KEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
2074-2274 7.14e-28

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: 112.90  E-value: 7.14e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2074 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVM----IPDGQNMAEDefvYWPNK-DEPINCESFKVTL 2148
Cdd:cd14542     1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMacreFEMGKKKCER---YWPEEgEEQLQFGPFKISL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2149 MSEEHKClsneeklivQDFI---LEATQDDYVLEVRHFQCPKWPNPDSPISKT--FELISIIKEEAANRDGPMIVHDEHG 2223
Cdd:cd14542    78 EKEKRVG---------PDFLirtLKVTFQKESRTVYQFHYTAWPDHGVPSSVDpiLDLVRLVRDYQGSEDVPICVHCSAG 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 124486807 2224 GVTAGTFCALT---TLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYK 2274
Cdd:cd14542   149 CGRTGTICAIDyvwNLLKTGKIPEEFSLFDLVREMRKQRPAMVQTKEQYELVYR 202
alpha_CARP_VIII cd03120
Carbonic anhydrase alpha related protein, group VIII. Carbonic anhydrase related proteins ...
49-289 9.29e-28

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: 114.57  E-value: 9.29e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807   49 WGKKYPICNSPKQSPINI-------DEDLTQVNVNLKKLKFQGWEkaslentfIHNTGKTVEINLTNDYYLSGGL--SEK 119
Cdd:cd03120     4 WGLLFPEANGEYQSPINLnsrearyDPSLLEVRLSPNYVVCRDCE--------VINDGHTIQIILKSKSVLSGGPlpQGH 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807  120 VFKASKITFHWGKCNvsSEGSEHSLEGQKFPLEMQVYCFDADRFSSFEEAVKGKGRLRALSILFEVGvEENLDYKAIIDG 199
Cdd:cd03120    76 EFELAEVRFHWGREN--QRGSEHTVNFKAFPMELHLIHWNSTLYSSLEEAMGKPHGIAIIALFVQIG-KEHVGLKAVTEI 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807  200 TESVSRFGKQAALDPFVLQNLLPNSTDK-YYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLAVFCEvLTMQQSGYVMLM 278
Cdd:cd03120   153 LQDIQYKGKSKTIPCFNPNTLLPDPLLRdYWVYEGSLTTPPCSEGVTWILFRYPLTISQSQIEEFRR-LRTHVKGAELVE 231
                         250
                  ....*....|....
gi 124486807  279 --DY-LQNNFREQQ 289
Cdd:cd03120   232 gcDGlLGDNFRPTQ 245
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
1779-1988 9.47e-28

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: 113.08  E-value: 9.47e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1779 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRR-KCDQYWPTDGSEEYGSFLVNQKSVQ 1857
Cdd:cd14637     1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWPEPGLQQYGPMEVEFVSGS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1858 VLAYYTVRNFTLRN-TKLKKGSqkgrssgRLVTQYHYTQW-PDMGVPEYS---LPVLAFVRKAAQAKRHavGPVVVHCSA 1932
Cdd:cd14637    81 ADEDIVTRLFRVQNiTRLQEGH-------LMVRHFQFLRWsAYRDTPDSKkafLHLLASVEKWQRESGE--GRTVVHCLN 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 124486807 1933 GVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVE 1988
Cdd:cd14637   152 GGGRSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
2033-2277 1.04e-27

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: 115.51  E-value: 1.04e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2033 LQSDYSTALKQCNREKNRTSSIIPVERSRVGISSLSG-EGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHN 2111
Cdd:cd14621    40 IQATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGvPDSDYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQN 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2112 AQLVVMIPDGQNMAEDEFV-YWPNKdepiNCESFKVTLMSEEHKCLSNE---EKLIVQDfILEATQDDYVLEVRHFQCPK 2187
Cdd:cd14621   120 TATIVMVTNLKERKECKCAqYWPDQ----GCWTYGNIRVSVEDVTVLVDytvRKFCIQQ-VGDVTNKKPQRLITQFHFTS 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2188 WPN---PDSPISkTFELISIIKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFT 2264
Cdd:cd14621   195 WPDfgvPFTPIG-MLKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQ 273
                         250
                  ....*....|...
gi 124486807 2265 DIEQYQFLYKVVL 2277
Cdd:cd14621   274 TDMQYVFIYQALL 286
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
2074-2277 1.36e-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: 112.32  E-value: 1.36e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2074 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIpdgQNMAEDEFV----YWPNKDEPINceSFKVTLM 2149
Cdd:cd14555     1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMV---TNLVEVGRVkcsrYWPDDTEVYG--DIKVTLV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2150 SEEHKClsneeKLIVQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKT--FELISIIKEEAANRDGPMIVHDEHGGVTA 2227
Cdd:cd14555    76 ETEPLA-----EYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATglLGFIRRVKASNPPSAGPIVVHCSAGAGRT 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 124486807 2228 GTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVVL 2277
Cdd:cd14555   151 GCYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAIL 200
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
2045-2276 1.79e-27

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


Pssm-ID: 350392 [Multi-domain]  Cd Length: 251  Bit Score: 113.71  E-value: 1.79e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2045 NREKNRTSSIIPVERSRVGISSL--SGEGTDYINASYIM-------GYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLV 2115
Cdd:cd14544     1 NKGKNRYKNILPFDHTRVILKDRdpNVPGSDYINANYIRnenegptTDENAKTYIATQGCLENTVSDFWSMVWQENSRVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2116 VMIPDGQNMAEDEFV-YWPNKDEPINCESFKVTLMSEehkclSNEEKLIVQDFILEAT-QDDYVLEVRHFQCPKWPNPDS 2193
Cdd:cd14544    81 VMTTKEVERGKNKCVrYWPDEGMQKQYGPYRVQNVSE-----HDTTDYTLRELQVSKLdQGDPIREIWHYQYLSWPDHGV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2194 PiSKTFELISII-----KEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKEN---AMDVYQVAKMINLMRPGVFTD 2265
Cdd:cd14544   156 P-SDPGGVLNFLedvnqRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGldcDIDIQKTIQMVRSQRSGMVQT 234
                         250
                  ....*....|.
gi 124486807 2266 IEQYQFLYKVV 2276
Cdd:cd14544   235 EAQYKFIYVAV 245
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
2045-2280 4.19e-27

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


Pssm-ID: 350505 [Multi-domain]  Cd Length: 274  Bit Score: 113.21  E-value: 4.19e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2045 NREKNRTSSIIPVERSRVGISSLSGEGT---DYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIpdg 2121
Cdd:cd17667    27 NKHKNRYINILAYDHSRVKLRPLPGKDSkhsDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMI--- 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2122 QNMAE------DEfvYWPNKdepiNCESFK---VTLMSEE-HKCLSneekliVQDFILEATQDDYVLE-----------V 2180
Cdd:cd17667   104 TNLVEkgrrkcDQ--YWPTE----NSEEYGniiVTLKSTKiHACYT------VRRFSIRNTKVKKGQKgnpkgrqnertV 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2181 RHFQCPKWPNPDSPiSKTFELISIIKEEAANRD---GPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINL 2257
Cdd:cd17667   172 IQYHYTQWPDMGVP-EYALPVLTFVRRSSAARTpemGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRT 250
                         250       260
                  ....*....|....*....|...
gi 124486807 2258 MRPGVFTDIEQYQFLYKVVLSLV 2280
Cdd:cd17667   251 QRNYLVQTEEQYIFIHDALLEAI 273
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
2072-2277 4.93e-27

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: 111.27  E-value: 4.93e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2072 TDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIpdgQNMAE----DEFVYWPNKDEPINceSFKVT 2147
Cdd:cd14631    13 SDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMV---TNLVEvgrvKCYKYWPDDTEVYG--DFKVT 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2148 LMSEEHKClsneeKLIVQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTFELISIIKEEAAN--RDGPMIVHDEHGGV 2225
Cdd:cd14631    88 CVEMEPLA-----EYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNppSAGPIVVHCSAGAG 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 124486807 2226 TAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVVL 2277
Cdd:cd14631   163 RTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAIL 214
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
1779-1988 8.35e-27

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: 110.16  E-value: 8.35e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1779 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLveKGRRKCDQYWPTDGSEEYGSFLVNQKSVQV 1858
Cdd:cd14635     1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDV--DPAQLCPQYWPENGVHRHGPIQVEFVSADL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1859 LAYYTVRNFTLRNtklkkgSQKGRSSGRLVTQYHYTQWP---DMGVPEYS-LPVLAFVRKAAQAKRHAVGPVVVHCSAGV 1934
Cdd:cd14635    79 EEDIISRIFRIYN------AARPQDGYRMVQQFQFLGWPmyrDTPVSKRSfLKLIRQVDKWQEEYNGGEGRTVVHCLNGG 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 124486807 1935 GRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVE 1988
Cdd:cd14635   153 GRSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
2046-2274 9.68e-27

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: 110.94  E-value: 9.68e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2046 REKNRTSSIIPVERSRVgisSLSGEGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVM----IPDG 2121
Cdd:cd14545     1 LNRYRDRDPYDHDRSRV---KLKQGDNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMlnklMEKG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2122 QNMAEDefvYWPNKDEPINC---ESFKVTLMSEEHKclsneEKLIVQDFILEATQDDYVLEVRHFQCPKWPN---PDSPI 2195
Cdd:cd14545    78 QIKCAQ---YWPQGEGNAMIfedTGLKVTLLSEEDK-----SYYTVRTLELENLKTQETREVLHFHYTTWPDfgvPESPA 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2196 SKTFELISIIKEEAANRD-GPMIVHDEHGGVTAGTFCALTTLMHQLEKEN--AMDVYQVAKMINLMRPGVFTDIEQYQFL 2272
Cdd:cd14545   150 AFLNFLQKVRESGSLSSDvGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNpsSVDVKKVLLEMRKYRMGLIQTPDQLRFS 229

                  ..
gi 124486807 2273 YK 2274
Cdd:cd14545   230 YL 231
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
2074-2277 1.16e-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: 109.78  E-value: 1.16e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2074 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDgQNMAEDEFVYWP----NKDEPINCESFKVTLm 2149
Cdd:cd14635     1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLND-VDPAQLCPQYWPengvHRHGPIQVEFVSADL- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2150 seehkclsnEEKLIVQDF-ILEAT--QDDYVLeVRHFQCPKWP-NPDSPISKT--FELISII---KEEAANRDGPMIVHD 2220
Cdd:cd14635    79 ---------EEDIISRIFrIYNAArpQDGYRM-VQQFQFLGWPmYRDTPVSKRsfLKLIRQVdkwQEEYNGGEGRTVVHC 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 124486807 2221 EHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVVL 2277
Cdd:cd14635   149 LNGGGRSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVAL 205
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
2017-2276 1.71e-26

PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type tyrosine-protein phosphatase N2 (PTPRN2 or R-PTP-N2), also called islet cell autoantigen-related protein (IAR), ICAAR, phogrin, or IA-2beta, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). It consists of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. It is mainly expressed in neuropeptidergic neurons and peptide-secreting endocrine cells, including insulin-producing pancreatic beta-cells. It may function as a phosphatidylinositol phosphatase to regulate insulin secretion. It is also required for normal accumulation of the neurotransmitters norepinephrine, dopamine and serotonin in the brain.


Pssm-ID: 350458 [Multi-domain]  Cd Length: 283  Bit Score: 111.69  E-value: 1.71e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2017 KTKLEKQFQLLSQSNILQSDYSTALKQCNREKNRTSSIIPVERSRVGISSL-SGEGTDYINASYIMGYYQSN-EFIITQH 2094
Cdd:cd14610    16 KNRLEKEWEALCAYQAEPNATNVAQREENVQKNRSLAVLPYDHSRIILKAEnSHSHSDYINASPIMDHDPRNpAYIATQG 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2095 PLLHTIKDFWRMIWDHNAQLVVMI-PDGQNMAEDEFVYWPnkDEPINC-ESFKVTLMSEEHKClsneEKLIVQDFILEAT 2172
Cdd:cd14610    96 PLPATVADFWQMVWESGCVVIVMLtPLAENGVKQCYHYWP--DEGSNLyHIYEVNLVSEHIWC----EDFLVRSFYLKNL 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2173 QDDYVLEVRHFQCPKWPNPDSPIS--KTFELISIIKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEK-ENAMDVY 2249
Cdd:cd14610   170 QTNETRTVTQFHFLSWNDQGVPAStrSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLNKMAKgAKEIDIA 249
                         250       260
                  ....*....|....*....|....*..
gi 124486807 2250 QVAKMINLMRPGVFTDIEQYQFLYKVV 2276
Cdd:cd14610   250 ATLEHLRDQRPGMVQTKEQFEFALTAV 276
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
2045-2277 2.15e-26

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


Pssm-ID: 350456 [Multi-domain]  Cd Length: 277  Bit Score: 111.27  E-value: 2.15e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2045 NREKNRTSSIIPVERSRVgisSLSGEGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIpdgQNM 2124
Cdd:cd14608    25 NKNRNRYRDVSPFDHSRI---KLHQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVML---NRV 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2125 AEDEFV----YWPNKDEP---INCESFKVTLMSEEHKCLSNEEKLIVQDFILEATQddyvlEVRHFQCPKWPN---PDSP 2194
Cdd:cd14608    99 MEKGSLkcaqYWPQKEEKemiFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETR-----EILHFHYTTWPDfgvPESP 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2195 ISKTFELISIIKEEAANRD-GPMIVHDEHGGVTAGTFCALTT---LMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQ 2270
Cdd:cd14608   174 ASFLNFLFKVRESGSLSPEhGPVVVHCSAGIGRSGTFCLADTcllLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLR 253

                  ....*..
gi 124486807 2271 FLYKVVL 2277
Cdd:cd14608   254 FSYLAVI 260
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
2043-2281 2.26e-26

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


Pssm-ID: 350472 [Multi-domain]  Cd Length: 284  Bit Score: 111.36  E-value: 2.26e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2043 QCNREKNRTSSIIPVERSRVGISSLSG-EGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDG 2121
Cdd:cd14624    45 EVNKPKNRYANVIAYDHSRVLLSAIEGiPGSDYINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKL 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2122 QNMAE---DEfvYWPNKDEPINcESFKVTLMSEEHKClsneeKLIVQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKT 2198
Cdd:cd14624   125 EERSRvkcDQ--YWPSRGTETY-GLIQVTLLDTVELA-----TYCVRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPT 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2199 FELISIIKEEAAN--RDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVV 2276
Cdd:cd14624   197 PFLAFLRRVKTCNppDAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDAL 276

                  ....*
gi 124486807 2277 LSLVS 2281
Cdd:cd14624   277 LEAVT 281
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
1779-1988 3.45e-26

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


Pssm-ID: 350484 [Multi-domain]  Cd Length: 206  Bit Score: 108.57  E-value: 3.45e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1779 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNL-VEKGrrkCDQYWPTDGSEEYGSFLVNQKSVQ 1857
Cdd:cd14636     1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVdLAQG---CPQYWPEEGMLRYGPIQVECMSCS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1858 VLAYYTVRNFTLRN-TKLKKGSQkgrssgrLVTQYHYTQWPD-MGVPEYS---LPVLAFVRKAAQAKRHAVGPVVVHCSA 1932
Cdd:cd14636    78 MDCDVISRIFRICNlTRPQEGYL-------MVQQFQYLGWAShREVPGSKrsfLKLILQVEKWQEECDEGEGRTIIHCLN 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 124486807 1933 GVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVE 1988
Cdd:cd14636   151 GGGRSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
2019-2281 5.73e-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: 110.18  E-value: 5.73e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2019 KLEKQFQLLSQSNILQSDYSTAlkQCNREKNRTSSIIPVERSRVGISSLSG-EGTDYINASYIMGYYQSNEFIITQHPLL 2097
Cdd:cd14625    23 KLSQEYESIDPGQQFTWEHSNL--EVNKPKNRYANVIAYDHSRVILQPIEGiMGSDYINANYIDGYRKQNAYIATQGPLP 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2098 HTIKDFWRMIWDHNAQLVVM---IPDGQNMAEDEfvYWPNKdepiNCESF---KVTLMSEEHKClsneeKLIVQDFILEA 2171
Cdd:cd14625   101 ETFGDFWRMVWEQRSATVVMmtkLEEKSRIKCDQ--YWPSR----GTETYgmiQVTLLDTIELA-----TFCVRTFSLHK 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2172 TQDDYVLEVRHFQCPKWPNPDSPISKTFELISIIKEEAAN--RDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVY 2249
Cdd:cd14625   170 NGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNppDAGPIVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIY 249
                         250       260       270
                  ....*....|....*....|....*....|..
gi 124486807 2250 QVAKMINLMRPGVFTDIEQYQFLYKVVLSLVS 2281
Cdd:cd14625   250 GHVTLMRSQRNYMVQTEDQYSFIHDALLEAVA 281
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
2017-2276 1.82e-25

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


Pssm-ID: 350457 [Multi-domain]  Cd Length: 281  Bit Score: 108.59  E-value: 1.82e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2017 KTKLEKQFQLLSQSNILQSDYSTALKQCNREKNRTSSIIPVERSRVGI-SSLSGEGTDYINASYIMGY-YQSNEFIITQH 2094
Cdd:cd14609    14 RDRLAKEWQALCAYQAEPNTCSTAQGEANVKKNRNPDFVPYDHARIKLkAESNPSRSDYINASPIIEHdPRMPAYIATQG 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2095 PLLHTIKDFWRMIWDHNAQLVVM----IPDGQNMAEDefvYWPNKDEPINcESFKVTLMSEEHKClsneEKLIVQDFILE 2170
Cdd:cd14609    94 PLSHTIADFWQMVWENGCTVIVMltplVEDGVKQCDR---YWPDEGSSLY-HIYEVNLVSEHIWC----EDFLVRSFYLK 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2171 ATQDDYVLEVRHFQCPKWPNPDSPiSKTFELISI---IKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKE-NAM 2246
Cdd:cd14609   166 NVQTQETRTLTQFHFLSWPAEGIP-SSTRPLLDFrrkVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKGvKEI 244
                         250       260       270
                  ....*....|....*....|....*....|
gi 124486807 2247 DVYQVAKMINLMRPGVFTDIEQYQFLYKVV 2276
Cdd:cd14609   245 DIAATLEHVRDQRPGMVRTKDQFEFALTAV 274
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
2074-2277 3.55e-25

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


Pssm-ID: 350480 [Multi-domain]  Cd Length: 205  Bit Score: 105.52  E-value: 3.55e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2074 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIpdgQNMAEDEFV----YWPNKDEPINceSFKVTLM 2149
Cdd:cd14632     1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMI---TKLVEVGRVkcskYWPDDSDTYG--DIKITLL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2150 SEEhkclsNEEKLIVQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKT--FELISIIKEEAANRDGPMIVHDEHGGVTA 2227
Cdd:cd14632    76 KTE-----TLAEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATglLAFIRRVKASTPPDAGPVVVHCSAGAGRT 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 124486807 2228 GTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVVL 2277
Cdd:cd14632   151 GCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAIL 200
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
2048-2273 6.50e-25

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: 105.39  E-value: 6.50e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2048 KNRTSSIIPVERSRVGI--SSLSGEGTDYINASYIMGYY-QSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNM 2124
Cdd:cd14611     2 KNRYKTILPNPHSRVCLkpKNSNDSLSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2125 AEDEFVYWPNKDEPINcesfKVTLMSeehKCLSNEEKLIVQDFILEatQDDYVLEVRHFQCPKWPNPDSPISKT--FELI 2202
Cdd:cd14611    82 NEKCVLYWPEKRGIYG----KVEVLV---NSVKECDNYTIRNLTLK--QGSQSRSVKHYWYTSWPDHKTPDSAQplLQLM 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124486807 2203 SIIKEE--AANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLY 2273
Cdd:cd14611   153 LDVEEDrlASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
2045-2277 9.91e-25

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: 104.91  E-value: 9.91e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2045 NREKNRTSSIIPVERSRVgissLSGEGTDYINASYIMGYYQSNEF--IITQHPLLHTIKDFWRMIWDHNAQLVVMIpdgQ 2122
Cdd:cd14597     3 NRKKNRYKNILPYDTTRV----PLGDEGGYINASFIKMPVGDEEFvyIACQGPLPTTVADFWQMVWEQKSTVIAMM---T 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2123 NMAEDEFV----YWP---NKDEPINcESFKVTLMSEEHkclsnEEKLIVQDFILEATQDDYVLEVRHFQCPKWPNPDSPi 2195
Cdd:cd14597    76 QEVEGGKIkcqrYWPeilGKTTMVD-NRLQLTLVRMQQ-----LKNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTP- 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2196 SKTFELISIIK-EEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYK 2274
Cdd:cd14597   149 SQPEQLLTFISyMRHIHKSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQ 228

                  ...
gi 124486807 2275 VVL 2277
Cdd:cd14597   229 VIL 231
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
2074-2277 1.38e-24

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: 103.95  E-value: 1.38e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2074 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDgQNMAEDEFVYWPnKDEPINCESFKVTLMSEEH 2153
Cdd:cd14636     1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNE-VDLAQGCPQYWP-EEGMLRYGPIQVECMSCSM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2154 KClsneeKLIVQDFI---LEATQDDYVLeVRHFQCPKWP-NPDSPISKTFELISII-----KEEAANRDGPMIVHDEHGG 2224
Cdd:cd14636    79 DC-----DVISRIFRicnLTRPQEGYLM-VQQFQYLGWAsHREVPGSKRSFLKLILqvekwQEECDEGEGRTIIHCLNGG 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 124486807 2225 VTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVVL 2277
Cdd:cd14636   153 GRSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVAL 205
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
2074-2274 5.12e-24

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: 101.91  E-value: 5.12e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2074 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAEDEFV-YWPNKdepiNCESFkvtlmSEE 2152
Cdd:cd14551     1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSqYWPDQ----GCWTY-----GNL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2153 HKCLSNEEKLI---VQDFILEATQDDY----VLEVRHFQCPKWPN---PDSPISkTFELISIIKEEAANRDGPMIVHDEH 2222
Cdd:cd14551    72 RVRVEDTVVLVdytTRKFCIQKVNRGIgekrVRLVTQFHFTSWPDfgvPFTPIG-MLKFLKKVKSANPPRAGPIVVHCSA 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 124486807 2223 GGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYK 2274
Cdd:cd14551   151 GVGRTGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
2179-2278 2.21e-23

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: 96.66  E-value: 2.21e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807   2179 EVRHFQCPKWPNPDSPISKT--FELISIIKEE--AANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKE-NAMDVYQVAK 2253
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDsiLELLRAVKKNlnQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80
                            90       100
                    ....*....|....*....|....*
gi 124486807   2254 MINLMRPGVFTDIEQYQFLYKVVLS 2278
Cdd:smart00012   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
2179-2278 2.21e-23

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 96.66  E-value: 2.21e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807   2179 EVRHFQCPKWPNPDSPISKT--FELISIIKEE--AANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKE-NAMDVYQVAK 2253
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDsiLELLRAVKKNlnQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80
                            90       100
                    ....*....|....*....|....*
gi 124486807   2254 MINLMRPGVFTDIEQYQFLYKVVLS 2278
Cdd:smart00404   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
1741-1986 2.45e-23

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 102.74  E-value: 2.45e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1741 SSNHPDNKHK--NRYVNIVAYDHSRVKLtqlaEKDGKLTDyinANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVE 1818
Cdd:PHA02740   45 ACAQAENKAKdeNLALHITRLLHRRIKL----FNDEKVLD---ARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQ 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1819 VIVMITNLVEKgrrKC-DQYWptdGSEEYGSFLVNQKSVQVLAYYTVRNFTLrnTKLKKGSQKGRSsgRLVTQYHYTQWP 1897
Cdd:PHA02740  118 IIVLISRHADK---KCfNQFW---SLKEGCVITSDKFQIETLEIIIKPHFNL--TLLSLTDKFGQA--QKISHFQYTAWP 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1898 DMGVPEYSLPVLAFVRKA----AQAKRHA----VGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQR 1969
Cdd:PHA02740  188 ADGFSHDPDAFIDFFCNIddlcADLEKHKadgkIAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKK 267
                         250
                  ....*....|....*..
gi 124486807 1970 NYLVQTEEQYVFIHDTL 1986
Cdd:PHA02740  268 YGCMNCLDDYVFCYHLI 284
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
2074-2277 1.07e-22

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


Pssm-ID: 350386 [Multi-domain]  Cd Length: 207  Bit Score: 98.22  E-value: 1.07e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2074 YINASYIMGYYQSNEF--IITQHPLLHTIKDFWRMIWDHNAQLVVMIPdgQNMaEDEFV----YWPnkdepincESFKVT 2147
Cdd:cd14538     1 YINASHIRIPVGGDTYhyIACQGPLPNTTGDFWQMVWEQKSEVIAMVT--QDV-EGGKVkchrYWP--------DSLNKP 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2148 LMSEEHKCLSNEEKLIVQDFI-----LEATQDDYVLEVRHFQCPKWPNPDSPISkTFELISIIKE-EAANRDGPMIVHDE 2221
Cdd:cd14538    70 LICGGRLEVSLEKYQSLQDFVirrisLRDKETGEVHHITHLNFTTWPDHGTPQS-ADPLLRFIRYmRRIHNSGPIVVHCS 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 124486807 2222 HGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVVL 2277
Cdd:cd14538   149 AGIGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACL 204
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
2074-2277 1.35e-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: 97.90  E-value: 1.35e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2074 YINASYIMGYYQSNE--FIITQHPLLHTIKDFWRMIWDHNAQLVVMIPD----GQNMAEDefvYWPNK-DEPINCESFKV 2146
Cdd:cd14596     1 YINASYITMPVGEEElfYIATQGPLPSTIDDFWQMVWENRSDVIAMMTReverGKVKCHR---YWPETlQEPMELENYQL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2147 TLmseehkclsnEEKLIVQDFILEATQddyVLE--------VRHFQCPKWPNPDSPISKTFELISIIKEEAANRDGPMIV 2218
Cdd:cd14596    78 RL----------ENYQALQYFIIRIIK---LVEketgenrlIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHNTGPIVV 144
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 124486807 2219 HDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVVL 2277
Cdd:cd14596   145 HCSAGIGRAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVL 203
PHA02738 PHA02738
hypothetical protein; Provisional
2045-2276 2.12e-22

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 100.77  E-value: 2.12e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2045 NREKNRTSSIIPVERSRVGISSLSGEGtDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMI-PDGQN 2123
Cdd:PHA02738   49 NRKLNRYLDAVCFDHSRVILPAERNRG-DYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLcKKKEN 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2124 MAEDEFVYWPNKDE-PINCESFKVTLMSEEHKCLSNEEKLIVQDFIlEATQddyvlEVRHFQCPKWPNPDSPiSKTFELI 2202
Cdd:PHA02738  128 GREKCFPYWSDVEQgSIRFGKFKITTTQVETHPHYVKSTLLLTDGT-SATQ-----TVTHFNFTAWPDHDVP-KNTSEFL 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2203 SII-------KEEAANR---------DGPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDI 2266
Cdd:PHA02738  201 NFVlevrqcqKELAQESlqighnrlqPPPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIP 280
                         250
                  ....*....|
gi 124486807 2267 EQYQFLYKVV 2276
Cdd:PHA02738  281 FQYFFCYRAV 290
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
2074-2273 2.25e-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: 97.36  E-value: 2.25e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2074 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIpdgQNMAE------DEfvYWPNKDEPiNCESFKVT 2147
Cdd:cd17668     1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMI---TNLVEkgrrkcDQ--YWPADGSE-EYGNFLVT 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2148 LMSEEHKCLSNEEKLIVQDF-ILEATQDDYVLE--VRHFQCPKWPNPDSPiSKTFELISIIKEEAANRD---GPMIVHDE 2221
Cdd:cd17668    75 QKSVQVLAYYTVRNFTLRNTkIKKGSQKGRPSGrvVTQYHYTQWPDMGVP-EYTLPVLTFVRKASYAKRhavGPVVVHCS 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 124486807 2222 HGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLY 2273
Cdd:cd17668   154 AGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIH 205
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
1779-1987 5.33e-22

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


Pssm-ID: 350507 [Multi-domain]  Cd Length: 204  Bit Score: 96.22  E-value: 5.33e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1779 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCdQYWPT-DGSEEYGSFLVNQKSVQ 1857
Cdd:cd17669     1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEF-VYWPNkDEPINCETFKVTLIAEE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1858 VLAYYTVRNFTLRNTKLKKGSQKGRSSgrlVTQYHYTQWPDMGVP-EYSLPVLAFVRKAAQAKRhavGPVVVHCSAGVGR 1936
Cdd:cd17669    80 HKCLSNEEKLIIQDFILEATQDDYVLE---VRHFQCPKWPNPDSPiSKTFELISIIKEEAANRD---GPMIVHDEHGGVT 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 124486807 1937 TGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLV 1987
Cdd:cd17669   154 AGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
1779-1987 7.64e-22

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


Pssm-ID: 350508 [Multi-domain]  Cd Length: 205  Bit Score: 95.90  E-value: 7.64e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1779 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITN---LVEkgrrkcDQ--YWPTD----GSEEYGSF 1849
Cdd:cd17670     1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDnqgLAE------DEfvYWPSReesmNCEAFTVT 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1850 LVNQKSV------QVLayytVRNFTLRNTKLKKGSQkgrssgrlVTQYHYTQWPDMGVPEYSLPVLAFVRKAAQAKRHav 1923
Cdd:cd17670    75 LISKDRLclsneeQII----IHDFILEATQDDYVLE--------VRHFQCPKWPNPDAPISSTFELINVIKEEALTRD-- 140
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124486807 1924 GPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLV 1987
Cdd:cd17670   141 GPTIVHDEFGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
2074-2274 2.45e-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: 94.12  E-value: 2.45e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2074 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAEDE-FVYWPNKDEPINC-ESFKVTLMSE 2151
Cdd:cd14557     1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKcAQYWPSMEEGSRAfGDVVVKINEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2152 EHkClsneEKLIVQDFILEATQDDY-VLEVRHFQCPKWPN---PDSPiSKTFELISIIKEEAANRDGPMIVHDEHGGVTA 2227
Cdd:cd14557    81 KI-C----PDYIIRKLNINNKKEKGsGREVTHIQFTSWPDhgvPEDP-HLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRT 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 124486807 2228 GTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYK 2274
Cdd:cd14557   155 GTYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
2045-2276 8.04e-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: 94.26  E-value: 8.04e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2045 NREKNRTSSIIPVERSRVgisSLSGEGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIpdgQNM 2124
Cdd:cd14607    24 NRNRNRYRDVSPYDHSRV---KLQNTENDYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVML---NRI 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2125 AEDEFV----YWPNKDEPINCES---FKVTLMSEEHKCLSNEEKLIVQDFILEATQDdyvleVRHFQCPKWPN---PDSP 2194
Cdd:cd14607    98 VEKDSVkcaqYWPTDEEEVLSFKetgFSVKLLSEDVKSYYTVHLLQLENINSGETRT-----ISHFHYTTWPDfgvPESP 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2195 ISKTFELISIIKEEAANRD-GPMIVHDEHGGVTAGTFCALTTLMHQLEKEN--AMDVYQVAKMINLMRPGVFTDIEQYQF 2271
Cdd:cd14607   173 ASFLNFLFKVRESGSLSPEhGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDIKQVLLDMRKYRMGLIQTPDQLRF 252

                  ....*
gi 124486807 2272 LYKVV 2276
Cdd:cd14607   253 SYMAV 257
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
2045-2277 1.43e-20

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: 94.15  E-value: 1.43e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2045 NREKNRTSSIIPVERSRVgissLSGEGTDYINASY----IMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPD 2120
Cdd:cd14600    40 NMDKNRYKDVLPYDATRV----VLQGNEDYINASYvnmeIPSANIVNKYIATQGPLPHTCAQFWQVVWEQKLSLIVMLTT 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2121 ----GQNMAEDefvYWPNKDEPINCESFKVTLMSEEHKClsneeKLIVQDFILEATQDDYVLEVRHFQCPKWPN---PDS 2193
Cdd:cd14600   116 lterGRTKCHQ---YWPDPPDVMEYGGFRVQCHSEDCTI-----AYVFREMLLTNTQTGEERTVTHLQYVAWPDhgvPDD 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2194 PiSKTFELISIIKEEAANRDgPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLY 2273
Cdd:cd14600   188 S-SDFLEFVNYVRSKRVENE-PVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKFVC 265

                  ....
gi 124486807 2274 KVVL 2277
Cdd:cd14600   266 EAIL 269
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
2074-2276 2.30e-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: 91.74  E-value: 2.30e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2074 YINASYIMGYYQSNE-FIITQHPLLHTIKDFWRMIWDHNAQLVVMI-PDGQNMAEDEFVYWPNKDEPINcESFKVTLMSE 2151
Cdd:cd14546     1 YINASTIYDHDPRNPaYIATQGPLPHTIADFWQMIWEQGCVVIVMLtRLQENGVKQCARYWPEEGSEVY-HIYEVHLVSE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2152 EHKClsneEKLIVQDFILEATQDDYVLEVRHFQCPKWPNPDSPIS-KTF-ELISIIKEEAANRDGPMIVHDEHGGVTAGT 2229
Cdd:cd14546    80 HIWC----DDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASaKPLlEFRRKVNKSYRGRSCPIVVHCSDGAGRTGT 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 124486807 2230 FCALTTLMHQLEK-ENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVV 2276
Cdd:cd14546   156 YILIDMVLNRMAKgAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAV 203
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
2074-2274 1.91e-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: 88.98  E-value: 1.91e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2074 YINASYIMGYYQ-SNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAEDEFV-YWP-NKDEPINCESFKVTLMS 2150
Cdd:cd14539     1 YINASLIEDLTPyCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHrYWPtERGQALVYGAITVSLQS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2151 EEhkclsneekliVQDF----ILEATQDDYVLE--VRHFQCPKWPNPDSPISKTfELISIIKE------EAANRDGPMIV 2218
Cdd:cd14539    81 VR-----------TTPThverIISIQHKDTRLSrsVVHLQFTTWPELGLPDSPN-PLLRFIEEvhshylQQRSLQTPIVV 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 124486807 2219 HDEHGGVTAGTFCALTTLMHQLEKENAM-DVYQVAKMINLMRPGVFTDIEQYQFLYK 2274
Cdd:cd14539   149 HCSSGVGRTGAFCLLYAAVQEIEAGNGIpDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
2045-2282 1.93e-19

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: 90.08  E-value: 1.93e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2045 NREKNRTSSIIPVERSRVGISS--LSGEGTDYINASYIMGYYQSN--------EFIITQHPLLHTIKDFWRMIWDHNAQL 2114
Cdd:cd14605     2 NKNKNRYKNILPFDHTRVVLHDgdPNEPVSDYINANIIMPEFETKcnnskpkkSYIATQGCLQNTVNDFWRMVFQENSRV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2115 VVMIPDGQNMAEDEFV-YWPNKDEPINCESFKVTLMSEE--HKCLSNEEKLIvqdfilEATQDDYVLEVRHFQCPKWPN- 2190
Cdd:cd14605    82 IVMTTKEVERGKSKCVkYWPDEYALKEYGVMRVRNVKESaaHDYILRELKLS------KVGQGNTERTVWQYHFRTWPDh 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2191 --PDSP--ISKTFELISiIKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENA---MDVYQVAKMINLMRPGVF 2263
Cdd:cd14605   156 gvPSDPggVLDFLEEVH-HKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRSGMV 234
                         250
                  ....*....|....*....
gi 124486807 2264 TDIEQYQFLYKVVLSLVST 2282
Cdd:cd14605   235 QTEAQYRFIYMAVQHYIET 253
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
2020-2283 2.07e-19

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 91.22  E-value: 2.07e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2020 LEKQFQLLSQSNILQSDYsTALKQCNREKNRTSSIIPVERSRVGISSLSGeGTDYINASYIMGYYQSNEFIITQHPLLHT 2099
Cdd:PHA02742   28 LKEEHEHIMQEIVAFSCN-ESLELKNMKKCRYPDAPCFDRNRVILKIEDG-GDDFINASYVDGHNAKGRFICTQAPLEET 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2100 IKDFWRMIWDHNAQLVVMIP----DGQnmaEDEFVYWpNKDEPINCESFKVTLMSEEHKCLSNEEkliVQDFILEATQDD 2175
Cdd:PHA02742  106 ALDFWQAIFQDQVRVIVMITkimeDGK---EACYPYW-MPHERGKATHGEFKIKTKKIKSFRNYA---VTNLCLTDTNTG 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2176 YVLEVRHFQCPKWPNPDSP--ISKTFELISIIKE-----------EAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEK 2242
Cdd:PHA02742  179 ASLDIKHFAYEDWPHGGLPrdPNKFLDFVLAVREadlkadvdikgENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNE 258
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 124486807 2243 ENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVVL---SLVSTR 2283
Cdd:PHA02742  259 RAIIPLLSIVRDLRKQRHNCLSLPQQYIFCYFIVLifaKLMADK 302
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
2045-2282 4.70e-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: 4.70e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2045 NREKNRTSSIIPVERSRVGISSLSGE--GTDYINASYIMGYYQSNE-----FIITQHPLLHTIKDFWRMIWDHNAQLVVM 2117
Cdd:cd14606    18 NKSKNRYKNILPFDHSRVILQGRDSNipGSDYINANYVKNQLLGPDenaktYIASQGCLEATVNDFWQMAWQENSRVIVM 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2118 ----IPDGQNMAedeFVYWPNKDEPINCESFKVTLMSEEHkclSNEEKL-IVQDFILEATqdDYVLEVRHFQCPKWPNPD 2192
Cdd:cd14606    98 ttreVEKGRNKC---VPYWPEVGMQRAYGPYSVTNCGEHD---TTEYKLrTLQVSPLDNG--ELIREIWHYQYLSWPDHG 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2193 SPiSKTFELISII-----KEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENA---MDVYQVAKMINLMRPGVFT 2264
Cdd:cd14606   170 VP-SEPGGVLSFLdqinqRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVRAQRSGMVQ 248
                         250
                  ....*....|....*...
gi 124486807 2265 DIEQYQFLYKVVLSLVST 2282
Cdd:cd14606   249 TEAQYKFIYVAIAQFIET 266
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
2037-2280 2.46e-18

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


Pssm-ID: 350447 [Multi-domain]  Cd Length: 287  Bit Score: 87.75  E-value: 2.46e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2037 YSTALKQCNREKNRTSSIIPVERSRVGISSLSGEGTDYINASYIMGYYQSNE--FIITQHPLLHTIKDFWRMIWDHNAQL 2114
Cdd:cd14599    30 FTTATLPENAERNRIREVVPYEENRVELVPTKENNTGYINASHIKVTVGGEEwhYIATQGPLPHTCHDFWQMVWEQGVNV 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2115 VVMIpdgqnMAEDE------FVYWPNKDEPINCES---FKVTLMSEEHKCLSNEEKLIVQDFIleATQDDYVLevrHFQC 2185
Cdd:cd14599   110 IAMV-----TAEEEggrsksHRYWPKLGSKHSSATygkFKVTTKFRTDSGCYATTGLKVKHLL--SGQERTVW---HLQY 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2186 PKWPNPDSP------ISKTFELISI------IKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAK 2253
Cdd:cd14599   180 TDWPDHGCPeevqgfLSYLEEIQSVrrhtnsMLDSTKNCNPPIVVHCSAGVGRTGVVILTELMIGCLEHNEKVEVPVMLR 259
                         250       260
                  ....*....|....*....|....*..
gi 124486807 2254 MINLMRPGVFTDIEQYQFLYKVVLSLV 2280
Cdd:cd14599   260 HLREQRMFMIQTIAQYKFVYQVLIQFL 286
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
2073-2278 1.06e-17

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: 83.92  E-value: 1.06e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2073 DYINASY----IMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVM----IPDGQNMAEDefvYWPNKDEPINCESF 2144
Cdd:cd14541     1 DYINANYvnmeIPGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMlttlVERGRVKCHQ---YWPDLGETMQFGNL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2145 KVTLMSEEhkclsNEEKLIVQDFILEATQDDYVLEVRHFQCPKWPNPDSPiSKTFELISIIKEEAANRDG---PMIVHDE 2221
Cdd:cd14541    78 QITCVSEE-----VTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVP-DDSSDFLDFVKRVRQNRVGmvePTVVHCS 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 124486807 2222 HG-GVTaGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVVLS 2278
Cdd:cd14541   152 AGiGRT-GVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAILR 208
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
2073-2277 6.12e-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: 81.92  E-value: 6.12e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2073 DYINASYIMGYYQS----NEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIpdgQNMAEDEFV----YWPNKDEPINCESF 2144
Cdd:cd14601     1 DYINANYINMEIPSssiiNRYIACQGPLPNTCSDFWQMTWEQGSSMVVML---TTQVERGRVkchqYWPEPSGSSSYGGF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2145 KVTLMSEEhkclsNEEKLIVQDFILEATQDDYVLEVRHFQCPKWPN---PDSPiSKTFELISIIKEEAANRDGPMIVHDE 2221
Cdd:cd14601    78 QVTCHSEE-----GNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDhgvPDDS-SDFLDFVCLVRNKRAGKDEPVVVHCS 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 124486807 2222 HGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVVL 2277
Cdd:cd14601   152 AGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAIL 207
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
2074-2277 6.38e-17

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: 82.12  E-value: 6.38e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2074 YINASYIMGYYQSNE--FIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQ-NMAEDEFVYWPNkdepincesfkvtlMS 2150
Cdd:cd14540     1 YINASHITATVGGKQrfYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEeGGREKCFRYWPT--------------LG 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2151 EEHKCLSNEEKLIVQDF------------ILEATQDDYVLEVRHFQCPKWPN---PDSPisKTF-----ELISI---IKE 2207
Cdd:cd14540    67 GEHDALTFGEYKVSTKFsvssgcytttglRVKHTLSGQSRTVWHLQYTDWPDhgcPEDV--SGFldfleEINSVrrhTNQ 144
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124486807 2208 EAA--NRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVVL 2277
Cdd:cd14540   145 DVAghNRNPPTLVHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLI 216
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
2074-2273 2.05e-16

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


Pssm-ID: 350496 [Multi-domain]  Cd Length: 206  Bit Score: 80.20  E-value: 2.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2074 YINASYIMGYYQSN--EFIITQHPLLHTIKDFWRMIWDHNAQLVVMIP---DGQNMAEDEFVYWPNKDEPINCESFKVTL 2148
Cdd:cd17658     1 YINASLVETPASESlpKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTrlvDNYSTAKCADYFPAEENESREFGRISVTN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2149 MSEEHKCLSNEEK-LIVQDFILEatqdDYVLEVRHFQCPKWPN---PDS--PISKTFELISIIKEEAanrdGPMIVHDEH 2222
Cdd:cd17658    81 KKLKHSQHSITLRvLEVQYIESE----EPPLSVLHIQYPEWPDhgvPKDtrSVRELLKRLYGIPPSA----GPIVVHCSA 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 124486807 2223 GGVTAGTFCALTTLMHQLEKEN--AMDVYQVAKMINLMRPGVFTDIEQYQFLY 2273
Cdd:cd17658   153 GIGRTGAYCTIHNTIRRILEGDmsAVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
1751-1988 5.16e-14

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


Pssm-ID: 350407 [Multi-domain]  Cd Length: 227  Bit Score: 73.59  E-value: 5.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1751 NRYVNIvaydHSRVKltqlaEKDGKLtdyINANYVDGYNRPKAyIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKG 1830
Cdd:cd14559     1 NRFTNI----QTRVS-----TPVGKN---LNANRVQIGNKNVA-IACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQ 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1831 RRKCDQYWPTDGSeeYGSFLVNQKsvQVLAYYTVRNFTLRNTKLK-KGSQKGRSsgrlVTQYHYTQWPDMG-VPEYSLPV 1908
Cdd:cd14559    68 RKGLPPYFRQSGT--YGSVTVKSK--KTGKDELVDGLKADMYNLKiTDGNKTIT----IPVVHVTNWPDHTaISSEGLKE 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1909 LA-FVRKAAQAKRHAVGPV-------------VVHCSAGVGRTGTYIvldSMLQQIQHEGTVNIFGFLKHIRSQRN-YLV 1973
Cdd:cd14559   140 LAdLVNKSAEEKRNFYKSKgssaindknkllpVIHCRAGVGRTGQLA---AAMELNKSPNNLSVEDIVSDMRTSRNgKMV 216
                         250
                  ....*....|....*
gi 124486807 1974 QTEEQYvfihDTLVE 1988
Cdd:cd14559   217 QKDEQL----DTLKE 227
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
2074-2280 6.29e-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: 70.39  E-value: 6.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2074 YINASYIMGYYQSNE--FIITQHPLLHTIKDFWRMIWDHNAQLVVMIP-DGQNMAEDEFVYWP---NKDEPINCESFKVT 2147
Cdd:cd14598     1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTaEEEGGREKSFRYWPrlgSRHNTVTYGRFKIT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2148 L-MSEEHKCLSNEEKLIVQdfiLEATQDDYVLevrHFQCPKWPNPDSP------ISKTFELISIIKEEAANRD-----GP 2215
Cdd:cd14598    81 TrFRTDSGCYATTGLKIKH---LLTGQERTVW---HLQYTDWPEHGCPedlkgfLSYLEEIQSVRRHTNSTIDpkspnPP 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124486807 2216 MIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVVLSLV 2280
Cdd:cd14598   155 VLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFL 219
fn3 pfam00041
Fibronectin type III domain;
313-401 9.77e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 57.04  E-value: 9.77e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807   313 SEPENVQADPENYTSLLVTWERPRVVyDAMIEKFAVLYQPLaGNDQAKHEFLTDGYQDlGAILNNLLPNMSYVLQIVAVC 392
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDG-NGPITGYEVEYRPK-NSGEPWNEITVPGTTT-SVTLTGLKPGTEYEVRVQAVN 77

                   ....*....
gi 124486807   393 SNGlYGKYS 401
Cdd:pfam00041   78 GGG-EGPPS 85
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
1890-1984 4.85e-09

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 56.90  E-value: 4.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1890 QYHYTQWPDMGVPEYS--LPVLAFVRKAAQAKRhavgPVVVHCSAGVGRTGT----YIVLDSM-LQQIqhegtvnifgfL 1962
Cdd:COG2453    49 EYLHLPIPDFGAPDDEqlQEAVDFIDEALREGK----KVLVHCRGGIGRTGTvaaaYLVLLGLsAEEA-----------L 113
                          90       100
                  ....*....|....*....|..
gi 124486807 1963 KHIRSQRNYLVQTEEQYVFIHD 1984
Cdd:COG2453   114 ARVRAARPGAVETPAQRAFLER 135
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
2042-2281 7.09e-09

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 59.60  E-value: 7.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2042 KQCNREKNRT---SSIIPVER---SRVGISSlsgeGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLV 2115
Cdd:PHA02740   44 KACAQAENKAkdeNLALHITRllhRRIKLFN----DEKVLDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQII 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2116 VMI---PDGQNMAEdefvYWPNKDEP-INCESFKVTLMSEEHKCLSNEEKLIVQDfileatQDDYVLEVRHFQCPKWP-- 2189
Cdd:PHA02740  120 VLIsrhADKKCFNQ----FWSLKEGCvITSDKFQIETLEIIIKPHFNLTLLSLTD------KFGQAQKISHFQYTAWPad 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 2190 ----NPDSPISKTFELISII----KEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPG 2261
Cdd:PHA02740  190 gfshDPDAFIDFFCNIDDLCadleKHKADGKIAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYG 269
                         250       260
                  ....*....|....*....|
gi 124486807 2262 VFTDIEQYQFLYKVVLSLVS 2281
Cdd:PHA02740  270 CMNCLDDYVFCYHLIAAYLK 289
PLN02179 PLN02179
carbonic anhydrase
49-253 1.83e-08

carbonic anhydrase


Pssm-ID: 177835  Cd Length: 235  Bit Score: 57.30  E-value: 1.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807   49 WGKKYP---ICNSPK-QSPInideDLTQVNVNLkkLKFQGWEKA-SLENTFIHNTGKTVEINLTNDyylsgglsekvfkA 123
Cdd:PLN02179   50 WGKLNPqwkVCSTGKyQSPI----DLTDERVSL--IHDQALSRHyKPAPAVIQSRGHDVMVSWKGD-------------A 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807  124 SKITFHWG-----KCNVSSEgSEHSLEGQKFPLEMQVYCFDAdrfssfeeavkgKGRLRALSILFEVGvEENLDYKAIID 198
Cdd:PLN02179  111 GKITIHQTdyklvQCHWHSP-SEHTINGTSYDLELHMVHTSA------------SGKTAVVGVLYKLG-EPDEFLTKLLN 176
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 124486807  199 GTESVsrfGKQ----AALDPFVLQNllpnSTDKYYIYNGSLTSPPCTDTVEWIVFKDTV 253
Cdd:PLN02179  177 GIKGV---GKKeinlGIVDPRDIRF----ETNNFYRYIGSLTIPPCTEGVIWTVVKRVV 228
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
1908-1984 1.18e-07

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


Pssm-ID: 350344 [Multi-domain]  Cd Length: 113  Bit Score: 51.97  E-value: 1.18e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124486807 1908 VLAFVRKAAQAKRHAvGPVVVHCSAGVGRTGTYIVLDSMLQQIqhegtVNIFGFLKHIRSQR-NYLVQTEEQYVFIHD 1984
Cdd:cd14494    42 VDRFLEVLDQAEKPG-EPVLVHCKAGVGRTGTLVACYLVLLGG-----MSAEEAVRIVRLIRpGGIPQTIEQLDFLIK 113
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
313-406 6.20e-06

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: 46.72  E-value: 6.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807  313 SEPENVQADPENYTSLLVTWERPRvVYDAMIEKFAVLYQPLAGNDQakHEFLTDGYQDLGAILNNLLPNMSYVLQIVAVC 392
Cdd:cd00063     2 SPPTNLRVTDVTSTSVTLSWTPPE-DDGGPITGYVVEYREKGSGDW--KEVEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78
                          90
                  ....*....|....
gi 124486807  393 SNGlYGKYSDQLIV 406
Cdd:cd00063    79 GGG-ESPPSESVTV 91
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
1891-1984 1.08e-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: 48.50  E-value: 1.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1891 YHYT-QWPDMGVPEYSLpVLAFVRKAAQAKRHAvGPVVVHCSAGVGRTG----TYIVldsMLQQIQHEGTVnifgflKHI 1965
Cdd:cd14506    78 YFYNfGWKDYGVPSLTT-ILDIVKVMAFALQEG-GKVAVHCHAGLGRTGvliaCYLV---YALRMSADQAI------RLV 146
                          90
                  ....*....|....*....
gi 124486807 1966 RSQRNYLVQTEEQYVFIHD 1984
Cdd:cd14506   147 RSKRPNSIQTRGQVLCVRE 165
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
313-395 2.57e-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: 44.53  E-value: 2.57e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807    313 SEPENVQADPENYTSLLVTWERPRvvyDAMIEKFAVLYQPLAGNDQAKHEFLTDGYQDLGAILNNLLPNMSYVLQIVAVC 392
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPP---DDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                    ...
gi 124486807    393 SNG 395
Cdd:smart00060   79 GAG 81
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
1889-1984 2.59e-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: 46.87  E-value: 2.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1889 TQYHYTqWPDMGVP---EYSLPVLAFVRKAAQAKRHavgpVVVHCSAGVGRTGTyiVLDSMLQQIQ----HEGTVNIfgf 1961
Cdd:cd14505    74 TWHHLP-IPDGGVPsdiAQWQELLEELLSALENGKK----VLIHCKGGLGRTGL--IAACLLLELGdtldPEQAIAA--- 143
                          90       100
                  ....*....|....*....|...
gi 124486807 1962 lkhIRSQRNYLVQTEEQYVFIHD 1984
Cdd:cd14505   144 ---VRALRPGAIQTPKQENFLHQ 163
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
1890-1982 6.45e-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: 6.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486807 1890 QYHYTQWPDMGVPEYSL--PVLAFVRKAaqakrHAVG-PVVVHCSAGVGRTGT----YIVLDSMLQQIQHegtvnifgfL 1962
Cdd:cd14504    51 RYHHIPIEDYTPPTLEQidEFLDIVEEA-----NAKNeAVLVHCLAGKGRTGTmlacYLVKTGKISAVDA---------I 116
                          90       100
                  ....*....|....*....|
gi 124486807 1963 KHIRSQRNYLVQTEEQYVFI 1982
Cdd:cd14504   117 NEIRRIRPGSIETSEQEKFV 136
PLN02202 PLN02202
carbonate dehydratase
225-263 2.78e-03

carbonate dehydratase


Pssm-ID: 177853 [Multi-domain]  Cd Length: 284  Bit Score: 41.97  E-value: 2.78e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 124486807  225 TDKYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLAVF 263
Cdd:PLN02202  201 TRKYFRYIGSLTTPPCSENVSWTILGKVRSMSKEQVELL 239
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
1908-1968 3.31e-03

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 39.96  E-value: 3.31e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124486807   1908 VLAFVRKAAQAKrhavGPVVVHCSAGVGRTGTYIVldSMLQQIQHEGTVNIFGFLKHIRSQ 1968
Cdd:smart00195   67 AVEFIEDAESKG----GKVLVHCQAGVSRSATLII--AYLMKTRNMSLNDAYDFVKDRRPI 121
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
1892-1941 9.64e-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: 39.36  E-value: 9.64e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 124486807 1892 HYtqwpDMGVPEYSLPVLAFVRKAAQAKRHAVGPVVVHCSAGVGRTGTYI 1941
Cdd:cd14499    82 HY----DLYFPDGSTPSDDIVKKFLDICENEKGAIAVHCKAGLGRTGTLI 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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