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Conserved domains on  [gi|332205945|ref|NP_001193768|]
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receptor-type tyrosine-protein phosphatase zeta isoform 3 precursor [Homo sapiens]

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 ...
 857-1127 2.39e-166

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: 499.56  E-value: 2.39e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  857 FTEEFEEVQSCTVDLGITADSSNHPDNKHKNRYINIVAYDHSRVKLAQLAEKDGKLTDYINANYVDGYNRPKAYIAAQGP 936
Cdd:cd17667     1 FSEDFEEVQRCTADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSKHSDYINANYVDGYNKAKAYIATQGP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  937 LKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQVLAYYTVRNFTLRNTKIKKGSQ- 1015
Cdd:cd17667    81 LKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTKVKKGQKg 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1016 --KGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKAAYAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVN 1093
Cdd:cd17667   161 npKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVN 240

                         250       260       270
                  ....*....|....*....|....*....|....
gi 332205945 1094 IFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAIL 1127
Cdd:cd17667   241 VLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 274
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 1210-1413 6.44e-157

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: 471.79  E-value: 6.44e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1210 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAEDEFVYWPNKDEPINCESFKVTLMAEEH 1289
Cdd:cd17669     1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFVYWPNKDEPINCETFKVTLIAEEH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1290 KCLSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTFELISVIKEEAANRDGPMIVHDEHGGVTAGTFCAL 1369
Cdd:cd17669    81 KCLSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTFELISIIKEEAANRDGPMIVHDEHGGVTAGTFCAL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 332205945 1370 TTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKVIL 1413
Cdd:cd17669   161 TTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
alpha_CARP_receptor_like cd03122
Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related ...
 45-298 1.84e-115

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: 362.83  E-value: 1.84e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945   45 NQKNWGKKYPTCNS-PKQSPINIDEDlTQVNVN-LKKLKFQGWDKTSLEnTFIHNTGKTVEINLTN---DYRVSGGVSEM 119
Cdd:cd03122     1 NPKHWAKKYPACGEgRQQSPIDIVED-TQVQRQgLQPLHFDGYEELTAS-TTLENTGKTVILRLEGnssDPFVSGGPLLG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  120 VFKASKITFHWGKCNMssDGSEHSLEGQKFPLEMQIYCFDADRFSSFEeAVKGKGKLRALSILFEVGTEENLDFKAIIDG 199
Cdd:cd03122    79 RYKFSEITFHWGTCNS--DGSEHSIDGHKFPLEMQILHRNTDFFDSFE-AIKSPGGVLALAYLFELSHEDNPFLDPIIEG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  200 VESVSRFGKQAALDPFILLNLLPNSTDKYYIYNGSLTSPPCTDTVDWIVFKDTVSISESQLAVFCEVLTMQQSGyVMLMD 279
Cdd:cd03122   156 LRNVSRPGKEVELPPFPLSDLLPPFTDKYYSYEGSLTTPPCSETVEWIVFREPVPISSRQLEAFRELLTRRQDG-VMSGD 234

                         250
                  ....*....|....*....
gi 332205945  280 YLQNNFREQQYKFSRQVFS 298
Cdd:cd03122   235 YLPNNGRPQQPLGSRTVFS 253
fn3 pfam00041
Fibronectin type III domain;
313-401 2.24e-10

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 58.20  E-value: 2.24e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945   313 SEPENVQADPENYTSLLVTWERPRVVYDTmIEKFAVLYQQLDGEDQtKHEFLTDGYQDlGAILNNLLPNMSYVLQIVAIC 392
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGP-ITGYEVEYRPKNSGEP-WNEITVPGTTT-SVTLTGLKPGTEYEVRVQAVN 77


                   ....*....
gi 332205945   393 TNGlYGKYS 401
Cdd:pfam00041   78 GGG-EGPPS 85
 
Name Accession Description Interval E-value
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 857-1127 2.39e-166

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: 499.56  E-value: 2.39e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  857 FTEEFEEVQSCTVDLGITADSSNHPDNKHKNRYINIVAYDHSRVKLAQLAEKDGKLTDYINANYVDGYNRPKAYIAAQGP 936
Cdd:cd17667     1 FSEDFEEVQRCTADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSKHSDYINANYVDGYNKAKAYIATQGP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  937 LKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQVLAYYTVRNFTLRNTKIKKGSQ- 1015
Cdd:cd17667    81 LKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTKVKKGQKg 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1016 --KGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKAAYAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVN 1093
Cdd:cd17667   161 npKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVN 240

                         250       260       270
                  ....*....|....*....|....*....|....
gi 332205945 1094 IFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAIL 1127
Cdd:cd17667   241 VLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 274
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 1210-1413 6.44e-157

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: 471.79  E-value: 6.44e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1210 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAEDEFVYWPNKDEPINCESFKVTLMAEEH 1289
Cdd:cd17669     1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFVYWPNKDEPINCETFKVTLIAEEH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1290 KCLSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTFELISVIKEEAANRDGPMIVHDEHGGVTAGTFCAL 1369
Cdd:cd17669    81 KCLSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTFELISIIKEEAANRDGPMIVHDEHGGVTAGTFCAL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 332205945 1370 TTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKVIL 1413
Cdd:cd17669   161 TTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
856-1124 1.52e-116

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 365.83  E-value: 1.52e-116
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945    856 GFTEEFEEVQSCTVDLgITADSSNHPDNKHKNRYINIVAYDHSRVKLAQLaekDGKLTDYINANYVDGYNRPKAYIAAQG 935
Cdd:smart00194    1 GLEEEFEKLDRLKPDD-ESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPP---PGEGSDYINASYIDGPNGPKAYIATQG 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945    936 PLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSE--EYGNFLVTQKSVQVLAYYTVRNFTLRNTkikkg 1013
Cdd:smart00194   77 PLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEplTYGDITVTLKSVEKVDDYTIRTLEVTNT----- 151

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945   1014 sqkGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKAAYAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVN 1093
Cdd:smart00194  152 ---GCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVD 228

                           250       260       270
                    ....*....|....*....|....*....|.
gi 332205945   1094 IFGFLKHIRSQRNYLVQTEEQYVFIHDTLVE 1124
Cdd:smart00194  229 IFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
alpha_CARP_receptor_like cd03122
Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related ...
 45-298 1.84e-115

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: 362.83  E-value: 1.84e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945   45 NQKNWGKKYPTCNS-PKQSPINIDEDlTQVNVN-LKKLKFQGWDKTSLEnTFIHNTGKTVEINLTN---DYRVSGGVSEM 119
Cdd:cd03122     1 NPKHWAKKYPACGEgRQQSPIDIVED-TQVQRQgLQPLHFDGYEELTAS-TTLENTGKTVILRLEGnssDPFVSGGPLLG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  120 VFKASKITFHWGKCNMssDGSEHSLEGQKFPLEMQIYCFDADRFSSFEeAVKGKGKLRALSILFEVGTEENLDFKAIIDG 199
Cdd:cd03122    79 RYKFSEITFHWGTCNS--DGSEHSIDGHKFPLEMQILHRNTDFFDSFE-AIKSPGGVLALAYLFELSHEDNPFLDPIIEG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  200 VESVSRFGKQAALDPFILLNLLPNSTDKYYIYNGSLTSPPCTDTVDWIVFKDTVSISESQLAVFCEVLTMQQSGyVMLMD 279
Cdd:cd03122   156 LRNVSRPGKEVELPPFPLSDLLPPFTDKYYSYEGSLTTPPCSETVEWIVFREPVPISSRQLEAFRELLTRRQDG-VMSGD 234

                         250
                  ....*....|....*....
gi 332205945  280 YLQNNFREQQYKFSRQVFS 298
Cdd:cd03122   235 YLPNNGRPQQPLGSRTVFS 253
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
883-1124 6.32e-112

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 352.31  E-value: 6.32e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945   883 NKHKNRYINIVAYDHSRVKLaqlaEKDGKLTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNL 962
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKL----TGDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTEL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945   963 VEKGRRKCDQYWP--ADGSEEYGNFLVT-QKSVQVLAYYTVRNFTLRNtkikkgsqKGRPSGRVVTQYHYTQWPDMGVPE 1039
Cdd:pfam00102   77 EEKGREKCAQYWPeeEGESLEYGDFTVTlKKEKEDEKDYTVRTLEVSN--------GGSEETRTVKHFHYTGWPDHGVPE 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  1040 YSLPVLTFVRKAAYAKRHA-VGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFI 1118
Cdd:pfam00102  149 SPNSLLDLLRKVRKSSLDGrSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFL 228


                   ....*.
gi 332205945  1119 HDTLVE 1124
Cdd:pfam00102  229 YDAILE 234
Carb_anhydrase smart01057
Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse ...
 38-295 3.28e-87

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: 284.21  E-value: 3.28e-87
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945     38 WSYTGALNQKNWGKKYPT-CNSPKQSPINIDEDLTQVNVNLKKLKFQgWDKTSleNTFIHNTGKTVEINL-TNDYRVSGG 115
Cdd:smart01057    1 WGYEGKNGPEHWGKLDPPfCGGKRQSPIDIVTAEAQYDPSLKPLKLS-YDQPT--AKRILNNGHTVQVNFdDDGSTLSGG 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945    116 VSEMVFKASKITFHWGKCNmsSDGSEHSLEGQKFPLEMQIYCFDADrfSSFEEAVKGKGKLRALSILFEVGTEENLDFKA 195
Cdd:smart01057   78 PLPGRYRLKQFHFHWGGSD--SEGSEHTIDGKRFPLELHLVHYNSK--GSFSEAVSKPGGLAVVAVFFKVGAEENPALQA 153

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945    196 IIDGVESVSRFGKQAALDPFILLNLLPNSTDKYYIYNGSLTSPPCTDTVDWIVFKDTVSISESQLAVFCEVLTMQQSgyv 275
Cdd:smart01057  154 ILDHLPLIKYKGQETELTPFDLSSLLPASTRHYYTYNGSLTTPPCSEGVTWIVFKEPITISTEQLEKFRTLLPMEGN--- 230

                           250       260
                    ....*....|....*....|
gi 332205945    276 mlmDYLQNNFREQQYKFSRQ 295
Cdd:smart01057  231 ---EPLVNNARPLQPLNGRV 247
Carb_anhydrase pfam00194
Eukaryotic-type carbonic anhydrase;
44-300 3.31e-85

Eukaryotic-type carbonic anhydrase;


Pssm-ID: 459707 [Multi-domain]  Cd Length: 252  Bit Score: 278.77  E-value: 3.31e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945    44 LNQKNWGKKYPTCNSPKQSPINIDEDLTQVNVNLKKLKFQGWDKTSLENTfIHNTGKTVEINLTNDYR--VSGGVSEMVF 121
Cdd:pfam00194    1 LGPEHWGKVYPSCGGKRQSPINIDTRKVRYDPSLPPLTFQGYDVPPGKNT-LTNNGHTVQVSLDDGDPstISGGPLATRY 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945   122 KASKITFHWGKCNmsSDGSEHSLEGQKFPLEMQIYCFDADRfSSFEEAVKGKGKLRALSILFEVGTEENLDFKAIIDGVE 201
Cdd:pfam00194   80 RLVQFHFHWGSTD--SRGSEHTIDGKRYPAELHIVHYNSKY-KSFDEAAKHPDGLAVLGVFFEVGDENNPYLQPIVSALD 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945   202 SVSRFGKQAALDPFILLNLLPNSTDKYYIYNGSLTSPPCTDTVDWIVFKDTVSISESQLAVFCEVLTMQQSGYvmlMDYL 281
Cdd:pfam00194  157 NIKYKGKSVLLPPFDLSDLLPEDLTSYYTYNGSLTTPPCSESVTWIVFKEPISISEEQLEAFRTLLFSDGGEE---PRPL 233

                          250
                   ....*....|....*....
gi 332205945   282 QNNFREQQYKFSRQVFSSY 300
Cdd:pfam00194  234 VNNFRPTQPLNGRVVFASF 252
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1155-1413 9.10e-77

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 254.89  E-value: 9.10e-77
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945   1155 KLEKQFQLLSQSNIQQSDYSAALKQCNREKNRTSSIIPVERSRVGISSLSGEGTDYINASYIMGYYQSNEFIITQHPLLH 1234
Cdd:smart00194    1 GLEEEFEKLDRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGPLPS 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945   1235 TIKDFWRMIWDHNAQLVVMI-PDGQNMAEDEFVYWPNK-DEPINCESFKVTLMAEEHKclsneEKLIIQDFILEATQDDY 1312
Cdd:smart00194   81 TVEDFWRMVWEQKVTVIVMLtELVEKGREKCAQYWPDEeGEPLTYGDITVTLKSVEKV-----DDYTIRTLEVTNTGCSE 155

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945   1313 VLEVRHFQCPKWP---NPDSPISkTFELISVIKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAK 1389
Cdd:smart00194  156 TRTVTHYHYTNWPdhgVPESPES-ILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVK 234

                           250       260
                    ....*....|....*....|....
gi 332205945   1390 MINLMRPGVFADIEQYQFLYKVIL 1413
Cdd:smart00194  235 ELRSQRPGMVQTEEQYIFLYRAIL 258
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1181-1413 7.32e-75

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 248.70  E-value: 7.32e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  1181 NREKNRTSSIIPVERSRVGISSLSGeGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNM 1260
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPG-PSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  1261 A-EDEFVYWPNK-DEPINCESFKVTLMAEEhkclSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPN---PDSPISkTF 1335
Cdd:pfam00102   80 GrEKCAQYWPEEeGESLEYGDFTVTLKKEK----EDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDhgvPESPNS-LL 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332205945  1336 ELISVIKE-EAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKVIL 1413
Cdd:pfam00102  155 DLLRKVRKsSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233
PHA02738 PHA02738
hypothetical protein; Provisional
 858-1134 6.19e-54

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 191.68  E-value: 6.19e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  858 TEEFEEVQSCTVDLGITADSSNhpdnKHKNRYINIVAYDHSRVKLAqlAEKDgkLTDYINANYVDGYNRPKAYIAAQGPL 937
Cdd:PHA02738   28 TREHQKVISEKVDGTFNAEKKN----RKLNRYLDAVCFDHSRVILP--AERN--RGDYINANYVDGFEYKKKFICGQAPT 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  938 KSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWP--ADGSEEYGNFLVTQKSVQVLAYYTVRNFTLRNtkikkgsq 1015
Cdd:PHA02738  100 RQTCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSdvEQGSIRFGKFKITTTQVETHPHYVKSTLLLTD-------- 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1016 kGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFV------RKAAYAKRHAVG-------PVVVHCSAGVGRTGTYIVLDSM 1082
Cdd:PHA02738  172 -GTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVlevrqcQKELAQESLQIGhnrlqppPIVVHCNAGLGRTPCYCVVDIS 250

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 332205945 1083 LQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAILSKETEVL 1134
Cdd:PHA02738  251 ISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAVKRYVNLTVNKVS 302
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
858-1118 7.24e-40

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 149.86  E-value: 7.24e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  858 TEEFEEVQSCTVDLGITADSSNHPDN---KHKNRYINIVAYDHSRVklaqlaEKDGKltdYINANYVDGYNrPKAYIAAQ 934
Cdd:COG5599    14 EKINSRLSTLTNELAPSHNDPQYLQNingSPLNRFRDIQPYKETAL------RANLG---YLNANYIQVIG-NHRYIATQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  935 GPLKSTAEDFWRMIWEHNVEVIVMITNLVE--KGRRKCDQYWPADGseEYGNFLVTQKSVQVlaYYTVRNFTLRNTKIK- 1011
Cdd:COG5599    84 YPLEEQLEDFFQMLFDNNTPVLVVLASDDEisKPKVKMPVYFRQDG--EYGKYEVSSELTES--IQLRDGIEARTYVLTi 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1012 KGS-QKGRPsgrvVTQYHYTQWPDMGVP--EYSLPVLTFVRKAAYAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQ- 1087
Cdd:COG5599   160 KGTgQKKIE----IPVLHVKNWPDHGAIsaEALKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINa 235

                         250       260       270
                  ....*....|....*....|....*....|...
gi 332205945 1088 -HEGTVNIFGFLKHIRSQRNY-LVQTEEQYVFI 1118
Cdd:COG5599   236 lVQITLSVEEIVIDMRTSRNGgMVQTSEQLDVL 268
Cah COG3338
Carbonic anhydrase [Inorganic ion transport and metabolism];
38-263 1.53e-32

Carbonic anhydrase [Inorganic ion transport and metabolism];


Pssm-ID: 442567 [Multi-domain]  Cd Length: 247  Bit Score: 127.31  E-value: 1.53e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945   38 WSYTGALNQKNWGK---KYPTCNS-PKQSPINIDedlTQVNVNLKKLKFQgWDKTSLEntfIHNTGKTVEINL-TNDYRV 112
Cdd:COG3338    28 WSYEGETGPEHWGElspEFATCATgKNQSPIDIR---TAIKADLPPLKFD-YKPTPLE---IVNNGHTIQVNVdPGSTLT 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  113 SGGVsemVFKASKITFHwgkcnmssDGSEHSLEGQKFPLEMQiycF---DADrfssfeeavkgkGKLRALSILFEVGtEE 189
Cdd:COG3338   101 VDGK---RYELKQFHFH--------TPSEHTINGKSYPMEAH---LvhkDAD------------GELAVVGVLFEEG-AE 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332205945  190 NLDFKAIIDGVESvsRFGKQAALD-PFILLNLLPNSTDkYYIYNGSLTSPPCTDTVDWIVFKDTVSISESQLAVF 263
Cdd:COG3338   154 NPALAKLWANLPL--EAGEEVALDaTIDLNDLLPEDRS-YYRYSGSLTTPPCSEGVLWIVLKQPITVSAEQIEAF 225
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 1174-1412 9.71e-29

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 118.59  E-value: 9.71e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1174 SAALKQCNREKNRTSSIIPVERSRVGISS------------------LSGEGTD--YINASYIMGYYQSNEFIITQHPLL 1233
Cdd:PHA02746   44 NHFLKKENLKKNRFHDIPCWDHSRVVINAheslkmfdvgdsdgkkieVTSEDNAenYIHANFVDGFKEANKFICAQGPKE 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1234 HTIKDFWRMIWDHNAQLVVMIPDGQNMAEDEFVYWPN-KDEPINCESFKVTLMAEEHKCLSNEEKLIIQDFILEATQddy 1312
Cdd:PHA02746  124 DTSEDFFKLISEHESQVIVSLTDIDDDDEKCFELWTKeEDSELAFGRFVAKILDIIEELSFTKTRLMITDKISDTSR--- 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1313 vlEVRHFQCPKWP---NPDSPiSKTFELISVIKEEAA----------NRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKE 1379
Cdd:PHA02746  201 --EIHHFWFPDWPdngIPTGM-AEFLELINKVNEEQAelikqadndpQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKE 277

                         250       260       270
                  ....*....|....*....|....*....|...
gi 332205945 1380 NSVDVYQVAKMINLMRPGVFADIEQYQFLYKVI 1412
Cdd:PHA02746  278 KEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
fn3 pfam00041
Fibronectin type III domain;
313-401 2.24e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 58.20  E-value: 2.24e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945   313 SEPENVQADPENYTSLLVTWERPRVVYDTmIEKFAVLYQQLDGEDQtKHEFLTDGYQDlGAILNNLLPNMSYVLQIVAIC 392
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGP-ITGYEVEYRPKNSGEP-WNEITVPGTTT-SVTLTGLKPGTEYEVRVQAVN 77


                   ....*....
gi 332205945   393 TNGlYGKYS 401
Cdd:pfam00041   78 GGG-EGPPS 85
PLN02179 PLN02179
carbonic anhydrase
 49-253 5.90e-09

carbonic anhydrase


Pssm-ID: 177835  Cd Length: 235  Bit Score: 58.07  E-value: 5.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945   49 WGKKYP---TCNSPK-QSPInideDLTQVNVNLkkLKFQGWDKT-SLENTFIHNTGKTVEINLTNDyrvsggvsemvfkA 123
Cdd:PLN02179   50 WGKLNPqwkVCSTGKyQSPI----DLTDERVSL--IHDQALSRHyKPAPAVIQSRGHDVMVSWKGD-------------A 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  124 SKITFHWG-----KCNMSSDgSEHSLEGQKFPLEMQIYCFDAdrfssfeeavkgKGKLRALSILFEVGtEENLDFKAIID 198
Cdd:PLN02179  111 GKITIHQTdyklvQCHWHSP-SEHTINGTSYDLELHMVHTSA------------SGKTAVVGVLYKLG-EPDEFLTKLLN 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 332205945  199 GVESVsrfGKQ----AALDPfillNLLPNSTDKYYIYNGSLTSPPCTDTVDWIVFKDTV 253
Cdd:PLN02179  177 GIKGV---GKKeinlGIVDP----RDIRFETNNFYRYIGSLTIPPCTEGVIWTVVKRVV 228
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 313-406 3.39e-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: 3.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  313 SEPENVQADPENYTSLLVTWERPRvVYDTMIEKFAVLYQQLDGEDQTKHEflTDGYQDLGAILNNLLPNMSYVLQIVAIC 392
Cdd:cd00063     2 SPPTNLRVTDVTSTSVTLSWTPPE-DDGGPITGYVVEYREKGSGDWKEVE--VTPGSETSYTLTGLKPGTEYEFRVRAVN 78

                          90
                  ....*....|....
gi 332205945  393 TNGlYGKYSDQLIV 406
Cdd:cd00063    79 GGG-ESPPSESVTV 91
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 313-395 7.29e-06

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: 45.68  E-value: 7.29e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945    313 SEPENVQADPENYTSLLVTWERPRvvyDTMIEKFAVLYQQLDGEDQTKHEFLTDGYQDLGAILNNLLPNMSYVLQIVAIC 392
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPP---DDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78


                    ...
gi 332205945    393 TNG 395
Cdd:smart00060   79 GAG 81
 
Name Accession Description Interval E-value
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 857-1127 2.39e-166

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: 499.56  E-value: 2.39e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  857 FTEEFEEVQSCTVDLGITADSSNHPDNKHKNRYINIVAYDHSRVKLAQLAEKDGKLTDYINANYVDGYNRPKAYIAAQGP 936
Cdd:cd17667     1 FSEDFEEVQRCTADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSKHSDYINANYVDGYNKAKAYIATQGP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  937 LKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQVLAYYTVRNFTLRNTKIKKGSQ- 1015
Cdd:cd17667    81 LKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTKVKKGQKg 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1016 --KGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKAAYAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVN 1093
Cdd:cd17667   161 npKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVN 240

                         250       260       270
                  ....*....|....*....|....*....|....
gi 332205945 1094 IFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAIL 1127
Cdd:cd17667   241 VLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 274
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 915-1123 3.04e-157

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: 472.93  E-value: 3.04e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  915 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQV 994
Cdd:cd17668     1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  995 LAYYTVRNFTLRNTKIKKGSQKGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKAAYAKRHAVGPVVVHCSAGVGRTG 1074
Cdd:cd17668    81 LAYYTVRNFTLRNTKIKKGSQKGRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVGPVVVHCSAGVGRTG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 332205945 1075 TYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLV 1123
Cdd:cd17668   161 TYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 1210-1413 6.44e-157

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: 471.79  E-value: 6.44e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1210 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAEDEFVYWPNKDEPINCESFKVTLMAEEH 1289
Cdd:cd17669     1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFVYWPNKDEPINCETFKVTLIAEEH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1290 KCLSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTFELISVIKEEAANRDGPMIVHDEHGGVTAGTFCAL 1369
Cdd:cd17669    81 KCLSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTFELISIIKEEAANRDGPMIVHDEHGGVTAGTFCAL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 332205945 1370 TTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKVIL 1413
Cdd:cd17669   161 TTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 915-1120 1.14e-145

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


Pssm-ID: 350397 [Multi-domain]  Cd Length: 204  Bit Score: 441.79  E-value: 1.14e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  915 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQV 994
Cdd:cd14549     1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTETYGNIQVTLLSTEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  995 LAYYTVRNFTLRNTKIKKGsqKGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKAAYAKRHAVGPVVVHCSAGVGRTG 1074
Cdd:cd14549    81 LATYTVRTFSLKNLKLKKV--KGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAGVGRTG 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 332205945 1075 TYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHD 1120
Cdd:cd14549   159 TYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 1210-1414 4.97e-130

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: 400.21  E-value: 4.97e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1210 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAEDEFVYWPNKDEPINCESFKVTLMAEEH 1289
Cdd:cd17670     1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQGLAEDEFVYWPSREESMNCEAFTVTLISKDR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1290 KCLSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTFELISVIKEEAANRDGPMIVHDEHGGVTAGTFCAL 1369
Cdd:cd17670    81 LCLSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISSTFELINVIKEEALTRDGPTIVHDEFGAVSAGTLCAL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 332205945 1370 TTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKVILS 1414
Cdd:cd17670   161 TTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAMLS 205
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 1210-1410 2.08e-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: 392.84  E-value: 2.08e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1210 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQnMAEDEFVYWPNKDEPINCESFKVTLMAEEH 1289
Cdd:cd14550     1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNE-LNEDEPIYWPTKEKPLECETFKVTLSGEDH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1290 KCLSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTFELISVIKEEAANRDGPMIVHDEHGGVTAGTFCAL 1369
Cdd:cd14550    80 SCLSNEIRLIVRDFILESTQDDYVLEVRQFQCPSWPNPCSPIHTVFELINTVQEWAQQRDGPIVVHDRYGGVQAATFCAL 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 332205945 1370 TTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYK 1410
Cdd:cd14550   160 TTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
856-1124 1.52e-116

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 365.83  E-value: 1.52e-116
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945    856 GFTEEFEEVQSCTVDLgITADSSNHPDNKHKNRYINIVAYDHSRVKLAQLaekDGKLTDYINANYVDGYNRPKAYIAAQG 935
Cdd:smart00194    1 GLEEEFEKLDRLKPDD-ESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPP---PGEGSDYINASYIDGPNGPKAYIATQG 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945    936 PLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSE--EYGNFLVTQKSVQVLAYYTVRNFTLRNTkikkg 1013
Cdd:smart00194   77 PLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEplTYGDITVTLKSVEKVDDYTIRTLEVTNT----- 151

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945   1014 sqkGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKAAYAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVN 1093
Cdd:smart00194  152 ---GCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVD 228

                           250       260       270
                    ....*....|....*....|....*....|.
gi 332205945   1094 IFGFLKHIRSQRNYLVQTEEQYVFIHDTLVE 1124
Cdd:smart00194  229 IFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
alpha_CARP_receptor_like cd03122
Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related ...
 45-298 1.84e-115

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: 362.83  E-value: 1.84e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945   45 NQKNWGKKYPTCNS-PKQSPINIDEDlTQVNVN-LKKLKFQGWDKTSLEnTFIHNTGKTVEINLTN---DYRVSGGVSEM 119
Cdd:cd03122     1 NPKHWAKKYPACGEgRQQSPIDIVED-TQVQRQgLQPLHFDGYEELTAS-TTLENTGKTVILRLEGnssDPFVSGGPLLG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  120 VFKASKITFHWGKCNMssDGSEHSLEGQKFPLEMQIYCFDADRFSSFEeAVKGKGKLRALSILFEVGTEENLDFKAIIDG 199
Cdd:cd03122    79 RYKFSEITFHWGTCNS--DGSEHSIDGHKFPLEMQILHRNTDFFDSFE-AIKSPGGVLALAYLFELSHEDNPFLDPIIEG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  200 VESVSRFGKQAALDPFILLNLLPNSTDKYYIYNGSLTSPPCTDTVDWIVFKDTVSISESQLAVFCEVLTMQQSGyVMLMD 279
Cdd:cd03122   156 LRNVSRPGKEVELPPFPLSDLLPPFTDKYYSYEGSLTTPPCSETVEWIVFREPVPISSRQLEAFRELLTRRQDG-VMSGD 234

                         250
                  ....*....|....*....
gi 332205945  280 YLQNNFREQQYKFSRQVFS 298
Cdd:cd03122   235 YLPNNGRPQQPLGSRTVFS 253
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
883-1124 6.32e-112

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 352.31  E-value: 6.32e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945   883 NKHKNRYINIVAYDHSRVKLaqlaEKDGKLTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNL 962
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKL----TGDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTEL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945   963 VEKGRRKCDQYWP--ADGSEEYGNFLVT-QKSVQVLAYYTVRNFTLRNtkikkgsqKGRPSGRVVTQYHYTQWPDMGVPE 1039
Cdd:pfam00102   77 EEKGREKCAQYWPeeEGESLEYGDFTVTlKKEKEDEKDYTVRTLEVSN--------GGSEETRTVKHFHYTGWPDHGVPE 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  1040 YSLPVLTFVRKAAYAKRHA-VGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFI 1118
Cdd:pfam00102  149 SPNSLLDLLRKVRKSSLDGrSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFL 228


                   ....*.
gi 332205945  1119 HDTLVE 1124
Cdd:pfam00102  229 YDAILE 234
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 883-1128 2.26e-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: 348.23  E-value: 2.26e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  883 NKHKNRYINIVAYDHSRVKLAQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNL 962
Cdd:cd14553     3 NKPKNRYANVIAYDHSRVILQPIEGVPG--SDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  963 VEKGRRKCDQYWPADGSEEYGNFLVTQKSVQVLAYYTVRNFTLRNTkikkgsqkGRPSGRVVTQYHYTQWPDMGVPEYSL 1042
Cdd:cd14553    81 EERSRVKCDQYWPTRGTETYGLIQVTLLDTVELATYTVRTFALHKN--------GSSEKREVRQFQFTAWPDHGVPEHPT 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1043 PVLTFVRKAAYAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTL 1122
Cdd:cd14553   153 PFLAFLRRVKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDAL 232


                  ....*.
gi 332205945 1123 VEAILS 1128
Cdd:cd14553   233 LEAVTC 238
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 915-1120 7.59e-95

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


Pssm-ID: 350343 [Multi-domain]  Cd Length: 200  Bit Score: 303.82  E-value: 7.59e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  915 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSE--EYGNFLVTQKSV 992
Cdd:cd00047     1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKplEYGDITVTLVSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  993 QVLAYYTVRNFTLRNTKIKKGsqkgrpsgRVVTQYHYTQWPDMGVPEYSLPVLTFVRKAAYAKRHAVGPVVVHCSAGVGR 1072
Cdd:cd00047    81 EELSDYTIRTLELSPKGCSES--------REVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCSAGVGR 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 332205945 1073 TGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHD 1120
Cdd:cd00047   153 TGTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 847-1126 7.71e-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: 304.27  E-value: 7.71e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  847 HVADLHASSG--FTEEFEevqscTVDLG--ITADSSNHPDNKHKNRYINIVAYDHSRVKLAQLAEKDGklTDYINANYVD 922
Cdd:cd14626     6 NIERLKANDGlkFSQEYE-----SIDPGqqFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPG--SDYINANYID 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  923 GYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQVLAYYTVRN 1002
Cdd:cd14626    79 GYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIRGTETYGMIQVTLLDTVELATYSVRT 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1003 FTLRntkiKKGSQKGRPsgrvVTQYHYTQWPDMGVPEYSLPVLTFVRKAAYAKRHAVGPVVVHCSAGVGRTGTYIVLDSM 1082
Cdd:cd14626   159 FALY----KNGSSEKRE----VRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVIDAM 230

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 332205945 1083 LQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAI 1126
Cdd:cd14626   231 LERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLEAA 274
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 888-1119 1.21e-91

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: 295.80  E-value: 1.21e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  888 RYINIVAYDHSRVKLAQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGR 967
Cdd:cd14548     1 RYTNILPYDHSRVKLIPINEEEG--SDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  968 RKCDQYWPADGSE-EYGNFLVTQKSVQVLAYYTVRNFTLrntkikkgsqKGRPSGRVVTQYHYTQWPDMGVPEYSLPVLT 1046
Cdd:cd14548    79 VKCDHYWPFDQDPvYYGDITVTMLSESVLPDWTIREFKL----------ERGDEVRSVRQFHFTAWPDHGVPEAPDSLLR 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332205945 1047 FVRKAAYAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIH 1119
Cdd:cd14548   149 FVRLVRDYIKQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLH 221
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 855-1119 2.04e-91

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


Pssm-ID: 350391 [Multi-domain]  Cd Length: 271  Bit Score: 296.97  E-value: 2.04e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  855 SGFTEEFEEVQSCTVdlGITADSSNHPDNKHKNRYINIVAYDHSRVKLAQLAEKDgkLTDYINANYVDGYNRPKAYIAAQ 934
Cdd:cd14543     3 RGIYEEYEDIRREPP--AGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDE--RTDYINANFMDGYKQKNAYIATQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  935 GPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWP--ADGSEEYGNFLVTQKSVQVLAYYTVRNFTLRNTKIKk 1012
Cdd:cd14543    79 GPLPKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPleEGSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETD- 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1013 gsqkgrpSGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKAAYAKRHAVG-------------PVVVHCSAGVGRTGTYIVL 1079
Cdd:cd14543   158 -------ESRQVTHFQFTSWPDFGVPSSAAALLDFLGEVRQQQALAVKamgdrwkghppgpPIVVHCSAGIGRTGTFCTL 230

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 332205945 1080 DSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIH 1119
Cdd:cd14543   231 DICLSQLEDVGTLNVMQTVRRMRTQRAFSIQTPDQYYFCY 270
Carb_anhydrase smart01057
Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse ...
 38-295 3.28e-87

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: 284.21  E-value: 3.28e-87
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945     38 WSYTGALNQKNWGKKYPT-CNSPKQSPINIDEDLTQVNVNLKKLKFQgWDKTSleNTFIHNTGKTVEINL-TNDYRVSGG 115
Cdd:smart01057    1 WGYEGKNGPEHWGKLDPPfCGGKRQSPIDIVTAEAQYDPSLKPLKLS-YDQPT--AKRILNNGHTVQVNFdDDGSTLSGG 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945    116 VSEMVFKASKITFHWGKCNmsSDGSEHSLEGQKFPLEMQIYCFDADrfSSFEEAVKGKGKLRALSILFEVGTEENLDFKA 195
Cdd:smart01057   78 PLPGRYRLKQFHFHWGGSD--SEGSEHTIDGKRFPLELHLVHYNSK--GSFSEAVSKPGGLAVVAVFFKVGAEENPALQA 153

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945    196 IIDGVESVSRFGKQAALDPFILLNLLPNSTDKYYIYNGSLTSPPCTDTVDWIVFKDTVSISESQLAVFCEVLTMQQSgyv 275
Cdd:smart01057  154 ILDHLPLIKYKGQETELTPFDLSSLLPASTRHYYTYNGSLTTPPCSEGVTWIVFKEPITISTEQLEKFRTLLPMEGN--- 230

                           250       260
                    ....*....|....*....|
gi 332205945    276 mlmDYLQNNFREQQYKFSRQ 295
Cdd:smart01057  231 ---EPLVNNARPLQPLNGRV 247
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 839-1126 5.31e-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: 285.06  E-value: 5.31e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  839 IPIKHFPKHVADLHASSGF--TEEFEevqscTVDLG--ITADSSNHPDNKHKNRYINIVAYDHSRVKLAQLAEKDGklTD 914
Cdd:cd14625     4 IPISELAEHTERLKANDNLklSQEYE-----SIDPGqqFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMG--SD 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  915 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQV 994
Cdd:cd14625    77 YINANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSRGTETYGMIQVTLLDTIE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  995 LAYYTVRNFTLRntkiKKGSQKGRPsgrvVTQYHYTQWPDMGVPEYSLPVLTFVRKAAYAKRHAVGPVVVHCSAGVGRTG 1074
Cdd:cd14625   157 LATFCVRTFSLH----KNGSSEKRE----VRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPPDAGPIVVHCSAGVGRTG 228

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 332205945 1075 TYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAI 1126
Cdd:cd14625   229 CFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEAV 280
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 825-1126 6.79e-86

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


Pssm-ID: 350472 [Multi-domain]  Cd Length: 284  Bit Score: 282.01  E-value: 6.79e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  825 PPTPIFPISDdvgaipikhfpkHVADLHASSG--FTEEFEevqscTVDLG--ITADSSNHPDNKHKNRYINIVAYDHSRV 900
Cdd:cd14624     2 PPIPILELAD------------HIERLKANDNlkFSQEYE-----SIDPGqqFTWEHSNLEVNKPKNRYANVIAYDHSRV 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  901 KLAQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSE 980
Cdd:cd14624    65 LLSAIEGIPG--SDYINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSRGTE 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  981 EYGNFLVTQKSVQVLAYYTVRNFTLrntkIKKGSQKGRPsgrvVTQYHYTQWPDMGVPEYSLPVLTFVRKAAYAKRHAVG 1060
Cdd:cd14624   143 TYGLIQVTLLDTVELATYCVRTFAL----YKNGSSEKRE----VRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPPDAG 214

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332205945 1061 PVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAI 1126
Cdd:cd14624   215 PMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLEAV 280
Carb_anhydrase pfam00194
Eukaryotic-type carbonic anhydrase;
44-300 3.31e-85

Eukaryotic-type carbonic anhydrase;


Pssm-ID: 459707 [Multi-domain]  Cd Length: 252  Bit Score: 278.77  E-value: 3.31e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945    44 LNQKNWGKKYPTCNSPKQSPINIDEDLTQVNVNLKKLKFQGWDKTSLENTfIHNTGKTVEINLTNDYR--VSGGVSEMVF 121
Cdd:pfam00194    1 LGPEHWGKVYPSCGGKRQSPINIDTRKVRYDPSLPPLTFQGYDVPPGKNT-LTNNGHTVQVSLDDGDPstISGGPLATRY 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945   122 KASKITFHWGKCNmsSDGSEHSLEGQKFPLEMQIYCFDADRfSSFEEAVKGKGKLRALSILFEVGTEENLDFKAIIDGVE 201
Cdd:pfam00194   80 RLVQFHFHWGSTD--SRGSEHTIDGKRYPAELHIVHYNSKY-KSFDEAAKHPDGLAVLGVFFEVGDENNPYLQPIVSALD 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945   202 SVSRFGKQAALDPFILLNLLPNSTDKYYIYNGSLTSPPCTDTVDWIVFKDTVSISESQLAVFCEVLTMQQSGYvmlMDYL 281
Cdd:pfam00194  157 NIKYKGKSVLLPPFDLSDLLPEDLTSYYTYNGSLTTPPCSESVTWIVFKEPISISEEQLEAFRTLLFSDGGEE---PRPL 233

                          250
                   ....*....|....*....
gi 332205945   282 QNNFREQQYKFSRQVFSSY 300
Cdd:pfam00194  234 VNNFRPTQPLNGRVVFASF 252
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 882-1127 9.51e-84

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


Pssm-ID: 350478 [Multi-domain]  Cd Length: 237  Bit Score: 274.21  E-value: 9.51e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  882 DNKHKNRYINIVAYDHSRVKLAQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITN 961
Cdd:cd14630     2 ENRNKNRYGNIISYDHSRVRLQLLDGDPH--SDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  962 LVEKGRRKCDQYWPaDGSEEYGNFLVTQKSVQVLAYYTVRNFTLRntkiKKGSQKGRPsgrvVTQYHYTQWPDMGVPEYS 1041
Cdd:cd14630    80 LVEVGRVKCVRYWP-DDTEVYGDIKVTLIETEPLAEYVIRTFTVQ----KKGYHEIRE----IRQFHFTSWPDHGVPCYA 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1042 LPVLTFVRKAAYAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDT 1121
Cdd:cd14630   151 TGLLGFVRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDA 230


                  ....*.
gi 332205945 1122 LVEAIL 1127
Cdd:cd14630   231 ILEACL 236
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 887-1118 9.09e-81

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: 265.14  E-value: 9.09e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  887 NRYINIVAYDHSRVKLAQLAEKdgkLTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKG 966
Cdd:cd14615     1 NRYNNVLPYDISRVKLSVQSHS---TDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  967 RRKCDQYWPADGSEEYGNFLVTQKSVQVLAYYTVRNFTLRNtkiKKGSQKgrpsgRVVTQYHYTQWPDMGVPEYSLPVLT 1046
Cdd:cd14615    78 RTKCEEYWPSKQKKDYGDITVTMTSEIVLPEWTIRDFTVKN---AQTNES-----RTVRHFHFTSWPDHGVPETTDLLIN 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332205945 1047 F---VRKaaYAKRHAV-GPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFI 1118
Cdd:cd14615   150 FrhlVRE--YMKQNPPnSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFL 223
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 825-1133 1.69e-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: 267.27  E-value: 1.69e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  825 PPTPIFPISDDVGaipikhfpKHVADlhASSGFTEEFEEVQSCTVDlgITADSSNHPDNKHKNRYINIVAYDHSRVKLAQ 904
Cdd:cd14621     6 PPLPVDKLEEEIN--------RRMAD--DNKLFREEFNALPACPIQ--ATCEAASKEENKEKNRYVNILPYDHSRVHLTP 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  905 LAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGN 984
Cdd:cd14621    74 VEGVPD--SDYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQGCWTYGN 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  985 FLVTQKSVQVLAYYTVRNFTLRNTkikkGSQKGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKAAYAKRHAVGPVVV 1064
Cdd:cd14621   152 IRVSVEDVTVLVDYTVRKFCIQQV----GDVTNKKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQYAGAIVV 227

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332205945 1065 HCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAILSKETEV 1133
Cdd:cd14621   228 HCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEHYLYGDTEL 296
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 846-1127 6.38e-78

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: 258.82  E-value: 6.38e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  846 KHVADLHASSG--FTEEFE---EVQSCTvdlgitADSSNHPDNKHKNRYINIVAYDHSRVKLAQLAEKDGklTDYINANY 920
Cdd:cd14633     4 QHITQMKCAEGygFKEEYEsffEGQSAP------WDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETS--SDYINGNY 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  921 VDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPaDGSEEYGNFLVTQKSVQVLAYYTV 1000
Cdd:cd14633    76 IDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWP-DDTEIYKDIKVTLIETELLAEYVI 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1001 RNFTLRntkikkgsQKGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKAAYAKRHAVGPVVVHCSAGVGRTGTYIVLD 1080
Cdd:cd14633   155 RTFAVE--------KRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVID 226

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 332205945 1081 SMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAIL 1127
Cdd:cd14633   227 IMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILEACL 273
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 887-1119 1.53e-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: 256.00  E-value: 1.53e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  887 NRYINIVAYDHSRVKLAQLaeKDGKLTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKG 966
Cdd:cd14617     1 NRYNNILPYDSTRVKLSNV--DDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  967 RRKCDQYWPAD-GSEEYGNFLVTQKSVQVLAYYTVRNFtlrntKIKKGSQKGRPsgRVVTQYHYTQWPDMGVPEYSLPVL 1045
Cdd:cd14617    79 RVKCDHYWPADqDSLYYGDLIVQMLSESVLPEWTIREF-----KICSEEQLDAP--RLVRHFHYTVWPDHGVPETTQSLI 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332205945 1046 TFVRKAA-YAKR-HAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIH 1119
Cdd:cd14617   152 QFVRTVRdYINRtPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 227
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 887-1126 6.70e-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: 254.43  E-value: 6.70e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  887 NRYINIVAYDHSRVKLAQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKG 966
Cdd:cd14619     1 NRFRNVLPYDWSRVPLKPIHEEPG--SDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  967 RRKCDQYWPADGSE-EYGNFLVTQKSVQVLAYYTVRNFTLRNTKIKKgsqkgrpsGRVVTQYHYTQWPDMGVPEYSLPVL 1045
Cdd:cd14619    79 RVKCEHYWPLDYTPcTYGHLRVTVVSEEVMENWTVREFLLKQVEEQK--------TLSVRHFHFTAWPDHGVPSSTDTLL 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1046 TF---VRKAAYAKRHAvGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTL 1122
Cdd:cd14619   151 AFrrlLRQWLDQTMSG-GPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCI 229


                  ....
gi 332205945 1123 VEAI 1126
Cdd:cd14619   230 LDFL 233
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 915-1127 7.04e-77

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


Pssm-ID: 350403 [Multi-domain]  Cd Length: 204  Bit Score: 252.92  E-value: 7.04e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  915 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADgSEEYGNFLVTQKSVQV 994
Cdd:cd14555     1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDD-TEVYGDIKVTLVETEP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  995 LAYYTVRNFTLRntkikkgsQKGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKAAYAKRHAVGPVVVHCSAGVGRTG 1074
Cdd:cd14555    80 LAEYVVRTFALE--------RRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAGPIVVHCSAGAGRTG 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 332205945 1075 TYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAIL 1127
Cdd:cd14555   152 CYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILEACL 204
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1155-1413 9.10e-77

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 254.89  E-value: 9.10e-77
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945   1155 KLEKQFQLLSQSNIQQSDYSAALKQCNREKNRTSSIIPVERSRVGISSLSGEGTDYINASYIMGYYQSNEFIITQHPLLH 1234
Cdd:smart00194    1 GLEEEFEKLDRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGPLPS 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945   1235 TIKDFWRMIWDHNAQLVVMI-PDGQNMAEDEFVYWPNK-DEPINCESFKVTLMAEEHKclsneEKLIIQDFILEATQDDY 1312
Cdd:smart00194   81 TVEDFWRMVWEQKVTVIVMLtELVEKGREKCAQYWPDEeGEPLTYGDITVTLKSVEKV-----DDYTIRTLEVTNTGCSE 155

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945   1313 VLEVRHFQCPKWP---NPDSPISkTFELISVIKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAK 1389
Cdd:smart00194  156 TRTVTHYHYTNWPdhgVPESPES-ILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVK 234

                           250       260
                    ....*....|....*....|....
gi 332205945   1390 MINLMRPGVFADIEQYQFLYKVIL 1413
Cdd:smart00194  235 ELRSQRPGMVQTEEQYIFLYRAIL 258
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 889-1124 2.54e-75

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: 249.86  E-value: 2.54e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  889 YINIVAYDHSRVKLAQLaekDGKL-TDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGR 967
Cdd:cd14620     1 YPNILPYDHSRVILSQL---DGIPcSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  968 RKCDQYWPADGSEEYGNFLVTQKSVQVLAYYTVRNFTLRntkiKKGSQKGRPSgRVVTQYHYTQWPDMGVPEYSLPVLTF 1047
Cdd:cd14620    78 EKCYQYWPDQGCWTYGNIRVAVEDCVVLVDYTIRKFCIQ----PQLPDGCKAP-RLVTQLHFTSWPDFGVPFTPIGMLKF 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 332205945 1048 VRKAAYAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVE 1124
Cdd:cd14620   153 LKKVKSVNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1181-1413 7.32e-75

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 248.70  E-value: 7.32e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  1181 NREKNRTSSIIPVERSRVGISSLSGeGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNM 1260
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPG-PSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  1261 A-EDEFVYWPNK-DEPINCESFKVTLMAEEhkclSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPN---PDSPISkTF 1335
Cdd:pfam00102   80 GrEKCAQYWPEEeGESLEYGDFTVTLKKEK----EDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDhgvPESPNS-LL 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332205945  1336 ELISVIKE-EAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKVIL 1413
Cdd:pfam00102  155 DLLRKVRKsSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 878-1119 7.18e-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: 245.90  E-value: 7.18e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  878 SNHPDNKHKNRYINIVAYDHSRVKLAQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIV 957
Cdd:cd14554     1 ANLPCNKFKNRLVNILPYESTRVCLQPIRGVEG--SDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  958 MITNLVEKGRRKCDQYWPADGSEEYGNFLvtqksVQVLAYYTVRNFTLRNTKIKKGSQKgrpSGRVVTQYHYTQWPDMGV 1037
Cdd:cd14554    79 MLTKLREMGREKCHQYWPAERSARYQYFV-----VDPMAEYNMPQYILREFKVTDARDG---QSRTVRQFQFTDWPEQGV 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1038 PEYSLPVLTFVRKA--AYAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQY 1115
Cdd:cd14554   151 PKSGEGFIDFIGQVhkTKEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQY 230


                  ....
gi 332205945 1116 VFIH 1119
Cdd:cd14554   231 QFCY 234
alpha_CA cd00326
Carbonic anhydrase alpha (vertebrate-like) group. Carbonic anhydrases (CAs) are ...
 60-297 8.44e-74

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: 245.27  E-value: 8.44e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945   60 KQSPINIDEDLTQVNVNLKKLKFQGWDKTSLEntfIHNTGKTVEINL-TNDYRVSGGVSEMVFKASKITFHWGKCNmsSD 138
Cdd:cd00326     3 RQSPINIVTSAVVYDPSLPPLNFDYYPTTSLT---LVNNGHTVQVNFdDDGGTLSGGGLPGRYKLVQFHFHWGSEN--SP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  139 GSEHSLEGQKFPLEMQIYCFDADRFSSfeEAVKGKGKLRALSILFEVGTEENLDFKAIIDGVESVSRFGKQAALDPFILL 218
Cdd:cd00326    78 GSEHTIDGKRYPLELHLVHYNSDYYSS--EAAKKPGGLAVLGVFFEVGEKENPFLKKILDALPKIKYKGKETTLPPFDLS 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332205945  219 NLLPNSTDKYYIYNGSLTSPPCTDTVDWIVFKDTVSISESQLAVFCEVLTMQqsgyvmlMDYLQNNFREQQYKFSRQVF 297
Cdd:cd00326   156 DLLPSSLRDYYTYEGSLTTPPCSEGVTWIVFKEPITISKEQLEAFRSLLDRE-------GKPLVNNYRPVQPLNGRVVY 227
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 908-1127 3.32e-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: 243.00  E-value: 3.32e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  908 KDGKLTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADgSEEYGNFLV 987
Cdd:cd14631     8 EDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDD-TEVYGDFKV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  988 TQKSVQVLAYYTVRNFTLrntkikkgSQKGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKAAYAKRHAVGPVVVHCS 1067
Cdd:cd14631    87 TCVEMEPLAEYVVRTFTL--------ERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVHCS 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1068 AGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAIL 1127
Cdd:cd14631   159 AGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACL 218
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 915-1119 7.43e-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: 238.66  E-value: 7.43e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  915 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQV 994
Cdd:cd14551     1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCWTYGNLRVRVEDTVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  995 LAYYTVRNFTLRntkiKKGSQKGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKAAYAKRHAVGPVVVHCSAGVGRTG 1074
Cdd:cd14551    81 LVDYTTRKFCIQ----KVNRGIGEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAGPIVVHCSAGVGRTG 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 332205945 1075 TYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIH 1119
Cdd:cd14551   157 TFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 887-1119 3.72e-71

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


Pssm-ID: 350395 [Multi-domain]  Cd Length: 224  Bit Score: 237.68  E-value: 3.72e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  887 NRYINIVAYDHSRVKLAQlaEKDGKLTDYINANYVDGYN-RPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEK 965
Cdd:cd14547     1 NRYKTILPNEHSRVCLPS--VDDDPLSSYINANYIRGYDgEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  966 gRRKCDQYWPADGSEEYGNFLVTQKSVQVLAYYTVRNFTLRNtkikkGSQKgrpsgRVVTQYHYTQWPDMGVPEYSLPVL 1045
Cdd:cd14547    79 -KEKCAQYWPEEENETYGDFEVTVQSVKETDGYTVRKLTLKY-----GGEK-----RYLKHYWYTSWPDHKTPEAAQPLL 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332205945 1046 TFVRKAAYAKRHAV--GPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIH 1119
Cdd:cd14547   148 SLVQEVEEARQTEPhrGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVH 223
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 915-1127 6.60e-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: 236.10  E-value: 6.60e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  915 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPaDGSEEYGNFLVTQKSVQV 994
Cdd:cd14632     1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWP-DDSDTYGDIKITLLKTET 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  995 LAYYTVRNFTLRntkikkgsQKGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKAAYAKRHAVGPVVVHCSAGVGRTG 1074
Cdd:cd14632    80 LAEYSVRTFALE--------RRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTG 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 332205945 1075 TYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAIL 1127
Cdd:cd14632   152 CYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILEACL 204
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 873-1119 1.50e-69

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


Pssm-ID: 350462 [Multi-domain]  Cd Length: 245  Bit Score: 233.63  E-value: 1.50e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  873 ITADSSNHPDNKHKNRYINIVAYDHSRVKLAQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHN 952
Cdd:cd14614     2 IPHFAADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEG--SDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  953 VEVIVMITNLVEKGRRKCDQYWP-ADGSEEYGNFLVTQKSVQVLAYYTVRNFtlrntKIKKGSQKGRpsgrvVTQYHYTQ 1031
Cdd:cd14614    80 SQIIVMLTQCNEKRRVKCDHYWPfTEEPVAYGDITVEMLSEEEQPDWAIREF-----RVSYADEVQD-----VMHFNYTA 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1032 WPDMGVPEYSL--PVLTFVRKAAYAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLV 1109
Cdd:cd14614   150 WPDHGVPTANAaeSILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMV 229

                         250
                  ....*....|
gi 332205945 1110 QTEEQYVFIH 1119
Cdd:cd14614   230 QTEEQYIFIH 239
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 883-1119 6.24e-69

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: 232.35  E-value: 6.24e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  883 NKHKNRYINIVAYDHSRVKLaQLAEKDGKLTDYINANYVDGYN-------RPKAYIAAQGPLKSTAEDFWRMIWEHNVEV 955
Cdd:cd14544     1 NKGKNRYKNILPFDHTRVIL-KDRDPNVPGSDYINANYIRNENegpttdeNAKTYIATQGCLENTVSDFWSMVWQENSRV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  956 IVMITNLVEKGRRKCDQYWPADG-SEEYGNFlvtqkSVQVLAYYTVRNFTLRNTKIKKGSQKGRPsgRVVTQYHYTQWPD 1034
Cdd:cd14544    80 IVMTTKEVERGKNKCVRYWPDEGmQKQYGPY-----RVQNVSEHDTTDYTLRELQVSKLDQGDPI--REIWHYQYLSWPD 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1035 MGVPEYSLPVLTFVRKA--AYAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEG---TVNIFGFLKHIRSQRNYLV 1109
Cdd:cd14544   153 HGVPSDPGGVLNFLEDVnqRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGldcDIDIQKTIQMVRSQRSGMV 232

                         250
                  ....*....|
gi 332205945 1110 QTEEQYVFIH 1119
Cdd:cd14544   233 QTEAQYKFIY 242
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 887-1123 7.79e-68

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: 228.29  E-value: 7.79e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  887 NRYINIVAYDHSRVKLAQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKG 966
Cdd:cd14618     1 NRYPHVLPYDHSRVRLSQLGGEPH--SDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  967 RRKCDQYWPADGSE-EYGnflvtQKSVQVLAYYTVRNFTLRNTKIKKGSQKGRpsgRVVTQYHYTQWPDMGVPEYSLPVL 1045
Cdd:cd14618    79 RVLCDHYWPSESTPvSYG-----HITVHLLAQSSEDEWTRREFKLWHEDLRKE---RRVKHLHYTAWPDHGIPESTSSLM 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1046 TF---VRKAAYAKRHAvGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTL 1122
Cdd:cd14618   151 AFrelVREHVQATKGK-GPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCI 229


                  .
gi 332205945 1123 V 1123
Cdd:cd14618   230 L 230
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 877-1124 1.45e-66

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


Pssm-ID: 350476 [Multi-domain]  Cd Length: 292  Bit Score: 227.31  E-value: 1.45e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  877 SSNHPDNKHKNRYINIVAYDHSRVKLAQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVI 956
Cdd:cd14628    46 SANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEG--SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIV 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  957 VMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQksvqvLAYYTVRNFTLRNTKIKKgSQKGRpsGRVVTQYHYTQWPDMG 1036
Cdd:cd14628   124 VMLTKLREMGREKCHQYWPAERSARYQYFVVDP-----MAEYNMPQYILREFKVTD-ARDGQ--SRTVRQFQFTDWPEQG 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1037 VPEYSLPVLTFVRKAAYAKRH--AVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQ 1114
Cdd:cd14628   196 VPKSGEGFIDFIGQVHKTKEQfgQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQ 275

                         250
                  ....*....|
gi 332205945 1115 YVFIHDTLVE 1124
Cdd:cd14628   276 YQFCYRAALE 285
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 915-1120 2.98e-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: 222.89  E-value: 2.98e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  915 YINANYVD-GYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSE-EYGNFLVTQKSV 992
Cdd:cd18533     1 YINASYITlPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEgEYGDLTVELVSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  993 QVL--AYYTVRNFTLRNTKIKKgsqkgrpsgRVVTQYHYTQWPDMGVPEYSLPVLTFVRKAAYAKRHA--VGPVVVHCSA 1068
Cdd:cd18533    81 EENddGGFIVREFELSKEDGKV---------KKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRELNDSAslDPPIIVHCSA 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 332205945 1069 GVGRTGTYIVLDSMLQQIQ--HEGTVN-------IFGFLKHIRSQRNYLVQTEEQYVFIHD 1120
Cdd:cd18533   152 GVGRTGTFIALDSLLDELKrgLSDSQDledsedpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 877-1128 1.36e-65

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


Pssm-ID: 350475 [Multi-domain]  Cd Length: 290  Bit Score: 224.23  E-value: 1.36e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  877 SSNHPDNKHKNRYINIVAYDHSRVKLAQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVI 956
Cdd:cd14627    47 SANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEG--SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIV 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  957 VMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQksvqvLAYYTVRNFTLRNTKIKKgSQKGRpsGRVVTQYHYTQWPDMG 1036
Cdd:cd14627   125 VMLTKLREMGREKCHQYWPAERSARYQYFVVDP-----MAEYNMPQYILREFKVTD-ARDGQ--SRTVRQFQFTDWPEQG 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1037 VPEYSLPVLTFVRKAAYAKRH--AVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQ 1114
Cdd:cd14627   197 VPKSGEGFIDFIGQVHKTKEQfgQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDE 276

                         250
                  ....*....|....
gi 332205945 1115 YVFIHDTLVEAILS 1128
Cdd:cd14627   277 YQFCYQAALEYLGS 290
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 915-1119 1.44e-65

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


Pssm-ID: 350405 [Multi-domain]  Cd Length: 201  Bit Score: 220.47  E-value: 1.44e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  915 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPA--DGSEEYGNFLVTQKSV 992
Cdd:cd14557     1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSmeEGSRAFGDVVVKINEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  993 QVLAYYTVRNFTLRNTKIKKgsqkgrpSGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKAAYAKRHAVGPVVVHCSAGVGR 1072
Cdd:cd14557    81 KICPDYIIRKLNINNKKEKG-------SGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGR 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 332205945 1073 TGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIH 1119
Cdd:cd14557   154 TGTYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIH 200
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 877-1128 6.42e-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: 222.29  E-value: 6.42e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  877 SSNHPDNKHKNRYINIVAYDHSRVKLAQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVI 956
Cdd:cd14629    47 SANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEG--SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIV 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  957 VMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQksvqvLAYYTVRNFTLRNTKIKKgSQKGRpsGRVVTQYHYTQWPDMG 1036
Cdd:cd14629   125 VMLTKLREMGREKCHQYWPAERSARYQYFVVDP-----MAEYNMPQYILREFKVTD-ARDGQ--SRTIRQFQFTDWPEQG 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1037 VPEYSLPVLTFVRKAAYAKRH--AVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQ 1114
Cdd:cd14629   197 VPKTGEGFIDFIGQVHKTKEQfgQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQ 276

                         250
                  ....*....|....
gi 332205945 1115 YVFIHDTLVEAILS 1128
Cdd:cd14629   277 YQLCYRAALEYLGS 290
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 859-1124 7.50e-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: 218.16  E-value: 7.50e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  859 EEFEEVQSCTV----DLGITADSSNHPDNKHKNRYINIVAYDHSRVKLAQLAEKDGklTDYINANYVDGYNRPKAYIAAQ 934
Cdd:cd14603     2 GEFSEIRACSAafkaDYVCSTVAGGRKENVKKNRYKDILPYDQTRVILSLLQEEGH--SDYINANFIKGVDGSRAYIATQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  935 GPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWP-ADGSEEYGNFLVTQ-KSVQVLAYYTVRNFTLrntKIKK 1012
Cdd:cd14603    80 GPLSHTVLDFWRMIWQYGVKVILMACREIEMGKKKCERYWAqEQEPLQTGPFTITLvKEKRLNEEVILRTLKV---TFQK 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1013 GSqkgrpsgRVVTQYHYTQWPDMGVPEYSLPVLTFVRKAAYAKRHAVGPVVVHCSAGVGRTGTYIVLDS-----MLQQIQ 1087
Cdd:cd14603   157 ES-------RSVSHFQYMAWPDHGIPDSPDCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYvrqllLTQRIP 229

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 332205945 1088 HEgtVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVE 1124
Cdd:cd14603   230 PD--FSIFDVVLEMRKQRPAAVQTEEQYEFLYHTVAQ 264
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 915-1126 7.88e-62

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


Pssm-ID: 350386 [Multi-domain]  Cd Length: 207  Bit Score: 209.92  E-value: 7.88e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  915 YINANYV--DGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPaDGSEE----YGNFLVT 988
Cdd:cd14538     1 YINASHIriPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWP-DSLNKplicGGRLEVS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  989 QKSVQVLAYYTVRNFTLRNTKIKKGsqkgrpsgRVVTQYHYTQWPDMGVPEYSLPVLTFVRkaaYAKR-HAVGPVVVHCS 1067
Cdd:cd14538    80 LEKYQSLQDFVIRRISLRDKETGEV--------HHITHLNFTTWPDHGTPQSADPLLRFIR---YMRRiHNSGPIVVHCS 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 332205945 1068 AGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAI 1126
Cdd:cd14538   149 AGIGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEVL 207
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 876-1128 6.12e-61

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: 209.74  E-value: 6.12e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  876 DSSNHPDNKHKNRYINIVAYDHSRVKLaQLAEKDGKLTDYINANYVDGY-----NRPKAYIAAQGPLKSTAEDFWRMIWE 950
Cdd:cd14606    11 LEGQRPENKSKNRYKNILPFDHSRVIL-QGRDSNIPGSDYINANYVKNQllgpdENAKTYIASQGCLEATVNDFWQMAWQ 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  951 HNVEVIVMITNLVEKGRRKCDQYWPADGSE-EYGNFLVTQKSVQVLAYYTVRnfTLRNTKIKKGSQKgrpsgRVVTQYHY 1029
Cdd:cd14606    90 ENSRVIVMTTREVEKGRNKCVPYWPEVGMQrAYGPYSVTNCGEHDTTEYKLR--TLQVSPLDNGELI-----REIWHYQY 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1030 TQWPDMGVPEYSLPVLTF---VRKAAYAKRHAvGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGT---VNIFGFLKHIRS 1103
Cdd:cd14606   163 LSWPDHGVPSEPGGVLSFldqINQRQESLPHA-GPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVRA 241

                         250       260
                  ....*....|....*....|....*
gi 332205945 1104 QRNYLVQTEEQYVFIHDTLVEAILS 1128
Cdd:cd14606   242 QRSGMVQTEAQYKFIYVAIAQFIET 266
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 887-1119 8.31e-61

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


Pssm-ID: 350464 [Multi-domain]  Cd Length: 224  Bit Score: 207.84  E-value: 8.31e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  887 NRYINIVAYDHSRVKLAQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKG 966
Cdd:cd14616     1 NRFPNIKPYNNNRVKLIADAGVPG--SDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  967 RRKCDQYWPADGS--EEYGNFLVTQksvqvLAYYTVRNFTLRNTKIKKGSQKgrpsgRVVTQYHYTQWPDMGVPEYSLPV 1044
Cdd:cd14616    79 RIRCHQYWPEDNKpvTVFGDIVITK-----LMEDVQIDWTIRDLKIERHGDY-----MMVRQCNFTSWPEHGVPESSAPL 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332205945 1045 LTFVRKAAYAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIH 1119
Cdd:cd14616   149 IHFVKLVRASRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLH 223
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 915-1123 1.55e-60

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: 206.35  E-value: 1.55e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  915 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQV 994
Cdd:cd14552     1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGSVSSGDITVELKDQTD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  995 LAYYTVRNFTLRNTKIKKgsqkgrpsGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKAAYAKRHA-VGPVVVHCSAGVGRT 1073
Cdd:cd14552    81 YEDYTLRDFLVTKGKGGS--------TRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQSgNHPITVHCSAGAGRT 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 332205945 1074 GTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLV 1123
Cdd:cd14552   153 GTFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVVQ 202
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 915-1119 2.50e-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: 205.73  E-value: 2.50e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  915 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEE--YGNFLVTQKSV 992
Cdd:cd14542     1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQlqFGPFKISLEKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  993 QVLAyytvRNFTLRNTKIKKGSQKgrpsgRVVTQYHYTQWPDMGVPEYSLPVLTFVRKAAYAKRHAVGPVVVHCSAGVGR 1072
Cdd:cd14542    81 KRVG----PDFLIRTLKVTFQKES-----RTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDVPICVHCSAGCGR 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 332205945 1073 TGTYIVLDSMLQQIQHEG---TVNIFGFLKHIRSQRNYLVQTEEQYVFIH 1119
Cdd:cd14542   152 TGTICAIDYVWNLLKTGKipeEFSLFDLVREMRKQRPAMVQTKEQYELVY 201
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 884-1117 4.01e-60

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


Pssm-ID: 350393 [Multi-domain]  Cd Length: 231  Bit Score: 206.09  E-value: 4.01e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  884 KHKNRYINIVAYDHSRVKLaqlaeKDGKlTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLV 963
Cdd:cd14545     1 LNRYRDRDPYDHDRSRVKL-----KQGD-NDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLM 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  964 EKGRRKCDQYWPADGSE----EYGNFLVTQKSVQVLAYYTVRNFTLRNTKIkkgsqkgrPSGRVVTQYHYTQWPDMGVPE 1039
Cdd:cd14545    75 EKGQIKCAQYWPQGEGNamifEDTGLKVTLLSEEDKSYYTVRTLELENLKT--------QETREVLHFHYTTWPDFGVPE 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1040 YSLPVLTF---VRKAAYAKRHaVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGT--VNIFGFLKHIRSQRNYLVQTEEQ 1114
Cdd:cd14545   147 SPAAFLNFlqkVRESGSLSSD-VGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYRMGLIQTPDQ 225


                  ...
gi 332205945 1115 YVF 1117
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 3.16e-59

Carbonic anhydrase alpha, isozymes VI, IX, XII and XIV. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Alpha CAs are mostly monomeric enzymes. The zinc ion is complexed by three histidine residues. This sub-family comprises the secreted CA VI, which is found in saliva, for example, and the membrane proteins CA IX, XII, and XIV.


Pssm-ID: 239397 [Multi-domain]  Cd Length: 248  Bit Score: 204.08  E-value: 3.16e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945   46 QKNWGKKYPTCNSPKQSPINIDEDLTQVNVNLKKLKFQGWDKTSLENTFIHNTGKTVEINLTNDYRVSGGVSEmVFKASK 125
Cdd:cd03123     2 EDHWPKKYPACGGKRQSPIDIQTDIVQFDPSLPPLELVGYDLPGTEEFTLTNNGHTVQLSLPPTMHIRGGPGT-EYTAAQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  126 ITFHWGKCNMSSdGSEHSLEGQKFPLEMQIYCFDADRFSSFEEAVKGKGKLRALSILFEVGTEENLDFKAIIDGVESVSR 205
Cdd:cd03123    81 LHLHWGGRGSLS-GSEHTIDGIRFAAELHIVHYNSDKYSSFDEAADKPDGLAVLAILIEVGYPENTYYEKIISHLHEIKY 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  206 FGKQAALDPFILLNLLPNSTDKYYIYNGSLTSPPCTDTVDWIVFKDTVSISESQLavfcevLTMQQSgyvmLMDY----L 281
Cdd:cd03123   160 KGQETTVPGFNVRELLPEDLSHYYRYEGSLTTPPCYESVLWTVFRDPVTLSKEQL------ETLENT----LMDThnktL 229

                         250
                  ....*....|....*....
gi 332205945  282 QNNFREQQYKFSRQVFSSY 300
Cdd:cd03123   230 QNNYRATQPLNGRVVEASF 248
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 873-1122 4.05e-59

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


Pssm-ID: 350460 [Multi-domain]  Cd Length: 247  Bit Score: 203.91  E-value: 4.05e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  873 ITADSSNHPDNKHKNRYINIVAYDHSRVKLAQLAEKDgKLTDYINANYVDGYN-RPKAYIAAQGPLKSTAEDFWRMIWEH 951
Cdd:cd14612     5 VSPEELDIPGHASKDRYKTILPNPQSRVCLRRAGSQE-EEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  952 NVEVIVMITNLVEKgRRKCDQYWPaDGSEEYGNFLVTQKSVQVLAYYTVRNFTlrntkIKKGSQKgrpsgRVVTQYHYTQ 1031
Cdd:cd14612    84 ECPIIVMITKLKEK-KEKCVHYWP-EKEGTYGRFEIRVQDMKECDGYTIRDLT-----IQLEEES-----RSVKHYWFSS 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1032 WPDMGVPEYSLPVLTFVRKAAYAKRHAV--GPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLV 1109
Cdd:cd14612   152 WPDHQTPESAGPLLRLVAEVEESRQTAAspGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMI 231

                         250
                  ....*....|...
gi 332205945 1110 QTEEQYVFIHDTL 1122
Cdd:cd14612   232 QTSEQYQFLHHTL 244
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 914-1128 1.28e-58

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: 201.02  E-value: 1.28e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  914 DYINANYVDgYNRPKA-----YIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPA-DGSEEYGNFLV 987
Cdd:cd14541     1 DYINANYVN-MEIPGSgivnrYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDlGETMQFGNLQI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  988 TQKSVQVLAYYTVRNFTLRNTKIKKgsqkgrpsGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKAAYAKRHAVGPVVVHCS 1067
Cdd:cd14541    80 TCVSEEVTPSFAFREFILTNTNTGE--------ERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVEPTVVHCS 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 332205945 1068 AGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIhdtlVEAILS 1128
Cdd:cd14541   152 AGIGRTGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFV----CEAILR 208
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 882-1119 2.06e-58

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: 204.01  E-value: 2.06e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  882 DNKHKNRYINIVAYDHSRVKLA-QLAEKDgklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMIT 960
Cdd:cd14604    56 ENVKKNRYKDILPFDHSRVKLTlKTSSQD---SDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMAC 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  961 NLVEKGRRKCDQYWPADGSE--EYGNFLVTQKSVQVLAYYTVRNFTLrntkikkgsqKGRPSGRVVTQYHYTQWPDMGVP 1038
Cdd:cd14604   133 REFEMGRKKCERYWPLYGEEpmTFGPFRISCEAEQARTDYFIRTLLL----------EFQNETRRLYQFHYVNWPDHDVP 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1039 EYSLPVLTFVRKAAYAKRHAVGPVVVHCSAGVGRTGTYIVLD---SMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQY 1115
Cdd:cd14604   203 SSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQY 282


                  ....
gi 332205945 1116 VFIH 1119
Cdd:cd14604   283 ELVH 286
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 888-1124 2.42e-58

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


Pssm-ID: 350471 [Multi-domain]  Cd Length: 228  Bit Score: 201.04  E-value: 2.42e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  888 RYINIVAYDHSRVKLAqlAEKDGKLTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGR 967
Cdd:cd14623     1 RVLQIIPYEFNRVIIP--VKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  968 RKCDQYWPADGSEEYGNFLVTQKSVQVLAYYTVRNFTLRNTKIKKgsqkgrpsGRVVTQYHYTQWPDMGVPEYSLPVLTF 1047
Cdd:cd14623    79 EKCAQYWPSDGSVSYGDITIELKKEEECESYTVRDLLVTNTRENK--------SRQIRQFHFHGWPEVGIPSDGKGMINI 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1048 VrkAAYAKRHAVG---PVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVE 1124
Cdd:cd14623   151 I--AAVQKQQQQSgnhPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 874-1126 3.22e-58

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: 202.57  E-value: 3.22e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  874 TADSSNHPDNKHKNRYINIVAYDHSRVKLAqlAEKDGKLTDYINAN-YVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHN 952
Cdd:cd14609    33 TCSTAQGEANVKKNRNPDFVPYDHARIKLK--AESNPSRSDYINASpIIEHDPRMPAYIATQGPLSHTIADFWQMVWENG 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  953 VEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQVLAY-YTVRNFTLRNTKIKKgsqkgrpsGRVVTQYHYTQ 1031
Cdd:cd14609   111 CTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHIYEVNLVSEHIWCEdFLVRSFYLKNVQTQE--------TRTLTQFHFLS 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1032 WPDMGVPEYSLPVLTFVRKAAYAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQhEGT--VNIFGFLKHIRSQRNYLV 1109
Cdd:cd14609   183 WPAEGIPSSTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMA-KGVkeIDIAATLEHVRDQRPGMV 261

                         250
                  ....*....|....*..
gi 332205945 1110 QTEEQYVFIHDTLVEAI 1126
Cdd:cd14609   262 RTKDQFEFALTAVAEEV 278
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 882-1119 5.83e-58

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: 201.01  E-value: 5.83e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  882 DNKHKNRYINIVAYDHSRVKLAQlAEKDGKLTDYINANYVDGYN-------RPK-AYIAAQGPLKSTAEDFWRMIWEHNV 953
Cdd:cd14605     1 ENKNKNRYKNILPFDHTRVVLHD-GDPNEPVSDYINANIIMPEFetkcnnsKPKkSYIATQGCLQNTVNDFWRMVFQENS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  954 EVIVMITNLVEKGRRKCDQYWPADGS-EEYGNFLVTQKSVQVLAYYTVRNFTLrnTKIKKGSQKgrpsgRVVTQYHYTQW 1032
Cdd:cd14605    80 RVIVMTTKEVERGKSKCVKYWPDEYAlKEYGVMRVRNVKESAAHDYILRELKL--SKVGQGNTE-----RTVWQYHFRTW 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1033 PDMGVPEYSLPVLTFVRKAAYaKRHAV---GPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGT---VNIFGFLKHIRSQRN 1106
Cdd:cd14605   153 PDHGVPSDPGGVLDFLEEVHH-KQESImdaGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRS 231

                         250
                  ....*....|...
gi 332205945 1107 YLVQTEEQYVFIH 1119
Cdd:cd14605   232 GMVQTEAQYRFIY 244
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 1210-1410 2.80e-57

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


Pssm-ID: 350343 [Multi-domain]  Cd Length: 200  Bit Score: 196.74  E-value: 2.80e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1210 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPD----GQNMAEDefvYWPNK-DEPINCESFKVTL 1284
Cdd:cd00047     1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNlvekGREKCER---YWPEEgGKPLEYGDITVTL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1285 MAEEHKclsneEKLIIQDFILEATQDDYVLEVRHFQCPKWPN---PDSPISkTFELISVIKEEAANRDGPMIVHDEHGGV 1361
Cdd:cd00047    78 VSEEEL-----SDYTIRTLELSPKGCSESREVTHLHYTGWPDhgvPSSPED-LLALVRRVRKEARKPNGPIVVHCSAGVG 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 332205945 1362 TAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYK 1410
Cdd:cd00047   152 RTGTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 915-1124 3.70e-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: 3.70e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  915 YINANYVDGY--NRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEE----YGNFLVT 988
Cdd:cd14540     1 YINASHITATvgGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGGEHdaltFGEYKVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  989 QKSVQVLAYYTVRNFTLRNTkikkgsqkgrPSGRVVTQYH--YTQWPDMGVPEYSLPVLTFVRKAAYAKRHAVG------ 1060
Cdd:cd14540    81 TKFSVSSGCYTTTGLRVKHT----------LSGQSRTVWHlqYTDWPDHGCPEDVSGFLDFLEEINSVRRHTNQdvaghn 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 332205945 1061 ---PVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVE 1124
Cdd:cd14540   151 rnpPTLVHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQ 217
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 882-1126 4.33e-57

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: 199.51  E-value: 4.33e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  882 DNKHKNRYINIVAYDHSRVKLAqlAEKDGKLTDYINANYV-DGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMIT 960
Cdd:cd14610    43 ENVQKNRSLAVLPYDHSRIILK--AENSHSHSDYINASPImDHDPRNPAYIATQGPLPATVADFWQMVWESGCVVIVMLT 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  961 NLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQVLAY-YTVRNFTLRNTKIKKgsqkgrpsGRVVTQYHYTQWPDMGVPE 1039
Cdd:cd14610   121 PLAENGVKQCYHYWPDEGSNLYHIYEVNLVSEHIWCEdFLVRSFYLKNLQTNE--------TRTVTQFHFLSWNDQGVPA 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1040 YSLPVLTFVRKAAYAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQI-QHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFI 1118
Cdd:cd14610   193 STRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLNKMaKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFA 272


                  ....*...
gi 332205945 1119 HDTLVEAI 1126
Cdd:cd14610   273 LTAVAEEV 280
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 881-1127 2.18e-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: 196.99  E-value: 2.18e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  881 PDNKHKNRYINIVAYDHSRVKLaqlaekDGKlTDYINANYVD----GYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVI 956
Cdd:cd14600    38 PQNMDKNRYKDVLPYDATRVVL------QGN-EDYINASYVNmeipSANIVNKYIATQGPLPHTCAQFWQVVWEQKLSLI 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  957 VMITNLVEKGRRKCDQYWPaDGSE--EYGNFLVTQKSVQVLAYYTVRNFTLrnTKIKKGSQkgrpsgRVVTQYHYTQWPD 1034
Cdd:cd14600   111 VMLTTLTERGRTKCHQYWP-DPPDvmEYGGFRVQCHSEDCTIAYVFREMLL--TNTQTGEE------RTVTHLQYVAWPD 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1035 MGVPEYSLPVLTFVrKAAYAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQ 1114
Cdd:cd14600   182 HGVPDDSSDFLEFV-NYVRSKRVENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQ 260

                         250
                  ....*....|...
gi 332205945 1115 YVFIhdtlVEAIL 1127
Cdd:cd14600   261 YKFV----CEAIL 269
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 886-1124 4.33e-56

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: 194.67  E-value: 4.33e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  886 KNRYINIVAYDHSRVKLAQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEK 965
Cdd:cd14602     1 KNRYKDILPYDHSRVELSLITSDED--SDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  966 GRRKCDQYWPADGSE--EYGNFLVTQKSVQVLAYYTVRNFtlrntKIKKGSQKgrpsgRVVTQYHYTQWPDMGVPEYSLP 1043
Cdd:cd14602    79 GKKKCERYWAEPGEMqlEFGPFSVTCEAEKRKSDYIIRTL-----KVKFNSET-----RTIYQFHYKNWPDHDVPSSIDP 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1044 VLTFVRKAAYAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQhEGTV----NIFGFLKHIRSQRNYLVQTEEQYVFIH 1119
Cdd:cd14602   149 ILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLK-DGIIpenfSVFSLIQEMRTQRPSLVQTKEQYELVY 227


                  ....*
gi 332205945 1120 DTLVE 1124
Cdd:cd14602   228 NAVIE 232
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 915-1126 6.50e-56

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


Pssm-ID: 350394 [Multi-domain]  Cd Length: 208  Bit Score: 193.04  E-value: 6.50e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  915 YINANYVDGYN-RPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQ 993
Cdd:cd14546     1 YINASTIYDHDpRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEVYHIYEVHLVSEH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  994 VL-AYYTVRNFTLRNTKIKKgsqkgrpsGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKAAYAKRHAVGPVVVHCSAGVGR 1072
Cdd:cd14546    81 IWcDDYLVRSFYLKNLQTSE--------TRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYRGRSCPIVVHCSDGAGR 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 332205945 1073 TGTYIVLDSMLQQIQhEGT--VNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAI 1126
Cdd:cd14546   153 TGTYILIDMVLNRMA-KGAkeIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAEEV 207
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 886-1122 1.33e-55

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


Pssm-ID: 350461 [Multi-domain]  Cd Length: 258  Bit Score: 194.31  E-value: 1.33e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  886 KNRYINIVAYDHSRVKLAQlAEKDGKLTDYINANYVDGYN-RPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVE 964
Cdd:cd14613    28 KNRYKTILPNPHSRVCLTS-PDQDDPLSSYINANYIRGYGgEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEE 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  965 KGRrKCDQYWPADgSEEYGNFLVTQKSVQVLAYYTVRNFTLrntkiKKGSQKgrpsgRVVTQYHYTQWPDMGVPEYSLPV 1044
Cdd:cd14613   107 MNE-KCTEYWPEE-QVTYEGIEITVKQVIHADDYRLRLITL-----KSGGEE-----RGLKHYWYTSWPDQKTPDNAPPL 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1045 LTFVRKAAYAKRHA---VGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDT 1121
Cdd:cd14613   175 LQLVQEVEEARQQAepnCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVHHV 254


                  .
gi 332205945 1122 L 1122
Cdd:cd14613   255 L 255
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 886-1119 1.68e-55

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: 192.83  E-value: 1.68e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  886 KNRYINIVAYDHSRVKLAQLAEKDgKLTDYINANYVDGY-NRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVE 964
Cdd:cd14611     2 KNRYKTILPNPHSRVCLKPKNSND-SLSTYINANYIRGYgGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  965 KGRrKCDQYWPaDGSEEYGNFLVTQKSVQVLAYYTVRNFTLrntkiKKGSQKgrpsgRVVTQYHYTQWPDMGVPEYSLPV 1044
Cdd:cd14611    81 KNE-KCVLYWP-EKRGIYGKVEVLVNSVKECDNYTIRNLTL-----KQGSQS-----RSVKHYWYTSWPDHKTPDSAQPL 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1045 LTFV------RKAAYAKrhavGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFI 1118
Cdd:cd14611   149 LQLMldveedRLASPGR----GPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFV 224


                  .
gi 332205945 1119 H 1119
Cdd:cd14611   225 H 225
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 914-1119 1.52e-54

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


Pssm-ID: 350470 [Multi-domain]  Cd Length: 205  Bit Score: 189.06  E-value: 1.52e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  914 DYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQ 993
Cdd:cd14622     1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEGSVTHGEITIEIKNDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  994 VLAYYTVRNFTLRNTKIKKgsqkgrpsGRVVTQYHYTQWPDMGVPEYSLPVLTFVrKAAYAKRHAVG--PVVVHCSAGVG 1071
Cdd:cd14622    81 LLETISIRDFLVTYNQEKQ--------TRLVRQFHFHGWPEIGIPAEGKGMIDLI-AAVQKQQQQTGnhPIVVHCSAGAG 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 332205945 1072 RTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIH 1119
Cdd:cd14622   152 RTGTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCY 199
PHA02738 PHA02738
hypothetical protein; Provisional
 858-1134 6.19e-54

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 191.68  E-value: 6.19e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  858 TEEFEEVQSCTVDLGITADSSNhpdnKHKNRYINIVAYDHSRVKLAqlAEKDgkLTDYINANYVDGYNRPKAYIAAQGPL 937
Cdd:PHA02738   28 TREHQKVISEKVDGTFNAEKKN----RKLNRYLDAVCFDHSRVILP--AERN--RGDYINANYVDGFEYKKKFICGQAPT 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  938 KSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWP--ADGSEEYGNFLVTQKSVQVLAYYTVRNFTLRNtkikkgsq 1015
Cdd:PHA02738  100 RQTCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSdvEQGSIRFGKFKITTTQVETHPHYVKSTLLLTD-------- 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1016 kGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFV------RKAAYAKRHAVG-------PVVVHCSAGVGRTGTYIVLDSM 1082
Cdd:PHA02738  172 -GTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVlevrqcQKELAQESLQIGhnrlqppPIVVHCNAGLGRTPCYCVVDIS 250

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 332205945 1083 LQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAILSKETEVL 1134
Cdd:PHA02738  251 ISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAVKRYVNLTVNKVS 302
alpha_CA_XII_XIV cd03126
Carbonic anhydrase alpha, isozymes XII and XIV. Carbonic anhydrases (CAs) are zinc-containing ...
 46-300 9.55e-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: 185.81  E-value: 9.55e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945   46 QKNWGKKYPTCNSPKQSPINIDEDLTQVNVNLKKLKFQGWDKTSLENTFIHNTGKTVEINLTNDYRVSGGVSEmvFKASK 125
Cdd:cd03126     2 ENSWPKKYPFCGGVAQSPIDIHTDILQYDSSLPPLEFHGYNVSGTEQFTLTNNGHTVQLSLPPTMHIGGLPFK--YTASQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  126 ITFHWGKCNmSSDGSEHSLEGQKFPLEMQIYCFDADRFSSFEEAVKGKGKLRALSILFEVGtEENLDFKAIIDGVESVSR 205
Cdd:cd03126    80 LHLHWGQRG-SPEGSEHTISGKHFAAELHIVHYNSDKYPDISTAMNKSQGLAVLGILIEVG-PFNPSYEKIFSHLHEVKY 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  206 FGKQAALDPFILLNLLPNSTDKYYIYNGSLTSPPCTDTVDWIVFKDTVSISESQLavfcevLTMQQSGYVMLMD---YLQ 282
Cdd:cd03126   158 KDQKVSVPGFNVQELLPKRLDEYYRYEGSLTTPPCYPSVLWTVFRNPVQISQEQL------LALETALYSTEEDesrEMV 231

                         250
                  ....*....|....*...
gi 332205945  283 NNFREQQYKFSRQVFSSY 300
Cdd:cd03126   232 NNYRQVQPFNERLVFASF 249
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 882-1117 3.25e-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: 183.49  E-value: 3.25e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  882 DNKHKNRYINIVAYDHSRVKLAQlaekDGkltDYINANYVD---GyNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVM 958
Cdd:cd14597     2 ENRKKNRYKNILPYDTTRVPLGD----EG---GYINASFIKmpvG-DEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAM 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  959 ITNLVEKGRRKCDQYWPadgsEEYGNFLVTQKSVQV--LAYYTVRNFTLRNTKIKKgSQKGRPsgRVVTQYHYTQWPDMG 1036
Cdd:cd14597    74 MTQEVEGGKIKCQRYWP----EILGKTTMVDNRLQLtlVRMQQLKNFVIRVLELED-IQTREV--RHITHLNFTAWPDHD 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1037 VPEYSLPVLTFVrkaAYAKR-HAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQY 1115
Cdd:cd14597   147 TPSQPEQLLTFI---SYMRHiHKSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQY 223


                  ..
gi 332205945 1116 VF 1117
Cdd:cd14597   224 IF 225
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 878-1117 6.68e-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: 183.63  E-value: 6.68e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  878 SNHPDNKHKNRYINIVAYDHSRVKLaQLAEkdgklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIV 957
Cdd:cd14607    19 AKYPENRNRNRYRDVSPYDHSRVKL-QNTE-----NDYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVV 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  958 MITNLVEKGRRKCDQYWPADGSEEYG----NFLVTQKSVQVLAYYTVRNFTLRNtkIKKGSQkgrpsgRVVTQYHYTQWP 1033
Cdd:cd14607    93 MLNRIVEKDSVKCAQYWPTDEEEVLSfketGFSVKLLSEDVKSYYTVHLLQLEN--INSGET------RTISHFHYTTWP 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1034 DMGVPEYSLPVLTFVRKAAYAKRHAV--GPVVVHCSAGVGRTGTYIVLDS--MLQQIQHEGTVNIFGFLKHIRSQRNYLV 1109
Cdd:cd14607   165 DFGVPESPASFLNFLFKVRESGSLSPehGPAVVHCSAGIGRSGTFSLVDTclVLMEKKDPDSVDIKQVLLDMRKYRMGLI 244


                  ....*...
gi 332205945 1110 QTEEQYVF 1117
Cdd:cd14607   245 QTPDQLRF 252
alpha_CA_IV_XV_like cd03117
Carbonic anhydrase alpha, CA_IV, CA_XV, like isozymes. Carbonic anhydrases (CAs) are ...
 59-298 8.71e-52

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: 182.47  E-value: 8.71e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945   59 PKQSPINIDEDLTQVNVNLKKLKFQGWDKTSLeNTFIHNTGKTVEINLTNDYRVSGGVSEMVFKASKITFHWGkcNMSSD 138
Cdd:cd03117     2 KRQSPINIVTKKVQYDENLTPFTFTGYDDTTT-NWTITNNGHTVQVTLPDGAKISGGGLPGTYKALQFHFHWG--SNGSP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  139 GSEHSLEGQKFPLEMQIYCFDADrFSSFEEAVKGKGKLRALSILFEVGTEENLDFKAIIDGVESVSRFGKQAALDPFILL 218
Cdd:cd03117    79 GSEHTIDGERYPMELHIVHIKES-YNSLLEALKDSDGLAVLGFFIEEGEEENTNFDPLISALSNIPQKGGSTNLTPFSLR 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  219 NLLP-NSTDKYYIYNGSLTSPPCTDTVDWIVFKDTVSISESQLAVFCEVLTMQQSGYVMLMdylqNNFREQQYKFSRQVF 297
Cdd:cd03117   158 SLLPsVLLTKYYRYNGSLTTPGCNEAVIWTVFEEPIPISRAQLDAFSTVLFFDTDNGQPMV----NNFRPVQPLNGRVVY 233


                  .
gi 332205945  298 S 298
Cdd:cd03117   234 A 234
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 878-1124 9.67e-52

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: 9.67e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  878 SNHPDNKHKNRYINIVAYDHSRVKLAQlaekdgKLTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIV 957
Cdd:cd14608    20 AKLPKNKNRNRYRDVSPFDHSRIKLHQ------EDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVV 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  958 MITNLVEKGRRKCDQYWPADGSEEY----GNFLVTQKSVQVLAYYTVRNFTLRNTKIKKgsqkgrpsGRVVTQYHYTQWP 1033
Cdd:cd14608    94 MLNRVMEKGSLKCAQYWPQKEEKEMifedTNLKLTLISEDIKSYYTVRQLELENLTTQE--------TREILHFHYTTWP 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1034 DMGVPEYSLPVLTFVRK----AAYAKRHavGPVVVHCSAGVGRTGTYIVLDS---MLQQIQHEGTVNIFGFLKHIRSQRN 1106
Cdd:cd14608   166 DFGVPESPASFLNFLFKvresGSLSPEH--GPVVVHCSAGIGRSGTFCLADTcllLMDKRKDPSSVDIKKVLLEMRKFRM 243

                         250
                  ....*....|....*...
gi 332205945 1107 YLVQTEEQYVFIHDTLVE 1124
Cdd:cd14608   244 GLIQTADQLRFSYLAVIE 261
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 915-1120 4.24e-50

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: 176.43  E-value: 4.24e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  915 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPaDGSEEYGNFLVTQKSVQV 994
Cdd:cd14558     1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWG-DEKKTYGDIEVELKDTEK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  995 LAYYTVRNFTLRNTKIKKgsqkgrpsGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKA------AYAKRHAVGPVVVHCSA 1068
Cdd:cd14558    80 SPTYTVRVFEITHLKRKD--------SRTVYQYQYHKWKGEELPEKPKDLVDMIKSIkqklpyKNSKHGRSVPIVVHCSD 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 332205945 1069 GVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHD 1120
Cdd:cd14558   152 GSSRTGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 857-1124 4.83e-49

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


Pssm-ID: 350447 [Multi-domain]  Cd Length: 287  Bit Score: 176.34  E-value: 4.83e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  857 FTEeFEEVQSCTVDLGITadSSNHPDNKHKNRYINIVAYDHSRVKLAQLAEKDgklTDYINANYVDGYNRPKA--YIAAQ 934
Cdd:cd14599    15 FTE-YEQIPKKKADGVFT--TATLPENAERNRIREVVPYEENRVELVPTKENN---TGYINASHIKVTVGGEEwhYIATQ 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  935 GPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADG----SEEYGNFLVTQKSVQVLAYYTVRNFTLRNtkI 1010
Cdd:cd14599    89 GPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKLGskhsSATYGKFKVTTKFRTDSGCYATTGLKVKH--L 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1011 KKGSQkgrpsgRVVTQYHYTQWPDMGVPEYSLPVLTFVRKAAYAKRHAVG----------PVVVHCSAGVGRTGTYIVLD 1080
Cdd:cd14599   167 LSGQE------RTVWHLQYTDWPDHGCPEEVQGFLSYLEEIQSVRRHTNSmldstkncnpPIVVHCSAGVGRTGVVILTE 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 332205945 1081 SMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVE 1124
Cdd:cd14599   241 LMIGCLEHNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQ 284
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 915-1126 5.10e-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: 173.39  E-value: 5.10e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  915 YINANYVDGYNRPKA--YIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWP--ADGSEEYGNFLVTQK 990
Cdd:cd14596     1 YINASYITMPVGEEElfYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPetLQEPMELENYQLRLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  991 SVQVLAYYTVRNFTLrntkikkgSQKGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFVRkaaYAKR-HAVGPVVVHCSAG 1069
Cdd:cd14596    81 NYQALQYFIIRIIKL--------VEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFIC---YMRKvHNTGPIVVHCSAG 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 332205945 1070 VGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAI 1126
Cdd:cd14596   150 IGRAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVL 206
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 914-1127 7.22e-49

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


Pssm-ID: 350449 [Multi-domain]  Cd Length: 212  Bit Score: 173.21  E-value: 7.22e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  914 DYINANYVDG-------YNRpkaYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWP-ADGSEEYGNF 985
Cdd:cd14601     1 DYINANYINMeipsssiINR---YIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPePSGSSSYGGF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  986 LVTQKSVQVLAYYTVRNFTLRNTKikkgSQKGRPsgrvVTQYHYTQWPDMGVPEYSLPVLTFVRKAAYAKRHAVGPVVVH 1065
Cdd:cd14601    78 QVTCHSEEGNPAYVFREMTLTNLE----KNESRP----LTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDEPVVVH 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 332205945 1066 CSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIhdtlVEAIL 1127
Cdd:cd14601   150 CSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFV----CEAIL 207
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 915-1120 7.01e-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: 167.18  E-value: 7.01e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  915 YINANYVDGY-NRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPAD-GSE-EYGNFLVTQKS 991
Cdd:cd14539     1 YINASLIEDLtPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTErGQAlVYGAITVSLQS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  992 VQVLAYYTVRNFTlrntkIKKGSQKGRpsgRVVTQYHYTQWPDMGVPEYSLPVLTF---VRKAAYAKRHAVGPVVVHCSA 1068
Cdd:cd14539    81 VRTTPTHVERIIS-----IQHKDTRLS---RSVVHLQFTTWPELGLPDSPNPLLRFieeVHSHYLQQRSLQTPIVVHCSS 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 332205945 1069 GVGRTGTYIVLDSMLQQIQHE-GTVNIFGFLKHIRSQRNYLVQTEEQYVFIHD 1120
Cdd:cd14539   153 GVGRTGAFCLLYAAVQEIEAGnGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 1131-1418 1.25e-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: 169.53  E-value: 1.25e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1131 TEVLDSHIHAYVNALL-IPGPAGKTKLEKQFQLLSQSNIQQSDYSAALKQCNREKNRTSSIIPVERSRVGISSLSG-EGT 1208
Cdd:cd14628     1 TEVPARNLYAYIQKLTqIETGENVTGMELEFKRLASSKAHTSRFISANLPCNKFKNRLVNIMPYESTRVCLQPIRGvEGS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1209 DYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAEDE-FVYWPnKDEPINCESFKVTLMAE 1287
Cdd:cd14628    81 DYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKcHQYWP-AERSARYQYFVVDPMAE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1288 ehkclSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKT--FELISVI--KEEAANRDGPMIVHDEHGGVTA 1363
Cdd:cd14628   160 -----YNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEgfIDFIGQVhkTKEQFGQDGPISVHCSAGVGRT 234

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 332205945 1364 GTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKVILSLVST 1418
Cdd:cd14628   235 GVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEYLGS 289
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 1180-1413 4.17e-46

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: 166.16  E-value: 4.17e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1180 CNREKNRTSSIIPVERSRVGISSLSG-EGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQ 1258
Cdd:cd14554     5 CNKFKNRLVNILPYESTRVCLQPIRGvEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTKLR 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1259 NMAEDE-FVYWPNkDEPINCESFKVTLMAEehkclSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPisKTFE- 1336
Cdd:cd14554    85 EMGREKcHQYWPA-ERSARYQYFVVDPMAE-----YNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVP--KSGEg 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1337 LISVIKE-----EAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKV 1411
Cdd:cd14554   157 FIDFIGQvhktkEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRA 236


                  ..
gi 332205945 1412 IL 1413
Cdd:cd14554   237 AL 238
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 915-1119 4.54e-46

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


Pssm-ID: 350496 [Multi-domain]  Cd Length: 206  Bit Score: 164.94  E-value: 4.54e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  915 YINANYV---DGYNRPKaYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRR-KCDQYWPAD--GSEEYGNFLVT 988
Cdd:cd17658     1 YINASLVetpASESLPK-FIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTaKCADYFPAEenESREFGRISVT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  989 QKSVQvlayYTVRNFTLRNTKIKKGSQKGRPsgRVVTQYHYTQWPDMGVPEYSLPVLTFVrKAAYAKRHAVGPVVVHCSA 1068
Cdd:cd17658    80 NKKLK----HSQHSITLRVLEVQYIESEEPP--LSVLHIQYPEWPDHGVPKDTRSVRELL-KRLYGIPPSAGPIVVHCSA 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 332205945 1069 GVGRTGTYIVLDSMLQQIQhEG---TVNIFGFLKHIRSQRNYLVQTEEQYVFIH 1119
Cdd:cd17658   153 GIGRTGAYCTIHNTIRRIL-EGdmsAVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 1131-1418 2.58e-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: 2.58e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1131 TEVLDSHIHAYVNALLIPGPAGK-TKLEKQFQLLSQSNIQQSDYSAALKQCNREKNRTSSIIPVERSRVGISSLSG-EGT 1208
Cdd:cd14627     2 TEVPARNLYSYIQKLAQVEVGEHvTGMELEFKRLANSKAHTSRFISANLPCNKFKNRLVNIMPYETTRVCLQPIRGvEGS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1209 DYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAEDE-FVYWPnKDEPINCESFKVTLMAE 1287
Cdd:cd14627    82 DYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGREKcHQYWP-AERSARYQYFVVDPMAE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1288 ehkclSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKT--FELISVI--KEEAANRDGPMIVHDEHGGVTA 1363
Cdd:cd14627   161 -----YNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEgfIDFIGQVhkTKEQFGQDGPISVHCSAGVGRT 235

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 332205945 1364 GTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKVILSLVST 1418
Cdd:cd14627   236 GVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALEYLGS 290
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 874-1119 2.89e-45

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 166.33  E-value: 2.89e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  874 TADSSNHPDNKHKNRYINIVAYDHSRVKLAQlaeKDGKLTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNV 953
Cdd:PHA02747   42 LIANFEKPENQPKNRYWDIPCWDHNRVILDS---GGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHC 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  954 EVIVMIT-NLVEKGRRKCDQYW--PADGSEEYGNFLVTQKSVQVLAYYTVRNFTLRNtKIKKGSQKgrpsgrvVTQYHYT 1030
Cdd:PHA02747  119 SIIVMLTpTKGTNGEEKCYQYWclNEDGNIDMEDFRIETLKTSVRAKYILTLIEITD-KILKDSRK-------ISHFQCS 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1031 QWPDMGVPEYSLPVLTFVR----------KAAYAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKH 1100
Cdd:PHA02747  191 EWFEDETPSDHPDFIKFIKiidinrkksgKLFNPKDALLCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEK 270

                         250
                  ....*....|....*....
gi 332205945 1101 IRSQRNYLVQTEEQYVFIH 1119
Cdd:PHA02747  271 IREQRHAGIMNFDDYLFIQ 289
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 862-1127 3.20e-45

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 166.74  E-value: 3.20e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  862 EEVQSCTVDLGITADSSNHPDNKHKNRYINIVAYDHSRV--------KLAQLAEKDGKL---------TDYINANYVDGY 924
Cdd:PHA02746   30 EHAEVMDIPIRGTTNHFLKKENLKKNRFHDIPCWDHSRVvinaheslKMFDVGDSDGKKievtsednaENYIHANFVDGF 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  925 NRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNlVEKGRRKCDQYW--PADGSEEYGNFLvtqksVQVLAYYTVRN 1002
Cdd:PHA02746  110 KEANKFICAQGPKEDTSEDFFKLISEHESQVIVSLTD-IDDDDEKCFELWtkEEDSELAFGRFV-----AKILDIIEELS 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1003 FTLRNTKIkkgSQKGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFV----------RKAAYAKRHAVGPVVVHCSAGVGR 1072
Cdd:PHA02746  184 FTKTRLMI---TDKISDTSREIHHFWFPDWPDNGIPTGMAEFLELInkvneeqaelIKQADNDPQTLGPIVVHCSAGIGR 260

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 332205945 1073 TGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAIL 1127
Cdd:PHA02746  261 AGTFCAIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKALKYAII 315
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 915-1120 3.36e-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: 3.36e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  915 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMItNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQV 994
Cdd:cd14556     1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVML-NQLDPKDQSCPQYWPDEGSGTYGPIQVEFVSTTI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  995 LAYYTVRNFTLRNTKikkgsqkgRPS--GRVVTQYHYTQWPDMG----VPEYSLPVLTFVRKaaYAKRHAVGPVVVHCSA 1068
Cdd:cd14556    80 DEDVISRIFRLQNTT--------RPQegYRMVQQFQFLGWPRDRdtppSKRALLKLLSEVEK--WQEQSGEGPIVVHCLN 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 332205945 1069 GVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHD 1120
Cdd:cd14556   150 GVGRSGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 883-1124 5.02e-45

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 165.56  E-value: 5.02e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  883 NKHKNRYINIVAYDHSRVKLAQlaeKDGkLTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNL 962
Cdd:PHA02742   52 NMKKCRYPDAPCFDRNRVILKI---EDG-GDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKI 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  963 VEKGRRKCDQYWPAD--GSEEYGNFLVTQKSVQVLAYYTVRNFTLRNTKikkgsqkgrpSGRV--VTQYHYTQWPDMGVP 1038
Cdd:PHA02742  128 MEDGKEACYPYWMPHerGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTN----------TGASldIKHFAYEDWPHGGLP 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1039 EYSLPVLTFVRKAAYAK-----------RHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNY 1107
Cdd:PHA02742  198 RDPNKFLDFVLAVREADlkadvdikgenIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHN 277

                         250
                  ....*....|....*..
gi 332205945 1108 LVQTEEQYVFIHDTLVE 1124
Cdd:PHA02742  278 CLSLPQQYIFCYFIVLI 294
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 1131-1418 6.51e-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: 164.51  E-value: 6.51e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1131 TEVLDSHIHAYVNAL-LIPGPAGKTKLEKQFQLLSQSNIQQSDYSAALKQCNREKNRTSSIIPVERSRVGISSLSG-EGT 1208
Cdd:cd14629     2 TEVPARNLYAHIQKLtQVPPGESVTAMELEFKLLANSKAHTSRFISANLPCNKFKNRLVNIMPYELTRVCLQPIRGvEGS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1209 DYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAEDE-FVYWPnKDEPINCESFKVTLMAE 1287
Cdd:cd14629    82 DYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKcHQYWP-AERSARYQYFVVDPMAE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1288 ehkclSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPisKTFE-LISVIKE-----EAANRDGPMIVHDEHGGV 1361
Cdd:cd14629   161 -----YNMPQYILREFKVTDARDGQSRTIRQFQFTDWPEQGVP--KTGEgFIDFIGQvhktkEQFGQDGPITVHCSAGVG 233

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 332205945 1362 TAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKVILSLVST 1418
Cdd:cd14629   234 RTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALEYLGS 290
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 1186-1410 1.77e-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: 157.90  E-value: 1.77e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1186 RTSSIIPVERSRVGISSLSG-EGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIpdgQNMAEDE 1264
Cdd:cd14548     1 RYTNILPYDHSRVKLIPINEeEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVML---TQCMEKG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1265 FV----YWPNKDEPINCESFKVTLMAEEHkclsnEEKLIIQDFILEatQDDYVLEVRHFQCPKWPN---PDSPISkTFEL 1337
Cdd:cd14548    78 RVkcdhYWPFDQDPVYYGDITVTMLSESV-----LPDWTIREFKLE--RGDEVRSVRQFHFTAWPDhgvPEAPDS-LLRF 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332205945 1338 ISVIKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYK 1410
Cdd:cd14548   150 VRLVRDYIKQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLHQ 222
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 1210-1409 2.32e-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: 154.10  E-value: 2.32e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1210 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAEDEFVYWPNKdepincESFKVTLMAEEH 1289
Cdd:cd14556     1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDQSCPQYWPDE------GSGTYGPIQVEF 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1290 KCLSNEEKLIIQDFILEAT---QDDYVLeVRHFQCPKWP-NPDSPISKT--FELIS-VIKEEAANRDGPMIVHDEHGGVT 1362
Cdd:cd14556    75 VSTTIDEDVISRIFRLQNTtrpQEGYRM-VQQFQFLGWPrDRDTPPSKRalLKLLSeVEKWQEQSGEGPIVVHCLNGVGR 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 332205945 1363 AGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLY 1409
Cdd:cd14556   154 SGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCY 200
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 1186-1412 4.52e-42

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: 154.43  E-value: 4.52e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1186 RTSSIIPVERSRVGISSLSGE-GTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAEDE 1264
Cdd:cd14623     1 RVLQIIPYEFNRVIIPVKRGEeNTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1265 FV-YWPNkDEPINCESFKVTLMAEEhKClsneEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPiSKTFELISVI-- 1341
Cdd:cd14623    81 CAqYWPS-DGSVSYGDITIELKKEE-EC----ESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIP-SDGKGMINIIaa 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332205945 1342 --KEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKVI 1412
Cdd:cd14623   154 vqKQQQQSGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVV 226
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 1210-1412 6.59e-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: 150.11  E-value: 6.59e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1210 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAEDE-FVYWPNkDEPINCESFKVTLMAEE 1288
Cdd:cd14552     1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKcAQYWPE-DGSVSSGDITVELKDQT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1289 hkclsNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPI--SKTFELI-SVIKEEAANRDGPMIVHDEHGGVTAGT 1365
Cdd:cd14552    80 -----DYEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDngKGMIDLIaAVQKQQQQSGNHPITVHCSAGAGRTGT 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 332205945 1366 FCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKVI 1412
Cdd:cd14552   155 FCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
alpha_CA_IX cd03150
Carbonic anhydrase alpha, isozyme IX. Carbonic anhydrases (CAs) are zinc-containing enzymes ...
 45-300 1.31e-40

Carbonic anhydrase alpha, isozyme IX. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Alpha CAs are strictly monomeric enzymes. The zinc ion is complexed by three histidine residues. This sub-family comprises the membrane protein CA IX. CA IX is functionally implicated in tumor growth and survival. CA IX is mainly present in solid tumors and its expression in normal tissues is limited to the mucosa of alimentary tract. CA IX is a transmembrane protein with two extracellular domains: carbonic anhydrase and, a proteoglycan-like segment mediating cell-cell adhesion. There is evidence for an involvement of the MAPK pathway in the regulation of CA9 expression.


Pssm-ID: 239403  Cd Length: 247  Bit Score: 150.88  E-value: 1.31e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945   45 NQKNWGKKYPTCNSPKQSPINIDEDLTQVNVNLKKLKFQGWDKTSLENTFIHNTGKTVEINLTNDYRVSGGVSEmVFKAS 124
Cdd:cd03150     1 GQPPWPSVSPACAGRFQSPVDIRPHLVAFCPALRPLELLGFDLPPSPSLRLLNNGHTVQLSLPSGLRMALGPGQ-EYRAL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  125 KITFHWGKCNMSsdGSEHSLEGQKFPLEMQIYCFDAdRFSSFEEAVKGKGKLRALSILFEVGTEENLDFKAIIDGVESVS 204
Cdd:cd03150    80 QLHLHWGAAGRP--GSEHTVDGHRFPAEIHVVHLST-AFANLDEALGRPGGLAVLAAFLAEGLHENSAYEQLLSRLSEIS 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  205 RFGKQAALDPFILLNLLPNSTDKYYIYNGSLTSPPCTDTVDWIVFKDTVSISESQLAVFCEVLTMQQSgyvmlmDYLQNN 284
Cdd:cd03150   157 EEESETVVPGLDVSALLPSDLSRYFRYEGSLTTPPCAQGVIWTVFNQTVRLSAKQLHTLSDSLWGPHD------SRLQLN 230

                         250
                  ....*....|....*.
gi 332205945  285 FREQQYKFSRQVFSSY 300
Cdd:cd03150   231 FRATQPLNGRKIEASF 246
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 1210-1409 1.62e-40

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


Pssm-ID: 350406 [Multi-domain]  Cd Length: 203  Bit Score: 148.69  E-value: 1.62e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1210 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPD-GQNMAEDEFVYWPNKDEpiNCESFKVTLMAEE 1288
Cdd:cd14558     1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTElKEGDQEQCAQYWGDEKK--TYGDIEVELKDTE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1289 hkclsNEEKLIIQDFILEATQDDYVLEVRHFQCPKWpNPDSPISKTFELISVIKE---------EAANRDGPMIVHDEHG 1359
Cdd:cd14558    79 -----KSPTYTVRVFEITHLKRKDSRTVYQYQYHKW-KGEELPEKPKDLVDMIKSikqklpyknSKHGRSVPIVVHCSDG 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 332205945 1360 GVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLY 1409
Cdd:cd14558   153 SSRTGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 915-1124 2.51e-40

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


Pssm-ID: 350446 [Multi-domain]  Cd Length: 220  Bit Score: 148.97  E-value: 2.51e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  915 YINANYVDGYNRPKA--YIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEE----YGNFLVT 988
Cdd:cd14598     1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRLGSRHntvtYGRFKIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  989 QKSVQVLAYYTVRNFTLRNtkIKKGSQkgrpsgRVVTQYHYTQWPDMGVPEYSLPVLTFVRKAAYAKRHAVG-------- 1060
Cdd:cd14598    81 TRFRTDSGCYATTGLKIKH--LLTGQE------RTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHTNStidpkspn 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332205945 1061 -PVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVE 1124
Cdd:cd14598   153 pPVLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQ 217
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
858-1118 7.24e-40

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 149.86  E-value: 7.24e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  858 TEEFEEVQSCTVDLGITADSSNHPDN---KHKNRYINIVAYDHSRVklaqlaEKDGKltdYINANYVDGYNrPKAYIAAQ 934
Cdd:COG5599    14 EKINSRLSTLTNELAPSHNDPQYLQNingSPLNRFRDIQPYKETAL------RANLG---YLNANYIQVIG-NHRYIATQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  935 GPLKSTAEDFWRMIWEHNVEVIVMITNLVE--KGRRKCDQYWPADGseEYGNFLVTQKSVQVlaYYTVRNFTLRNTKIK- 1011
Cdd:COG5599    84 YPLEEQLEDFFQMLFDNNTPVLVVLASDDEisKPKVKMPVYFRQDG--EYGKYEVSSELTES--IQLRDGIEARTYVLTi 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1012 KGS-QKGRPsgrvVTQYHYTQWPDMGVP--EYSLPVLTFVRKAAYAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQ- 1087
Cdd:COG5599   160 KGTgQKKIE----IPVLHVKNWPDHGAIsaEALKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINa 235

                         250       260       270
                  ....*....|....*....|....*....|...
gi 332205945 1088 -HEGTVNIFGFLKHIRSQRNY-LVQTEEQYVFI 1118
Cdd:COG5599   236 lVQITLSVEEIVIDMRTSRNGgMVQTSEQLDVL 268
alpha_CA_VI cd03125
Carbonic anhydrase alpha, isozyme VI. Carbonic anhydrases (CAs) are zinc-containing enzymes ...
 45-300 1.29e-39

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: 148.01  E-value: 1.29e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945   45 NQKNWGKKYPTCNSPKQSPINIDEDLTQVNVNLKKLKFQGWDKTSLENTFIHNtGKTVEINLTNDYRVSGGVSEmVFKAS 124
Cdd:cd03125     1 DESHWPEKYPACGGKRQSPIDIQRREVRFNPSLLQLELVGYEKEQGEFTMTNN-GHTVQIDLPPTMSITTGDGT-VYTAV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  125 KITFHWGKCNMSSDGSEHSLEGQKFPLEMQIYCFDADrFSSFEEAVKGKGKLRALSILFEVGTE-ENLDFKAIIDGVESV 203
Cdd:cd03125    79 QMHFHWGGRDSEISGSEHTIDGMRYVAELHIVHYNSK-YKSYEEAKDKPDGLAVLAFLYKVGHYaENTYYSDFISKLAKI 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  204 SRFGKQAALDPFILLNLLPNSTDKYYIYNGSLTSPPCTDTVDWIVFKDTVSISESQlavfceVLTMQQSgyvmLMDY--- 280
Cdd:cd03125   158 KYAGQTTTLTSLDVRDMLPENLHHYYTYQGSLTTPPCTENVLWFVFDDPVTLSKTQ------IVKLENT----LMDHhnk 227

                         250       260
                  ....*....|....*....|.
gi 332205945  281 -LQNNFREQQYKFSRQVFSSY 300
Cdd:cd03125   228 tIRNDYRRTQPLNHRVVEANF 248
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 1185-1413 2.50e-39

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


Pssm-ID: 350466 [Multi-domain]  Cd Length: 230  Bit Score: 146.24  E-value: 2.50e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1185 NRTSSIIPVERSRVGISSLSGE-GTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIP----DGQN 1259
Cdd:cd14618     1 NRYPHVLPYDHSRVRLSQLGGEpHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTvgmeNGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1260 MAEDefvYWPNKDEPINCESFKVTLMAEEhkclsNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPN---PDSPiSKTFE 1336
Cdd:cd14618    81 LCDH---YWPSESTPVSYGHITVHLLAQS-----SEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDhgiPEST-SSLMA 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332205945 1337 LISVIKEE--AANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKVIL 1413
Cdd:cd14618   152 FRELVREHvqATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 1024-1124 3.16e-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: 141.34  E-value: 3.16e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945   1024 VTQYHYTQWPDMGVPEYSLPVLTFVR--KAAYAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHE-GTVNIFGFLKH 1100
Cdd:smart00012    2 VKHYHYTGWPDHGVPESPDSILELLRavKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVKE 81

                            90       100
                    ....*....|....*....|....
gi 332205945   1101 IRSQRNYLVQTEEQYVFIHDTLVE 1124
Cdd:smart00012   82 LRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1024-1124 3.16e-39

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 141.34  E-value: 3.16e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945   1024 VTQYHYTQWPDMGVPEYSLPVLTFVR--KAAYAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHE-GTVNIFGFLKH 1100
Cdd:smart00404    2 VKHYHYTGWPDHGVPESPDSILELLRavKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVKE 81

                            90       100
                    ....*....|....*....|....
gi 332205945   1101 IRSQRNYLVQTEEQYVFIHDTLVE 1124
Cdd:smart00404   82 LRSQRPGMVQTEEQYLFLYRALLE 105
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 1185-1413 3.02e-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: 140.34  E-value: 3.02e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1185 NRTSSIIPVERSRVGISSLSGEGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVM----IPDGQNM 1260
Cdd:cd14615     1 NRYNNVLPYDISRVKLSVQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMltkcVEQGRTK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1261 AEDefvYWPNKdEPINCESFKVTLMAEehkclSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWpnPDSPISKTFELI-- 1338
Cdd:cd14615    81 CEE---YWPSK-QKKDYGDITVTMTSE-----IVLPEWTIRDFTVKNAQTNESRTVRHFHFTSW--PDHGVPETTDLLin 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332205945 1339 --SVIKE--EAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKVIL 1413
Cdd:cd14615   150 frHLVREymKQNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCAL 228
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 1179-1417 8.41e-37

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: 139.45  E-value: 8.41e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1179 QCNREKNRTSSIIPVERSRVGISSLSG-EGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIpdg 1257
Cdd:cd14553     1 EVNKPKNRYANVIAYDHSRVILQPIEGvPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMM--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1258 QNMAEDEFV----YWPNKDEPiNCESFKVTLMAEEHkcLSNeekLIIQDFILEATQDDYVLEVRHFQCPKWPN---PDSP 1330
Cdd:cd14553    78 TKLEERSRVkcdqYWPTRGTE-TYGLIQVTLLDTVE--LAT---YTVRTFALHKNGSSEKREVRQFQFTAWPDhgvPEHP 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1331 ISkTFELISVIKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYK 1410
Cdd:cd14553   152 TP-FLAFLRRVKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHD 230


                  ....*..
gi 332205945 1411 VILSLVS 1417
Cdd:cd14553   231 ALLEAVT 237
alpha_CA_I_II_III_XIII cd03119
Carbonic anhydrase alpha, isozymes I, II, and III and XIII. Carbonic anhydrases (CAs) are ...
 38-300 9.70e-37

Carbonic anhydrase alpha, isozymes I, II, and III and XIII. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. Most alpha CAs are monomeric enzymes. The zinc ion is complexed by three histidines. This vertebrate subgroup comprises isozymes I, II, and III, which are cytoplasmic enzymes. CA I, for example, is expressed in erythrocyes of many vertebrates; CA II is the most active cytosolic isozyme; while it is being expressed nearly ubiquitously, it comprises 95% of the renal carbonic anhydrase and is required for renal acidification; CA III has been implicated in protection from the damaging effect of oxidizing agents in hepatocytes. CAXIII may play important physiological roles in several organs.


Pssm-ID: 239393 [Multi-domain]  Cd Length: 259  Bit Score: 139.88  E-value: 9.70e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945   38 WSYTGALNQKNWGKKYPTCNSPKQSPINIDEDLTQVNVNLKKLKFQgWDKTSLENtfIHNTGKTVEINLTNDYRVS---G 114
Cdd:cd03119     5 WGYDSHNGPEHWHELFPIAKGDRQSPIDIKTKDAKHDPSLKPLSVS-YDPATAKT--ILNNGHSFNVEFDDTDDRSvlrG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  115 GVSEMVFKASKITFHWGKCNmsSDGSEHSLEGQKFPLEMQIYCFDAdRFSSFEEAVKGKGKLRALSILFEVGtEENLDFK 194
Cdd:cd03119    82 GPLTGSYRLRQFHFHWGSSD--DHGSEHTVDGVKYAAELHLVHWNS-KYGSFGEAAKQPDGLAVVGVFLKVG-EANPELQ 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  195 AIIDGVESVSRFGKQAALDPFILLNLLPNSTDkYYIYNGSLTSPPCTDTVDWIVFKDTVSISESQLAVFCEVLTMQQSGY 274
Cdd:cd03119   158 KVLDALDSIKTKGKQAPFTNFDPSCLLPASLD-YWTYPGSLTTPPLLECVTWIVLKEPISVSSEQMAKFRSLLFNAEGEP 236

                         250       260
                  ....*....|....*....|....*.
gi 332205945  275 VMLMdylQNNFREQQYKFSRQVFSSY 300
Cdd:cd03119   237 PCPM---VDNWRPPQPLKGRKVRASF 259
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 1209-1412 1.46e-36

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


Pssm-ID: 350470 [Multi-domain]  Cd Length: 205  Bit Score: 137.44  E-value: 1.46e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1209 DYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAEDE-FVYWPNKDEPINCEsfkVTLmae 1287
Cdd:cd14622     1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKcVQYWPSEGSVTHGE---ITI--- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1288 EHKCLSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPIS--KTFELISVI-KEEAANRDGPMIVHDEHGGVTAG 1364
Cdd:cd14622    75 EIKNDTLLETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEgkGMIDLIAAVqKQQQQTGNHPIVVHCSAGAGRTG 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 332205945 1365 TFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKVI 1412
Cdd:cd14622   155 TFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 1173-1410 5.12e-36

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: 138.27  E-value: 5.12e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1173 YSAALKQCNREKNRTSSIIPVERSRVGISSLSG-EGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLV 1251
Cdd:cd14543    21 FLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNGdERTDYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKVLVI 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1252 VMIPD---------GQnmaedefvYWPNKDEpiNCESF-KVTLmaeEHKCLSNEEKLIIQDFILEATQDDYVLEVRHFQC 1321
Cdd:cd14543   101 VMTTRvvergrvkcGQ--------YWPLEEG--SSLRYgDLTV---TNLSVENKEHYKKTTLEIHNTETDESRQVTHFQF 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1322 PKWPN---PDSPISKTFELISVIKEEAAN------------RDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQ 1386
Cdd:cd14543   168 TSWPDfgvPSSAAALLDFLGEVRQQQALAvkamgdrwkghpPGPPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQ 247

                         250       260
                  ....*....|....*....|....
gi 332205945 1387 VAKMINLMRPGVFADIEQYQFLYK 1410
Cdd:cd14543   248 TVRRMRTQRAFSIQTPDQYYFCYK 271
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 1181-1413 1.46e-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: 1.46e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1181 NREKNRTSSIIPVERSRVGISSLSG-EGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIP---D 1256
Cdd:cd14614    12 NRCKNRYTNILPYDFSRVKLVSMHEeEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTqcnE 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1257 GQNMAEDEfvYWPNKDEPINCESFKVTLMAEEhkclsNEEKLIIQDFILeaTQDDYVLEVRHFQCPKWPNPDSPISKTFE 1336
Cdd:cd14614    92 KRRVKCDH--YWPFTEEPVAYGDITVEMLSEE-----EQPDWAIREFRV--SYADEVQDVMHFNYTAWPDHGVPTANAAE 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1337 ----LISVIKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKVI 1412
Cdd:cd14614   163 silqFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 242


                  .
gi 332205945 1413 L 1413
Cdd:cd14614   243 Q 243
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 1185-1416 1.66e-35

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: 135.40  E-value: 1.66e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1185 NRTSSIIPVERSRVGISSLSGEGT-DYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIpdgQNMAED 1263
Cdd:cd14619     1 NRFRNVLPYDWSRVPLKPIHEEPGsDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVML---TNCMEA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1264 EFV----YWPNKDEPINCESFKVTLMAEEhkclsNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPiSKTFELIS 1339
Cdd:cd14619    78 GRVkcehYWPLDYTPCTYGHLRVTVVSEE-----VMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVP-SSTDTLLA 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1340 ---VIKE--EAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKVILS 1414
Cdd:cd14619   152 frrLLRQwlDQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILD 231


                  ..
gi 332205945 1415 LV 1416
Cdd:cd14619   232 FL 233
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 1185-1409 7.76e-35

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: 133.29  E-value: 7.76e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1185 NRTSSIIPVERSRVGISSL-SGEGTDYINASYIMGY-YQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAE 1262
Cdd:cd14547     1 NRYKTILPNEHSRVCLPSVdDDPLSSYINANYIRGYdGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEAKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1263 DEFVYWPNKdEPINCESFKVTLMAEEHKclsneEKLIIQDFILEatqddYVLEVR---HFQCPKWPNPDSPiSKTFELIS 1339
Cdd:cd14547    81 KCAQYWPEE-ENETYGDFEVTVQSVKET-----DGYTVRKLTLK-----YGGEKRylkHYWYTSWPDHKTP-EAAQPLLS 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332205945 1340 VIKE-----EAANRDGPMIVHDEHG-GVTaGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLY 1409
Cdd:cd14547   149 LVQEveearQTEPHRGPIVVHCSAGiGRT-GCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVH 223
alpha_CA_V cd03118
Carbonic anhydrase alpha, CA isozyme V_like subgroup. Carbonic anhydrases (CAs) are ...
 60-300 1.07e-34

Carbonic anhydrase alpha, CA isozyme V_like subgroup. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. Most alpha CAs are monomeric enzymes. The zinc ion is complexed by three histidines. This vertebrate subgroup comprises isozyme V. CA V is the mitochondrial isozyme, which may play a role in gluconeogenesis and ureagenesis and possibly also in lipogenesis.


Pssm-ID: 239392  Cd Length: 236  Bit Score: 133.43  E-value: 1.07e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945   60 KQSPINIDEDLTQVNVNLKKLKFQGWDKTSLentFIHNTGKTVEINL---TNDYRVSGGVSEMVFKASKITFHWGKCNms 136
Cdd:cd03118     3 RQSPINIQWRDSVYDPQLAPLRVSYDPATCL---YIWNNGYSFQVEFddsTDKSGISGGPLENHYRLKQFHFHWGANN-- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  137 SDGSEHSLEGQKFPLEMQIYCFDADRFSSFEEAVKGKGKLRALSILFEVGTEENlDFKAIIDGVESVSRFGKQAALDPFI 216
Cdd:cd03118    78 EWGSEHTVDGHTYPAELHLVHWNSVKYENFEEAVMEENGLAVIGVFLKLGAHHE-GLQKLVDALPEVRHKDTVVEFNPFD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  217 LLNLLPNSTDkYYIYNGSLTSPPCTDTVDWIVFKDTVSISESQLAVFCEVLTmqqSGYVMLMDYLQNNFREQQYKFSRQV 296
Cdd:cd03118   157 PSCLLPACRD-YWTYPGSLTTPPLTESVTWIIQKQPIEVSPSQLSVFRTLLF---TSRGEEEKVMVNNFRPLQPLMNRKV 232


                  ....
gi 332205945  297 FSSY 300
Cdd:cd03118   233 RSSF 236
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 915-1118 1.49e-34

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: 131.67  E-value: 1.49e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  915 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGrrKCDQYWPADGSE-EYGNFLVTQ---- 989
Cdd:cd14550     1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNE--DEPIYWPTKEKPlECETFKVTLsged 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  990 -KSVQVLAYYTVRNFTLRNTKikkgsqkgrpSGRVVT--QYHYTQWPDMGVPEYSlpVLTFVRKAAYAKRHAVGPVVVHC 1066
Cdd:cd14550    79 hSCLSNEIRLIVRDFILESTQ----------DDYVLEvrQFQCPSWPNPCSPIHT--VFELINTVQEWAQQRDGPIVVHD 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 332205945 1067 SAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFI 1118
Cdd:cd14550   147 RYGGVQAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFL 198
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 1169-1413 1.96e-34

catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type tyrosine-protein phosphatase M (PTPRM), also known as protein-tyrosine phosphatase mu (R-PTP-mu or PTPmu), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRM/PTPmu is a homophilic cell adhesion molecule expressed in CNS neurons and glia. It is required for E-, N-, and R-cadherin-dependent neurite outgrowth. Loss of PTPmu contributes to tumor cell migration and dispersal of human glioblastomas. PTPRM contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350481 [Multi-domain]  Cd Length: 273  Bit Score: 133.63  E-value: 1.96e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1169 QQSDYSAALKQCNREKNRTSSIIPVERSRVGISSLSGE-GTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHN 1247
Cdd:cd14633    28 QSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGEtSSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHEN 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1248 AQLVVMIpdgQNMAEDEFV----YWPNKDEPIncESFKVTLMaeEHKCLSneeKLIIQDFILEATQDDYVLEVRHFQCPK 1323
Cdd:cd14633   108 TASIIMV---TNLVEVGRVkcckYWPDDTEIY--KDIKVTLI--ETELLA---EYVIRTFAVEKRGVHEIREIRQFHFTG 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1324 WPNPDSPISKT--FELISVIKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFAD 1401
Cdd:cd14633   178 WPDHGVPYHATglLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQT 257

                         250
                  ....*....|..
gi 332205945 1402 IEQYQFLYKVIL 1413
Cdd:cd14633   258 EEQYVFIHDAIL 269
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 1158-1412 2.44e-34

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


Pssm-ID: 350451 [Multi-domain]  Cd Length: 266  Bit Score: 133.41  E-value: 2.44e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1158 KQFQLL-SQSNIQQSDYS----AALKQCNREKNRTSSIIPVERSRVGISSLSGEG-TDYINASYIMGYYQSNEFIITQHP 1231
Cdd:cd14603     2 GEFSEIrACSAAFKADYVcstvAGGRKENVKKNRYKDILPYDQTRVILSLLQEEGhSDYINANFIKGVDGSRAYIATQGP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1232 LLHTIKDFWRMIWDHNAQLVVM----IPDGQNMAEdefVYWPNKDEPINCESFKVTLMAEEHkclSNEEkLIIQdfILEA 1307
Cdd:cd14603    82 LSHTVLDFWRMIWQYGVKVILMacreIEMGKKKCE---RYWAQEQEPLQTGPFTITLVKEKR---LNEE-VILR--TLKV 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1308 TQDDYVLEVRHFQCPKWPN---PDSPiSKTFELISVIKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDV 1384
Cdd:cd14603   153 TFQKESRSVSHFQYMAWPDhgiPDSP-DCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPD 231

                         250       260       270
                  ....*....|....*....|....*....|.
gi 332205945 1385 YQVAKMINLM---RPGVFADIEQYQFLYKVI 1412
Cdd:cd14603   232 FSIFDVVLEMrkqRPAAVQTEEQYEFLYHTV 262
Cah COG3338
Carbonic anhydrase [Inorganic ion transport and metabolism];
38-263 1.53e-32

Carbonic anhydrase [Inorganic ion transport and metabolism];


Pssm-ID: 442567 [Multi-domain]  Cd Length: 247  Bit Score: 127.31  E-value: 1.53e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945   38 WSYTGALNQKNWGK---KYPTCNS-PKQSPINIDedlTQVNVNLKKLKFQgWDKTSLEntfIHNTGKTVEINL-TNDYRV 112
Cdd:COG3338    28 WSYEGETGPEHWGElspEFATCATgKNQSPIDIR---TAIKADLPPLKFD-YKPTPLE---IVNNGHTIQVNVdPGSTLT 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  113 SGGVsemVFKASKITFHwgkcnmssDGSEHSLEGQKFPLEMQiycF---DADrfssfeeavkgkGKLRALSILFEVGtEE 189
Cdd:COG3338   101 VDGK---RYELKQFHFH--------TPSEHTINGKSYPMEAH---LvhkDAD------------GELAVVGVLFEEG-AE 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332205945  190 NLDFKAIIDGVESvsRFGKQAALD-PFILLNLLPNSTDkYYIYNGSLTSPPCTDTVDWIVFKDTVSISESQLAVF 263
Cdd:COG3338   154 NPALAKLWANLPL--EAGEEVALDaTIDLNDLLPEDRS-YYRYSGSLTTPPCSEGVLWIVLKQPITVSAEQIEAF 225
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 1184-1409 2.00e-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: 127.26  E-value: 2.00e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1184 KNRTSSIIPVERSRVGISSL--SGEGTDYINASYIMGYY-QSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNM 1260
Cdd:cd14612    18 KDRYKTILPNPQSRVCLRRAgsQEEEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMITKLKEK 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1261 AEDEFVYWPNKDEPINCESFKVTLMAEehkClsneEKLIIQDFILEATQDDYvlEVRHFQCPKWPNPDSPISKT--FELI 1338
Cdd:cd14612    98 KEKCVHYWPEKEGTYGRFEIRVQDMKE---C----DGYTIRDLTIQLEEESR--SVKHYWFSSWPDHQTPESAGplLRLV 168

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332205945 1339 SVIKE--EAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLY 1409
Cdd:cd14612   169 AEVEEsrQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLH 241
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 1181-1413 2.98e-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: 126.29  E-value: 2.98e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1181 NREKNRTSSIIPVERSRVGISSLSGE-GTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQN 1259
Cdd:cd14630     3 NRNKNRYGNIISYDHSRVRLQLLDGDpHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1260 MAEDEFV-YWPNKDEPINceSFKVTLMAEEHKClsneeKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKT--FE 1336
Cdd:cd14630    83 VGRVKCVrYWPDDTEVYG--DIKVTLIETEPLA-----EYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATglLG 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 332205945 1337 LISVIKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKVIL 1413
Cdd:cd14630   156 FVRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAIL 232
alpha_CA_prokaryotic_like cd03124
Carbonic anhydrase alpha, prokaryotic-like subfamily. Carbonic anhydrases (CAs) are ...
 45-263 5.35e-32

Carbonic anhydrase alpha, prokaryotic-like subfamily. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. Most alpha CAs are monomeric enzymes. The zinc ion is complexed by three histidines. This sub-family includes bacterial carbonic anhydrase alpha, as well as plant enzymes such as tobacco nectarin III and yam dioscorin and, carbonic anhydrases from molluscs, such as nacrein, which are part of the organic matrix layer in shells. Other members of this family may be involved in maintaining pH balance, in facilitating transport of carbon dioxide or carbonic acid, or in sensing carbon dioxide levels in the environment. Dioscorin is the major storage protein of yam tubers and may play a role as an antioxidant. Tobacco Nectarin may play a role in the maintenace of pH and oxidative balance in nectar. Mollusc nacrein may participate in calcium carbonate crystal formation of the nacreous layer. This subfamily also includes three alpha carbonic anhydrases from Chlamydomonas reinhardtii (CAH 1-3). CAHs1-2 are localized in the periplasmic space. CAH1 faciliates the movement of carbon dioxide across the plasma membrane when the medium is alkaline. CAH3 is localized to the thylakoid lumen and provides CO2 to Rubisco.


Pssm-ID: 239398 [Multi-domain]  Cd Length: 216  Bit Score: 124.69  E-value: 5.35e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945   45 NQKNWG---KKYPTCNS-PKQSPINIDEDLTQVNVnLKKLKFQgWDKTSLEntfIHNTGKTVEINLTNDyrvsGGVSE-- 118
Cdd:cd03124     1 GPEHWGnldPEFALCATgKNQSPIDITTKAVVSDK-LPPLNYN-YKPTSAT---LVNNGHTIQVNFEGN----GGTLTid 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  119 -MVFKASKITFHwgkcnmssDGSEHSLEGQKFPLEMQIycfdadrfsSFEEAvkgKGKLRALSILFEVGtEENLDFKAII 197
Cdd:cd03124    72 gETYQLLQFHFH--------SPSEHLINGKRYPLEAHL---------VHKSK---DGQLAVVAVLFEEG-KENPFLKKIL 130

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 332205945  198 DGVESvsRFGKQAALDPFILLN-LLPNSTDkYYIYNGSLTSPPCTDTVDWIVFKDTVSISESQLAVF 263
Cdd:cd03124   131 DNMPK--KEGTEVNLPAILDPNeLLPESRS-YYRYEGSLTTPPCSEGVRWIVLKQPITISKEQLAKF 194
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 1184-1415 8.73e-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: 124.95  E-value: 8.73e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1184 KNRTSSIIPVERSRVGISSL-SGEGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAE 1262
Cdd:cd14602     1 KNRYKDILPYDHSRVELSLItSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1263 DEFV-YWPN-KDEPINCESFKVTLMAEEHKclsneEKLIIQdfILEATQDDYVLEVRHFQCPKWPNPDSP--ISKTFELI 1338
Cdd:cd14602    81 KKCErYWAEpGEMQLEFGPFSVTCEAEKRK-----SDYIIR--TLKVKFNSETRTIYQFHYKNWPDHDVPssIDPILELI 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1339 SVIKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEK----ENsVDVYQVAKMINLMRPGVFADIEQYQFLYKVILS 1414
Cdd:cd14602   154 WDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDgiipEN-FSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIE 232


                  .
gi 332205945 1415 L 1415
Cdd:cd14602   233 L 233
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 1184-1415 1.31e-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: 1.31e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1184 KNRTSSIIPVERSRVGISSLSGEG--TDYINASYIMGY-YQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNM 1260
Cdd:cd14613    28 KNRYKTILPNPHSRVCLTSPDQDDplSSYINANYIRGYgGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEM 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1261 AEDEFVYWPnkDEPINCESFKVTLMAEEHkclsnEEKLIIQDFILEATQDDYVLevRHFQCPKWPN---PDS--PISKTF 1335
Cdd:cd14613   108 NEKCTEYWP--EEQVTYEGIEITVKQVIH-----ADDYRLRLITLKSGGEERGL--KHYWYTSWPDqktPDNapPLLQLV 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1336 ELISVIKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKViLSL 1415
Cdd:cd14613   179 QEVEEARQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVHHV-LSL 257
alpha_CA_VII cd03149
Carbonic anhydrase alpha, CA isozyme VII_like subgroup. Carbonic anhydrases (CAs) are ...
 60-300 5.62e-31

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: 122.64  E-value: 5.62e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945   60 KQSPINIDEDLTQVNVNLKKLKFQGWDKTSLEntfIHNTGKT--VEINLTNDYRV-SGGVSEMVFKASKITFHWGKcnMS 136
Cdd:cd03149     3 RQSPIDIVSSEAVYDPKLKPLSLSYDPCTSLS---ISNNGHSvmVEFDDSDDKTViTGGPLENPYRLKQFHFHWGA--KH 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  137 SDGSEHSLEGQKFPLEMQIYCFDADRFSSFEEAVKGKGKLRALSILFEVGtEENLDFKAIIDGVESVSRFGKQAALDPFI 216
Cdd:cd03149    78 GSGSEHTVDGKTFPSELHLVHWNAKKYKSFGEAAAAPDGLAVLGVFLETG-DEHPGLNRLTDALYMVRFKGTKAQFLDFN 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  217 LLNLLPNSTDkYYIYNGSLTSPPCTDTVDWIVFKDTVSISESQLAVFCEVLTMQQSGYVMLMdylQNNFREQQYKFSRQV 296
Cdd:cd03149   157 PKCLLPKSLD-YWTYPGSLTTPPLNESVTWIVLKEPIPVSEKQMGKFRELLFTSEEDQRNHM---VNNFRPPQPLKGRTV 232


                  ....
gi 332205945  297 FSSY 300
Cdd:cd03149   233 RASF 236
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 1169-1417 1.48e-30

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


Pssm-ID: 350474 [Multi-domain]  Cd Length: 276  Bit Score: 122.45  E-value: 1.48e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1169 QQSDYSAALKQCNREKNRTSSIIPVERSRVGISSLSG-EGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHN 1247
Cdd:cd14626    29 QQFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGvPGSDYINANYIDGYRKQNAYIATQGPLPETLSDFWRMVWEQR 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1248 AQLVVMIpdgQNMAEDEFV----YWPNKDEPiNCESFKVTLM-AEEHKCLSneekliIQDFILEATQDDYVLEVRHFQCP 1322
Cdd:cd14626   109 TATIVMM---TRLEEKSRVkcdqYWPIRGTE-TYGMIQVTLLdTVELATYS------VRTFALYKNGSSEKREVRQFQFM 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1323 KWPNPDSPISKTFELISVIKEEAAN--RDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFA 1400
Cdd:cd14626   179 AWPDHGVPEYPTPILAFLRRVKACNppDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQ 258

                         250
                  ....*....|....*..
gi 332205945 1401 DIEQYQFLYKVILSLVS 1417
Cdd:cd14626   259 TEDQYIFIHEALLEAAT 275
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 1185-1410 3.29e-30

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: 120.02  E-value: 3.29e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1185 NRTSSIIPVERSRVGISSLSGEG-TDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIpdgQNMAED 1263
Cdd:cd14617     1 NRYNNILPYDSTRVKLSNVDDDPcSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMV---TQCVEK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1264 EFV----YWPNKDEPINCESFKVTLMAEehkclSNEEKLIIQDF-ILEATQDDYVLEVRHFQCPKWPNPDSPiSKTFELI 1338
Cdd:cd14617    78 GRVkcdhYWPADQDSLYYGDLIVQMLSE-----SVLPEWTIREFkICSEEQLDAPRLVRHFHYTVWPDHGVP-ETTQSLI 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 332205945 1339 SVIK--EEAANRD---GPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYK 1410
Cdd:cd14617   152 QFVRtvRDYINRTpgsGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 1210-1413 4.17e-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: 119.24  E-value: 4.17e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1210 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIP--DGQNMAEDEFVYWPnkdEPINCesfKVTLMAE 1287
Cdd:cd14637     1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNqlNQSNSAWPCLQYWP---EPGLQ---QYGPMEV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1288 EHKCLSNEEKLIIQDFILE--ATQDDYVLEVRHFQCPKWP----NPDSPISKTFELISVIKEEAANRDGPMIVHDEHGGV 1361
Cdd:cd14637    75 EFVSGSADEDIVTRLFRVQniTRLQEGHLMVRHFQFLRWSayrdTPDSKKAFLHLLASVEKWQRESGEGRTVVHCLNGGG 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 332205945 1362 TAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKVIL 1413
Cdd:cd14637   155 RSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIAL 206
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 915-1124 5.10e-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: 118.97  E-value: 5.10e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  915 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLveKGRRKCDQYWPADGSEEYGNFLVTQKSVQV 994
Cdd:cd14634     1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEM--DAAQLCMQYWPEKTSCCYGPIQVEFVSADI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  995 LAYYTVRNFTLRNTkikkgsqkGRPSG--RVVTQYHYTQWPDM-GVPEYSLPVLTFVRKAA-----YAKRHavGPVVVHC 1066
Cdd:cd14634    79 DEDIISRIFRICNM--------ARPQDgyRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLEkwqeqYDGRE--GRTVVHC 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 332205945 1067 SAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVE 1124
Cdd:cd14634   149 LNGGGRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 1178-1415 6.92e-30

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: 121.19  E-value: 6.92e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1178 KQCNREKNRTSSIIPVERSRVGIS-SLSGEGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPD 1256
Cdd:cd14604    54 KEENVKKNRYKDILPFDHSRVKLTlKTSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACR 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1257 GQNMAEDEFV-YWPN-KDEPINCESFKVTLMAEEHKclsneEKLIIQDFILEATQDDYVLEVRHFQcpKWPNPDSPIS-- 1332
Cdd:cd14604   134 EFEMGRKKCErYWPLyGEEPMTFGPFRISCEAEQAR-----TDYFIRTLLLEFQNETRRLYQFHYV--NWPDHDVPSSfd 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1333 KTFELISVIKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADI---EQYQFLY 1409
Cdd:cd14604   207 SILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVqtkEQYELVH 286


                  ....*.
gi 332205945 1410 KVILSL 1415
Cdd:cd14604   287 RAIAQL 292
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 1210-1409 7.32e-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: 118.51  E-value: 7.32e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1210 YINASYI-MGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMI-PDGQNMAEDEFVYWPNKDEPINCESFKVTLMAE 1287
Cdd:cd18533     1 YINASYItLPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLtPLVENGREKCDQYWPSGEYEGEYGDLTVELVSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1288 EHKclsNEEKLIIQDFILeATQDDYVLEVRHFQCPKWPN---PDSPISkTFELISVIKE--EAANRDGPMIVHDEHG-GV 1361
Cdd:cd18533    81 EEN---DDGGFIVREFEL-SKEDGKVKKVYHIQYKSWPDfgvPDSPED-LLTLIKLKRElnDSASLDPPIIVHCSAGvGR 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 332205945 1362 TaGTFCALTTLMHQLEKENSVDVYQ------VAKMINLM---RPGVFADIEQYQFLY 1409
Cdd:cd18533   156 T-GTFIALDSLLDELKRGLSDSQDLedsedpVYEIVNQLrkqRMSMVQTLRQYIFLY 211
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 1185-1410 1.18e-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: 118.47  E-value: 1.18e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1185 NRTSSIIPVERSRVGISSLSG-EGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPD----GQN 1259
Cdd:cd14616     1 NRFPNIKPYNNNRVKLIADAGvPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQcfekGRI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1260 MAEDefvYWPNKDEPINCES-FKVTLMAEEhkclsNEEKLIIQDFILEaTQDDYVLeVRHFQCPKWPNPDSPISkTFELI 1338
Cdd:cd14616    81 RCHQ---YWPEDNKPVTVFGdIVITKLMED-----VQIDWTIRDLKIE-RHGDYMM-VRQCNFTSWPEHGVPES-SAPLI 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332205945 1339 SVIKEEAANRDG---PMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYK 1410
Cdd:cd14616   150 HFVKLVRASRAHdntPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLHQ 224
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 1189-1413 2.47e-29

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type tyrosine-protein phosphatase E (PTPRE), also known as receptor-type tyrosine-protein phosphatase epsilon (R-PTP-epsilon), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. The PTPRE gene contains two distinct promoters that generate the two major isoforms: transmembrane (receptor type RPTPe or PTPeM) and cytoplasmic (cyt-PTPe or PTPeC). Receptor type RPTPe plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells, and may also play a role in osteoclast formation and function. It also negatively regulates PDGFRbeta-mediated signaling pathways that are crucial for the pathogenesis of atherosclerosis. cyt-PTPe acts as a negative regulator of insulin receptor signaling in skeletal muscle. It regulates insulin-induced phosphorylation of proteins downstream of the insulin receptor. Receptor type RPTPe contains a small extracellular region, a single transmembrane segment, and an intracellular region two tandem catalytic PTP domains. This model represents the first PTP domain (repeat 1).


Pssm-ID: 350468 [Multi-domain]  Cd Length: 229  Bit Score: 117.73  E-value: 2.47e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1189 SIIPVERSRVGISSLSG-EGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAEDE-FV 1266
Cdd:cd14620     3 NILPYDHSRVILSQLDGiPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKcYQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1267 YWPNKdepiNCESF-KVTLMAEEHKCLSNeekLIIQDFILEATQDDYVLEVR-----HFQcpKWPN---PDSPISkTFEL 1337
Cdd:cd14620    83 YWPDQ----GCWTYgNIRVAVEDCVVLVD---YTIRKFCIQPQLPDGCKAPRlvtqlHFT--SWPDfgvPFTPIG-MLKF 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332205945 1338 ISVIKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKVIL 1413
Cdd:cd14620   153 LKKVKSVNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALL 228
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 1210-1413 3.64e-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: 116.27  E-value: 3.64e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1210 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDgQNMAEDEFVYWPNKDE----PINCESFKVTLm 1285
Cdd:cd14634     1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNE-MDAAQLCMQYWPEKTSccygPIQVEFVSADI- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1286 aeehkclsnEEKLIIQDFI---LEATQDDYVLeVRHFQCPKWPN-PDSPISKTfELISVIK------EEAANRDGPMIVH 1355
Cdd:cd14634    79 ---------DEDIISRIFRicnMARPQDGYRI-VQHLQYIGWPAyRDTPPSKR-SILKVVRrlekwqEQYDGREGRTVVH 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 332205945 1356 DEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKVIL 1413
Cdd:cd14634   148 CLNGGGRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVAL 205
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 1156-1413 3.83e-29

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


Pssm-ID: 350469 [Multi-domain]  Cd Length: 296  Bit Score: 118.97  E-value: 3.83e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1156 LEKQFQLLSQSNIQQSdYSAALKQCNREKNRTSSIIPVERSRVGISSLSG-EGTDYINASYIMGYYQSNEFIITQHPLLH 1234
Cdd:cd14621    28 FREEFNALPACPIQAT-CEAASKEENKEKNRYVNILPYDHSRVHLTPVEGvPDSDYINASFINGYQEKNKFIAAQGPKEE 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1235 TIKDFWRMIWDHNAQLVVMIPDGQNMAEDEFV-YWPNKdepiNCESF-KVTLMAEEHKCLSNE--EKLIIQDfILEATQD 1310
Cdd:cd14621   107 TVNDFWRMIWEQNTATIVMVTNLKERKECKCAqYWPDQ----GCWTYgNIRVSVEDVTVLVDYtvRKFCIQQ-VGDVTNK 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1311 DYVLEVRHFQCPKWPN---PDSPISkTFELISVIKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQV 1387
Cdd:cd14621   182 KPQRLITQFHFTSWPDfgvPFTPIG-MLKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGF 260

                         250       260
                  ....*....|....*....|....*.
gi 332205945 1388 AKMINLMRPGVFADIEQYQFLYKVIL 1413
Cdd:cd14621   261 VSRIRAQRCQMVQTDMQYVFIYQALL 286
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 1210-1409 6.14e-29

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: 6.14e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1210 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIpdgQNMAE------DEfvYWPNKDEPiNCESFKVT 1283
Cdd:cd14549     1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMI---TNLVErgrrkcDQ--YWPKEGTE-TYGNIQVT 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1284 LMAEEHkcLSNeekLIIQDFILEATQ------DDYVLEVRHFQCPKWPN---PDSPISK-TFelisVIKEEAANRD--GP 1351
Cdd:cd14549    75 LLSTEV--LAT---YTVRTFSLKNLKlkkvkgRSSERVVYQYHYTQWPDhgvPDYTLPVlSF----VRKSSAANPPgaGP 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 332205945 1352 MIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLY 1409
Cdd:cd14549   146 IVVHCSAGVGRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203
alpha_CARP_X_XI_like cd03121
Carbonic anhydrase alpha related protein: groups X, XI and related proteins. This subgroup ...
 49-296 7.19e-29

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: 117.13  E-value: 7.19e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945   49 WGKKYPT---CNSPK-QSPINIDEDLTQVNVNLKKLKFQGWDKTSLEntfIHNTGKTVEINLTNDYRV--SGGVSEMVFK 122
Cdd:cd03121     5 WGLVNSAwnlCSKGRrQSPVDIEPSRLLFDPFLTPLRIDTGRKVSGT---FYNTGRHVSFRPDKDPVVniSGGPLSYRYR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  123 ASKITFHWGKCNmsSDGSEHSLEGQKFPLEMQIYCFDADRFSSFEEAVKGKGKLRALSILFEVGTEENLDFKAIIDGVES 202
Cdd:cd03121    82 LEEIRLHFGRED--EQGSEHTVNGQAFPGEVQLIHYNSELYPNFSEASKSPNGLVIVSLFVKIGETSNPELRRLTNRDTI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  203 VS-RFGKQAALDPFILLNLLPNSTDKYYIYNGSLTSPPCTDTVDWIVFKDTVSISESQLAvfcEVLTMQQSGYVMLMDYL 281
Cdd:cd03121   160 TSiRYKGDAYFLQDLSIELLLPETDHYITYEGSLTSPGCHETVTWIILNKPIYITKEQMH---SLRLLSQNSPSQEKAPM 236

                         250
                  ....*....|....*
gi 332205945  282 QNNFREQQYKFSRQV 296
Cdd:cd03121   237 SPNFRPVQPLNNRPV 251
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 1174-1412 9.71e-29

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 118.59  E-value: 9.71e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1174 SAALKQCNREKNRTSSIIPVERSRVGISS------------------LSGEGTD--YINASYIMGYYQSNEFIITQHPLL 1233
Cdd:PHA02746   44 NHFLKKENLKKNRFHDIPCWDHSRVVINAheslkmfdvgdsdgkkieVTSEDNAenYIHANFVDGFKEANKFICAQGPKE 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1234 HTIKDFWRMIWDHNAQLVVMIPDGQNMAEDEFVYWPN-KDEPINCESFKVTLMAEEHKCLSNEEKLIIQDFILEATQddy 1312
Cdd:PHA02746  124 DTSEDFFKLISEHESQVIVSLTDIDDDDEKCFELWTKeEDSELAFGRFVAKILDIIEELSFTKTRLMITDKISDTSR--- 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1313 vlEVRHFQCPKWP---NPDSPiSKTFELISVIKEEAA----------NRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKE 1379
Cdd:PHA02746  201 --EIHHFWFPDWPdngIPTGM-AEFLELINKVNEEQAelikqadndpQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKE 277

                         250       260       270
                  ....*....|....*....|....*....|...
gi 332205945 1380 NSVDVYQVAKMINLMRPGVFADIEQYQFLYKVI 1412
Cdd:PHA02746  278 KEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 1210-1413 1.92e-28

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: 114.24  E-value: 1.92e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1210 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIpdgQNMAEDEFV----YWPNKDEPINceSFKVTLM 1285
Cdd:cd14555     1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMV---TNLVEVGRVkcsrYWPDDTEVYG--DIKVTLV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1286 AEEHKClsneeKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKT--FELISVIKEEAANRDGPMIVHDEHGGVTA 1363
Cdd:cd14555    76 ETEPLA-----EYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATglLGFIRRVKASNPPSAGPIVVHCSAGAGRT 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 332205945 1364 GTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKVIL 1413
Cdd:cd14555   151 GCYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAIL 200
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 1173-1417 2.40e-28

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 117.02  E-value: 2.40e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1173 YSAALKQCNREKNRTSSIIPVERSRVGISSLSGEGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVV 1252
Cdd:PHA02747   43 IANFEKPENQPKNRYWDIPCWDHNRVILDSGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIV 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1253 MI--PDGQNMAEDEFVYW-PNKDEPINCESFKVTLMAEEHKCLSNEEKLIIQDFILEATQddyvlEVRHFQCPKWPNPDS 1329
Cdd:PHA02747  123 MLtpTKGTNGEEKCYQYWcLNEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILKDSR-----KISHFQCSEWFEDET 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1330 PiSKTFELISVIKEEAANRD-------------GPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRP 1396
Cdd:PHA02747  198 P-SDHPDFIKFIKIIDINRKksgklfnpkdallCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRH 276

                         250       260
                  ....*....|....*....|....
gi 332205945 1397 GVFADIEQYQFL---YKVILSLVS 1417
Cdd:PHA02747  277 AGIMNFDDYLFIqpgYEVLHYFLS 300
alpha_CARP_VIII cd03120
Carbonic anhydrase alpha related protein, group VIII. Carbonic anhydrase related proteins ...
 49-289 8.57e-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: 113.80  E-value: 8.57e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945   49 WGKKYPTCNSPKQSPINI-------DEDLTQVNVNLKKLKFQGWDKTslentfihNTGKTVEINLTNDYRVSGGV--SEM 119
Cdd:cd03120     4 WGLLFPEANGEYQSPINLnsrearyDPSLLEVRLSPNYVVCRDCEVI--------NDGHTIQIILKSKSVLSGGPlpQGH 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  120 VFKASKITFHWGKCNMSsdGSEHSLEGQKFPLEMQIYCFDADRFSSFEEAVKGKGKLRALSILFEVGtEENLDFKAIIDG 199
Cdd:cd03120    76 EFELAEVRFHWGRENQR--GSEHTVNFKAFPMELHLIHWNSTLYSSLEEAMGKPHGIAIIALFVQIG-KEHVGLKAVTEI 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  200 VESVSRFGKQAALDPFILLNLLPNSTDK-YYIYNGSLTSPPCTDTVDWIVFKDTVSISESQLAVFCEvLTMQQSGY--VM 276
Cdd:cd03120   153 LQDIQYKGKSKTIPCFNPNTLLPDPLLRdYWVYEGSLTTPPCSEGVTWILFRYPLTISQSQIEEFRR-LRTHVKGAelVE 231

                         250
                  ....*....|....
gi 332205945  277 LMDY-LQNNFREQQ 289
Cdd:cd03120   232 GCDGlLGDNFRPTQ 245
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 1182-1410 1.13e-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: 112.87  E-value: 1.13e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1182 REKNRTSSIIPVERSRVgisSLSGEGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVM----IPDG 1257
Cdd:cd14545     1 LNRYRDRDPYDHDRSRV---KLKQGDNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMlnklMEKG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1258 QNMAEDefvYWPNKDEPINC---ESFKVTLMAEEHKclsneEKLIIQDFILEATQDDYVLEVRHFQCPKWPN---PDSPI 1331
Cdd:cd14545    78 QIKCAQ---YWPQGEGNAMIfedTGLKVTLLSEEDK-----SYYTVRTLELENLKTQETREVLHFHYTTWPDfgvPESPA 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1332 SKTFELISVIKEEAANRD-GPMIVHDEHGGVTAGTFCALTTLMHQLEKEN--SVDVYQVAKMINLMRPGVFADIEQYQFL 1408
Cdd:cd14545   150 AFLNFLQKVRESGSLSSDvGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNpsSVDVKKVLLEMRKYRMGLIQTPDQLRFS 229


                  ..
gi 332205945 1409 YK 1410
Cdd:cd14545   230 YL 231
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 1169-1413 1.33e-27

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


Pssm-ID: 350456 [Multi-domain]  Cd Length: 277  Bit Score: 113.97  E-value: 1.33e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1169 QQSDY--SAALKQCNREKNRTSSIIPVERSRVgisSLSGEGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDH 1246
Cdd:cd14608    11 EASDFpcRVAKLPKNKNRNRYRDVSPFDHSRI---KLHQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQ 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1247 NAQLVVMIpdgQNMAEDEFV----YWPNKDEP---INCESFKVTLMAEEHKCLSNEEKLIIQDFILEATQddyvlEVRHF 1319
Cdd:cd14608    88 KSRGVVML---NRVMEKGSLkcaqYWPQKEEKemiFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETR-----EILHF 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1320 QCPKWPN---PDSPISKTFELISVIKEEAANRD-GPMIVHDEHGGVTAGTFCALTT---LMHQLEKENSVDVYQVAKMIN 1392
Cdd:cd14608   160 HYTTWPDfgvPESPASFLNFLFKVRESGSLSPEhGPVVVHCSAGIGRSGTFCLADTcllLMDKRKDPSSVDIKKVLLEMR 239

                         250       260
                  ....*....|....*....|.
gi 332205945 1393 LMRPGVFADIEQYQFLYKVIL 1413
Cdd:cd14608   240 KFRMGLIQTADQLRFSYLAVI 260
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 1210-1410 2.11e-27

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


Pssm-ID: 350390 [Multi-domain]  Cd Length: 202  Bit Score: 110.98  E-value: 2.11e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1210 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVM----IPDGQNMAEDefvYWPNK-DEPINCESFKVTL 1284
Cdd:cd14542     1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMacreFEMGKKKCER---YWPEEgEEQLQFGPFKISL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1285 MAEEHKClsneekliiQDFI---LEATQDDYVLEVRHFQCPKWPNPDSPISKT--FELISVIKEEAANRDGPMIVHDEHG 1359
Cdd:cd14542    78 EKEKRVG---------PDFLirtLKVTFQKESRTVYQFHYTAWPDHGVPSSVDpiLDLVRLVRDYQGSEDVPICVHCSAG 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 332205945 1360 GVTAGTFCALT---TLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYK 1410
Cdd:cd14542   149 CGRTGTICAIDyvwNLLKTGKIPEEFSLFDLVREMRKQRPAMVQTKEQYELVYR 202
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 1169-1417 2.55e-27

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


Pssm-ID: 350472 [Multi-domain]  Cd Length: 284  Bit Score: 113.29  E-value: 2.55e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1169 QQSDYSAALKQCNREKNRTSSIIPVERSRVGISSLSG-EGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHN 1247
Cdd:cd14624    35 QQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGiPGSDYINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQR 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1248 AQLVVMIPDGQNMAE---DEfvYWPNKDEPINcESFKVTLMAEEHKClsneeKLIIQDFILEATQDDYVLEVRHFQCPKW 1324
Cdd:cd14624   115 SATVVMMTKLEERSRvkcDQ--YWPSRGTETY-GLIQVTLLDTVELA-----TYCVRTFALYKNGSSEKREVRQFQFTAW 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1325 PNPDSPISKTFELISVIKEEAAN--RDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADI 1402
Cdd:cd14624   187 PDHGVPEHPTPFLAFLRRVKTCNppDAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTE 266

                         250
                  ....*....|....*
gi 332205945 1403 EQYQFLYKVILSLVS 1417
Cdd:cd14624   267 DQYIFIHDALLEAVT 281
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 1210-1413 2.64e-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: 110.93  E-value: 2.64e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1210 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDgQNMAEDEFVYWP----NKDEPINCESFKVTLm 1285
Cdd:cd14635     1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLND-VDPAQLCPQYWPengvHRHGPIQVEFVSADL- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1286 aeehkclsnEEKLIIQDF-ILEAT--QDDYVLeVRHFQCPKWP-NPDSPISKT--FELISVI---KEEAANRDGPMIVHD 1356
Cdd:cd14635    79 ---------EEDIISRIFrIYNAArpQDGYRM-VQQFQFLGWPmYRDTPVSKRsfLKLIRQVdkwQEEYNGGEGRTVVHC 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 332205945 1357 EHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKVIL 1413
Cdd:cd14635   149 LNGGGRSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVAL 205
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 1208-1413 4.60e-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: 110.50  E-value: 4.60e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1208 TDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAEDE-FVYWPNKDEPINceSFKVTLMA 1286
Cdd:cd14631    13 SDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKcYKYWPDDTEVYG--DFKVTCVE 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1287 EEHKClsneeKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKT--FELISVIKEEAANRDGPMIVHDEHGGVTAG 1364
Cdd:cd14631    91 MEPLA-----EYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATglLSFIRRVKLSNPPSAGPIVVHCSAGAGRTG 165

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 332205945 1365 TFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKVIL 1413
Cdd:cd14631   166 CYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAIL 214
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 1155-1417 5.45e-27

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


Pssm-ID: 350473 [Multi-domain]  Cd Length: 282  Bit Score: 112.49  E-value: 5.45e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1155 KLEKQFQLLSQSniQQSDYSAALKQCNREKNRTSSIIPVERSRVGISSLSG-EGTDYINASYIMGYYQSNEFIITQHPLL 1233
Cdd:cd14625    23 KLSQEYESIDPG--QQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGiMGSDYINANYIDGYRKQNAYIATQGPLP 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1234 HTIKDFWRMIWDHNAQLVVM---IPDGQNMAEDEfvYWPNKdepiNCESF---KVTLMAEEHKClsneeKLIIQDFILEA 1307
Cdd:cd14625   101 ETFGDFWRMVWEQRSATVVMmtkLEEKSRIKCDQ--YWPSR----GTETYgmiQVTLLDTIELA-----TFCVRTFSLHK 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1308 TQDDYVLEVRHFQCPKWPNPDSPISKTFELISVIKEEAAN--RDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVY 1385
Cdd:cd14625   170 NGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNppDAGPIVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIY 249

                         250       260       270
                  ....*....|....*....|....*....|..
gi 332205945 1386 QVAKMINLMRPGVFADIEQYQFLYKVILSLVS 1417
Cdd:cd14625   250 GHVTLMRSQRNYMVQTEDQYSFIHDALLEAVA 281
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 1153-1407 5.61e-27

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


Pssm-ID: 350458 [Multi-domain]  Cd Length: 283  Bit Score: 112.46  E-value: 5.61e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1153 KTKLEKQFQLLSQSNIQQSDYSAALKQCNREKNRTSSIIPVERSRVGISSL-SGEGTDYINASYIMGYYQSN-EFIITQH 1230
Cdd:cd14610    16 KNRLEKEWEALCAYQAEPNATNVAQREENVQKNRSLAVLPYDHSRIILKAEnSHSHSDYINASPIMDHDPRNpAYIATQG 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1231 PLLHTIKDFWRMIWDHNAQLVVMI-PDGQNMAEDEFVYWPnkDEPINC-ESFKVTLMAEEHKClsneEKLIIQDFILEAT 1308
Cdd:cd14610    96 PLPATVADFWQMVWESGCVVIVMLtPLAENGVKQCYHYWP--DEGSNLyHIYEVNLVSEHIWC----EDFLVRSFYLKNL 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1309 QDDYVLEVRHFQCPKWPNPDSPIS--KTFELISVIKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEK-ENSVDVY 1385
Cdd:cd14610   170 QTNETRTVTQFHFLSWNDQGVPAStrSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLNKMAKgAKEIDIA 249

                         250       260
                  ....*....|....*....|..
gi 332205945 1386 QVAKMINLMRPGVFADIEQYQF 1407
Cdd:cd14610   250 ATLEHLRDQRPGMVQTKEQFEF 271
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 1181-1416 6.36e-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: 112.05  E-value: 6.36e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1181 NREKNRTSSIIPVERSRVGISSLSGEGT---DYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIpdg 1257
Cdd:cd17667    27 NKHKNRYINILAYDHSRVKLRPLPGKDSkhsDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMI--- 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1258 QNMAE------DEfvYWPNKdepiNCESFK---VTLMAEE-HKCLSneekliIQDFILEATQDDYVLE-----------V 1316
Cdd:cd17667   104 TNLVEkgrrkcDQ--YWPTE----NSEEYGniiVTLKSTKiHACYT------VRRFSIRNTKVKKGQKgnpkgrqnertV 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1317 RHFQCPKWPNPDSPiSKTFELISVIKEEAANRD---GPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINL 1393
Cdd:cd17667   172 IQYHYTQWPDMGVP-EYALPVLTFVRRSSAARTpemGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRT 250

                         250       260
                  ....*....|....*....|...
gi 332205945 1394 MRPGVFADIEQYQFLYKVILSLV 1416
Cdd:cd17667   251 QRNYLVQTEEQYIFIHDALLEAI 273
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 915-1124 1.26e-26

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


Pssm-ID: 350485 [Multi-domain]  Cd Length: 207  Bit Score: 109.23  E-value: 1.26e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  915 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRR-KCDQYWPADGSEEYGNFLVTQKSVQ 993
Cdd:cd14637     1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWPEPGLQQYGPMEVEFVSGS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  994 VLAYYTVRNFTLRN-TKIKKGSQkgrpsgrVVTQYHYTQW-PDMGVPEYS---LPVLTFVRKaaYAKRHAVGPVVVHCSA 1068
Cdd:cd14637    81 ADEDIVTRLFRVQNiTRLQEGHL-------MVRHFQFLRWsAYRDTPDSKkafLHLLASVEK--WQRESGEGRTVVHCLN 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 332205945 1069 GVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVE 1124
Cdd:cd14637   152 GGGRSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 1181-1412 2.58e-26

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


Pssm-ID: 350392 [Multi-domain]  Cd Length: 251  Bit Score: 109.47  E-value: 2.58e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1181 NREKNRTSSIIPVERSRVGISSL--SGEGTDYINASYIM-------GYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLV 1251
Cdd:cd14544     1 NKGKNRYKNILPFDHTRVILKDRdpNVPGSDYINANYIRnenegptTDENAKTYIATQGCLENTVSDFWSMVWQENSRVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1252 VMIPDGQNMAEDEFV-YWPnkDEpincesfkVTLMAEEHKCLSNEEKLIIQDFIL------EATQDDYVLEVRHFQCPKW 1324
Cdd:cd14544    81 VMTTKEVERGKNKCVrYWP--DE--------GMQKQYGPYRVQNVSEHDTTDYTLrelqvsKLDQGDPIREIWHYQYLSW 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1325 PNPDSPiSKTFELISVI-----KEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKEN---SVDVYQVAKMINLMRP 1396
Cdd:cd14544   151 PDHGVP-SDPGGVLNFLedvnqRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGldcDIDIQKTIQMVRSQRS 229

                         250
                  ....*....|....*.
gi 332205945 1397 GVFADIEQYQFLYKVI 1412
Cdd:cd14544   230 GMVQTEAQYKFIYVAV 245
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 915-1124 5.46e-26

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


Pssm-ID: 350483 [Multi-domain]  Cd Length: 206  Bit Score: 107.08  E-value: 5.46e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  915 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLveKGRRKCDQYWPADGSEEYGNFLVTQKSVQV 994
Cdd:cd14635     1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDV--DPAQLCPQYWPENGVHRHGPIQVEFVSADL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  995 LAYYTVRNFTLRNTkikkgsqkGRPSG--RVVTQYHYTQWPDM-GVPEYSLPVLTFVRKAAYAKRH---AVGPVVVHCSA 1068
Cdd:cd14635    79 EEDIISRIFRIYNA--------ARPQDgyRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEyngGEGRTVVHCLN 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 332205945 1069 GVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVE 1124
Cdd:cd14635   151 GGGRSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 1153-1407 1.10e-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: 1.10e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1153 KTKLEKQFQLLSQSNIQQSDYSAALKQCNREKNRTSSIIPVERSRVGI-SSLSGEGTDYINASYIMGY-YQSNEFIITQH 1230
Cdd:cd14609    14 RDRLAKEWQALCAYQAEPNTCSTAQGEANVKKNRNPDFVPYDHARIKLkAESNPSRSDYINASPIIEHdPRMPAYIATQG 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1231 PLLHTIKDFWRMIWDHNAQLVVM----IPDGQNMAEDefvYWPNKDEPINcESFKVTLMAEEHKClsneEKLIIQDFILE 1306
Cdd:cd14609    94 PLSHTIADFWQMVWENGCTVIVMltplVEDGVKQCDR---YWPDEGSSLY-HIYEVNLVSEHIWC----EDFLVRSFYLK 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1307 ATQDDYVLEVRHFQCPKWPNPDSPiSKTFELISV---IKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKE-NSV 1382
Cdd:cd14609   166 NVQTQETRTLTQFHFLSWPAEGIP-SSTRPLLDFrrkVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKGvKEI 244

                         250       260
                  ....*....|....*....|....*
gi 332205945 1383 DVYQVAKMINLMRPGVFADIEQYQF 1407
Cdd:cd14609   245 DIAATLEHVRDQRPGMVRTKDQFEF 269
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 1210-1413 1.20e-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: 106.29  E-value: 1.20e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1210 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIpdgQNMAEDEFV----YWPNKDEPINceSFKVTLM 1285
Cdd:cd14632     1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMI---TKLVEVGRVkcskYWPDDSDTYG--DIKITLL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1286 AEEhkclsNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKT--FELISVIKEEAANRDGPMIVHDEHGGVTA 1363
Cdd:cd14632    76 KTE-----TLAEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATglLAFIRRVKASTPPDAGPVVVHCSAGAGRT 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 332205945 1364 GTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKVIL 1413
Cdd:cd14632   151 GCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAIL 200
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 1184-1409 1.32e-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: 106.54  E-value: 1.32e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1184 KNRTSSIIPVERSRVGI--SSLSGEGTDYINASYIMGYY-QSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNM 1260
Cdd:cd14611     2 KNRYKTILPNPHSRVCLkpKNSNDSLSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1261 AEDEFVYWPNKDEPINcesfKVTLMAeehKCLSNEEKLIIQDFILEatQDDYVLEVRHFQCPKWPNPDSPISKT--FELI 1338
Cdd:cd14611    82 NEKCVLYWPEKRGIYG----KVEVLV---NSVKECDNYTIRNLTLK--QGSQSRSVKHYWYTSWPDHKTPDSAQplLQLM 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332205945 1339 SVIKEE--AANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLY 1409
Cdd:cd14611   153 LDVEEDrlASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 915-1124 2.41e-25

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


Pssm-ID: 350484 [Multi-domain]  Cd Length: 206  Bit Score: 105.49  E-value: 2.41e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  915 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNL-VEKGrrkCDQYWPADGSEEYGNFLVTQKSVQ 993
Cdd:cd14636     1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVdLAQG---CPQYWPEEGMLRYGPIQVECMSCS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  994 VLAYYTVRNFTLRN-TKIKKGSQkgrpsgrVVTQYHYTQWPD-MGVPEYS---LPVLTFVRKAAYAKRHAVGPVVVHCSA 1068
Cdd:cd14636    78 MDCDVISRIFRICNlTRPQEGYL-------MVQQFQYLGWAShREVPGSKrsfLKLILQVEKWQEECDEGEGRTIIHCLN 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 332205945 1069 GVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVE 1124
Cdd:cd14636   151 GGGRSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 1181-1413 6.77e-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: 6.77e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1181 NREKNRTSSIIPVERSRVgissLSGEGTDYINASYIMGYYQSNEF--IITQHPLLHTIKDFWRMIWDHNAQLVVMIpdgQ 1258
Cdd:cd14597     3 NRKKNRYKNILPYDTTRV----PLGDEGGYINASFIKMPVGDEEFvyIACQGPLPTTVADFWQMVWEQKSTVIAMM---T 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1259 NMAEDEFV----YWP---NKDEPINcESFKVTLMAEEHkclsnEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPi 1331
Cdd:cd14597    76 QEVEGGKIkcqrYWPeilGKTTMVD-NRLQLTLVRMQQ-----LKNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTP- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1332 SKTFELISVIK-EEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYK 1410
Cdd:cd14597   149 SQPEQLLTFISyMRHIHKSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQ 228


                  ...
gi 332205945 1411 VIL 1413
Cdd:cd14597   229 VIL 231
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 1210-1413 1.96e-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: 102.80  E-value: 1.96e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1210 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDgQNMAEDEFVYWPNKDE----PINCESFKVTLM 1285
Cdd:cd14636     1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNE-VDLAQGCPQYWPEEGMlrygPIQVECMSCSMD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1286 AEehkCLSNeeklIIQDFILEATQDDYVLeVRHFQCPKWP-NPDSPISKT--FELISVI---KEEAANRDGPMIVHDEHG 1359
Cdd:cd14636    80 CD---VISR----IFRICNLTRPQEGYLM-VQQFQYLGWAsHREVPGSKRsfLKLILQVekwQEECDEGEGRTIIHCLNG 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 332205945 1360 GVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKVIL 1413
Cdd:cd14636   152 GGRSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVAL 205
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 1210-1410 2.89e-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: 2.89e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1210 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAEDEFV-YWPNKdepiNCESFKVTLMaee 1288
Cdd:cd14551     1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSqYWPDQ----GCWTYGNLRV--- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1289 hkCLSNEEKLI---IQDFILEATQDDY----VLEVRHFQCPKWPN---PDSPISkTFELISVIKEEAANRDGPMIVHDEH 1358
Cdd:cd14551    74 --RVEDTVVLVdytTRKFCIQKVNRGIgekrVRLVTQFHFTSWPDfgvPFTPIG-MLKFLKKVKSANPPRAGPIVVHCSA 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 332205945 1359 GGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYK 1410
Cdd:cd14551   151 GVGRTGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 1210-1413 1.17e-23

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


Pssm-ID: 350386 [Multi-domain]  Cd Length: 207  Bit Score: 100.53  E-value: 1.17e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1210 YINASYIMGYYQSNEF--IITQHPLLHTIKDFWRMIWDHNAQLVVMIPdgQNMaEDEFV----YWPnkdepincESFKVT 1283
Cdd:cd14538     1 YINASHIRIPVGGDTYhyIACQGPLPNTTGDFWQMVWEQKSEVIAMVT--QDV-EGGKVkchrYWP--------DSLNKP 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1284 LMAEEHKCLSNEEKLIIQDFI-----LEATQDDYVLEVRHFQCPKWPNPDSPISkTFELISVIKE-EAANRDGPMIVHDE 1357
Cdd:cd14538    70 LICGGRLEVSLEKYQSLQDFVirrisLRDKETGEVHHITHLNFTTWPDHGTPQS-ADPLLRFIRYmRRIHNSGPIVVHCS 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 332205945 1358 HGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKVIL 1413
Cdd:cd14538   149 AGIGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACL 204
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 915-1123 3.51e-23

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


Pssm-ID: 350508 [Multi-domain]  Cd Length: 205  Bit Score: 98.98  E-value: 3.51e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  915 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITN---LVEkgrrkcDQ--YWPAdgSEEYGN---FL 986
Cdd:cd17670     1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDnqgLAE------DEfvYWPS--REESMNceaFT 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  987 VTQKSVQVLAYYT-----VRNFTLRNTKIKKGSQkgrpsgrvVTQYHYTQWPDMGVPEYSLPVLTFVRKAAYAKRHavGP 1061
Cdd:cd17670    73 VTLISKDRLCLSNeeqiiIHDFILEATQDDYVLE--------VRHFQCPKWPNPDAPISSTFELINVIKEEALTRD--GP 142

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 332205945 1062 VVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLV 1123
Cdd:cd17670   143 TIVHDEFGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1315-1414 5.69e-23

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 95.12  E-value: 5.69e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945   1315 EVRHFQCPKWPNPDSPISKT--FELISVIKEE--AANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKE-NSVDVYQVAK 1389
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDsiLELLRAVKKNlnQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 332205945   1390 MINLMRPGVFADIEQYQFLYKVILS 1414
Cdd:smart00404   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 1315-1414 5.69e-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: 95.12  E-value: 5.69e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945   1315 EVRHFQCPKWPNPDSPISKT--FELISVIKEE--AANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKE-NSVDVYQVAK 1389
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDsiLELLRAVKKNlnQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 332205945   1390 MINLMRPGVFADIEQYQFLYKVILS 1414
Cdd:smart00012   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 1210-1413 2.07e-22

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


Pssm-ID: 350506 [Multi-domain]  Cd Length: 209  Bit Score: 96.97  E-value: 2.07e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1210 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIpdgQNMAE------DEfvYWPNKDEPiNCESFKVT 1283
Cdd:cd17668     1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMI---TNLVEkgrrkcDQ--YWPADGSE-EYGNFLVT 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1284 LmaeehKCLSNEEKLIIQDFILEATQDDYVLE--------VRHFQCPKWPNPDSPiSKTFELISVIKEEAANRD---GPM 1352
Cdd:cd17668    75 Q-----KSVQVLAYYTVRNFTLRNTKIKKGSQkgrpsgrvVTQYHYTQWPDMGVP-EYTLPVLTFVRKASYAKRhavGPV 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 332205945 1353 IVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKVIL 1413
Cdd:cd17668   149 VVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 1210-1413 3.29e-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: 96.35  E-value: 3.29e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1210 YINASYIMGYYQSNE--FIITQHPLLHTIKDFWRMIWDHNAQLVVMIPD----GQNMAEDefvYWPNK-DEPINCESFKV 1282
Cdd:cd14596     1 YINASYITMPVGEEElfYIATQGPLPSTIDDFWQMVWENRSDVIAMMTReverGKVKCHR---YWPETlQEPMELENYQL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1283 TLmaEEHKCLsneEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTfELISVIK-EEAANRDGPMIVHDEHGGV 1361
Cdd:cd14596    78 RL--ENYQAL---QYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSD-QLVKFICyMRKVHNTGPIVVHCSAGIG 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 332205945 1362 TAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKVIL 1413
Cdd:cd14596   152 RAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVL 203
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 1210-1410 3.61e-22

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: 96.05  E-value: 3.61e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1210 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAEDE-FVYWPNKDEPINC-ESFKVTLMAE 1287
Cdd:cd14557     1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKcAQYWPSMEEGSRAfGDVVVKINEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1288 EHkClsneEKLIIQDFILEATQDDY-VLEVRHFQCPKWPN---PDSPiSKTFELISVIKEEAANRDGPMIVHDEHGGVTA 1363
Cdd:cd14557    81 KI-C----PDYIIRKLNINNKKEKGsGREVTHIQFTSWPDhgvPEDP-HLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRT 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 332205945 1364 GTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYK 1410
Cdd:cd14557   155 GTYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 915-1123 3.85e-22

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


Pssm-ID: 350507 [Multi-domain]  Cd Length: 204  Bit Score: 95.83  E-value: 3.85e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  915 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCdQYWPA-DGSEEYGNFLVTQKSVQ 993
Cdd:cd17669     1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEF-VYWPNkDEPINCETFKVTLIAEE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  994 VLAYYTVRNFTLRNTkIKKGSQkgrpSGRVVTQYHYT--QWPDMGVP-EYSLPVLTFVRKAAYAKRhavGPVVVHCSAGV 1070
Cdd:cd17669    80 HKCLSNEEKLIIQDF-ILEATQ----DDYVLEVRHFQcpKWPNPDSPiSKTFELISIIKEEAANRD---GPMIVHDEHGG 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 332205945 1071 GRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLV 1123
Cdd:cd17669   152 VTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 877-1134 4.83e-22

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 98.50  E-value: 4.83e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  877 SSNHPDNKHK--NRYINIVAYDHSRVKLaqlaEKDGKLTDyinANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVE 954
Cdd:PHA02740   45 ACAQAENKAKdeNLALHITRLLHRRIKL----FNDEKVLD---ARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQ 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  955 VIVMITNLVEKgrrKC-DQYWpadgSEEYGNFLVTQK-SVQVLAYYTVRNFTLrnTKIKKGSQKGRpsGRVVTQYHYTQW 1032
Cdd:PHA02740  118 IIVLISRHADK---KCfNQFW----SLKEGCVITSDKfQIETLEIIIKPHFNL--TLLSLTDKFGQ--AQKISHFQYTAW 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1033 PDMGVPEYSLPVLTFV--RKAAYA--KRHA----VGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQ 1104
Cdd:PHA02740  187 PADGFSHDPDAFIDFFcnIDDLCAdlEKHKadgkIAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQK 266

                         250       260       270
                  ....*....|....*....|....*....|
gi 332205945 1105 RNYLVQTEEQYVFIHDtLVEAILSKETEVL 1134
Cdd:PHA02740  267 KYGCMNCLDDYVFCYH-LIAAYLKEKFDIL 295
PHA02738 PHA02738
hypothetical protein; Provisional
 1170-1412 5.81e-22

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 98.46  E-value: 5.81e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1170 QSDYSAALKqcNREKNRTSSIIPVERSRVGISSLSGEGtDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQ 1249
Cdd:PHA02738   40 DGTFNAEKK--NRKLNRYLDAVCFDHSRVILPAERNRG-DYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQ 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1250 LVVMI-PDGQNMAEDEFVYWPNKDE-PINCESFKVTLMAEEHKCLSNEEKLIIQDFIlEATQddyvlEVRHFQCPKWPNP 1327
Cdd:PHA02738  117 IIVMLcKKKENGREKCFPYWSDVEQgSIRFGKFKITTTQVETHPHYVKSTLLLTDGT-SATQ-----TVTHFNFTAWPDH 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1328 DSPiSKTFELISVI-------KEEAANR---------DGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMI 1391
Cdd:PHA02738  191 DVP-KNTSEFLNFVlevrqcqKELAQESlqighnrlqPPPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSI 269

                         250       260
                  ....*....|....*....|.
gi 332205945 1392 NLMRPGVFADIEQYQFLYKVI 1412
Cdd:PHA02738  270 RNQRYYSLFIPFQYFFCYRAV 290
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 1181-1412 1.04e-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: 96.19  E-value: 1.04e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1181 NREKNRTSSIIPVERSRVgisSLSGEGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIpdgQNM 1260
Cdd:cd14607    24 NRNRNRYRDVSPYDHSRV---KLQNTENDYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVML---NRI 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1261 AEDEFV----YWPNKDEPINCES---FKVTLMAEEHKCLSNEEKLIIQDFILEATQDdyvleVRHFQCPKWPN---PDSP 1330
Cdd:cd14607    98 VEKDSVkcaqYWPTDEEEVLSFKetgFSVKLLSEDVKSYYTVHLLQLENINSGETRT-----ISHFHYTTWPDfgvPESP 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1331 ISKTFELISVIKEEAANRD-GPMIVHDEHGGVTAGTFCALTTLMHQLEKEN--SVDVYQVAKMINLMRPGVFADIEQYQF 1407
Cdd:cd14607   173 ASFLNFLFKVRESGSLSPEhGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDIKQVLLDMRKYRMGLIQTPDQLRF 252


                  ....*
gi 332205945 1408 LYKVI 1412
Cdd:cd14607   253 SYMAV 257
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 1181-1413 6.13e-21

catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein phosphatase non-receptor type 3 (PTPN3), also called protein-tyrosine phosphatase H1 (PTP-H1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN3 interacts with mitogen-activated protein kinase p38gamma and serves as its specific phosphatase. PTPN3 and p38gamma cooperate to promote Ras-induced oncogenesis. PTPN3 is a large modular protein containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain. Its PDZ domain binds with the PDZ-binding motif of p38gamma and enables efficient tyrosine dephosphorylation.


Pssm-ID: 350448 [Multi-domain]  Cd Length: 274  Bit Score: 94.53  E-value: 6.13e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1181 NREKNRTSSIIPVERSRVgissLSGEGTDYINASY----IMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPD 1256
Cdd:cd14600    40 NMDKNRYKDVLPYDATRV----VLQGNEDYINASYvnmeIPSANIVNKYIATQGPLPHTCAQFWQVVWEQKLSLIVMLTT 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1257 ----GQNMAEDefvYWPNKDEPINCESFKVTLMAEEHKClsneeKLIIQDFILEATQDDYVLEVRHFQCPKWPN---PDS 1329
Cdd:cd14600   116 lterGRTKCHQ---YWPDPPDVMEYGGFRVQCHSEDCTI-----AYVFREMLLTNTQTGEERTVTHLQYVAWPDhgvPDD 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1330 PiSKTFELISVIKEEAANRDgPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLY 1409
Cdd:cd14600   188 S-SDFLEFVNYVRSKRVENE-PVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKFVC 265


                  ....
gi 332205945 1410 KVIL 1413
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 ...
 1210-1412 1.24e-19

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


Pssm-ID: 350394 [Multi-domain]  Cd Length: 208  Bit Score: 89.04  E-value: 1.24e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1210 YINASYIMGYYQSNE-FIITQHPLLHTIKDFWRMIWDHNAQLVVMI-PDGQNMAEDEFVYWPNKDEPINcESFKVTLMAE 1287
Cdd:cd14546     1 YINASTIYDHDPRNPaYIATQGPLPHTIADFWQMIWEQGCVVIVMLtRLQENGVKQCARYWPEEGSEVY-HIYEVHLVSE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1288 EHKClsneEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPIS-KTF-ELISVIKEEAANRDGPMIVHDEHGGVTAGT 1365
Cdd:cd14546    80 HIWC----DDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASaKPLlEFRRKVNKSYRGRSCPIVVHCSDGAGRTGT 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 332205945 1366 FCALTTLMHQLEK-ENSVDVYQVAKMINLMRPGVFADIEQYQFLYKVI 1412
Cdd:cd14546   156 YILIDMVLNRMAKgAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAV 203
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 1181-1418 1.70e-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: 89.69  E-value: 1.70e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1181 NREKNRTSSIIPVERSRVGISS--LSGEGTDYINASYIMGYYQSN--------EFIITQHPLLHTIKDFWRMIWDHNAQL 1250
Cdd:cd14605     2 NKNKNRYKNILPFDHTRVVLHDgdPNEPVSDYINANIIMPEFETKcnnskpkkSYIATQGCLQNTVNDFWRMVFQENSRV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1251 VVMIPDGQNMAEDEFV-YWPNKDEPINCESFKVTLMAEE--HKCLSNEEKLIiqdfilEATQDDYVLEVRHFQCPKWPN- 1326
Cdd:cd14605    82 IVMTTKEVERGKSKCVkYWPDEYALKEYGVMRVRNVKESaaHDYILRELKLS------KVGQGNTERTVWQYHFRTWPDh 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1327 --PDSP--ISKTFELISvIKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKEN---SVDVYQVAKMINLMRPGVF 1399
Cdd:cd14605   156 gvPSDPggVLDFLEEVH-HKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGvdcDIDVPKTIQMVRSQRSGMV 234

                         250
                  ....*....|....*....
gi 332205945 1400 ADIEQYQFLYKVILSLVST 1418
Cdd:cd14605   235 QTEAQYRFIYMAVQHYIET 253
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 1210-1410 3.78e-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: 87.44  E-value: 3.78e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1210 YINASYIMGYYQ-SNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAEDEFV-YWP-NKDEPINCESFKVTLMA 1286
Cdd:cd14539     1 YINASLIEDLTPyCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHrYWPtERGQALVYGAITVSLQS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1287 EehKCLSNEEKLIIQDFILEATQDDYVLevrHFQCPKWPNPDSPISKTfELISVIKE------EAANRDGPMIVHDEHGG 1360
Cdd:cd14539    81 V--RTTPTHVERIISIQHKDTRLSRSVV---HLQFTTWPELGLPDSPN-PLLRFIEEvhshylQQRSLQTPIVVHCSSGV 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 332205945 1361 VTAGTFCALTTLMHQLEKENSV-DVYQVAKMINLMRPGVFADIEQYQFLYK 1410
Cdd:cd14539   155 GRTGAFCLLYAAVQEIEAGNGIpDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 1156-1419 5.95e-19

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 89.29  E-value: 5.95e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1156 LEKQFQLLSQSNIQQSDYSAaLKQCNREKNRTSSIIPVERSRVGISSLSGeGTDYINASYIMGYYQSNEFIITQHPLLHT 1235
Cdd:PHA02742   28 LKEEHEHIMQEIVAFSCNES-LELKNMKKCRYPDAPCFDRNRVILKIEDG-GDDFINASYVDGHNAKGRFICTQAPLEET 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1236 IKDFWRMIWDHNAQLVVMIP----DGQnmaEDEFVYWpNKDEPINCESFKVTLMAEEHKCLSNEEkliIQDFILEATQDD 1311
Cdd:PHA02742  106 ALDFWQAIFQDQVRVIVMITkimeDGK---EACYPYW-MPHERGKATHGEFKIKTKKIKSFRNYA---VTNLCLTDTNTG 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1312 YVLEVRHFQCPKWPNPDSP--ISKTFELISVIKE-----------EAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEK 1378
Cdd:PHA02742  179 ASLDIKHFAYEDWPHGGLPrdPNKFLDFVLAVREadlkadvdikgENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNE 258

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 332205945 1379 ENSVDVYQVAKMINLMRPGVFADIEQYQFLYKVIL---SLVSTR 1419
Cdd:PHA02742  259 RAIIPLLSIVRDLRKQRHNCLSLPQQYIFCYFIVLifaKLMADK 302
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 1181-1418 8.41e-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: 88.01  E-value: 8.41e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1181 NREKNRTSSIIPVERSRVGISSLSGE--GTDYINASYIMGYYQSNE-----FIITQHPLLHTIKDFWRMIWDHNAQLVVM 1253
Cdd:cd14606    18 NKSKNRYKNILPFDHSRVILQGRDSNipGSDYINANYVKNQLLGPDenaktYIASQGCLEATVNDFWQMAWQENSRVIVM 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1254 ----IPDGQNMAedeFVYWPNKDEPINCESFKVTLMAEEHkclSNEEKL-IIQDFILEATqdDYVLEVRHFQCPKWPNPD 1328
Cdd:cd14606    98 ttreVEKGRNKC---VPYWPEVGMQRAYGPYSVTNCGEHD---TTEYKLrTLQVSPLDNG--ELIREIWHYQYLSWPDHG 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1329 SPiSKTFELISVI-----KEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKEN---SVDVYQVAKMINLMRPGVFA 1400
Cdd:cd14606   170 VP-SEPGGVLSFLdqinqRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGldcDIDIQKTIQMVRAQRSGMVQ 248

                         250
                  ....*....|....*...
gi 332205945 1401 DIEQYQFLYKVILSLVST 1418
Cdd:cd14606   249 TEAQYKFIYVAIAQFIET 266
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 1174-1416 1.05e-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: 88.13  E-value: 1.05e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1174 SAALKQcNREKNRTSSIIPVERSRVGISSLSGEGTDYINASYIMGYYQSNE--FIITQHPLLHTIKDFWRMIWDHNAQLV 1251
Cdd:cd14599    32 TATLPE-NAERNRIREVVPYEENRVELVPTKENNTGYINASHIKVTVGGEEwhYIATQGPLPHTCHDFWQMVWEQGVNVI 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1252 VMIpdgqnMAEDE------FVYWPNKDEPINCES---FKVTLMAEEHKCLSNEEKLIIQDFIleATQDDYVLevrHFQCP 1322
Cdd:cd14599   111 AMV-----TAEEEggrsksHRYWPKLGSKHSSATygkFKVTTKFRTDSGCYATTGLKVKHLL--SGQERTVW---HLQYT 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1323 KWPNPDSP------ISKTFELISV------IKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKM 1390
Cdd:cd14599   181 DWPDHGCPeevqgfLSYLEEIQSVrrhtnsMLDSTKNCNPPIVVHCSAGVGRTGVVILTELMIGCLEHNEKVEVPVMLRH 260

                         250       260
                  ....*....|....*....|....*.
gi 332205945 1391 INLMRPGVFADIEQYQFLYKVILSLV 1416
Cdd:cd14599   261 LREQRMFMIQTIAQYKFVYQVLIQFL 286
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1209-1414 1.20e-18

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


Pssm-ID: 350389 [Multi-domain]  Cd Length: 212  Bit Score: 86.23  E-value: 1.20e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1209 DYINASY----IMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVM----IPDGQNMAEDefvYWPNKDEPINCESF 1280
Cdd:cd14541     1 DYINANYvnmeIPGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMlttlVERGRVKCHQ---YWPDLGETMQFGNL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1281 KVTLMAEEhkclsNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPiSKTFELISVIKEEAANRDG---PMIVHDE 1357
Cdd:cd14541    78 QITCVSEE-----VTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVP-DDSSDFLDFVKRVRQNRVGmvePTVVHCS 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 332205945 1358 HG-GVTaGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKVILS 1414
Cdd:cd14541   152 AGiGRT-GVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAILR 208
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1210-1413 1.57e-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: 82.89  E-value: 1.57e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1210 YINASYIMGYYQSNE--FIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQ-NMAEDEFVYWP---NKDEPINCESFKVT 1283
Cdd:cd14540     1 YINASHITATVGGKQrfYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEeGGREKCFRYWPtlgGEHDALTFGEYKVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1284 LmaeehKCLSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPN---PDSPisKTF-----ELISV---IKEEAA--NRDG 1350
Cdd:cd14540    81 T-----KFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDhgcPEDV--SGFldfleEINSVrrhTNQDVAghNRNP 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332205945 1351 PMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKVIL 1413
Cdd:cd14540   154 PTLVHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLI 216
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 1209-1413 3.79e-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: 3.79e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1209 DYINASYIMGYYQS----NEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIpdgQNMAEDEFV----YWPNKDEPINCESF 1280
Cdd:cd14601     1 DYINANYINMEIPSssiiNRYIACQGPLPNTCSDFWQMTWEQGSSMVVML---TTQVERGRVkchqYWPEPSGSSSYGGF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1281 KVTLMAEEhkclsNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPN---PDSPiSKTFELISVIKEEAANRDGPMIVHDE 1357
Cdd:cd14601    78 QVTCHSEE-----GNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDhgvPDDS-SDFLDFVCLVRNKRAGKDEPVVVHCS 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 332205945 1358 HGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKVIL 1413
Cdd:cd14601   152 AGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAIL 207
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 1210-1409 1.34e-15

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


Pssm-ID: 350496 [Multi-domain]  Cd Length: 206  Bit Score: 77.12  E-value: 1.34e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1210 YINASYIMGYYQSN--EFIITQHPLLHTIKDFWRMIWDHNAQLVVMIP---DGQNMAEDEFVYWPNKDEPINCESFKVTL 1284
Cdd:cd17658     1 YINASLVETPASESlpKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTrlvDNYSTAKCADYFPAEENESREFGRISVTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1285 MAEEHKCLSNEEK-LIIQDFILEatqdDYVLEVRHFQCPKWPN---PDS--PISKTFELISVIKEEAanrdGPMIVHDEH 1358
Cdd:cd17658    81 KKLKHSQHSITLRvLEVQYIESE----EPPLSVLHIQYPEWPDhgvPKDtrSVRELLKRLYGIPPSA----GPIVVHCSA 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 332205945 1359 GGVTAGTFCAL-TTLMHQLEKENS-VDVYQVAKMINLMRPGVFADIEQYQFLY 1409
Cdd:cd17658   153 GIGRTGAYCTIhNTIRRILEGDMSaVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 1210-1416 1.54e-13

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


Pssm-ID: 350446 [Multi-domain]  Cd Length: 220  Bit Score: 71.54  E-value: 1.54e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1210 YINASYIMGYYQSNE--FIITQHPLLHTIKDFWRMIWDHNAQLVVMIP-DGQNMAEDEFVYWP---NKDEPINCESFKVT 1283
Cdd:cd14598     1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTaEEEGGREKSFRYWPrlgSRHNTVTYGRFKIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1284 LMAEEHKCLSNEEKLIIQDFIL--EATqddyvleVRHFQCPKWPNPDSP------ISKTFELISVIKEEAANRD-----G 1350
Cdd:cd14598    81 TRFRTDSGCYATTGLKIKHLLTgqERT-------VWHLQYTDWPEHGCPedlkgfLSYLEEIQSVRRHTNSTIDpkspnP 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332205945 1351 PMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKVILSLV 1416
Cdd:cd14598   154 PVLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFL 219
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 887-1124 5.41e-12

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


Pssm-ID: 350407 [Multi-domain]  Cd Length: 227  Bit Score: 67.04  E-value: 5.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  887 NRYINIvaydHSRVKLAqlaekDGKLtdyINANYVDGYNRPKAyIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKG 966
Cdd:cd14559     1 NRFTNI----QTRVSTP-----VGKN---LNANRVQIGNKNVA-IACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQ 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  967 RRKCDQYWPADGSeeYGNFLVTQKSVQVLAYYTVRNFTLRNTKIKKGSQKgrpsgRVVTQYHYTQWPDMG---------- 1036
Cdd:cd14559    68 RKGLPPYFRQSGT--YGSVTVKSKKTGKDELVDGLKADMYNLKITDGNKT-----ITIPVVHVTNWPDHTaisseglkel 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1037 ------VPEYSLPVLTFVRKAAYAKRHAVGPVVvHCSAGVGRTGTYIvldSMLQQIQHEGTVNIFGFLKHIRSQRN-YLV 1109
Cdd:cd14559   141 adlvnkSAEEKRNFYKSKGSSAINDKNKLLPVI-HCRAGVGRTGQLA---AAMELNKSPNNLSVEDIVSDMRTSRNgKMV 216

                         250
                  ....*....|....*
gi 332205945 1110 QTEEQYvfihDTLVE 1124
Cdd:cd14559   217 QKDEQL----DTLKE 227
fn3 pfam00041
Fibronectin type III domain;
313-401 2.24e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 58.20  E-value: 2.24e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945   313 SEPENVQADPENYTSLLVTWERPRVVYDTmIEKFAVLYQQLDGEDQtKHEFLTDGYQDlGAILNNLLPNMSYVLQIVAIC 392
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGP-ITGYEVEYRPKNSGEP-WNEITVPGTTT-SVTLTGLKPGTEYEVRVQAVN 77


                   ....*....
gi 332205945   393 TNGlYGKYS 401
Cdd:pfam00041   78 GGG-EGPPS 85
PLN02179 PLN02179
carbonic anhydrase
 49-253 5.90e-09

carbonic anhydrase


Pssm-ID: 177835  Cd Length: 235  Bit Score: 58.07  E-value: 5.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945   49 WGKKYP---TCNSPK-QSPInideDLTQVNVNLkkLKFQGWDKT-SLENTFIHNTGKTVEINLTNDyrvsggvsemvfkA 123
Cdd:PLN02179   50 WGKLNPqwkVCSTGKyQSPI----DLTDERVSL--IHDQALSRHyKPAPAVIQSRGHDVMVSWKGD-------------A 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  124 SKITFHWG-----KCNMSSDgSEHSLEGQKFPLEMQIYCFDAdrfssfeeavkgKGKLRALSILFEVGtEENLDFKAIID 198
Cdd:PLN02179  111 GKITIHQTdyklvQCHWHSP-SEHTINGTSYDLELHMVHTSA------------SGKTAVVGVLYKLG-EPDEFLTKLLN 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 332205945  199 GVESVsrfGKQ----AALDPfillNLLPNSTDKYYIYNGSLTSPPCTDTVDWIVFKDTV 253
Cdd:PLN02179  177 GIKGV---GKKeinlGIVDP----RDIRFETNNFYRYIGSLTIPPCTEGVIWTVVKRVV 228
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 1178-1417 9.18e-09

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 58.44  E-value: 9.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1178 KQCNREKNRT---SSIIPVER---SRVGISSlsgeGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLV 1251
Cdd:PHA02740   44 KACAQAENKAkdeNLALHITRllhRRIKLFN----DEKVLDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQII 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1252 VMI---PDGQNMAEdefvYWPNKDEP-INCESFKVTLMAEEHKCLSNEEKLIIQDfileatQDDYVLEVRHFQCPKWP-- 1325
Cdd:PHA02740  120 VLIsrhADKKCFNQ----FWSLKEGCvITSDKFQIETLEIIIKPHFNLTLLSLTD------KFGQAQKISHFQYTAWPad 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1326 ----NPDSPISKTFELISVI----KEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPG 1397
Cdd:PHA02740  190 gfshDPDAFIDFFCNIDDLCadleKHKADGKIAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYG 269

                         250       260
                  ....*....|....*....|
gi 332205945 1398 VFADIEQYQFLYKVILSLVS 1417
Cdd:PHA02740  270 CMNCLDDYVFCYHLIAAYLK 289
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
1026-1120 2.84e-08

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 54.21  E-value: 2.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1026 QYHYTQWPDMGVPEYS--LPVLTFVRKAAYAKRhavgPVVVHCSAGVGRTGT----YIVLDSM-LQQIqhegtvnifgfL 1098
Cdd:COG2453    49 EYLHLPIPDFGAPDDEqlQEAVDFIDEALREGK----KVLVHCRGGIGRTGTvaaaYLVLLGLsAEEA-----------L 113

                          90       100
                  ....*....|....*....|..
gi 332205945 1099 KHIRSQRNYLVQTEEQYVFIHD 1120
Cdd:COG2453   114 ARVRAARPGAVETPAQRAFLER 135
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 1060-1120 6.54e-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: 49.27  E-value: 6.54e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 332205945 1060 GPVVVHCSAGVGRTGTYIVLDSMLQQIqhegtVNIFGFLKHIRSQR-NYLVQTEEQYVFIHD 1120
Cdd:cd14494    57 EPVLVHCKAGVGRTGTLVACYLVLLGG-----MSAEEAVRIVRLIRpGGIPQTIEQLDFLIK 113
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 1027-1120 3.31e-06

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


Pssm-ID: 350356 [Multi-domain]  Cd Length: 206  Bit Score: 49.65  E-value: 3.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1027 YHYT-QWPDMGVPEYSLpVLTFVRKAAYAKRHAvGPVVVHCSAGVGRTG----TYIVldsMLQQIQHEGTVnifgflKHI 1101
Cdd:cd14506    78 YFYNfGWKDYGVPSLTT-ILDIVKVMAFALQEG-GKVAVHCHAGLGRTGvliaCYLV---YALRMSADQAI------RLV 146

                          90
                  ....*....|....*....
gi 332205945 1102 RSQRNYLVQTEEQYVFIHD 1120
Cdd:cd14506   147 RSKRPNSIQTRGQVLCVRE 165
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 313-406 3.39e-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: 3.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  313 SEPENVQADPENYTSLLVTWERPRvVYDTMIEKFAVLYQQLDGEDQTKHEflTDGYQDLGAILNNLLPNMSYVLQIVAIC 392
Cdd:cd00063     2 SPPTNLRVTDVTSTSVTLSWTPPE-DDGGPITGYVVEYREKGSGDWKEVE--VTPGSETSYTLTGLKPGTEYEFRVRAVN 78

                          90
                  ....*....|....
gi 332205945  393 TNGlYGKYSDQLIV 406
Cdd:cd00063    79 GGG-ESPPSESVTV 91
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 313-395 7.29e-06

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: 45.68  E-value: 7.29e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945    313 SEPENVQADPENYTSLLVTWERPRvvyDTMIEKFAVLYQQLDGEDQTKHEFLTDGYQDLGAILNNLLPNMSYVLQIVAIC 392
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPP---DDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78


                    ...
gi 332205945    393 TNG 395
Cdd:smart00060   79 GAG 81
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 1025-1120 5.58e-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: 44.95  E-value: 5.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1025 TQYHYTqWPDMGVP---EYSLPVLTFVRKAAYAKRHavgpVVVHCSAGVGRTGTyiVLDSMLQQIQ----HEGTVNIfgf 1097
Cdd:cd14505    74 TWHHLP-IPDGGVPsdiAQWQELLEELLSALENGKK----VLIHCKGGLGRTGL--IAACLLLELGdtldPEQAIAA--- 143

                          90       100
                  ....*....|....*....|...
gi 332205945 1098 lkhIRSQRNYLVQTEEQYVFIHD 1120
Cdd:cd14505   144 ---VRALRPGAIQTPKQENFLHQ 163
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 1026-1118 7.66e-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: 44.19  E-value: 7.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945 1026 QYHYTQWPDMGVPEYSLpVLTFVRKAAYAKrhAVG-PVVVHCSAGVGRTGT----YIVLDSMLQQIQHegtvnifgfLKH 1100
Cdd:cd14504    51 RYHHIPIEDYTPPTLEQ-IDEFLDIVEEAN--AKNeAVLVHCLAGKGRTGTmlacYLVKTGKISAVDA---------INE 118

                          90
                  ....*....|....*...
gi 332205945 1101 IRSQRNYLVQTEEQYVFI 1118
Cdd:cd14504   119 IRRIRPGSIETSEQEKFV 136
PLN02202 PLN02202
carbonate dehydratase
 1-263 1.45e-04

carbonate dehydratase


Pssm-ID: 177853 [Multi-domain]  Cd Length: 284  Bit Score: 45.43  E-value: 1.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945    1 MRILKRFLACIQLLCVCRLDwangyyrqqrKLVEEIGWSYTGALNQKNWGKKYP---TCNSPK-QSPINIDEDLTQVNVN 76
Cdd:PLN02202    4 MMMIKLCFFAIALICIAPAD----------AQTEGVVFGYKGKNGPNQWGHLNPhftKCAVGKlQSPIDIQRRQIFYNHK 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945   77 LKKLKFQgwdktslentfIHNTGKTVEINLTNDYRVSG-GVSEMVFKASKITF---HWgkcnmsSDGSEHSLEGQKFPLE 152
Cdd:PLN02202   74 LESIHRD-----------YYFTNATLVNHVCNVAMFFGeGAGDVIIDNKNYTLlqmHW------HTPSEHHLHGVQYAAE 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205945  153 MQIYCFDADrfssfeeavkgkGKLRALSILFEVGTEENL--DFKAIIDGVESVSRFGKQAALDPF--ILLNLLPNSTDKY 228
Cdd:PLN02202  137 LHMVHQAKD------------GSFAVVASLFKIGTEEPFlsQMKDKLVKLKEERFKGNHTAQVEVgkIDTRHIERKTRKY 204

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 332205945  229 YIYNGSLTSPPCTDTVDWIVFKDTVSISESQLAVF 263
Cdd:PLN02202  205 FRYIGSLTTPPCSENVSWTILGKVRSMSKEQVELL 239
 
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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