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Conserved domains on  [gi|901694078|ref|NP_001297993|]
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receptor-type tyrosine-protein phosphatase zeta isoform 4 precursor [Mus musculus]

Protein Classification

alpha_CARP_receptor_like and R-PTP-Z-2 domain-containing protein( domain architecture ID 12931151)

protein containing domains alpha_CARP_receptor_like, FN3, PTP_DSP_cys, and R-PTP-Z-2

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 ...
 865-1142 2.93e-162

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: 489.16  E-value: 2.93e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  865 FTEEFEtlkefyqEVQSCTADLGITADSSNHPDNKHKNRYVNIVAYDHSRVKLTQLAEKDGKLTDYINANYVDGYNRPKA 944
Cdd:cd17667     1 FSEDFE-------EVQRCTADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSKHSDYINANYVDGYNKAKA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  945 YIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPTDGSEEYGSFLVNQKSVQVLAYYTVRNFTLRNTK 1024
Cdd:cd17667    74 YIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTK 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1025 LKKGSQ---KGRSSGRLVTQYHYTQWPDMGVPEYSLPVLAFVRKAAQAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQI 1101
Cdd:cd17667   154 VKKGQKgnpKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQI 233

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 901694078 1102 QHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAIL 1142
Cdd:cd17667   234 KDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 274
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 1225-1428 2.57e-155

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: 467.93  E-value: 2.57e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1225 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAEDEFVYWPNKDEPINCESFKVTLMSEEH 1304
Cdd:cd17669     1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFVYWPNKDEPINCETFKVTLIAEEH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1305 KCLSNEEKLIVQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTFELISIIKEEAANRDGPMIVHDEHGGVTAGTFCAL 1384
Cdd:cd17669    81 KCLSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTFELISIIKEEAANRDGPMIVHDEHGGVTAGTFCAL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 901694078 1385 TTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVVL 1428
Cdd:cd17669   161 TTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
alpha_CARP_receptor_like cd03122
Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related ...
 45-298 1.22e-111

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: 352.43  E-value: 1.22e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078   45 NQKNWGKKYPICNS-PKQSPINIDEDlTQVNVN-LKKLKFQGWEKASLEnTFIHNTGKTVEINLTN---DYYLSGGLSEK 119
Cdd:cd03122     1 NPKHWAKKYPACGEgRQQSPIDIVED-TQVQRQgLQPLHFDGYEELTAS-TTLENTGKTVILRLEGnssDPFVSGGPLLG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  120 VFKASKITFHWGKCNvsSEGSEHSLEGQKFPLEMQVYCFDADRFSSFEeAVKGKGRLRALSILFEVGVEENLDYKAIIDG 199
Cdd:cd03122    79 RYKFSEITFHWGTCN--SDGSEHSIDGHKFPLEMQILHRNTDFFDSFE-AIKSPGGVLALAYLFELSHEDNPFLDPIIEG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  200 TESVSRFGKQAALDPFVLQNLLPNSTDKYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLAVFCEVLTMQQSGyVMLMD 279
Cdd:cd03122   156 LRNVSRPGKEVELPPFPLSDLLPPFTDKYYSYEGSLTTPPCSETVEWIVFREPVPISSRQLEAFRELLTRRQDG-VMSGD 234

                         250
                  ....*....|....*....
gi 901694078  280 YLQNNFREQQYKFSRQVFS 298
Cdd:cd03122   235 YLPNNGRPQQPLGSRTVFS 253
fn3 pfam00041
Fibronectin type III domain;
313-401 1.83e-10

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 58.58  E-value: 1.83e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078   313 SEPENVQADPENYTSLLVTWERPRVVyDAMIEKFAVLYQPLaGNDQAKHEFLTDGYQDlGAILNNLLPNMSYVLQIVAVC 392
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDG-NGPITGYEVEYRPK-NSGEPWNEITVPGTTT-SVTLTGLKPGTEYEVRVQAVN 77


                   ....*....
gi 901694078   393 SNGlYGKYS 401
Cdd:pfam00041   78 GGG-EGPPS 85
 
Name Accession Description Interval E-value
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 865-1142 2.93e-162

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: 489.16  E-value: 2.93e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  865 FTEEFEtlkefyqEVQSCTADLGITADSSNHPDNKHKNRYVNIVAYDHSRVKLTQLAEKDGKLTDYINANYVDGYNRPKA 944
Cdd:cd17667     1 FSEDFE-------EVQRCTADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSKHSDYINANYVDGYNKAKA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  945 YIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPTDGSEEYGSFLVNQKSVQVLAYYTVRNFTLRNTK 1024
Cdd:cd17667    74 YIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTK 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1025 LKKGSQ---KGRSSGRLVTQYHYTQWPDMGVPEYSLPVLAFVRKAAQAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQI 1101
Cdd:cd17667   154 VKKGQKgnpKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQI 233

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 901694078 1102 QHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAIL 1142
Cdd:cd17667   234 KDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 274
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 1225-1428 2.57e-155

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: 467.93  E-value: 2.57e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1225 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAEDEFVYWPNKDEPINCESFKVTLMSEEH 1304
Cdd:cd17669     1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFVYWPNKDEPINCETFKVTLIAEEH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1305 KCLSNEEKLIVQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTFELISIIKEEAANRDGPMIVHDEHGGVTAGTFCAL 1384
Cdd:cd17669    81 KCLSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTFELISIIKEEAANRDGPMIVHDEHGGVTAGTFCAL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 901694078 1385 TTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVVL 1428
Cdd:cd17669   161 TTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
864-1139 8.32e-121

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 377.77  E-value: 8.32e-121
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078    864 GFTEEFETLKEFYQEVQSCTadlgitadSSNHPDNKHKNRYVNIVAYDHSRVKLTQLaekDGKLTDYINANYVDGYNRPK 943
Cdd:smart00194    1 GLEEEFEKLDRLKPDDESCT--------VAAFPENRDKNRYKDVLPYDHTRVKLKPP---PGEGSDYINASYIDGPNGPK 69

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078    944 AYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPTDGSE--EYGSFLVNQKSVQVLAYYTVRNFTLR 1021
Cdd:smart00194   70 AYIATQGPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEplTYGDITVTLKSVEKVDDYTIRTLEVT 149

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078   1022 NTklkkgsqkGRSSGRLVTQYHYTQWPDMGVPEYSLPVLAFVRKAAQAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQI 1101
Cdd:smart00194  150 NT--------GCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQL 221

                           250       260       270
                    ....*....|....*....|....*....|....*...
gi 901694078   1102 QHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVE 1139
Cdd:smart00194  222 EAGKEVDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
898-1139 4.60e-113

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 355.40  E-value: 4.60e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078   898 NKHKNRYVNIVAYDHSRVKLTqlaeKDGKLTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNL 977
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLT----GDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTEL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078   978 VEKGRRKCDQYWPT--DGSEEYGSFLVN-QKSVQVLAYYTVRNFTLRNtklkkgsqKGRSSGRLVTQYHYTQWPDMGVPE 1054
Cdd:pfam00102   77 EEKGREKCAQYWPEeeGESLEYGDFTVTlKKEKEDEKDYTVRTLEVSN--------GGSEETRTVKHFHYTGWPDHGVPE 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  1055 YSLPVLAFVRKAAQAKRHA-VGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFI 1133
Cdd:pfam00102  149 SPNSLLDLLRKVRKSSLDGrSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFL 228


                   ....*.
gi 901694078  1134 HDTLVE 1139
Cdd:pfam00102  229 YDAILE 234
alpha_CARP_receptor_like cd03122
Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related ...
 45-298 1.22e-111

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: 352.43  E-value: 1.22e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078   45 NQKNWGKKYPICNS-PKQSPINIDEDlTQVNVN-LKKLKFQGWEKASLEnTFIHNTGKTVEINLTN---DYYLSGGLSEK 119
Cdd:cd03122     1 NPKHWAKKYPACGEgRQQSPIDIVED-TQVQRQgLQPLHFDGYEELTAS-TTLENTGKTVILRLEGnssDPFVSGGPLLG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  120 VFKASKITFHWGKCNvsSEGSEHSLEGQKFPLEMQVYCFDADRFSSFEeAVKGKGRLRALSILFEVGVEENLDYKAIIDG 199
Cdd:cd03122    79 RYKFSEITFHWGTCN--SDGSEHSIDGHKFPLEMQILHRNTDFFDSFE-AIKSPGGVLALAYLFELSHEDNPFLDPIIEG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  200 TESVSRFGKQAALDPFVLQNLLPNSTDKYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLAVFCEVLTMQQSGyVMLMD 279
Cdd:cd03122   156 LRNVSRPGKEVELPPFPLSDLLPPFTDKYYSYEGSLTTPPCSETVEWIVFREPVPISSRQLEAFRELLTRRQDG-VMSGD 234

                         250
                  ....*....|....*....
gi 901694078  280 YLQNNFREQQYKFSRQVFS 298
Cdd:cd03122   235 YLPNNGRPQQPLGSRTVFS 253
Carb_anhydrase smart01057
Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse ...
 38-295 1.01e-86

Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse the reversible hydration of carbon dioxide to bicarbonate.. CAs have essential roles in facilitating the transport of carbon dioxide and protons in the intracellular space, across biological membranes and in the layers of the extracellular space; they are also involved in many other processes, from respiration and photosynthesis in eukaryotes to cyanate degradation in prokaryotes. There are five known evolutionarily distinct CA families (alpha, beta, gamma, delta and epsilon) that have no significant sequence identity and have structurally distinct overall folds. Some CAs are membrane-bound, while others act in the cytosol; there are several related proteins that lack enzymatic activity. The active site of alpha-CAs is well described, consisting of a zinc ion coordinated through 3 histidine residues and a water molecule/hydroxide ion that acts as a potent nucleophile. The enzyme employs a two-step mechanism: in the first step, there is a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide; in the second step, the active site is regenerated by the ionisation of the zinc-bound water molecule and the removal of a proton from the active site. Beta- and gamma-CAs also employ a zinc hydroxide mechanism, although at least some beta-class enzymes do not have water directly coordinated to the metal ion.


Pssm-ID: 215000 [Multi-domain]  Cd Length: 247  Bit Score: 282.67  E-value: 1.01e-86
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078     38 WSYTGALNQKNWGKKYP-ICNSPKQSPINIDEDLTQVNVNLKKLKFQgWEKASleNTFIHNTGKTVEINL-TNDYYLSGG 115
Cdd:smart01057    1 WGYEGKNGPEHWGKLDPpFCGGKRQSPIDIVTAEAQYDPSLKPLKLS-YDQPT--AKRILNNGHTVQVNFdDDGSTLSGG 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078    116 LSEKVFKASKITFHWGKCNvsSEGSEHSLEGQKFPLEMQVYCFDADrfSSFEEAVKGKGRLRALSILFEVGVEENLDYKA 195
Cdd:smart01057   78 PLPGRYRLKQFHFHWGGSD--SEGSEHTIDGKRFPLELHLVHYNSK--GSFSEAVSKPGGLAVVAVFFKVGAEENPALQA 153

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078    196 IIDGTESVSRFGKQAALDPFVLQNLLPNSTDKYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLAVFCEVLTMQQSgyv 275
Cdd:smart01057  154 ILDHLPLIKYKGQETELTPFDLSSLLPASTRHYYTYNGSLTTPPCSEGVTWIVFKEPITISTEQLEKFRTLLPMEGN--- 230

                           250       260
                    ....*....|....*....|
gi 901694078    276 mlmDYLQNNFREQQYKFSRQ 295
Cdd:smart01057  231 ---EPLVNNARPLQPLNGRV 247
Carb_anhydrase pfam00194
Eukaryotic-type carbonic anhydrase;
44-300 3.74e-83

Eukaryotic-type carbonic anhydrase;


Pssm-ID: 459707 [Multi-domain]  Cd Length: 252  Bit Score: 272.99  E-value: 3.74e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078    44 LNQKNWGKKYPICNSPKQSPINIDEDLTQVNVNLKKLKFQGWEKASLENTfIHNTGKTVEINLTNDY--YLSGGLSEKVF 121
Cdd:pfam00194    1 LGPEHWGKVYPSCGGKRQSPINIDTRKVRYDPSLPPLTFQGYDVPPGKNT-LTNNGHTVQVSLDDGDpsTISGGPLATRY 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078   122 KASKITFHWGKCNvsSEGSEHSLEGQKFPLEMQVYCFDADRfSSFEEAVKGKGRLRALSILFEVGVEENLDYKAIIDGTE 201
Cdd:pfam00194   80 RLVQFHFHWGSTD--SRGSEHTIDGKRYPAELHIVHYNSKY-KSFDEAAKHPDGLAVLGVFFEVGDENNPYLQPIVSALD 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078   202 SVSRFGKQAALDPFVLQNLLPNSTDKYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLAVFCEVLTMQQSGYvmlMDYL 281
Cdd:pfam00194  157 NIKYKGKSVLLPPFDLSDLLPEDLTSYYTYNGSLTTPPCSESVTWIVFKEPISISEEQLEAFRTLLFSDGGEE---PRPL 233

                          250
                   ....*....|....*....
gi 901694078   282 QNNFREQQYKFSRQVFSSY 300
Cdd:pfam00194  234 VNNFRPTQPLNGRVVFASF 252
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1170-1428 2.85e-77

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 256.43  E-value: 2.85e-77
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078   1170 KLEKQFQLLSQSNILQSDYSTALKQCNREKNRTSSIIPVERSRVGISSLSGEGTDYINASYIMGYYQSNEFIITQHPLLH 1249
Cdd:smart00194    1 GLEEEFEKLDRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGPLPS 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078   1250 TIKDFWRMIWDHNAQLVVMI-PDGQNMAEDEFVYWPNK-DEPINCESFKVTLMSEEHKclsneEKLIVQDFILEATQDDY 1327
Cdd:smart00194   81 TVEDFWRMVWEQKVTVIVMLtELVEKGREKCAQYWPDEeGEPLTYGDITVTLKSVEKV-----DDYTIRTLEVTNTGCSE 155

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078   1328 VLEVRHFQCPKWP---NPDSPISkTFELISIIKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAK 1404
Cdd:smart00194  156 TRTVTHYHYTNWPdhgVPESPES-ILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVK 234

                           250       260
                    ....*....|....*....|....
gi 901694078   1405 MINLMRPGVFTDIEQYQFLYKVVL 1428
Cdd:smart00194  235 ELRSQRPGMVQTEEQYIFLYRAIL 258
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1196-1428 8.10e-76

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 251.39  E-value: 8.10e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  1196 NREKNRTSSIIPVERSRVGISSLSGeGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNM 1275
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPG-PSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  1276 A-EDEFVYWPNK-DEPINCESFKVTLMSEEhkclSNEEKLIVQDFILEATQDDYVLEVRHFQCPKWPN---PDSPISkTF 1350
Cdd:pfam00102   80 GrEKCAQYWPEEeGESLEYGDFTVTLKKEK----EDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDhgvPESPNS-LL 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 901694078  1351 ELISIIKE-EAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVVL 1428
Cdd:pfam00102  155 DLLRKVRKsSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233
PHA02738 PHA02738
hypothetical protein; Provisional
 898-1132 6.51e-52

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 185.90  E-value: 6.51e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  898 NKHKNRYVNIVAYDHSRVKLTqlAEKDgkLTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNL 977
Cdd:PHA02738   49 NRKLNRYLDAVCFDHSRVILP--AERN--RGDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKK 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  978 VEKGRRKCDQYWPT--DGSEEYGSFLVNQKSVQVLAYYTVRNFTLRNtklkkgsqkGRSSGRLVTQYHYTQWPDMGVPEY 1055
Cdd:PHA02738  125 KENGREKCFPYWSDveQGSIRFGKFKITTTQVETHPHYVKSTLLLTD---------GTSATQTVTHFNFTAWPDHDVPKN 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1056 SLPVLAFVRKAAQA-------------KRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNY 1122
Cdd:PHA02738  196 TSEFLNFVLEVRQCqkelaqeslqighNRLQPPPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYY 275

                         250
                  ....*....|
gi 901694078 1123 LVQTEEQYVF 1132
Cdd:PHA02738  276 SLFIPFQYFF 285
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
873-1133 1.37e-42

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 157.56  E-value: 1.37e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  873 KEFYQEVQSCTADLGITADSSNHPDN---KHKNRYVNIVAYDHsrvklTQLAEKDGkltdYINANYVDGYNrPKAYIAAQ 949
Cdd:COG5599    14 EKINSRLSTLTNELAPSHNDPQYLQNingSPLNRFRDIQPYKE-----TALRANLG----YLNANYIQVIG-NHRYIATQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  950 GPLKSTAEDFWRMIWEHNVEVIVMITNLVE--KGRRKCDQYWPTDGseEYGSFLVNQKSVQVlaYYTVRNFTLRNTKLK- 1026
Cdd:COG5599    84 YPLEEQLEDFFQMLFDNNTPVLVVLASDDEisKPKVKMPVYFRQDG--EYGKYEVSSELTES--IQLRDGIEARTYVLTi 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1027 KGS-QKGRSsgrlVTQYHYTQWPDMGVP--EYSLPVLAFVRKAAQAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQ- 1102
Cdd:COG5599   160 KGTgQKKIE----IPVLHVKNWPDHGAIsaEALKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINa 235

                         250       260       270
                  ....*....|....*....|....*....|...
gi 901694078 1103 -HEGTVNIFGFLKHIRSQRNY-LVQTEEQYVFI 1133
Cdd:COG5599   236 lVQITLSVEEIVIDMRTSRNGgMVQTSEQLDVL 268
Cah COG3338
Carbonic anhydrase [Inorganic ion transport and metabolism];
38-263 4.01e-33

Carbonic anhydrase [Inorganic ion transport and metabolism];


Pssm-ID: 442567 [Multi-domain]  Cd Length: 247  Bit Score: 129.23  E-value: 4.01e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078   38 WSYTGALNQKNWGK---KYPICNS-PKQSPINIDedlTQVNVNLKKLKFQgWEKASLEntfIHNTGKTVEINLTNDYYLS 113
Cdd:COG3338    28 WSYEGETGPEHWGElspEFATCATgKNQSPIDIR---TAIKADLPPLKFD-YKPTPLE---IVNNGHTIQVNVDPGSTLT 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  114 ggLSEKVFKASKITFHwgkcnvssEGSEHSLEGQKFPLEMQ-VYcfdadrfssfeeaVKGKGRLRALSILFEVGvEENLD 192
Cdd:COG3338   101 --VDGKRYELKQFHFH--------TPSEHTINGKSYPMEAHlVH-------------KDADGELAVVGVLFEEG-AENPA 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 901694078  193 YKAIID------GTESVSrfgkQAALDPfvlQNLLPNSTDkYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLAVF 263
Cdd:COG3338   157 LAKLWAnlpleaGEEVAL----DATIDL---NDLLPEDRS-YYRYSGSLTTPPCSEGVLWIVLKQPITVSAEQIEAF 225
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 1188-1432 3.16e-28

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 117.02  E-value: 3.16e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1188 YSTALKQCNREKNRTSSIIPVERSRVGISSLSGEGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVV 1267
Cdd:PHA02747   43 IANFEKPENQPKNRYWDIPCWDHNRVILDSGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIV 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1268 MI--PDGQNMAEDEFVYW-PNKDEPINCESFKVTLMSEEHKCLSNEEKLIVQDFILEATQddyvlEVRHFQCPKWPNPDS 1344
Cdd:PHA02747  123 MLtpTKGTNGEEKCYQYWcLNEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILKDSR-----KISHFQCSEWFEDET 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1345 PiSKTFELISIIKEEAANRD-------------GPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRP 1411
Cdd:PHA02747  198 P-SDHPDFIKFIKIIDINRKksgklfnpkdallCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRH 276

                         250       260
                  ....*....|....*....|....
gi 901694078 1412 GVFTDIEQYQFL---YKVVLSLVS 1432
Cdd:PHA02747  277 AGIMNFDDYLFIqpgYEVLHYFLS 300
fn3 pfam00041
Fibronectin type III domain;
313-401 1.83e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 58.58  E-value: 1.83e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078   313 SEPENVQADPENYTSLLVTWERPRVVyDAMIEKFAVLYQPLaGNDQAKHEFLTDGYQDlGAILNNLLPNMSYVLQIVAVC 392
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDG-NGPITGYEVEYRPK-NSGEPWNEITVPGTTT-SVTLTGLKPGTEYEVRVQAVN 77


                   ....*....
gi 901694078   393 SNGlYGKYS 401
Cdd:pfam00041   78 GGG-EGPPS 85
PLN02179 PLN02179
carbonic anhydrase
 49-253 1.39e-08

carbonic anhydrase


Pssm-ID: 177835  Cd Length: 235  Bit Score: 57.30  E-value: 1.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078   49 WGKKYP---ICNSPK-QSPInideDLTQVNVNLkkLKFQGWEKA-SLENTFIHNTGKTVEINLTNDyylsgglsekvfkA 123
Cdd:PLN02179   50 WGKLNPqwkVCSTGKyQSPI----DLTDERVSL--IHDQALSRHyKPAPAVIQSRGHDVMVSWKGD-------------A 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  124 SKITFHWG-----KCNVSSEgSEHSLEGQKFPLEMQVYCFDAdrfssfeeavkgKGRLRALSILFEVGvEENLDYKAIID 198
Cdd:PLN02179  111 GKITIHQTdyklvQCHWHSP-SEHTINGTSYDLELHMVHTSA------------SGKTAVVGVLYKLG-EPDEFLTKLLN 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 901694078  199 GTESVsrfGKQ----AALDPFVLQNllpnSTDKYYIYNGSLTSPPCTDTVEWIVFKDTV 253
Cdd:PLN02179  177 GIKGV---GKKeinlGIVDPRDIRF----ETNNFYRYIGSLTIPPCTEGVIWTVVKRVV 228
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 313-406 1.46e-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: 47.88  E-value: 1.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  313 SEPENVQADPENYTSLLVTWERPRvVYDAMIEKFAVLYQPLAGNDQakHEFLTDGYQDLGAILNNLLPNMSYVLQIVAVC 392
Cdd:cd00063     2 SPPTNLRVTDVTSTSVTLSWTPPE-DDGGPITGYVVEYREKGSGDW--KEVEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78

                          90
                  ....*....|....
gi 901694078  393 SNGlYGKYSDQLIV 406
Cdd:cd00063    79 GGG-ESPPSESVTV 91
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 313-395 8.96e-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: 45.30  E-value: 8.96e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078    313 SEPENVQADPENYTSLLVTWERPRvvyDAMIEKFAVLYQPLAGNDQAKHEFLTDGYQDLGAILNNLLPNMSYVLQIVAVC 392
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPP---DDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78


                    ...
gi 901694078    393 SNG 395
Cdd:smart00060   79 GAG 81
 
Name Accession Description Interval E-value
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 865-1142 2.93e-162

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: 489.16  E-value: 2.93e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  865 FTEEFEtlkefyqEVQSCTADLGITADSSNHPDNKHKNRYVNIVAYDHSRVKLTQLAEKDGKLTDYINANYVDGYNRPKA 944
Cdd:cd17667     1 FSEDFE-------EVQRCTADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSKHSDYINANYVDGYNKAKA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  945 YIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPTDGSEEYGSFLVNQKSVQVLAYYTVRNFTLRNTK 1024
Cdd:cd17667    74 YIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTK 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1025 LKKGSQ---KGRSSGRLVTQYHYTQWPDMGVPEYSLPVLAFVRKAAQAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQI 1101
Cdd:cd17667   154 VKKGQKgnpKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQI 233

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 901694078 1102 QHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAIL 1142
Cdd:cd17667   234 KDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 274
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 1225-1428 2.57e-155

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: 467.93  E-value: 2.57e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1225 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAEDEFVYWPNKDEPINCESFKVTLMSEEH 1304
Cdd:cd17669     1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFVYWPNKDEPINCETFKVTLIAEEH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1305 KCLSNEEKLIVQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTFELISIIKEEAANRDGPMIVHDEHGGVTAGTFCAL 1384
Cdd:cd17669    81 KCLSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTFELISIIKEEAANRDGPMIVHDEHGGVTAGTFCAL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 901694078 1385 TTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVVL 1428
Cdd:cd17669   161 TTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 930-1138 5.38e-154

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: 464.45  E-value: 5.38e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  930 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPTDGSEEYGSFLVNQKSVQV 1009
Cdd:cd17668     1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1010 LAYYTVRNFTLRNTKLKKGSQKGRSSGRLVTQYHYTQWPDMGVPEYSLPVLAFVRKAAQAKRHAVGPVVVHCSAGVGRTG 1089
Cdd:cd17668    81 LAYYTVRNFTLRNTKIKKGSQKGRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVGPVVVHCSAGVGRTG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 901694078 1090 TYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLV 1138
Cdd:cd17668   161 TYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 930-1135 1.22e-142

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


Pssm-ID: 350397 [Multi-domain]  Cd Length: 204  Bit Score: 434.09  E-value: 1.22e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  930 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPTDGSEEYGSFLVNQKSVQV 1009
Cdd:cd14549     1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTETYGNIQVTLLSTEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1010 LAYYTVRNFTLRNTKLKKGsqKGRSSGRLVTQYHYTQWPDMGVPEYSLPVLAFVRKAAQAKRHAVGPVVVHCSAGVGRTG 1089
Cdd:cd14549    81 LATYTVRTFSLKNLKLKKV--KGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAGVGRTG 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 901694078 1090 TYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHD 1135
Cdd:cd14549   159 TYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 1225-1429 2.02e-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: 401.36  E-value: 2.02e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1225 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAEDEFVYWPNKDEPINCESFKVTLMSEEH 1304
Cdd:cd17670     1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQGLAEDEFVYWPSREESMNCEAFTVTLISKDR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1305 KCLSNEEKLIVQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTFELISIIKEEAANRDGPMIVHDEHGGVTAGTFCAL 1384
Cdd:cd17670    81 LCLSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISSTFELINVIKEEALTRDGPTIVHDEFGAVSAGTLCAL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 901694078 1385 TTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVVLS 1429
Cdd:cd17670   161 TTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAMLS 205
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 1225-1425 8.05e-128

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: 394.38  E-value: 8.05e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1225 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQnMAEDEFVYWPNKDEPINCESFKVTLMSEEH 1304
Cdd:cd14550     1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNE-LNEDEPIYWPTKEKPLECETFKVTLSGEDH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1305 KCLSNEEKLIVQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTFELISIIKEEAANRDGPMIVHDEHGGVTAGTFCAL 1384
Cdd:cd14550    80 SCLSNEIRLIVRDFILESTQDDYVLEVRQFQCPSWPNPCSPIHTVFELINTVQEWAQQRDGPIVVHDRYGGVQAATFCAL 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 901694078 1385 TTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYK 1425
Cdd:cd14550   160 TTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
864-1139 8.32e-121

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 377.77  E-value: 8.32e-121
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078    864 GFTEEFETLKEFYQEVQSCTadlgitadSSNHPDNKHKNRYVNIVAYDHSRVKLTQLaekDGKLTDYINANYVDGYNRPK 943
Cdd:smart00194    1 GLEEEFEKLDRLKPDDESCT--------VAAFPENRDKNRYKDVLPYDHTRVKLKPP---PGEGSDYINASYIDGPNGPK 69

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078    944 AYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPTDGSE--EYGSFLVNQKSVQVLAYYTVRNFTLR 1021
Cdd:smart00194   70 AYIATQGPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEplTYGDITVTLKSVEKVDDYTIRTLEVT 149

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078   1022 NTklkkgsqkGRSSGRLVTQYHYTQWPDMGVPEYSLPVLAFVRKAAQAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQI 1101
Cdd:smart00194  150 NT--------GCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQL 221

                           250       260       270
                    ....*....|....*....|....*....|....*...
gi 901694078   1102 QHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVE 1139
Cdd:smart00194  222 EAGKEVDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
898-1139 4.60e-113

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 355.40  E-value: 4.60e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078   898 NKHKNRYVNIVAYDHSRVKLTqlaeKDGKLTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNL 977
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLT----GDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTEL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078   978 VEKGRRKCDQYWPT--DGSEEYGSFLVN-QKSVQVLAYYTVRNFTLRNtklkkgsqKGRSSGRLVTQYHYTQWPDMGVPE 1054
Cdd:pfam00102   77 EEKGREKCAQYWPEeeGESLEYGDFTVTlKKEKEDEKDYTVRTLEVSN--------GGSEETRTVKHFHYTGWPDHGVPE 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  1055 YSLPVLAFVRKAAQAKRHA-VGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFI 1133
Cdd:pfam00102  149 SPNSLLDLLRKVRKSSLDGrSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFL 228


                   ....*.
gi 901694078  1134 HDTLVE 1139
Cdd:pfam00102  229 YDAILE 234
alpha_CARP_receptor_like cd03122
Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related ...
 45-298 1.22e-111

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: 352.43  E-value: 1.22e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078   45 NQKNWGKKYPICNS-PKQSPINIDEDlTQVNVN-LKKLKFQGWEKASLEnTFIHNTGKTVEINLTN---DYYLSGGLSEK 119
Cdd:cd03122     1 NPKHWAKKYPACGEgRQQSPIDIVED-TQVQRQgLQPLHFDGYEELTAS-TTLENTGKTVILRLEGnssDPFVSGGPLLG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  120 VFKASKITFHWGKCNvsSEGSEHSLEGQKFPLEMQVYCFDADRFSSFEeAVKGKGRLRALSILFEVGVEENLDYKAIIDG 199
Cdd:cd03122    79 RYKFSEITFHWGTCN--SDGSEHSIDGHKFPLEMQILHRNTDFFDSFE-AIKSPGGVLALAYLFELSHEDNPFLDPIIEG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  200 TESVSRFGKQAALDPFVLQNLLPNSTDKYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLAVFCEVLTMQQSGyVMLMD 279
Cdd:cd03122   156 LRNVSRPGKEVELPPFPLSDLLPPFTDKYYSYEGSLTTPPCSETVEWIVFREPVPISSRQLEAFRELLTRRQDG-VMSGD 234

                         250
                  ....*....|....*....
gi 901694078  280 YLQNNFREQQYKFSRQVFS 298
Cdd:cd03122   235 YLPNNGRPQQPLGSRTVFS 253
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 898-1143 3.33e-111

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


Pssm-ID: 350401 [Multi-domain]  Cd Length: 238  Bit Score: 350.54  E-value: 3.33e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  898 NKHKNRYVNIVAYDHSRVKLTQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNL 977
Cdd:cd14553     3 NKPKNRYANVIAYDHSRVILQPIEGVPG--SDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  978 VEKGRRKCDQYWPTDGSEEYGSFLVNQKSVQVLAYYTVRNFTLRNTklkkgsqkGRSSGRLVTQYHYTQWPDMGVPEYSL 1057
Cdd:cd14553    81 EERSRVKCDQYWPTRGTETYGLIQVTLLDTVELATYTVRTFALHKN--------GSSEKREVRQFQFTAWPDHGVPEHPT 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1058 PVLAFVRKAAQAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTL 1137
Cdd:cd14553   153 PFLAFLRRVKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDAL 232


                  ....*.
gi 901694078 1138 VEAILS 1143
Cdd:cd14553   233 LEAVTC 238
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 930-1135 1.41e-96

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: 308.45  E-value: 1.41e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  930 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPTDGSE--EYGSFLVNQKSV 1007
Cdd:cd00047     1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKplEYGDITVTLVSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1008 QVLAYYTVRNFTLRNtklkkgsqKGRSSGRLVTQYHYTQWPDMGVPEYSLPVLAFVRKAAQAKRHAVGPVVVHCSAGVGR 1087
Cdd:cd00047    81 EELSDYTIRTLELSP--------KGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCSAGVGR 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 901694078 1088 TGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHD 1135
Cdd:cd00047   153 TGTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 855-1141 7.93e-95

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


Pssm-ID: 350474 [Multi-domain]  Cd Length: 276  Bit Score: 306.96  E-value: 7.93e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  855 HVADLHASNGFteefetlkEFYQEVQSCTADLGITADSSNHPDNKHKNRYVNIVAYDHSRVKLTQLAEKDGklTDYINAN 934
Cdd:cd14626     6 NIERLKANDGL--------KFSQEYESIDPGQQFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPG--SDYINAN 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  935 YVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPTDGSEEYGSFLVNQKSVQVLAYYT 1014
Cdd:cd14626    76 YIDGYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIRGTETYGMIQVTLLDTVELATYS 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1015 VRNFTLRntklkkgsQKGRSSGRLVTQYHYTQWPDMGVPEYSLPVLAFVRKAAQAKRHAVGPVVVHCSAGVGRTGTYIVL 1094
Cdd:cd14626   156 VRTFALY--------KNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVI 227

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 901694078 1095 DSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAI 1141
Cdd:cd14626   228 DAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLEAA 274
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 903-1134 1.10e-92

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


Pssm-ID: 350396 [Multi-domain]  Cd Length: 222  Bit Score: 298.50  E-value: 1.10e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  903 RYVNIVAYDHSRVKLTQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGR 982
Cdd:cd14548     1 RYTNILPYDHSRVKLIPINEEEG--SDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  983 RKCDQYWPTDGSE-EYGSFLVNQKSVQVLAYYTVRNFTLrntklkkgsqKGRSSGRLVTQYHYTQWPDMGVPEYSLPVLA 1061
Cdd:cd14548    79 VKCDHYWPFDQDPvYYGDITVTMLSESVLPDWTIREFKL----------ERGDEVRSVRQFHFTAWPDHGVPEAPDSLLR 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 901694078 1062 FVRKAAQAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIH 1134
Cdd:cd14548   149 FVRLVRDYIKQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLH 221
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 889-1134 6.73e-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: 295.81  E-value: 6.73e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  889 TADSSNHPDNKHKNRYVNIVAYDHSRVKLTQLAEKDgkLTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNV 968
Cdd:cd14543    20 TFLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDE--RTDYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  969 EVIVMITNLVEKGRRKCDQYWPTDG--SEEYGSFLVNQKSVQVLAYYTVRNFTLRNTKlkkgsqkgRSSGRLVTQYHYTQ 1046
Cdd:cd14543    98 LVIVMTTRVVERGRVKCGQYWPLEEgsSLRYGDLTVTNLSVENKEHYKKTTLEIHNTE--------TDESRQVTHFQFTS 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1047 WPDMGVPEYSLPVLAFVRKAAQAKRHAVG-------------PVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFL 1113
Cdd:cd14543   170 WPDFGVPSSAAALLDFLGEVRQQQALAVKamgdrwkghppgpPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQTV 249

                         250       260
                  ....*....|....*....|.
gi 901694078 1114 KHIRSQRNYLVQTEEQYVFIH 1134
Cdd:cd14543   250 RRMRTQRAFSIQTPDQYYFCY 270
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 847-1141 9.27e-88

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: 287.37  E-value: 9.27e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  847 IPIKHFPKHVADLHASNGFteefetlkEFYQEVQSCTADLGITADSSNHPDNKHKNRYVNIVAYDHSRVKLTQLAEKDGk 926
Cdd:cd14625     4 IPISELAEHTERLKANDNL--------KLSQEYESIDPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMG- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  927 lTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPTDGSEEYGSFLVNQKS 1006
Cdd:cd14625    75 -SDYINANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSRGTETYGMIQVTLLD 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1007 VQVLAYYTVRNFTLRntklkkgsQKGRSSGRLVTQYHYTQWPDMGVPEYSLPVLAFVRKAAQAKRHAVGPVVVHCSAGVG 1086
Cdd:cd14625   154 TIELATFCVRTFSLH--------KNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPPDAGPIVVHCSAGVG 225

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 901694078 1087 RTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAI 1141
Cdd:cd14625   226 RTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEAV 280
Carb_anhydrase smart01057
Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse ...
 38-295 1.01e-86

Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse the reversible hydration of carbon dioxide to bicarbonate.. CAs have essential roles in facilitating the transport of carbon dioxide and protons in the intracellular space, across biological membranes and in the layers of the extracellular space; they are also involved in many other processes, from respiration and photosynthesis in eukaryotes to cyanate degradation in prokaryotes. There are five known evolutionarily distinct CA families (alpha, beta, gamma, delta and epsilon) that have no significant sequence identity and have structurally distinct overall folds. Some CAs are membrane-bound, while others act in the cytosol; there are several related proteins that lack enzymatic activity. The active site of alpha-CAs is well described, consisting of a zinc ion coordinated through 3 histidine residues and a water molecule/hydroxide ion that acts as a potent nucleophile. The enzyme employs a two-step mechanism: in the first step, there is a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide; in the second step, the active site is regenerated by the ionisation of the zinc-bound water molecule and the removal of a proton from the active site. Beta- and gamma-CAs also employ a zinc hydroxide mechanism, although at least some beta-class enzymes do not have water directly coordinated to the metal ion.


Pssm-ID: 215000 [Multi-domain]  Cd Length: 247  Bit Score: 282.67  E-value: 1.01e-86
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078     38 WSYTGALNQKNWGKKYP-ICNSPKQSPINIDEDLTQVNVNLKKLKFQgWEKASleNTFIHNTGKTVEINL-TNDYYLSGG 115
Cdd:smart01057    1 WGYEGKNGPEHWGKLDPpFCGGKRQSPIDIVTAEAQYDPSLKPLKLS-YDQPT--AKRILNNGHTVQVNFdDDGSTLSGG 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078    116 LSEKVFKASKITFHWGKCNvsSEGSEHSLEGQKFPLEMQVYCFDADrfSSFEEAVKGKGRLRALSILFEVGVEENLDYKA 195
Cdd:smart01057   78 PLPGRYRLKQFHFHWGGSD--SEGSEHTIDGKRFPLELHLVHYNSK--GSFSEAVSKPGGLAVVAVFFKVGAEENPALQA 153

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078    196 IIDGTESVSRFGKQAALDPFVLQNLLPNSTDKYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLAVFCEVLTMQQSgyv 275
Cdd:smart01057  154 ILDHLPLIKYKGQETELTPFDLSSLLPASTRHYYTYNGSLTTPPCSEGVTWIVFKEPITISTEQLEKFRTLLPMEGN--- 230

                           250       260
                    ....*....|....*....|
gi 901694078    276 mlmDYLQNNFREQQYKFSRQ 295
Cdd:smart01057  231 ---EPLVNNARPLQPLNGRV 247
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 833-1141 1.33e-86

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


Pssm-ID: 350472 [Multi-domain]  Cd Length: 284  Bit Score: 283.93  E-value: 1.33e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  833 PPTPIFPISDdigaipikhfpkHVADLHASNGFteefetlkEFYQEVQSCTADLGITADSSNHPDNKHKNRYVNIVAYDH 912
Cdd:cd14624     2 PPIPILELAD------------HIERLKANDNL--------KFSQEYESIDPGQQFTWEHSNLEVNKPKNRYANVIAYDH 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  913 SRVKLTQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPTD 992
Cdd:cd14624    62 SRVLLSAIEGIPG--SDYINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSR 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  993 GSEEYGSFLVNQKSVQVLAYYTVRNFTLRntklkkgsQKGRSSGRLVTQYHYTQWPDMGVPEYSLPVLAFVRKAAQAKRH 1072
Cdd:cd14624   140 GTETYGLIQVTLLDTVELATYCVRTFALY--------KNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPP 211

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 901694078 1073 AVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAI 1141
Cdd:cd14624   212 DAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLEAV 280
Carb_anhydrase pfam00194
Eukaryotic-type carbonic anhydrase;
44-300 3.74e-83

Eukaryotic-type carbonic anhydrase;


Pssm-ID: 459707 [Multi-domain]  Cd Length: 252  Bit Score: 272.99  E-value: 3.74e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078    44 LNQKNWGKKYPICNSPKQSPINIDEDLTQVNVNLKKLKFQGWEKASLENTfIHNTGKTVEINLTNDY--YLSGGLSEKVF 121
Cdd:pfam00194    1 LGPEHWGKVYPSCGGKRQSPINIDTRKVRYDPSLPPLTFQGYDVPPGKNT-LTNNGHTVQVSLDDGDpsTISGGPLATRY 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078   122 KASKITFHWGKCNvsSEGSEHSLEGQKFPLEMQVYCFDADRfSSFEEAVKGKGRLRALSILFEVGVEENLDYKAIIDGTE 201
Cdd:pfam00194   80 RLVQFHFHWGSTD--SRGSEHTIDGKRYPAELHIVHYNSKY-KSFDEAAKHPDGLAVLGVFFEVGDENNPYLQPIVSALD 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078   202 SVSRFGKQAALDPFVLQNLLPNSTDKYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLAVFCEVLTMQQSGYvmlMDYL 281
Cdd:pfam00194  157 NIKYKGKSVLLPPFDLSDLLPEDLTSYYTYNGSLTTPPCSESVTWIVFKEPISISEEQLEAFRTLLFSDGGEE---PRPL 233

                          250
                   ....*....|....*....
gi 901694078   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 ...
 897-1142 1.86e-82

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


Pssm-ID: 350478 [Multi-domain]  Cd Length: 237  Bit Score: 270.36  E-value: 1.86e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  897 DNKHKNRYVNIVAYDHSRVKLTQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITN 976
Cdd:cd14630     2 ENRNKNRYGNIISYDHSRVRLQLLDGDPH--SDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  977 LVEKGRRKCDQYWPtDGSEEYGSFLVNQKSVQVLAYYTVRNFTLRntklKKGSQKGRSsgrlVTQYHYTQWPDMGVPEYS 1056
Cdd:cd14630    80 LVEVGRVKCVRYWP-DDTEVYGDIKVTLIETEPLAEYVIRTFTVQ----KKGYHEIRE----IRQFHFTSWPDHGVPCYA 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1057 LPVLAFVRKAAQAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDT 1136
Cdd:cd14630   151 TGLLGFVRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDA 230


                  ....*.
gi 901694078 1137 LVEAIL 1142
Cdd:cd14630   231 ILEACL 236
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 833-1148 1.13e-79

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: 264.96  E-value: 1.13e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  833 PPTPIFPISDDIGaipikhfpKHVADlhASNGFTEEFETLKefyqevqscTADLGITADSSNHPDNKHKNRYVNIVAYDH 912
Cdd:cd14621     6 PPLPVDKLEEEIN--------RRMAD--DNKLFREEFNALP---------ACPIQATCEAASKEENKEKNRYVNILPYDH 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  913 SRVKLTQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPTD 992
Cdd:cd14621    67 SRVHLTPVEGVPD--SDYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQ 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  993 GSEEYGSFLVNQKSVQVLAYYTVRNFTLRNTklkkGSQKGRSSGRLVTQYHYTQWPDMGVPEYSLPVLAFVRKAAQAKRH 1072
Cdd:cd14621   145 GCWTYGNIRVSVEDVTVLVDYTVRKFCIQQV----GDVTNKKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQ 220

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 901694078 1073 AVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAILSKETEV 1148
Cdd:cd14621   221 YAGAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEHYLYGDTEL 296
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 902-1133 9.77e-79

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


Pssm-ID: 350463 [Multi-domain]  Cd Length: 229  Bit Score: 259.36  E-value: 9.77e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  902 NRYVNIVAYDHSRVKLTQLAEKdgkLTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKG 981
Cdd:cd14615     1 NRYNNVLPYDISRVKLSVQSHS---TDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  982 RRKCDQYWPTDGSEEYGSFLVNQKSVQVLAYYTVRNFTLRNTKlkkgsqkgRSSGRLVTQYHYTQWPDMGVPEYSLPVLA 1061
Cdd:cd14615    78 RTKCEEYWPSKQKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQ--------TNESRTVRHFHFTSWPDHGVPETTDLLIN 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 901694078 1062 F---VRK-AAQAKRHavGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFI 1133
Cdd:cd14615   150 FrhlVREyMKQNPPN--SPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFL 223
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 864-1142 1.46e-77

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: 258.05  E-value: 1.46e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  864 GFTEEFETlkefYQEVQSCTADlgitadSSNHPDNKHKNRYVNIVAYDHSRVKLTQLAEKDGklTDYINANYVDGYNRPK 943
Cdd:cd14633    16 GFKEEYES----FFEGQSAPWD------SAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETS--SDYINGNYIDGYHRPN 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  944 AYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPTDgSEEYGSFLVNQKSVQVLAYYTVRNFTLRnt 1023
Cdd:cd14633    84 HYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDD-TEIYKDIKVTLIETELLAEYVIRTFAVE-- 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1024 klkkgsQKGRSSGRLVTQYHYTQWPDMGVPEYSLPVLAFVRKAAQAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQH 1103
Cdd:cd14633   161 ------KRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAER 234

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 901694078 1104 EGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAIL 1142
Cdd:cd14633   235 EGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILEACL 273
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1170-1428 2.85e-77

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 256.43  E-value: 2.85e-77
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078   1170 KLEKQFQLLSQSNILQSDYSTALKQCNREKNRTSSIIPVERSRVGISSLSGEGTDYINASYIMGYYQSNEFIITQHPLLH 1249
Cdd:smart00194    1 GLEEEFEKLDRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGPLPS 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078   1250 TIKDFWRMIWDHNAQLVVMI-PDGQNMAEDEFVYWPNK-DEPINCESFKVTLMSEEHKclsneEKLIVQDFILEATQDDY 1327
Cdd:smart00194   81 TVEDFWRMVWEQKVTVIVMLtELVEKGREKCAQYWPDEeGEPLTYGDITVTLKSVEKV-----DDYTIRTLEVTNTGCSE 155

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078   1328 VLEVRHFQCPKWP---NPDSPISkTFELISIIKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAK 1404
Cdd:smart00194  156 TRTVTHYHYTNWPdhgVPESPES-ILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVK 234

                           250       260
                    ....*....|....*....|....
gi 901694078   1405 MINLMRPGVFTDIEQYQFLYKVVL 1428
Cdd:smart00194  235 ELRSQRPGMVQTEEQYIFLYRAIL 258
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 902-1141 4.26e-77

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


Pssm-ID: 350467 [Multi-domain]  Cd Length: 233  Bit Score: 254.81  E-value: 4.26e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  902 NRYVNIVAYDHSRVKLTQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKG 981
Cdd:cd14619     1 NRFRNVLPYDWSRVPLKPIHEEPG--SDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  982 RRKCDQYWPTDGSE-EYGSFLVNQKSVQVLAYYTVRNFTLRNTKlkkgSQKGRSsgrlVTQYHYTQWPDMGVPEYSLPVL 1060
Cdd:cd14619    79 RVKCEHYWPLDYTPcTYGHLRVTVVSEEVMENWTVREFLLKQVE----EQKTLS----VRHFHFTAWPDHGVPSSTDTLL 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1061 AF---VRKAAQAKRHAvGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTL 1137
Cdd:cd14619   151 AFrrlLRQWLDQTMSG-GPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCI 229


                  ....
gi 901694078 1138 VEAI 1141
Cdd:cd14619   230 LDFL 233
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 902-1134 5.30e-77

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


Pssm-ID: 350465 [Multi-domain]  Cd Length: 228  Bit Score: 254.46  E-value: 5.30e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  902 NRYVNIVAYDHSRVKLTQLaeKDGKLTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKG 981
Cdd:cd14617     1 NRYNNILPYDSTRVKLSNV--DDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  982 RRKCDQYWPTD-GSEEYGSFLVNQKSVQVLAYYTVRNFtlrntklKKGSQKGRSSGRLVTQYHYTQWPDMGVPEYSLPVL 1060
Cdd:cd14617    79 RVKCDHYWPADqDSLYYGDLIVQMLSESVLPEWTIREF-------KICSEEQLDAPRLVRHFHYTVWPDHGVPETTQSLI 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 901694078 1061 AFVRKAAQ--AKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIH 1134
Cdd:cd14617   152 QFVRTVRDyiNRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 227
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 930-1142 1.03e-76

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


Pssm-ID: 350403 [Multi-domain]  Cd Length: 204  Bit Score: 252.53  E-value: 1.03e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  930 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPTDgSEEYGSFLVNQKSVQV 1009
Cdd:cd14555     1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDD-TEVYGDIKVTLVETEP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1010 LAYYTVRNFTLRntklkkgsQKGRSSGRLVTQYHYTQWPDMGVPEYSLPVLAFVRKAAQAKRHAVGPVVVHCSAGVGRTG 1089
Cdd:cd14555    80 LAEYVVRTFALE--------RRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAGPIVVHCSAGAGRTG 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 901694078 1090 TYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAIL 1142
Cdd:cd14555   152 CYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILEACL 204
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1196-1428 8.10e-76

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 251.39  E-value: 8.10e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  1196 NREKNRTSSIIPVERSRVGISSLSGeGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNM 1275
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPG-PSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  1276 A-EDEFVYWPNK-DEPINCESFKVTLMSEEhkclSNEEKLIVQDFILEATQDDYVLEVRHFQCPKWPN---PDSPISkTF 1350
Cdd:pfam00102   80 GrEKCAQYWPEEeGESLEYGDFTVTLKKEK----EDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDhgvPESPNS-LL 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 901694078  1351 ELISIIKE-EAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVVL 1428
Cdd:pfam00102  155 DLLRKVRKsSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 904-1139 1.94e-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: 1.94e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  904 YVNIVAYDHSRVKLTQLaekDGKL-TDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGR 982
Cdd:cd14620     1 YPNILPYDHSRVILSQL---DGIPcSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  983 RKCDQYWPTDGSEEYGSFLVNQKSVQVLAYYTVRNFTLRNTklkkgSQKGRSSGRLVTQYHYTQWPDMGVPEYSLPVLAF 1062
Cdd:cd14620    78 EKCYQYWPDQGCWTYGNIRVAVEDCVVLVDYTIRKFCIQPQ-----LPDGCKAPRLVTQLHFTSWPDFGVPFTPIGMLKF 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 901694078 1063 VRKAAQAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVE 1139
Cdd:cd14620   153 LKKVKSVNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 893-1134 3.85e-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: 246.67  E-value: 3.85e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  893 SNHPDNKHKNRYVNIVAYDHSRVKLTQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIV 972
Cdd:cd14554     1 ANLPCNKFKNRLVNILPYESTRVCLQPIRGVEG--SDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  973 MITNLVEKGRRKCDQYWPTDGSEEYGSFLVNQksvqvLAYYTVRNFTLRNTKLKKgSQKGRSsgRLVTQYHYTQWPDMGV 1052
Cdd:cd14554    79 MLTKLREMGREKCHQYWPAERSARYQYFVVDP-----MAEYNMPQYILREFKVTD-ARDGQS--RTVRQFQFTDWPEQGV 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1053 PEYSLPVLAFVRKAAQAKRH--AVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQY 1130
Cdd:cd14554   151 PKSGEGFIDFIGQVHKTKEQfgQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQY 230


                  ....
gi 901694078 1131 VFIH 1134
Cdd:cd14554   231 QFCY 234
alpha_CA cd00326
Carbonic anhydrase alpha (vertebrate-like) group. Carbonic anhydrases (CAs) are ...
 60-297 5.15e-73

Carbonic anhydrase alpha (vertebrate-like) group. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Most alpha CAs are monomeric enzymes. The zinc ion is complexed by three histidine residues and a fourth conserved histidine plays a potential role in proton transfer.


Pssm-ID: 238200  Cd Length: 227  Bit Score: 242.96  E-value: 5.15e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078   60 KQSPINIDEDLTQVNVNLKKLKFQGWEKASLEntfIHNTGKTVEINL-TNDYYLSGGLSEKVFKASKITFHWGKCNvsSE 138
Cdd:cd00326     3 RQSPINIVTSAVVYDPSLPPLNFDYYPTTSLT---LVNNGHTVQVNFdDDGGTLSGGGLPGRYKLVQFHFHWGSEN--SP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  139 GSEHSLEGQKFPLEMQVYCFDADRFSSfeEAVKGKGRLRALSILFEVGVEENLDYKAIIDGTESVSRFGKQAALDPFVLQ 218
Cdd:cd00326    78 GSEHTIDGKRYPLELHLVHYNSDYYSS--EAAKKPGGLAVLGVFFEVGEKENPFLKKILDALPKIKYKGKETTLPPFDLS 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 901694078  219 NLLPNSTDKYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLAVFCEVLTMQqsgyvmlMDYLQNNFREQQYKFSRQVF 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 ...
 923-1142 1.01e-72

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: 241.85  E-value: 1.01e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  923 KDGKLTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPTDgSEEYGSFLV 1002
Cdd:cd14631     8 EDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDD-TEVYGDFKV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1003 NQKSVQVLAYYTVRNFTLrntklkkgSQKGRSSGRLVTQYHYTQWPDMGVPEYSLPVLAFVRKAAQAKRHAVGPVVVHCS 1082
Cdd:cd14631    87 TCVEMEPLAEYVVRTFTL--------ERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVHCS 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1083 AGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAIL 1142
Cdd:cd14631   159 AGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACL 218
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 902-1134 4.00e-72

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


Pssm-ID: 350395 [Multi-domain]  Cd Length: 224  Bit Score: 240.38  E-value: 4.00e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  902 NRYVNIVAYDHSRVKLTQlaEKDGKLTDYINANYVDGYN-RPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEK 980
Cdd:cd14547     1 NRYKTILPNEHSRVCLPS--VDDDPLSSYINANYIRGYDgEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  981 gRRKCDQYWPTDGSEEYGSFLVNQKSVQVLAYYTVRNFTLRNtklkkGSQKgrssgRLVTQYHYTQWPDMGVPEYSLPVL 1060
Cdd:cd14547    79 -KEKCAQYWPEEENETYGDFEVTVQSVKETDGYTVRKLTLKY-----GGEK-----RYLKHYWYTSWPDHKTPEAAQPLL 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 901694078 1061 AFVRKAAQAKRHAV--GPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIH 1134
Cdd:cd14547   148 SLVQEVEEARQTEPhrGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVH 223
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 930-1134 4.56e-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: 239.43  E-value: 4.56e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  930 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPTDGSEEYGSFLVNQKSVQV 1009
Cdd:cd14551     1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCWTYGNLRVRVEDTVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1010 LAYYTVRNFTLRntklKKGSQKGRSSGRLVTQYHYTQWPDMGVPEYSLPVLAFVRKAAQAKRHAVGPVVVHCSAGVGRTG 1089
Cdd:cd14551    81 LVDYTTRKFCIQ----KVNRGIGEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAGPIVVHCSAGVGRTG 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 901694078 1090 TYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIH 1134
Cdd:cd14551   157 TFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 930-1142 1.96e-71

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


Pssm-ID: 350480 [Multi-domain]  Cd Length: 205  Bit Score: 237.64  E-value: 1.96e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  930 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPtDGSEEYGSFLVNQKSVQV 1009
Cdd:cd14632     1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWP-DDSDTYGDIKITLLKTET 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1010 LAYYTVRNFTLRntklkkgsQKGRSSGRLVTQYHYTQWPDMGVPEYSLPVLAFVRKAAQAKRHAVGPVVVHCSAGVGRTG 1089
Cdd:cd14632    80 LAEYSVRTFALE--------RRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTG 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 901694078 1090 TYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAIL 1142
Cdd:cd14632   152 CYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILEACL 204
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 888-1134 3.14e-71

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


Pssm-ID: 350462 [Multi-domain]  Cd Length: 245  Bit Score: 238.63  E-value: 3.14e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  888 ITADSSNHPDNKHKNRYVNIVAYDHSRVKLTQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHN 967
Cdd:cd14614     2 IPHFAADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEG--SDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  968 VEVIVMITNLVEKGRRKCDQYWP-TDGSEEYGSFLVNQKSVQVLAYYTVRNFtlrNTKLKKGSQKgrssgrlVTQYHYTQ 1046
Cdd:cd14614    80 SQIIVMLTQCNEKRRVKCDHYWPfTEEPVAYGDITVEMLSEEEQPDWAIREF---RVSYADEVQD-------VMHFNYTA 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1047 WPDMGVPEYSL--PVLAFVRKAAQAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLV 1124
Cdd:cd14614   150 WPDHGVPTANAaeSILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMV 229

                         250
                  ....*....|
gi 901694078 1125 QTEEQYVFIH 1134
Cdd:cd14614   230 QTEEQYIFIH 239
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 902-1138 9.78e-70

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


Pssm-ID: 350466 [Multi-domain]  Cd Length: 230  Bit Score: 233.68  E-value: 9.78e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  902 NRYVNIVAYDHSRVKLTQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKG 981
Cdd:cd14618     1 NRYPHVLPYDHSRVRLSQLGGEPH--SDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  982 RRKCDQYWPTDGSE-EYGsflvnQKSVQVLAYYTVRNFTLRNTKLKKGSQKGRssgRLVTQYHYTQWPDMGVPEYSLPVL 1060
Cdd:cd14618    79 RVLCDHYWPSESTPvSYG-----HITVHLLAQSSEDEWTRREFKLWHEDLRKE---RRVKHLHYTAWPDHGIPESTSSLM 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1061 AF---VRKAAQAKRHAvGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTL 1137
Cdd:cd14618   151 AFrelVREHVQATKGK-GPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCI 229


                  .
gi 901694078 1138 V 1138
Cdd:cd14618   230 L 230
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 898-1134 8.21e-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: 231.97  E-value: 8.21e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  898 NKHKNRYVNIVAYDHSRVKLTQlAEKDGKLTDYINANYVDGYN-------RPKAYIAAQGPLKSTAEDFWRMIWEHNVEV 970
Cdd:cd14544     1 NKGKNRYKNILPFDHTRVILKD-RDPNVPGSDYINANYIRNENegpttdeNAKTYIATQGCLENTVSDFWSMVWQENSRV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  971 IVMITNLVEKGRRKCDQYWPTDG-SEEYGSFlvnqkSVQVLAYYTVRNFTLRNTKLKKGSQkgRSSGRLVTQYHYTQWPD 1049
Cdd:cd14544    80 IVMTTKEVERGKNKCVRYWPDEGmQKQYGPY-----RVQNVSEHDTTDYTLRELQVSKLDQ--GDPIREIWHYQYLSWPD 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1050 MGVPEYSLPVLAFVRKAAQAKRH--AVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEG---TVNIFGFLKHIRSQRNYLV 1124
Cdd:cd14544   153 HGVPSDPGGVLNFLEDVNQRQESlpHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGldcDIDIQKTIQMVRSQRSGMV 232

                         250
                  ....*....|
gi 901694078 1125 QTEEQYVFIH 1134
Cdd:cd14544   233 QTEAQYKFIY 242
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 892-1139 6.18e-67

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


Pssm-ID: 350476 [Multi-domain]  Cd Length: 292  Bit Score: 228.08  E-value: 6.18e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  892 SSNHPDNKHKNRYVNIVAYDHSRVKLTQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVI 971
Cdd:cd14628    46 SANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEG--SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIV 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  972 VMITNLVEKGRRKCDQYWPTDGSEEYGSFLVNQksvqvLAYYTVRNFTLRNTKLKKgSQKGRSsgRLVTQYHYTQWPDMG 1051
Cdd:cd14628   124 VMLTKLREMGREKCHQYWPAERSARYQYFVVDP-----MAEYNMPQYILREFKVTD-ARDGQS--RTVRQFQFTDWPEQG 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1052 VPEYSLPVLAFVRKAAQAKRH--AVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQ 1129
Cdd:cd14628   196 VPKSGEGFIDFIGQVHKTKEQfgQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQ 275

                         250
                  ....*....|
gi 901694078 1130 YVFIHDTLVE 1139
Cdd:cd14628   276 YQFCYRAALE 285
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 892-1143 5.07e-66

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


Pssm-ID: 350475 [Multi-domain]  Cd Length: 290  Bit Score: 225.38  E-value: 5.07e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  892 SSNHPDNKHKNRYVNIVAYDHSRVKLTQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVI 971
Cdd:cd14627    47 SANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEG--SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIV 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  972 VMITNLVEKGRRKCDQYWPTDGSEEYGSFLVNQksvqvLAYYTVRNFTLRNTKLKKgSQKGRSsgRLVTQYHYTQWPDMG 1051
Cdd:cd14627   125 VMLTKLREMGREKCHQYWPAERSARYQYFVVDP-----MAEYNMPQYILREFKVTD-ARDGQS--RTVRQFQFTDWPEQG 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1052 VPEYSLPVLAFVRKAAQAKRH--AVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQ 1129
Cdd:cd14627   197 VPKSGEGFIDFIGQVHKTKEQfgQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDE 276

                         250
                  ....*....|....
gi 901694078 1130 YVFIHDTLVEAILS 1143
Cdd:cd14627   277 YQFCYQAALEYLGS 290
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 930-1135 5.28e-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: 222.12  E-value: 5.28e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  930 YINANYVD-GYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPTDGSE-EYGSFLVNQKSV 1007
Cdd:cd18533     1 YINASYITlPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEgEYGDLTVELVSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1008 QVL--AYYTVRNFTLRNTKLKKgsqkgrssgRLVTQYHYTQWPDMGVPEYSLPVLAFVR--KAAQAKRHAVGPVVVHCSA 1083
Cdd:cd18533    81 EENddGGFIVREFELSKEDGKV---------KKVYHIQYKSWPDFGVPDSPEDLLTLIKlkRELNDSASLDPPIIVHCSA 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 901694078 1084 GVGRTGTYIVLDSMLQQIQ--HEGTVN-------IFGFLKHIRSQRNYLVQTEEQYVFIHD 1135
Cdd:cd18533   152 GVGRTGTFIALDSLLDELKrgLSDSQDledsedpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 930-1134 1.15e-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: 220.85  E-value: 1.15e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  930 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPT--DGSEEYGSFLVNQKSV 1007
Cdd:cd14557     1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSmeEGSRAFGDVVVKINEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1008 QVLAYYTVRNFTLRNTKLKkgsqkgrSSGRLVTQYHYTQWPDMGVPEYSLPVLAFVRKAAQAKRHAVGPVVVHCSAGVGR 1087
Cdd:cd14557    81 KICPDYIIRKLNINNKKEK-------GSGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGR 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 901694078 1088 TGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIH 1134
Cdd:cd14557   154 TGTYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIH 200
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 892-1143 2.37e-65

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


Pssm-ID: 350477 [Multi-domain]  Cd Length: 291  Bit Score: 223.45  E-value: 2.37e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  892 SSNHPDNKHKNRYVNIVAYDHSRVKLTQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVI 971
Cdd:cd14629    47 SANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEG--SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIV 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  972 VMITNLVEKGRRKCDQYWPTDGSEEYGSFLVNQksvqvLAYYTVRNFTLRNTKLKKgSQKGRSsgRLVTQYHYTQWPDMG 1051
Cdd:cd14629   125 VMLTKLREMGREKCHQYWPAERSARYQYFVVDP-----MAEYNMPQYILREFKVTD-ARDGQS--RTIRQFQFTDWPEQG 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1052 VPEYSLPVLAFVRKAAQAKRH--AVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQ 1129
Cdd:cd14629   197 VPKTGEGFIDFIGQVHKTKEQfgQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQ 276

                         250
                  ....*....|....
gi 901694078 1130 YVFIHDTLVEAILS 1143
Cdd:cd14629   277 YQLCYRAALEYLGS 290
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 873-1139 5.74e-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: 218.54  E-value: 5.74e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  873 KEFyQEVQSCTA----DLGITADSSNHPDNKHKNRYVNIVAYDHSRVKLTQLAEKDGklTDYINANYVDGYNRPKAYIAA 948
Cdd:cd14603     2 GEF-SEIRACSAafkaDYVCSTVAGGRKENVKKNRYKDILPYDQTRVILSLLQEEGH--SDYINANFIKGVDGSRAYIAT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  949 QGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWP-TDGSEEYGSFLVNQ-KSVQVLAYYTVRNFTLrntKLK 1026
Cdd:cd14603    79 QGPLSHTVLDFWRMIWQYGVKVILMACREIEMGKKKCERYWAqEQEPLQTGPFTITLvKEKRLNEEVILRTLKV---TFQ 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1027 KGSqkgrssgRLVTQYHYTQWPDMGVPEYSLPVLAFVRKAAQAKRHAVGPVVVHCSAGVGRTGTYIVLDS-----MLQQI 1101
Cdd:cd14603   156 KES-------RSVSHFQYMAWPDHGIPDSPDCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYvrqllLTQRI 228

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 901694078 1102 QHEgtVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVE 1139
Cdd:cd14603   229 PPD--FSIFDVVLEMRKQRPAAVQTEEQYEFLYHTVAQ 264
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 930-1138 1.57e-61

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


Pssm-ID: 350400 [Multi-domain]  Cd Length: 202  Bit Score: 209.05  E-value: 1.57e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  930 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPTDGSEEYGSFLVNQKSVQV 1009
Cdd:cd14552     1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGSVSSGDITVELKDQTD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1010 LAYYTVRNFTLRNTKlkkgsqkgRSSGRLVTQYHYTQWPDMGVPEYS---LPVLAFVRKaaQAKRHAVGPVVVHCSAGVG 1086
Cdd:cd14552    81 YEDYTLRDFLVTKGK--------GGSTRTVRQFHFHGWPEVGIPDNGkgmIDLIAAVQK--QQQQSGNHPITVHCSAGAG 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 901694078 1087 RTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLV 1138
Cdd:cd14552   151 RTGTFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVVQ 202
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 891-1143 1.97e-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: 211.28  E-value: 1.97e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  891 DSSNHPDNKHKNRYVNIVAYDHSRVKLtQLAEKDGKLTDYINANYVDGY-----NRPKAYIAAQGPLKSTAEDFWRMIWE 965
Cdd:cd14606    11 LEGQRPENKSKNRYKNILPFDHSRVIL-QGRDSNIPGSDYINANYVKNQllgpdENAKTYIASQGCLEATVNDFWQMAWQ 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  966 HNVEVIVMITNLVEKGRRKCDQYWPTDGSE-EYGSFLVNQKSVQVLAYYTVRnfTLRNTKLKKGSQKgrssgRLVTQYHY 1044
Cdd:cd14606    90 ENSRVIVMTTREVEKGRNKCVPYWPEVGMQrAYGPYSVTNCGEHDTTEYKLR--TLQVSPLDNGELI-----REIWHYQY 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1045 TQWPDMGVPEYSLPVLAFVRKAAQAK---RHAvGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGT---VNIFGFLKHIRS 1118
Cdd:cd14606   163 LSWPDHGVPSEPGGVLSFLDQINQRQeslPHA-GPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVRA 241

                         250       260
                  ....*....|....*....|....*
gi 901694078 1119 QRNYLVQTEEQYVFIHDTLVEAILS 1143
Cdd:cd14606   242 QRSGMVQTEAQYKFIYVAIAQFIET 266
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 930-1141 2.88e-61

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


Pssm-ID: 350386 [Multi-domain]  Cd Length: 207  Bit Score: 208.38  E-value: 2.88e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  930 YINANYV--DGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPtDGSEE----YGSFLVN 1003
Cdd:cd14538     1 YINASHIriPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWP-DSLNKplicGGRLEVS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1004 QKSVQVLAYYTVRNFTLRNTklkkgsQKGRSsgRLVTQYHYTQWPDMGVPEYSLPVLAFVRKAAqaKRHAVGPVVVHCSA 1083
Cdd:cd14538    80 LEKYQSLQDFVIRRISLRDK------ETGEV--HHITHLNFTTWPDHGTPQSADPLLRFIRYMR--RIHNSGPIVVHCSA 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 901694078 1084 GVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAI 1141
Cdd:cd14538   150 GIGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEVL 207
alpha_CA_VI_IX_XII_XIV cd03123
Carbonic anhydrase alpha, isozymes VI, IX, XII and XIV. Carbonic anhydrases (CAs) are ...
 46-300 8.25e-61

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: 208.70  E-value: 8.25e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078   46 QKNWGKKYPICNSPKQSPINIDEDLTQVNVNLKKLKFQGWEKASLENTFIHNTGKTVEINLTNDYYLSGGLSEKvFKASK 125
Cdd:cd03123     2 EDHWPKKYPACGGKRQSPIDIQTDIVQFDPSLPPLELVGYDLPGTEEFTLTNNGHTVQLSLPPTMHIRGGPGTE-YTAAQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  126 ITFHWGKCNvSSEGSEHSLEGQKFPLEMQVYCFDADRFSSFEEAVKGKGRLRALSILFEVGVEENLDYKAIIDGTESVSR 205
Cdd:cd03123    81 LHLHWGGRG-SLSGSEHTIDGIRFAAELHIVHYNSDKYSSFDEAADKPDGLAVLAILIEVGYPENTYYEKIISHLHEIKY 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  206 FGKQAALDPFVLQNLLPNSTDKYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLavfcevLTMQQSgyvmLMDY----L 281
Cdd:cd03123   160 KGQETTVPGFNVRELLPEDLSHYYRYEGSLTTPPCYESVLWTVFRDPVTLSKEQL------ETLENT----LMDThnktL 229

                         250
                  ....*....|....*....
gi 901694078  282 QNNFREQQYKFSRQVFSSY 300
Cdd:cd03123   230 QNNYRATQPLNGRVVEASF 248
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 867-1141 1.76e-60

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


Pssm-ID: 350457 [Multi-domain]  Cd Length: 281  Bit Score: 209.12  E-value: 1.76e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  867 EEFETLKEFYQEVQSCtadlgitaDSSNHPDNKHKNRYVNIVAYDHSRVKLTqlAEKDGKLTDYINAN-YVDGYNRPKAY 945
Cdd:cd14609    19 KEWQALCAYQAEPNTC--------STAQGEANVKKNRNPDFVPYDHARIKLK--AESNPSRSDYINASpIIEHDPRMPAY 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  946 IAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPTDGSEEYGSFLVNQKSVQVLAY-YTVRNFTLRNTK 1024
Cdd:cd14609    89 IATQGPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHIYEVNLVSEHIWCEdFLVRSFYLKNVQ 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1025 lkkgSQKGRSsgrlVTQYHYTQWPDMGVPEYSLPVLAFVRKAAQAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQhE 1104
Cdd:cd14609   169 ----TQETRT----LTQFHFLSWPAEGIPSSTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMA-K 239

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 901694078 1105 GT--VNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAI 1141
Cdd:cd14609   240 GVkeIDIAATLEHVRDQRPGMVRTKDQFEFALTAVAEEV 278
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 902-1134 3.44e-60

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


Pssm-ID: 350464 [Multi-domain]  Cd Length: 224  Bit Score: 206.30  E-value: 3.44e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  902 NRYVNIVAYDHSRVKLTQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKG 981
Cdd:cd14616     1 NRFPNIKPYNNNRVKLIADAGVPG--SDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  982 RRKCDQYWPTDGS--EEYGSFLVNQksvqvLAYYTVRNFTLRNTKLKKgsqkgRSSGRLVTQYHYTQWPDMGVPEYSLPV 1059
Cdd:cd14616    79 RIRCHQYWPEDNKpvTVFGDIVITK-----LMEDVQIDWTIRDLKIER-----HGDYMMVRQCNFTSWPEHGVPESSAPL 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 901694078 1060 LAFVrKAAQAKR-HAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIH 1134
Cdd:cd14616   149 IHFV-KLVRASRaHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLH 223
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 899-1132 4.34e-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: 4.34e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  899 KHKNRYVNIVAYDHSRVKLTQlaekdgKLTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLV 978
Cdd:cd14545     1 LNRYRDRDPYDHDRSRVKLKQ------GDNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLM 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  979 EKGRRKCDQYWPTDGSE----EYGSFLVNQKSVQVLAYYTVRNFTLRNtklKKGSQKgrssgRLVTQYHYTQWPDMGVPE 1054
Cdd:cd14545    75 EKGQIKCAQYWPQGEGNamifEDTGLKVTLLSEEDKSYYTVRTLELEN---LKTQET-----REVLHFHYTTWPDFGVPE 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1055 ---YSLPVLAFVRKAAQAKRHaVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGT--VNIFGFLKHIRSQRNYLVQTEEQ 1129
Cdd:cd14545   147 spaAFLNFLQKVRESGSLSSD-VGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYRMGLIQTPDQ 225


                  ...
gi 901694078 1130 YVF 1132
Cdd:cd14545   226 LRF 228
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 930-1134 5.13e-60

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


Pssm-ID: 350390 [Multi-domain]  Cd Length: 202  Bit Score: 204.58  E-value: 5.13e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  930 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPTDGSEE--YGSFLVNQKSV 1007
Cdd:cd14542     1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQlqFGPFKISLEKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1008 QVLAyytvRNFTLRNTKLKKGSQKgrssgRLVTQYHYTQWPDMGVPEYSLPVLAFVRKAAQAKRHAVGPVVVHCSAGVGR 1087
Cdd:cd14542    81 KRVG----PDFLIRTLKVTFQKES-----RTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDVPICVHCSAGCGR 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 901694078 1088 TGTYIVLDSMLQQIQHEG---TVNIFGFLKHIRSQRNYLVQTEEQYVFIH 1134
Cdd:cd14542   152 TGTICAIDYVWNLLKTGKipeEFSLFDLVREMRKQRPAMVQTKEQYELVY 201
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 888-1137 9.19e-60

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


Pssm-ID: 350460 [Multi-domain]  Cd Length: 247  Bit Score: 205.84  E-value: 9.19e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  888 ITADSSNHPDNKHKNRYVNIVAYDHSRVKLTQLAEKDgKLTDYINANYVDGYN-RPKAYIAAQGPLKSTAEDFWRMIWEH 966
Cdd:cd14612     5 VSPEELDIPGHASKDRYKTILPNPQSRVCLRRAGSQE-EEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  967 NVEVIVMITNLVEKgRRKCDQYWPTDgSEEYGSFLVNQKSVQVLAYYTVRNFTLrntklkkgsqKGRSSGRLVTQYHYTQ 1046
Cdd:cd14612    84 ECPIIVMITKLKEK-KEKCVHYWPEK-EGTYGRFEIRVQDMKECDGYTIRDLTI----------QLEEESRSVKHYWFSS 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1047 WPDMGVPEYSLPVLAFVRKAAQAKRHAV--GPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLV 1124
Cdd:cd14612   152 WPDHQTPESAGPLLRLVAEVEESRQTAAspGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMI 231

                         250
                  ....*....|...
gi 901694078 1125 QTEEQYVFIHDTL 1137
Cdd:cd14612   232 QTSEQYQFLHHTL 244
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 897-1134 1.99e-59

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


Pssm-ID: 350452 [Multi-domain]  Cd Length: 297  Bit Score: 206.71  E-value: 1.99e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  897 DNKHKNRYVNIVAYDHSRVKLT-QLAEKDgklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMIT 975
Cdd:cd14604    56 ENVKKNRYKDILPFDHSRVKLTlKTSSQD---SDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMAC 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  976 NLVEKGRRKCDQYWPTDGSE--EYGSFLVNQKSVQVLAYYTVRNFTLrntklkkgsqKGRSSGRLVTQYHYTQWPDMGVP 1053
Cdd:cd14604   133 REFEMGRKKCERYWPLYGEEpmTFGPFRISCEAEQARTDYFIRTLLL----------EFQNETRRLYQFHYVNWPDHDVP 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1054 EYSLPVLAFVRKAAQAKRHAVGPVVVHCSAGVGRTGTYIVLD---SMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQY 1130
Cdd:cd14604   203 SSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQY 282


                  ....
gi 901694078 1131 VFIH 1134
Cdd:cd14604   283 ELVH 286
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 903-1139 2.14e-59

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


Pssm-ID: 350471 [Multi-domain]  Cd Length: 228  Bit Score: 204.12  E-value: 2.14e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  903 RYVNIVAYDHSRVKLTqlAEKDGKLTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGR 982
Cdd:cd14623     1 RVLQIIPYEFNRVIIP--VKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  983 RKCDQYWPTDGSEEYGSFLVNQKSVQVLAYYTVRNFTLRNTKLKKgsqkgrssGRLVTQYHYTQWPDMGVPEYS---LPV 1059
Cdd:cd14623    79 EKCAQYWPSDGSVSYGDITIELKKEEECESYTVRDLLVTNTRENK--------SRQIRQFHFHGWPEVGIPSDGkgmINI 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1060 LAFVRKaaQAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVE 1139
Cdd:cd14623   151 IAAVQK--QQQQSGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 859-1141 2.80e-59

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


Pssm-ID: 350458 [Multi-domain]  Cd Length: 283  Bit Score: 205.68  E-value: 2.80e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  859 LHASNGFTEEFETLKEFYQEVQSCTADLgitadssnHPDNKHKNRYVNIVAYDHSRVKLTqlAEKDGKLTDYINANYV-D 937
Cdd:cd14610    13 LKNKNRLEKEWEALCAYQAEPNATNVAQ--------REENVQKNRSLAVLPYDHSRIILK--AENSHSHSDYINASPImD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  938 GYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPTDGSEEYGSFLVNQKSVQVLAY-YTVR 1016
Cdd:cd14610    83 HDPRNPAYIATQGPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEGSNLYHIYEVNLVSEHIWCEdFLVR 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1017 NFTLRNTKLKKgsqkgrssGRLVTQYHYTQWPDMGVPEYSLPVLAFVRKAAQAKRHAVGPVVVHCSAGVGRTGTYIVLDS 1096
Cdd:cd14610   163 SFYLKNLQTNE--------TRTVTQFHFLSWNDQGVPASTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILIDM 234

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 901694078 1097 MLQQI-QHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAI 1141
Cdd:cd14610   235 VLNKMaKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAEEV 280
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 897-1134 3.85e-59

catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein phosphatase non-receptor type 11 (PTPN11), also called SH2 domain-containing tyrosine phosphatase 2 (SHP-2 or SHP2), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN11 promotes the activation of the RAS/Mitogen-Activated Protein Kinases (MAPK) Extracellular-Regulated Kinases 1/2 (ERK1/2) pathway, a canonical signaling cascade that plays key roles in various cellular processes, including proliferation, survival, differentiation, migration, or metabolism. It also regulates the phosphoinositide 3-kinase (PI3K)/AKT pathway, a fundamental cascade that functions in cell survival, proliferation, migration, morphogenesis, and metabolism. PTPN11 dysregulation is associated with several developmental diseases and malignancies, such as Noonan syndrome and juvenile myelomonocytic leukemia. It contains two tandem SH2 domains, a catalytic PTP domain, and a C-terminal tail with regulatory properties.


Pssm-ID: 350453 [Multi-domain]  Cd Length: 253  Bit Score: 204.10  E-value: 3.85e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  897 DNKHKNRYVNIVAYDHSRVKLTQlAEKDGKLTDYINANYVDGYN-------RPK-AYIAAQGPLKSTAEDFWRMIWEHNV 968
Cdd:cd14605     1 ENKNKNRYKNILPFDHTRVVLHD-GDPNEPVSDYINANIIMPEFetkcnnsKPKkSYIATQGCLQNTVNDFWRMVFQENS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  969 EVIVMITNLVEKGRRKCDQYWPTDGS-EEYGSFLVnqKSVQVLAYYtvrNFTLRNTKLKKGSQKgrSSGRLVTQYHYTQW 1047
Cdd:cd14605    80 RVIVMTTKEVERGKSKCVKYWPDEYAlKEYGVMRV--RNVKESAAH---DYILRELKLSKVGQG--NTERTVWQYHFRTW 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1048 PDMGVPEYSLPVLAFVRKA--AQAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGT---VNIFGFLKHIRSQRNY 1122
Cdd:cd14605   153 PDHGVPSDPGGVLDFLEEVhhKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRSG 232

                         250
                  ....*....|..
gi 901694078 1123 LVQTEEQYVFIH 1134
Cdd:cd14605   233 MVQTEAQYRFIY 244
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 1225-1425 1.53e-57

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


Pssm-ID: 350343 [Multi-domain]  Cd Length: 200  Bit Score: 197.51  E-value: 1.53e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1225 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPD----GQNMAEDefvYWPNK-DEPINCESFKVTL 1299
Cdd:cd00047     1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNlvekGREKCER---YWPEEgGKPLEYGDITVTL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1300 MSEEHKclsneEKLIVQDFILEATQDDYVLEVRHFQCPKWPN---PDSPISkTFELISIIKEEAANRDGPMIVHDEHGGV 1376
Cdd:cd00047    78 VSEEEL-----SDYTIRTLELSPKGCSESREVTHLHYTGWPDhgvPSSPED-LLALVRRVRKEARKPNGPIVVHCSAGVG 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 901694078 1377 TAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYK 1425
Cdd:cd00047   152 RTGTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 930-1141 1.86e-57

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


Pssm-ID: 350394 [Multi-domain]  Cd Length: 208  Bit Score: 197.67  E-value: 1.86e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  930 YINANYVDGYN-RPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPTDGSEEYGSFLVNQKSVQ 1008
Cdd:cd14546     1 YINASTIYDHDpRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEVYHIYEVHLVSEH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1009 VL-AYYTVRNFTLRNTKlkkgsqkgRSSGRLVTQYHYTQWPDMGVPEYSLPVLAFVRKAAQAKRHAVGPVVVHCSAGVGR 1087
Cdd:cd14546    81 IWcDDYLVRSFYLKNLQ--------TSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYRGRSCPIVVHCSDGAGR 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 901694078 1088 TGTYIVLDSMLQQIQhEGT--VNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAI 1141
Cdd:cd14546   153 TGTYILIDMVLNRMA-KGAkeIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAEEV 207
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 929-1143 3.33e-57

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


Pssm-ID: 350389 [Multi-domain]  Cd Length: 212  Bit Score: 197.17  E-value: 3.33e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  929 DYINANYVDgYNRPKA-----YIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWP-TDGSEEYGSFLV 1002
Cdd:cd14541     1 DYINANYVN-MEIPGSgivnrYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPdLGETMQFGNLQI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1003 NQKSVQVLAYYTVRNFTLRNTKLKKgsqkgrssGRLVTQYHYTQWPDMGVPEYSLPVLAFVRKAAQAKRHAVGPVVVHCS 1082
Cdd:cd14541    80 TCVSEEVTPSFAFREFILTNTNTGE--------ERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVEPTVVHCS 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 901694078 1083 AGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIhdtlVEAILS 1143
Cdd:cd14541   152 AGIGRTGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFV----CEAILR 208
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 930-1139 8.35e-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: 196.14  E-value: 8.35e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  930 YINANYVDGY--NRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPTDGSEE----YGSFLVN 1003
Cdd:cd14540     1 YINASHITATvgGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGGEHdaltFGEYKVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1004 QKSVQVLAYYTVRNFTLRNTklkkgsqkgrSSGRLVTQYH--YTQWPDMGVPEYSLPVLAFVRKAAQAKRHAVG------ 1075
Cdd:cd14540    81 TKFSVSSGCYTTTGLRVKHT----------LSGQSRTVWHlqYTDWPDHGCPEDVSGFLDFLEEINSVRRHTNQdvaghn 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 901694078 1076 ---PVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVE 1139
Cdd:cd14540   151 rnpPTLVHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQ 217
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 901-1139 1.41e-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: 196.21  E-value: 1.41e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  901 KNRYVNIVAYDHSRVKLTQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEK 980
Cdd:cd14602     1 KNRYKDILPYDHSRVELSLITSDED--SDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  981 GRRKCDQYWPTDGSE--EYGSFLVNQKSVQVLAYYTVRnfTLRNTKLkkgsqkgrSSGRLVTQYHYTQWPDMGVPEYSLP 1058
Cdd:cd14602    79 GKKKCERYWAEPGEMqlEFGPFSVTCEAEKRKSDYIIR--TLKVKFN--------SETRTIYQFHYKNWPDHDVPSSIDP 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1059 VLAFVRKAAQAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQhEGTV----NIFGFLKHIRSQRNYLVQTEEQYVFIH 1134
Cdd:cd14602   149 ILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLK-DGIIpenfSVFSLIQEMRTQRPSLVQTKEQYELVY 227


                  ....*
gi 901694078 1135 DTLVE 1139
Cdd:cd14602   228 NAVIE 232
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 929-1134 4.82e-56

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


Pssm-ID: 350470 [Multi-domain]  Cd Length: 205  Bit Score: 193.68  E-value: 4.82e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  929 DYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPTDGSEEYGSFLVNQKSVQ 1008
Cdd:cd14622     1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEGSVTHGEITIEIKNDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1009 VLAYYTVRNFTLRNTKLKKgsqkgrssGRLVTQYHYTQWPDMGVPEYS---LPVLAFVRKaaQAKRHAVGPVVVHCSAGV 1085
Cdd:cd14622    81 LLETISIRDFLVTYNQEKQ--------TRLVRQFHFHGWPEIGIPAEGkgmIDLIAAVQK--QQQQTGNHPIVVHCSAGA 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 901694078 1086 GRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIH 1134
Cdd:cd14622   151 GRTGTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCY 199
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 901-1134 7.40e-56

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


Pssm-ID: 350459 [Multi-domain]  Cd Length: 226  Bit Score: 193.60  E-value: 7.40e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  901 KNRYVNIVAYDHSRVKLTQLAEKDgKLTDYINANYVDGY-NRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVE 979
Cdd:cd14611     2 KNRYKTILPNPHSRVCLKPKNSND-SLSTYINANYIRGYgGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  980 KGRrKCDQYWPtDGSEEYGSFLVNQKSVQVLAYYTVRNFTLrntklKKGSQKgrssgRLVTQYHYTQWPDMGVPEYSLPV 1059
Cdd:cd14611    81 KNE-KCVLYWP-EKRGIYGKVEVLVNSVKECDNYTIRNLTL-----KQGSQS-----RSVKHYWYTSWPDHKTPDSAQPL 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1060 LAFV------RKAAQAKrhavGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFI 1133
Cdd:cd14611   149 LQLMldveedRLASPGR----GPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFV 224


                  .
gi 901694078 1134 H 1134
Cdd:cd14611   225 H 225
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 896-1142 1.30e-55

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: 195.07  E-value: 1.30e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  896 PDNKHKNRYVNIVAYDHSRVKLTqlaEKDgkltDYINANYVD----GYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVI 971
Cdd:cd14600    38 PQNMDKNRYKDVLPYDATRVVLQ---GNE----DYINASYVNmeipSANIVNKYIATQGPLPHTCAQFWQVVWEQKLSLI 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  972 VMITNLVEKGRRKCDQYWPtDGSE--EYGSFLVNQKSVQVLAYYTVRNFTLrnTKLKKGSQkgrssgRLVTQYHYTQWPD 1049
Cdd:cd14600   111 VMLTTLTERGRTKCHQYWP-DPPDvmEYGGFRVQCHSEDCTIAYVFREMLL--TNTQTGEE------RTVTHLQYVAWPD 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1050 MGVPEYSLPVLAFVRKAAQaKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQ 1129
Cdd:cd14600   182 HGVPDDSSDFLEFVNYVRS-KRVENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQ 260

                         250
                  ....*....|...
gi 901694078 1130 YVFIhdtlVEAIL 1142
Cdd:cd14600   261 YKFV----CEAIL 269
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 901-1137 1.81e-55

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


Pssm-ID: 350461 [Multi-domain]  Cd Length: 258  Bit Score: 193.93  E-value: 1.81e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  901 KNRYVNIVAYDHSRVKLTQlAEKDGKLTDYINANYVDGYN-RPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVE 979
Cdd:cd14613    28 KNRYKTILPNPHSRVCLTS-PDQDDPLSSYINANYIRGYGgEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEE 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  980 KGRrKCDQYWPTDgSEEYGSFLVNQKSVQVLAYYTVRNFTLrntklKKGSQKgrssgRLVTQYHYTQWPDMGVPEYSLPV 1059
Cdd:cd14613   107 MNE-KCTEYWPEE-QVTYEGIEITVKQVIHADDYRLRLITL-----KSGGEE-----RGLKHYWYTSWPDQKTPDNAPPL 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1060 LAFVRKAAQAKRHA---VGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDT 1136
Cdd:cd14613   175 LQLVQEVEEARQQAepnCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVHHV 254


                  .
gi 901694078 1137 L 1137
Cdd:cd14613   255 L 255
alpha_CA_XII_XIV cd03126
Carbonic anhydrase alpha, isozymes XII and XIV. Carbonic anhydrases (CAs) are zinc-containing ...
 46-300 2.98e-54

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: 190.05  E-value: 2.98e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078   46 QKNWGKKYPICNSPKQSPINIDEDLTQVNVNLKKLKFQGWEKASLENTFIHNTGKTVEINLTNDYYLsGGLSEKvFKASK 125
Cdd:cd03126     2 ENSWPKKYPFCGGVAQSPIDIHTDILQYDSSLPPLEFHGYNVSGTEQFTLTNNGHTVQLSLPPTMHI-GGLPFK-YTASQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  126 ITFHWGKCNvSSEGSEHSLEGQKFPLEMQVYCFDADRFSSFEEAVKGKGRLRALSILFEVGvEENLDYKAIIDGTESVSR 205
Cdd:cd03126    80 LHLHWGQRG-SPEGSEHTISGKHFAAELHIVHYNSDKYPDISTAMNKSQGLAVLGILIEVG-PFNPSYEKIFSHLHEVKY 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  206 FGKQAALDPFVLQNLLPNSTDKYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLavfcevLTMQQSGYVMLMD---YLQ 282
Cdd:cd03126   158 KDQKVSVPGFNVQELLPKRLDEYYRYEGSLTTPPCYPSVLWTVFRNPVQISQEQL------LALETALYSTEEDesrEMV 231

                         250
                  ....*....|....*...
gi 901694078  283 NNFREQQYKFSRQVFSSY 300
Cdd:cd03126   232 NNYRQVQPFNERLVFASF 249
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 876-1132 9.11e-53

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: 185.94  E-value: 9.11e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  876 YQEVQSCTADLGITAdsSNHPDNKHKNRYVNIVAYDHSRVKLtQLAEkdgklTDYINANYVDGYNRPKAYIAAQGPLKST 955
Cdd:cd14607     4 YLEIRNESHDYPHRV--AKYPENRNRNRYRDVSPYDHSRVKL-QNTE-----NDYINASLVVIEEAQRSYILTQGPLPNT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  956 AEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPTDGSEEYG----SFLVNQKSVQVLAYYTVRNFTLRNTKlkkgsqK 1031
Cdd:cd14607    76 CCHFWLMVWQQKTKAVVMLNRIVEKDSVKCAQYWPTDEEEVLSfketGFSVKLLSEDVKSYYTVHLLQLENIN------S 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1032 GRSsgRLVTQYHYTQWPDMGVPEYSLPVLAFVRKAAQAKRHAV--GPVVVHCSAGVGRTGTYIVLDS--MLQQIQHEGTV 1107
Cdd:cd14607   150 GET--RTISHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSPehGPAVVHCSAGIGRSGTFSLVDTclVLMEKKDPDSV 227

                         250       260
                  ....*....|....*....|....*
gi 901694078 1108 NIFGFLKHIRSQRNYLVQTEEQYVF 1132
Cdd:cd14607   228 DIKQVLLDMRKYRMGLIQTPDQLRF 252
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 897-1132 2.11e-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: 184.26  E-value: 2.11e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  897 DNKHKNRYVNIVAYDHSRVKLtqlaekdGKLTDYINANYVD---GyNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVM 973
Cdd:cd14597     2 ENRKKNRYKNILPYDTTRVPL-------GDEGGYINASFIKmpvG-DEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAM 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  974 ITNLVEKGRRKCDQYWPtdgsEEYGSFLV--NQKSVQVLAYYTVRNFTLRNTKLKKgSQKGRSsgRLVTQYHYTQWPDMG 1051
Cdd:cd14597    74 MTQEVEGGKIKCQRYWP----EILGKTTMvdNRLQLTLVRMQQLKNFVIRVLELED-IQTREV--RHITHLNFTAWPDHD 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1052 V---PEYSLPVLAFVRKAaqakrHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEE 1128
Cdd:cd14597   147 TpsqPEQLLTFISYMRHI-----HKSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTED 221


                  ....
gi 901694078 1129 QYVF 1132
Cdd:cd14597   222 QYIF 225
PHA02738 PHA02738
hypothetical protein; Provisional
 898-1132 6.51e-52

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 185.90  E-value: 6.51e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  898 NKHKNRYVNIVAYDHSRVKLTqlAEKDgkLTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNL 977
Cdd:PHA02738   49 NRKLNRYLDAVCFDHSRVILP--AERN--RGDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKK 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  978 VEKGRRKCDQYWPT--DGSEEYGSFLVNQKSVQVLAYYTVRNFTLRNtklkkgsqkGRSSGRLVTQYHYTQWPDMGVPEY 1055
Cdd:PHA02738  125 KENGREKCFPYWSDveQGSIRFGKFKITTTQVETHPHYVKSTLLLTD---------GTSATQTVTHFNFTAWPDHDVPKN 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1056 SLPVLAFVRKAAQA-------------KRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNY 1122
Cdd:PHA02738  196 TSEFLNFVLEVRQCqkelaqeslqighNRLQPPPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYY 275

                         250
                  ....*....|
gi 901694078 1123 LVQTEEQYVF 1132
Cdd:PHA02738  276 SLFIPFQYFF 285
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 876-1139 9.07e-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: 9.07e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  876 YQEVQSCTADLgiTADSSNHPDNKHKNRYVNIVAYDHSRVKLTQlaekdgKLTDYINANYVDGYNRPKAYIAAQGPLKST 955
Cdd:cd14608     5 YQDIRHEASDF--PCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQ------EDNDYINASLIKMEEAQRSYILTQGPLPNT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  956 AEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPTDGSEEY----GSFLVNQKSVQVLAYYTVRNFTLRNTKlkkgSQK 1031
Cdd:cd14608    77 CGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMifedTNLKLTLISEDIKSYYTVRQLELENLT----TQE 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1032 GRSsgrlVTQYHYTQWPDMGVPEYSLPVLAFVRKAAQAK--RHAVGPVVVHCSAGVGRTGTYIVLDS---MLQQIQHEGT 1106
Cdd:cd14608   153 TRE----ILHFHYTTWPDFGVPESPASFLNFLFKVRESGslSPEHGPVVVHCSAGIGRSGTFCLADTcllLMDKRKDPSS 228

                         250       260       270
                  ....*....|....*....|....*....|...
gi 901694078 1107 VNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVE 1139
Cdd:cd14608   229 VDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIE 261
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 930-1135 1.20e-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: 177.97  E-value: 1.20e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  930 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPtDGSEEYGSFLVNQKSVQV 1009
Cdd:cd14558     1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWG-DEKKTYGDIEVELKDTEK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1010 LAYYTVRNFTLRNTKLKKGSQkgrssgrlVTQYHYTQWPDMGVPEYSLPVLAFVRKAAQ------AKRHAVGPVVVHCSA 1083
Cdd:cd14558    80 SPTYTVRVFEITHLKRKDSRT--------VYQYQYHKWKGEELPEKPKDLVDMIKSIKQklpyknSKHGRSVPIVVHCSD 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 901694078 1084 GVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHD 1135
Cdd:cd14558   152 GSSRTGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203
alpha_CA_IV_XV_like cd03117
Carbonic anhydrase alpha, CA_IV, CA_XV, like isozymes. Carbonic anhydrases (CAs) are ...
 59-298 1.31e-50

Carbonic anhydrase alpha, CA_IV, CA_XV, like isozymes. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Most alpha CAs are monomeric enzymes. The zinc ion is complexed by three histidine residues. This subgroup, restricted to animals, contains isozyme IV and similar proteins such as mouse CA XV. Isozymes IV is attached to membranes via a glycosylphosphatidylinositol (GPI) tail. In mammals, Isozyme IV plays crucial roles in kidney and lung function, amongst others. This subgroup also contains the dual domain CA from the giant clam, Tridacna gigas. T. gigas CA plays a role in the movement of inorganic carbon from the surrounding seawater to the symbiotic algae found in the clam's tissues. CA XV is expressed in several species but not in humans or chimps. Similar to isozyme CA IV, CA XV attaches to membranes via a GPI tail.


Pssm-ID: 239391  Cd Length: 234  Bit Score: 179.00  E-value: 1.31e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078   59 PKQSPINIDEDLTQVNVNLKKLKFQGWEKASLeNTFIHNTGKTVEINLTNDYYLSGG-LSEKvFKASKITFHWGkcNVSS 137
Cdd:cd03117     2 KRQSPINIVTKKVQYDENLTPFTFTGYDDTTT-NWTITNNGHTVQVTLPDGAKISGGgLPGT-YKALQFHFHWG--SNGS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  138 EGSEHSLEGQKFPLEMQVYCFDADrFSSFEEAVKGKGRLRALSILFEVGVEENLDYKAIIDGTESVSRFGKQAALDPFVL 217
Cdd:cd03117    78 PGSEHTIDGERYPMELHIVHIKES-YNSLLEALKDSDGLAVLGFFIEEGEEENTNFDPLISALSNIPQKGGSTNLTPFSL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  218 QNLLP-NSTDKYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLAVFCEVLTMQQSGYVMLMdylqNNFREQQYKFSRQV 296
Cdd:cd03117   157 RSLLPsVLLTKYYRYNGSLTTPGCNEAVIWTVFEEPIPISRAQLDAFSTVLFFDTDNGQPMV----NNFRPVQPLNGRVV 232


                  ..
gi 901694078  297 FS 298
Cdd:cd03117   233 YA 234
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 929-1142 9.66e-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: 172.82  E-value: 9.66e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  929 DYINANYVDG-------YNRpkaYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWP-TDGSEEYGSF 1000
Cdd:cd14601     1 DYINANYINMeipsssiINR---YIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPePSGSSSYGGF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1001 LVNQKSVQVLAYYTVRNFTLRNTklkkgsQKGRSsgRLVTQYHYTQWPDMGVPEYSLPVLAFVRKAAQAKRHAVGPVVVH 1080
Cdd:cd14601    78 QVTCHSEEGNPAYVFREMTLTNL------EKNES--RPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDEPVVVH 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 901694078 1081 CSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIhdtlVEAIL 1142
Cdd:cd14601   150 CSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFV----CEAIL 207
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 930-1141 1.01e-48

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


Pssm-ID: 350444 [Multi-domain]  Cd Length: 207  Bit Score: 172.62  E-value: 1.01e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  930 YINANYVDGYNRPKA--YIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWP-----TDGSEEYGSFLV 1002
Cdd:cd14596     1 YINASYITMPVGEEElfYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPetlqePMELENYQLRLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1003 NqksVQVLAYYTVRNFTLrntklkkgSQKGRSSGRLVTQYHYTQWPDMGVPEYSLPVLAFVRKAaqAKRHAVGPVVVHCS 1082
Cdd:cd14596    81 N---YQALQYFIIRIIKL--------VEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYM--RKVHNTGPIVVHCS 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 901694078 1083 AGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAI 1141
Cdd:cd14596   148 AGIGRAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVL 206
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 896-1139 2.45e-48

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


Pssm-ID: 350447 [Multi-domain]  Cd Length: 287  Bit Score: 174.42  E-value: 2.45e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  896 PDNKHKNRYVNIVAYDHSRVKLTQLAEKDgklTDYINANYVDGYNRPKA--YIAAQGPLKSTAEDFWRMIWEHNVEVIVM 973
Cdd:cd14599    36 PENAERNRIREVVPYEENRVELVPTKENN---TGYINASHIKVTVGGEEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAM 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  974 ITNLVEKGRRKCDQYWPTDG----SEEYGSFLVNQKSVQVLAYYTVRNFTLRNtkLKKGSQkgrssgRLVTQYHYTQWPD 1049
Cdd:cd14599   113 VTAEEEGGRSKSHRYWPKLGskhsSATYGKFKVTTKFRTDSGCYATTGLKVKH--LLSGQE------RTVWHLQYTDWPD 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1050 MGVPEYSLPVLAFVRKAAQAKRHAVG----------PVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQ 1119
Cdd:cd14599   185 HGCPEEVQGFLSYLEEIQSVRRHTNSmldstkncnpPIVVHCSAGVGRTGVVILTELMIGCLEHNEKVEVPVMLRHLREQ 264

                         250       260
                  ....*....|....*....|
gi 901694078 1120 RNYLVQTEEQYVFIHDTLVE 1139
Cdd:cd14599   265 RMFMIQTIAQYKFVYQVLIQ 284
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 930-1135 1.06e-47

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


Pssm-ID: 350387 [Multi-domain]  Cd Length: 205  Bit Score: 169.49  E-value: 1.06e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  930 YINANYVDGY-NRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPTD-GSE-EYGSFLVNQKS 1006
Cdd:cd14539     1 YINASLIEDLtPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTErGQAlVYGAITVSLQS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1007 VQVLAYYTVRNFTL--RNTKLKkgsqkgrssgRLVTQYHYTQWPDMGVPEYSLPVLAF---VRKAAQAKRHAVGPVVVHC 1081
Cdd:cd14539    81 VRTTPTHVERIISIqhKDTRLS----------RSVVHLQFTTWPELGLPDSPNPLLRFieeVHSHYLQQRSLQTPIVVHC 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 901694078 1082 SAGVGRTGTYIVLDSMLQQIQHE-GTVNIFGFLKHIRSQRNYLVQTEEQYVFIHD 1135
Cdd:cd14539   151 SSGVGRTGAFCLLYAAVQEIEAGnGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 1146-1433 1.73e-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: 169.14  E-value: 1.73e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1146 TEVPDSHIHSYVNTLL-IPGPTGKTKLEKQFQLLSQSNILQSDYSTALKQCNREKNRTSSIIPVERSRVGISSLSG-EGT 1223
Cdd:cd14628     1 TEVPARNLYAYIQKLTqIETGENVTGMELEFKRLASSKAHTSRFISANLPCNKFKNRLVNIMPYESTRVCLQPIRGvEGS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1224 DYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAEDE-FVYWPnKDEPINCESFKVTLMSE 1302
Cdd:cd14628    81 DYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKcHQYWP-AERSARYQYFVVDPMAE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1303 ehkclSNEEKLIVQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKT--FELISII--KEEAANRDGPMIVHDEHGGVTA 1378
Cdd:cd14628   160 -----YNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEgfIDFIGQVhkTKEQFGQDGPISVHCSAGVGRT 234

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 901694078 1379 GTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVVLSLVST 1433
Cdd:cd14628   235 GVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEYLGS 289
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 889-1142 6.43e-46

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 168.67  E-value: 6.43e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  889 TADSSNHPDNKHKNRYVNIVAYDHSRV--------KLTQLAEKDGKL---------TDYINANYVDGYNRPKAYIAAQGP 951
Cdd:PHA02746   42 TTNHFLKKENLKKNRFHDIPCWDHSRVvinaheslKMFDVGDSDGKKievtsednaENYIHANFVDGFKEANKFICAQGP 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  952 LKSTAEDFWRMIWEHNVEVIVMITNlVEKGRRKCDQYW--PTDGSEEYGSFLVNQKSVQVLAYYTVRNFTLRNtklkkgs 1029
Cdd:PHA02746  122 KEDTSEDFFKLISEHESQVIVSLTD-IDDDDEKCFELWtkEEDSELAFGRFVAKILDIIEELSFTKTRLMITD------- 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1030 qKGRSSGRLVTQYHYTQWPDMGVPEYSLPVL----------AFVRKAAQAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQ 1099
Cdd:PHA02746  194 -KISDTSREIHHFWFPDWPDNGIPTGMAEFLelinkvneeqAELIKQADNDPQTLGPIVVHCSAGIGRAGTFCAIDNALE 272

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 901694078 1100 QIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAIL 1142
Cdd:PHA02746  273 QLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKALKYAII 315
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 1195-1428 7.59e-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: 165.39  E-value: 7.59e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1195 CNREKNRTSSIIPVERSRVGISSLSG-EGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQ 1273
Cdd:cd14554     5 CNKFKNRLVNILPYESTRVCLQPIRGvEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTKLR 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1274 NMAEDE-FVYWPNkDEPINCESFKVTLMSEehkclSNEEKLIVQDFILEATQDDYVLEVRHFQCPKWPNPDSPisKTFE- 1351
Cdd:cd14554    85 EMGREKcHQYWPA-ERSARYQYFVVDPMAE-----YNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVP--KSGEg 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1352 LISIIKE-----EAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKV 1426
Cdd:cd14554   157 FIDFIGQvhktkEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRA 236


                  ..
gi 901694078 1427 VL 1428
Cdd:cd14554   237 AL 238
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 874-1134 1.66e-45

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 167.10  E-value: 1.66e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  874 EFYQEVqscTADLGITADSSNHPDNKHKNRYVNIVAYDHSRVKLTQlaeKDGKLTDYINANYVDGYNRPKAYIAAQGPLK 953
Cdd:PHA02747   30 EHHQII---LKPFDGLIANFEKPENQPKNRYWDIPCWDHNRVILDS---GGGSTSDYIHANWIDGFEDDKKFIATQGPFA 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  954 STAEDFWRMIWEHNVEVIVMIT-NLVEKGRRKCDQYW--PTDGSEEYGSFLVNQKSVQVLAYYTVRNFTLRNTKLKkgsq 1030
Cdd:PHA02747  104 ETCADFWKAVWQEHCSIIVMLTpTKGTNGEEKCYQYWclNEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILK---- 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1031 kgrsSGRLVTQYHYTQWPDMGVPEYSLPVLAFVR----------KAAQAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQ 1100
Cdd:PHA02747  180 ----DSRKISHFQCSEWFEDETPSDHPDFIKFIKiidinrkksgKLFNPKDALLCPIVVHCSDGVGKTGIFCAVDICLNQ 255

                         250       260       270
                  ....*....|....*....|....*....|....
gi 901694078 1101 IQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIH 1134
Cdd:PHA02747  256 LVKRKAICLAKTAEKIREQRHAGIMNFDDYLFIQ 289
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 898-1139 1.81e-45

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 166.72  E-value: 1.81e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  898 NKHKNRYVNIVAYDHSRVKLTQlaeKDGkLTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNL 977
Cdd:PHA02742   52 NMKKCRYPDAPCFDRNRVILKI---EDG-GDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKI 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  978 VEKGRRKCDQYWPTD--GSEEYGSFLVNQKSVQVLAYYTVRNFTLRNTklkkgsQKGRSSGrlVTQYHYTQWPDMGVPEY 1055
Cdd:PHA02742  128 MEDGKEACYPYWMPHerGKATHGEFKIKTKKIKSFRNYAVTNLCLTDT------NTGASLD--IKHFAYEDWPHGGLPRD 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1056 SLPVLAFVRKAAQAK-----------RHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLV 1124
Cdd:PHA02742  200 PNKFLDFVLAVREADlkadvdikgenIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCL 279

                         250
                  ....*....|....*
gi 901694078 1125 QTEEQYVFIHDTLVE 1139
Cdd:PHA02742  280 SLPQQYIFCYFIVLI 294
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 1146-1433 5.13e-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: 164.90  E-value: 5.13e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1146 TEVPDSHIHSYVNTL-LIPGPTGKTKLEKQFQLLSQSNILQSDYSTALKQCNREKNRTSSIIPVERSRVGISSLSG-EGT 1223
Cdd:cd14629     2 TEVPARNLYAHIQKLtQVPPGESVTAMELEFKLLANSKAHTSRFISANLPCNKFKNRLVNIMPYELTRVCLQPIRGvEGS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1224 DYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAEDE-FVYWPnKDEPINCESFKVTLMSE 1302
Cdd:cd14629    82 DYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKcHQYWP-AERSARYQYFVVDPMAE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1303 ehkclSNEEKLIVQDFILEATQDDYVLEVRHFQCPKWPNPDSPisKTFE-LISIIKE-----EAANRDGPMIVHDEHGGV 1376
Cdd:cd14629   161 -----YNMPQYILREFKVTDARDGQSRTIRQFQFTDWPEQGVP--KTGEgFIDFIGQvhktkEQFGQDGPITVHCSAGVG 233

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 901694078 1377 TAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVVLSLVST 1433
Cdd:cd14629   234 RTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALEYLGS 290
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 1146-1433 5.31e-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: 164.91  E-value: 5.31e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1146 TEVPDSHIHSYVNTLLIPGPTGK-TKLEKQFQLLSQSNILQSDYSTALKQCNREKNRTSSIIPVERSRVGISSLSG-EGT 1223
Cdd:cd14627     2 TEVPARNLYSYIQKLAQVEVGEHvTGMELEFKRLANSKAHTSRFISANLPCNKFKNRLVNIMPYETTRVCLQPIRGvEGS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1224 DYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAEDE-FVYWPnKDEPINCESFKVTLMSE 1302
Cdd:cd14627    82 DYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGREKcHQYWP-AERSARYQYFVVDPMAE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1303 ehkclSNEEKLIVQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKT--FELISII--KEEAANRDGPMIVHDEHGGVTA 1378
Cdd:cd14627   161 -----YNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEgfIDFIGQVhkTKEQFGQDGPISVHCSAGVGRT 235

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 901694078 1379 GTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVVLSLVST 1433
Cdd:cd14627   236 GVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALEYLGS 290
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 930-1135 7.43e-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: 161.04  E-value: 7.43e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  930 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMItNLVEKGRRKCDQYWPTDGSEEYGSFLVNQKSVQV 1009
Cdd:cd14556     1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVML-NQLDPKDQSCPQYWPDEGSGTYGPIQVEFVSTTI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1010 LAYYTVRNFTLRNTKlkkgsqKGRSSGRLVTQYHYTQWPDMG----VPEYSLPVLAFVRKAAQakRHAVGPVVVHCSAGV 1085
Cdd:cd14556    80 DEDVISRIFRLQNTT------RPQEGYRMVQQFQFLGWPRDRdtppSKRALLKLLSEVEKWQE--QSGEGPIVVHCLNGV 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 901694078 1086 GRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHD 1135
Cdd:cd14556   152 GRSGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 930-1134 1.44e-43

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


Pssm-ID: 350496 [Multi-domain]  Cd Length: 206  Bit Score: 157.63  E-value: 1.44e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  930 YINANYV---DGYNRPKaYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRR-KCDQYWPTD--GSEEYGSFLVN 1003
Cdd:cd17658     1 YINASLVetpASESLPK-FIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTaKCADYFPAEenESREFGRISVT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1004 QKSVQvlayYTVRNFTLRNTKLKKgsQKGRSSGRLVTQYHYTQWPDMGVPEYSLPVLAFVRKAAQAKRHAvGPVVVHCSA 1083
Cdd:cd17658    80 NKKLK----HSQHSITLRVLEVQY--IESEEPPLSVLHIQYPEWPDHGVPKDTRSVRELLKRLYGIPPSA-GPIVVHCSA 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 901694078 1084 GVGRTGTYIVLDSMLQQIQhEG---TVNIFGFLKHIRSQRNYLVQTEEQYVFIH 1134
Cdd:cd17658   153 GIGRTGAYCTIHNTIRRIL-EGdmsAVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 1201-1427 3.69e-43

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


Pssm-ID: 350471 [Multi-domain]  Cd Length: 228  Bit Score: 157.51  E-value: 3.69e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1201 RTSSIIPVERSRVGISSLSGE-GTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAEDE 1279
Cdd:cd14623     1 RVLQIIPYEFNRVIIPVKRGEeNTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1280 FV-YWPNkDEPINCESFKVTLMSEEhKClsneEKLIVQDFILEATQDDYVLEVRHFQCPKWPNPDSPiSKTFELISII-- 1356
Cdd:cd14623    81 CAqYWPS-DGSVSYGDITIELKKEE-EC----ESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIP-SDGKGMINIIaa 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 901694078 1357 --KEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVV 1427
Cdd:cd14623   154 vqKQQQQSGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVV 226
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 1201-1425 9.33e-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: 155.98  E-value: 9.33e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1201 RTSSIIPVERSRVGISSLSG-EGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIpdgQNMAEDE 1279
Cdd:cd14548     1 RYTNILPYDHSRVKLIPINEeEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVML---TQCMEKG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1280 FV----YWPNKDEPINCESFKVTLMSEEHkclsnEEKLIVQDFILEatQDDYVLEVRHFQCPKWPN---PDSPISktfeL 1352
Cdd:cd14548    78 RVkcdhYWPFDQDPVYYGDITVTMLSESV-----LPDWTIREFKLE--RGDEVRSVRQFHFTAWPDhgvPEAPDS----L 146

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 901694078 1353 ISIIK---EEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYK 1425
Cdd:cd14548   147 LRFVRlvrDYIKQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLHQ 222
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
873-1133 1.37e-42

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 157.56  E-value: 1.37e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  873 KEFYQEVQSCTADLGITADSSNHPDN---KHKNRYVNIVAYDHsrvklTQLAEKDGkltdYINANYVDGYNrPKAYIAAQ 949
Cdd:COG5599    14 EKINSRLSTLTNELAPSHNDPQYLQNingSPLNRFRDIQPYKE-----TALRANLG----YLNANYIQVIG-NHRYIATQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  950 GPLKSTAEDFWRMIWEHNVEVIVMITNLVE--KGRRKCDQYWPTDGseEYGSFLVNQKSVQVlaYYTVRNFTLRNTKLK- 1026
Cdd:COG5599    84 YPLEEQLEDFFQMLFDNNTPVLVVLASDDEisKPKVKMPVYFRQDG--EYGKYEVSSELTES--IQLRDGIEARTYVLTi 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1027 KGS-QKGRSsgrlVTQYHYTQWPDMGVP--EYSLPVLAFVRKAAQAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQ- 1102
Cdd:COG5599   160 KGTgQKKIE----IPVLHVKNWPDHGAIsaEALKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINa 235

                         250       260       270
                  ....*....|....*....|....*....|...
gi 901694078 1103 -HEGTVNIFGFLKHIRSQRNY-LVQTEEQYVFI 1133
Cdd:COG5599   236 lVQITLSVEEIVIDMRTSRNGgMVQTSEQLDVL 268
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 1225-1427 9.48e-42

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


Pssm-ID: 350400 [Multi-domain]  Cd Length: 202  Bit Score: 152.42  E-value: 9.48e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1225 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAEDE-FVYWPNkDEPINCESFKVTLMSEE 1303
Cdd:cd14552     1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKcAQYWPE-DGSVSSGDITVELKDQT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1304 hkclsNEEKLIVQDFILEATQDDYVLEVRHFQCPKWPNPDSPiSKTFELISII----KEEAANRDGPMIVHDEHGGVTAG 1379
Cdd:cd14552    80 -----DYEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIP-DNGKGMIDLIaavqKQQQQSGNHPITVHCSAGAGRTG 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 901694078 1380 TFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVV 1427
Cdd:cd14552   154 TFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 1225-1424 1.16e-41

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


Pssm-ID: 350404 [Multi-domain]  Cd Length: 201  Bit Score: 152.18  E-value: 1.16e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1225 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAEDEFVYWPNKdepincESFKVTLMSEEH 1304
Cdd:cd14556     1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDQSCPQYWPDE------GSGTYGPIQVEF 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1305 KCLSNEEKLIVQDFILEAT---QDDYVLeVRHFQCPKWP-NPDSPISKT--FELISII-KEEAANRDGPMIVHDEHGGVT 1377
Cdd:cd14556    75 VSTTIDEDVISRIFRLQNTtrpQEGYRM-VQQFQFLGWPrDRDTPPSKRalLKLLSEVeKWQEQSGEGPIVVHCLNGVGR 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 901694078 1378 AGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLY 1424
Cdd:cd14556   154 SGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCY 200
alpha_CA_VI cd03125
Carbonic anhydrase alpha, isozyme VI. Carbonic anhydrases (CAs) are zinc-containing enzymes ...
 45-300 7.01e-41

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


Pssm-ID: 239399  Cd Length: 249  Bit Score: 151.48  E-value: 7.01e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078   45 NQKNWGKKYPICNSPKQSPINIDEDLTQVNVNLKKLKFQGWEKASLENTFIHNtGKTVEINLTNDYYLSGGLSeKVFKAS 124
Cdd:cd03125     1 DESHWPEKYPACGGKRQSPIDIQRREVRFNPSLLQLELVGYEKEQGEFTMTNN-GHTVQIDLPPTMSITTGDG-TVYTAV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  125 KITFHWGKCNVSSEGSEHSLEGQKFPLEMQVYCFDADrFSSFEEAVKGKGRLRALSILFEVG-VEENLDYKAIIDGTESV 203
Cdd:cd03125    79 QMHFHWGGRDSEISGSEHTIDGMRYVAELHIVHYNSK-YKSYEEAKDKPDGLAVLAFLYKVGhYAENTYYSDFISKLAKI 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  204 SRFGKQAALDPFVLQNLLPNSTDKYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQlavfceVLTMQQSgyvmLMDY--- 280
Cdd:cd03125   158 KYAGQTTTLTSLDVRDMLPENLHHYYTYQGSLTTPPCTENVLWFVFDDPVTLSKTQ------IVKLENT----LMDHhnk 227

                         250       260
                  ....*....|....*....|.
gi 901694078  281 -LQNNFREQQYKFSRQVFSSY 300
Cdd:cd03125   228 tIRNDYRRTQPLNHRVVEANF 248
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 1225-1424 1.48e-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: 149.08  E-value: 1.48e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1225 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPD-GQNMAEDEFVYWPNKDEpiNCESFKVTLMSEE 1303
Cdd:cd14558     1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTElKEGDQEQCAQYWGDEKK--TYGDIEVELKDTE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1304 hkclsNEEKLIVQDFILEATQDDYVLEVRHFQCPKWpNPDSPISKTFELISIIKE---------EAANRDGPMIVHDEHG 1374
Cdd:cd14558    79 -----KSPTYTVRVFEITHLKRKDSRTVYQYQYHKW-KGEELPEKPKDLVDMIKSikqklpyknSKHGRSVPIVVHCSDG 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 901694078 1375 GVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLY 1424
Cdd:cd14558   153 SSRTGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202
alpha_CA_IX cd03150
Carbonic anhydrase alpha, isozyme IX. Carbonic anhydrases (CAs) are zinc-containing enzymes ...
 45-300 1.60e-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: 150.49  E-value: 1.60e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078   45 NQKNWGKKYPICNSPKQSPINIDEDLTQVNVNLKKLKFQGWEKASLENTFIHNTGKTVEINLTNDYYLSGGLsEKVFKAS 124
Cdd:cd03150     1 GQPPWPSVSPACAGRFQSPVDIRPHLVAFCPALRPLELLGFDLPPSPSLRLLNNGHTVQLSLPSGLRMALGP-GQEYRAL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  125 KITFHWGKCNVSseGSEHSLEGQKFPLEMQVYCFDAdRFSSFEEAVKGKGRLRALSILFEVGVEENLDYKAIIDGTESVS 204
Cdd:cd03150    80 QLHLHWGAAGRP--GSEHTVDGHRFPAEIHVVHLST-AFANLDEALGRPGGLAVLAAFLAEGLHENSAYEQLLSRLSEIS 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  205 RFGKQAALDPFVLQNLLPNSTDKYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLAVFCEVLTMQQSgyvmlmDYLQNN 284
Cdd:cd03150   157 EEESETVVPGLDVSALLPSDLSRYFRYEGSLTTPPCAQGVIWTVFNQTVRLSAKQLHTLSDSLWGPHD------SRLQLN 230

                         250
                  ....*....|....*.
gi 901694078  285 FREQQYKFSRQVFSSY 300
Cdd:cd03150   231 FRATQPLNGRKIEASF 246
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 930-1139 5.48e-40

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


Pssm-ID: 350446 [Multi-domain]  Cd Length: 220  Bit Score: 147.81  E-value: 5.48e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  930 YINANYVDGYNRPKA--YIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPTDGSEE----YGSFLVN 1003
Cdd:cd14598     1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRLGSRHntvtYGRFKIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1004 QKSVQVLAYYTVRNFTLRNtkLKKGSQkgrssgRLVTQYHYTQWPDMGVPEYSLPVLAFVRKAAQAKRHAVG-------- 1075
Cdd:cd14598    81 TRFRTDSGCYATTGLKIKH--LLTGQE------RTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHTNStidpkspn 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 901694078 1076 -PVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVE 1139
Cdd:cd14598   153 pPVLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQ 217
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1039-1139 5.18e-39

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 140.57  E-value: 5.18e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078   1039 VTQYHYTQWPDMGVPEYSLPVLAFVR--KAAQAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHE-GTVNIFGFLKH 1115
Cdd:smart00404    2 VKHYHYTGWPDHGVPESPDSILELLRavKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVKE 81

                            90       100
                    ....*....|....*....|....
gi 901694078   1116 IRSQRNYLVQTEEQYVFIHDTLVE 1139
Cdd:smart00404   82 LRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 1039-1139 5.18e-39

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


Pssm-ID: 214469 [Multi-domain]  Cd Length: 105  Bit Score: 140.57  E-value: 5.18e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078   1039 VTQYHYTQWPDMGVPEYSLPVLAFVR--KAAQAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHE-GTVNIFGFLKH 1115
Cdd:smart00012    2 VKHYHYTGWPDHGVPESPDSILELLRavKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVKE 81

                            90       100
                    ....*....|....*....|....
gi 901694078   1116 IRSQRNYLVQTEEQYVFIHDTLVE 1139
Cdd:smart00012   82 LRSQRPGMVQTEEQYLFLYRALLE 105
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 1200-1428 9.81e-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: 144.70  E-value: 9.81e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1200 NRTSSIIPVERSRVGISSLSGE-GTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIP----DGQN 1274
Cdd:cd14618     1 NRYPHVLPYDHSRVRLSQLGGEpHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTvgmeNGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1275 MAEDefvYWPNKDEPINCESFKVTLMSEEhkclsNEEKLIVQDFILEATQDDYVLEVRHFQCPKWPN---PDSPISkTFE 1351
Cdd:cd14618    81 LCDH---YWPSESTPVSYGHITVHLLAQS-----SEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDhgiPESTSS-LMA 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 901694078 1352 LISIIKEE--AANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVVL 1428
Cdd:cd14618   152 FRELVREHvqATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 1224-1427 4.66e-37

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


Pssm-ID: 350470 [Multi-domain]  Cd Length: 205  Bit Score: 138.98  E-value: 4.66e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1224 DYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAEDE-FVYWPNKDEPINCEsfkvtlMSE 1302
Cdd:cd14622     1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKcVQYWPSEGSVTHGE------ITI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1303 EHKCLSNEEKLIVQDFILEATQDDYVLEVRHFQCPKWPNPDSPiSKTFELISII----KEEAANRDGPMIVHDEHGGVTA 1378
Cdd:cd14622    75 EIKNDTLLETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIP-AEGKGMIDLIaavqKQQQQTGNHPIVVHCSAGAGRT 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 901694078 1379 GTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVV 1427
Cdd:cd14622   154 GTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 1200-1428 5.45e-37

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


Pssm-ID: 350463 [Multi-domain]  Cd Length: 229  Bit Score: 139.57  E-value: 5.45e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1200 NRTSSIIPVERSRVGISSLSGEGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVM----IPDGQNM 1275
Cdd:cd14615     1 NRYNNVLPYDISRVKLSVQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMltkcVEQGRTK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1276 AEDefvYWPNKdEPINCESFKVTLMSEehkclSNEEKLIVQDFILEATQDDYVLEVRHFQCPKWpnPDSPISKTFELI-- 1353
Cdd:cd14615    81 CEE---YWPSK-QKKDYGDITVTMTSE-----IVLPEWTIRDFTVKNAQTNESRTVRHFHFTSW--PDHGVPETTDLLin 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 901694078 1354 --SIIKE--EAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVVL 1428
Cdd:cd14615   150 frHLVREymKQNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCAL 228
alpha_CA_I_II_III_XIII cd03119
Carbonic anhydrase alpha, isozymes I, II, and III and XIII. Carbonic anhydrases (CAs) are ...
 38-300 7.36e-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: 140.27  E-value: 7.36e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078   38 WSYTGALNQKNWGKKYPICNSPKQSPINIDEDLTQVNVNLKKLKFQgWEKASLENtfIHNTGKTVEINLTNDY---YLSG 114
Cdd:cd03119     5 WGYDSHNGPEHWHELFPIAKGDRQSPIDIKTKDAKHDPSLKPLSVS-YDPATAKT--ILNNGHSFNVEFDDTDdrsVLRG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  115 GLSEKVFKASKITFHWGKCNvsSEGSEHSLEGQKFPLEMQVYCFDAdRFSSFEEAVKGKGRLRALSILFEVGvEENLDYK 194
Cdd:cd03119    82 GPLTGSYRLRQFHFHWGSSD--DHGSEHTVDGVKYAAELHLVHWNS-KYGSFGEAAKQPDGLAVVGVFLKVG-EANPELQ 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  195 AIIDGTESVSRFGKQAALDPFVLQNLLPNSTDkYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLAVFCEVLTMQQSGY 274
Cdd:cd03119   158 KVLDALDSIKTKGKQAPFTNFDPSCLLPASLD-YWTYPGSLTTPPLLECVTWIVLKEPISVSSEQMAKFRSLLFNAEGEP 236

                         250       260
                  ....*....|....*....|....*.
gi 901694078  275 VMLMdylQNNFREQQYKFSRQVFSSY 300
Cdd:cd03119   237 PCPM---VDNWRPPQPLKGRKVRASF 259
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 1194-1432 2.83e-36

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


Pssm-ID: 350401 [Multi-domain]  Cd Length: 238  Bit Score: 137.91  E-value: 2.83e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1194 QCNREKNRTSSIIPVERSRVGISSLSG-EGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIpdg 1272
Cdd:cd14553     1 EVNKPKNRYANVIAYDHSRVILQPIEGvPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMM--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1273 QNMAEDEFV----YWPNKDEPiNCESFKVTLMSEEHkcLSNeekLIVQDFILEATQDDYVLEVRHFQCPKWPN---PDSP 1345
Cdd:cd14553    78 TKLEERSRVkcdqYWPTRGTE-TYGLIQVTLLDTVE--LAT---YTVRTFALHKNGSSEKREVRQFQFTAWPDhgvPEHP 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1346 ISkTFELISIIKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVY-QVAKM---INLMrpgVFTDiEQYQ 1421
Cdd:cd14553   152 TP-FLAFLRRVKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYgHVTCLraqRNYM---VQTE-DQYI 226

                         250
                  ....*....|.
gi 901694078 1422 FLYKVVLSLVS 1432
Cdd:cd14553   227 FIHDALLEAVT 237
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 1173-1427 4.25e-36

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


Pssm-ID: 350451 [Multi-domain]  Cd Length: 266  Bit Score: 138.42  E-value: 4.25e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1173 KQFQLL-SQSNILQSDYSTAL----KQCNREKNRTSSIIPVERSRVGISSLSGEG-TDYINASYIMGYYQSNEFIITQHP 1246
Cdd:cd14603     2 GEFSEIrACSAAFKADYVCSTvaggRKENVKKNRYKDILPYDQTRVILSLLQEEGhSDYINANFIKGVDGSRAYIATQGP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1247 LLHTIKDFWRMIWDHNAQLVVM----IPDGQNMAEdefVYWPNKDEPINCESFKVTLMSEEHkclSNEEKLIVQdfiLEA 1322
Cdd:cd14603    82 LSHTVLDFWRMIWQYGVKVILMacreIEMGKKKCE---RYWAQEQEPLQTGPFTITLVKEKR---LNEEVILRT---LKV 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1323 TQDDYVLEVRHFQCPKWPN---PDSPiSKTFELISIIKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDV 1399
Cdd:cd14603   153 TFQKESRSVSHFQYMAWPDhgiPDSP-DCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPD 231

                         250       260       270
                  ....*....|....*....|....*....|.
gi 901694078 1400 YQVAKMINLM---RPGVFTDIEQYQFLYKVV 1427
Cdd:cd14603   232 FSIFDVVLEMrkqRPAAVQTEEQYEFLYHTV 262
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 1200-1431 4.86e-36

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


Pssm-ID: 350467 [Multi-domain]  Cd Length: 233  Bit Score: 136.94  E-value: 4.86e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1200 NRTSSIIPVERSRVGISSLSGEGT-DYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIpdgQNMAED 1278
Cdd:cd14619     1 NRFRNVLPYDWSRVPLKPIHEEPGsDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVML---TNCMEA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1279 EFV----YWPNKDEPINCESFKVTLMSEEhkclsNEEKLIVQDFILEATQDDYVLEVRHFQCPKWPNPDSPiSKTFELIS 1354
Cdd:cd14619    78 GRVkcehYWPLDYTPCTYGHLRVTVVSEE-----VMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVP-SSTDTLLA 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1355 ---IIKE--EAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVVLS 1429
Cdd:cd14619   152 frrLLRQwlDQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILD 231


                  ..
gi 901694078 1430 LV 1431
Cdd:cd14619   232 FL 233
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 1196-1428 3.15e-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: 135.02  E-value: 3.15e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1196 NREKNRTSSIIPVERSRVGISSLSG-EGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIP---D 1271
Cdd:cd14614    12 NRCKNRYTNILPYDFSRVKLVSMHEeEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTqcnE 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1272 GQNMAEDEfvYWPNKDEPINCESFKVTLMSEEhkclsNEEKLIVQDFILeaTQDDYVLEVRHFQCPKWPNPDSPISKTFE 1351
Cdd:cd14614    92 KRRVKCDH--YWPFTEEPVAYGDITVEMLSEE-----EQPDWAIREFRV--SYADEVQDVMHFNYTAWPDHGVPTANAAE 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1352 ----LISIIKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVV 1427
Cdd:cd14614   163 silqFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 242


                  .
gi 901694078 1428 L 1428
Cdd:cd14614   243 Q 243
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 930-1133 5.96e-35

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


Pssm-ID: 350398 [Multi-domain]  Cd Length: 200  Bit Score: 132.83  E-value: 5.96e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  930 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGrrKCDQYWPTDG----SEEYGSFLVNQK 1005
Cdd:cd14550     1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNE--DEPIYWPTKEkpleCETFKVTLSGED 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1006 SVQVLAY--YTVRNFTLRNTK----LKkgsqkgrssgrlVTQYHYTQWPDMGVPEYSlpVLAFVRKAAQAKRHAVGPVVV 1079
Cdd:cd14550    79 HSCLSNEirLIVRDFILESTQddyvLE------------VRQFQCPSWPNPCSPIHT--VFELINTVQEWAQQRDGPIVV 144

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 901694078 1080 HCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFI 1133
Cdd:cd14550   145 HDRYGGVQAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFL 198
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 1200-1424 1.09e-34

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


Pssm-ID: 350395 [Multi-domain]  Cd Length: 224  Bit Score: 132.91  E-value: 1.09e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1200 NRTSSIIPVERSRVGISSL-SGEGTDYINASYIMGY-YQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAE 1277
Cdd:cd14547     1 NRYKTILPNEHSRVCLPSVdDDPLSSYINANYIRGYdGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEAKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1278 DEFVYWPNKdEPINCESFKVTLMSEEHKclsneEKLIVQDFILEatqddYVLEVR---HFQCPKWPNPDSPiSKTFELIS 1354
Cdd:cd14547    81 KCAQYWPEE-ENETYGDFEVTVQSVKET-----DGYTVRKLTLK-----YGGEKRylkHYWYTSWPDHKTP-EAAQPLLS 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 901694078 1355 IIKE-----EAANRDGPMIVHDEHG-GVTaGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLY 1424
Cdd:cd14547   149 LVQEveearQTEPHRGPIVVHCSAGiGRT-GCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVH 223
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 1191-1425 3.18e-34

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


Pssm-ID: 350391 [Multi-domain]  Cd Length: 271  Bit Score: 133.26  E-value: 3.18e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1191 ALKQCNREKNRTSSIIPVERSRVGISSLSG-EGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMI 1269
Cdd:cd14543    24 SLAPANQEKNRYGDVLCLDQSRVKLPKRNGdERTDYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKVLVIVMT 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1270 PD---------GQnmaedefvYWPNKDEpiNCESF-KVTLmseEHKCLSNEEKLIVQDFILEATQDDYVLEVRHFQCPKW 1339
Cdd:cd14543   104 TRvvergrvkcGQ--------YWPLEEG--SSLRYgDLTV---TNLSVENKEHYKKTTLEIHNTETDESRQVTHFQFTSW 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1340 PN---PDSPISKTFELISIIKEEAAN------------RDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAK 1404
Cdd:cd14543   171 PDfgvPSSAAALLDFLGEVRQQQALAvkamgdrwkghpPGPPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQTVR 250

                         250       260
                  ....*....|....*....|.
gi 901694078 1405 MINLMRPGVFTDIEQYQFLYK 1425
Cdd:cd14543   251 RMRTQRAFSIQTPDQYYFCYK 271
alpha_CA_V cd03118
Carbonic anhydrase alpha, CA isozyme V_like subgroup. Carbonic anhydrases (CAs) are ...
 60-300 4.05e-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: 131.50  E-value: 4.05e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078   60 KQSPINIDEDLTQVNVNLKKLKFQgWEKASLEntFIHNTGKTVEINL---TNDYYLSGGLSEKVFKASKITFHWGKCNvs 136
Cdd:cd03118     3 RQSPINIQWRDSVYDPQLAPLRVS-YDPATCL--YIWNNGYSFQVEFddsTDKSGISGGPLENHYRLKQFHFHWGANN-- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  137 SEGSEHSLEGQKFPLEMQVYCFDADRFSSFEEAVKGKGRLRALSILFEVGVE-ENLdyKAIIDGTESVSRFGKQAALDPF 215
Cdd:cd03118    78 EWGSEHTVDGHTYPAELHLVHWNSVKYENFEEAVMEENGLAVIGVFLKLGAHhEGL--QKLVDALPEVRHKDTVVEFNPF 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  216 VLQNLLPNSTDkYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLAVFCEVLTmqqSGYVMLMDYLQNNFREQQYKFSRQ 295
Cdd:cd03118   156 DPSCLLPACRD-YWTYPGSLTTPPLTESVTWIIQKQPIEVSPSQLSVFRTLLF---TSRGEEEKVMVNNFRPLQPLMNRK 231


                  ....*
gi 901694078  296 VFSSY 300
Cdd:cd03118   232 VRSSF 236
Cah COG3338
Carbonic anhydrase [Inorganic ion transport and metabolism];
38-263 4.01e-33

Carbonic anhydrase [Inorganic ion transport and metabolism];


Pssm-ID: 442567 [Multi-domain]  Cd Length: 247  Bit Score: 129.23  E-value: 4.01e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078   38 WSYTGALNQKNWGK---KYPICNS-PKQSPINIDedlTQVNVNLKKLKFQgWEKASLEntfIHNTGKTVEINLTNDYYLS 113
Cdd:COG3338    28 WSYEGETGPEHWGElspEFATCATgKNQSPIDIR---TAIKADLPPLKFD-YKPTPLE---IVNNGHTIQVNVDPGSTLT 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  114 ggLSEKVFKASKITFHwgkcnvssEGSEHSLEGQKFPLEMQ-VYcfdadrfssfeeaVKGKGRLRALSILFEVGvEENLD 192
Cdd:COG3338   101 --VDGKRYELKQFHFH--------TPSEHTINGKSYPMEAHlVH-------------KDADGELAVVGVLFEEG-AENPA 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 901694078  193 YKAIID------GTESVSrfgkQAALDPfvlQNLLPNSTDkYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLAVF 263
Cdd:COG3338   157 LAKLWAnlpleaGEEVAL----DATIDL---NDLLPEDRS-YYRYSGSLTTPPCSEGVLWIVLKQPITVSAEQIEAF 225
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 1188-1428 6.38e-33

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


Pssm-ID: 350481 [Multi-domain]  Cd Length: 273  Bit Score: 129.39  E-value: 6.38e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1188 YSTALKQCNREKNRTSSIIPVERSRVGISSLSGE-GTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLV 1266
Cdd:cd14633    32 WDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGEtSSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASI 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1267 VMIpdgQNMAEDEFV----YWPNKDEPIncESFKVTLMseEHKCLSneeKLIVQDFILEATQDDYVLEVRHFQCPKWPNP 1342
Cdd:cd14633   112 IMV---TNLVEVGRVkcckYWPDDTEIY--KDIKVTLI--ETELLA---EYVIRTFAVEKRGVHEIREIRQFHFTGWPDH 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1343 DSPISKT--FELISIIKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQY 1420
Cdd:cd14633   182 GVPYHATglLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQY 261


                  ....*...
gi 901694078 1421 QFLYKVVL 1428
Cdd:cd14633   262 VFIHDAIL 269
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 1199-1424 5.22e-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: 125.72  E-value: 5.22e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1199 KNRTSSIIPVERSRVGISSL--SGEGTDYINASYIMGYY-QSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNM 1275
Cdd:cd14612    18 KDRYKTILPNPQSRVCLRRAgsQEEEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMITKLKEK 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1276 AEDEFVYWPNKDEPINCESFKVTLMSEehkClsneEKLIVQDFILEATQDDYvlEVRHFQCPKWPNPDSPISKT--FELI 1353
Cdd:cd14612    98 KEKCVHYWPEKEGTYGRFEIRVQDMKE---C----DGYTIRDLTIQLEEESR--SVKHYWFSSWPDHQTPESAGplLRLV 168

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 901694078 1354 SIIKE--EAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLY 1424
Cdd:cd14612   169 AEVEEsrQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLH 241
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 1199-1430 1.03e-31

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: 124.57  E-value: 1.03e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1199 KNRTSSIIPVERSRVGISSL-SGEGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAE 1277
Cdd:cd14602     1 KNRYKDILPYDHSRVELSLItSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1278 DEFV-YWPN-KDEPINCESFKVTLMSEEHKclsneEKLIVQdfILEATQDDYVLEVRHFQCPKWPNPDSP--ISKTFELI 1353
Cdd:cd14602    81 KKCErYWAEpGEMQLEFGPFSVTCEAEKRK-----SDYIIR--TLKVKFNSETRTIYQFHYKNWPDHDVPssIDPILELI 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1354 SIIKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEK----ENaMDVYQVAKMINLMRPGVFTDIEQYQFLYKVVLS 1429
Cdd:cd14602   154 WDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDgiipEN-FSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIE 232


                  .
gi 901694078 1430 L 1430
Cdd:cd14602   233 L 233
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 1196-1428 2.00e-31

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


Pssm-ID: 350478 [Multi-domain]  Cd Length: 237  Bit Score: 123.98  E-value: 2.00e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1196 NREKNRTSSIIPVERSRVGISSLSGE-GTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQN 1274
Cdd:cd14630     3 NRNKNRYGNIISYDHSRVRLQLLDGDpHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1275 MAEDEFV-YWPNKDEPINceSFKVTLMSEEHKClsneeKLIVQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKT--FE 1351
Cdd:cd14630    83 VGRVKCVrYWPDDTEVYG--DIKVTLIETEPLA-----EYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATglLG 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 901694078 1352 LISIIKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVVL 1428
Cdd:cd14630   156 FVRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAIL 232
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 1199-1430 4.32e-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: 123.43  E-value: 4.32e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1199 KNRTSSIIPVERSRVGISSLSGEG--TDYINASYIMGY-YQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNM 1275
Cdd:cd14613    28 KNRYKTILPNPHSRVCLTSPDQDDplSSYINANYIRGYgGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEM 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1276 AEDEFVYWPnkDEPINCESFKVTLMSEEHkclsnEEKLIVQDFILEATQDDYVLevRHFQCPKWPNPDSPiSKTFELISI 1355
Cdd:cd14613   108 NEKCTEYWP--EEQVTYEGIEITVKQVIH-----ADDYRLRLITLKSGGEERGL--KHYWYTSWPDQKTP-DNAPPLLQL 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1356 IKE------EAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKvVLS 1429
Cdd:cd14613   178 VQEveearqQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVHH-VLS 256


                  .
gi 901694078 1430 L 1430
Cdd:cd14613   257 L 257
alpha_CA_VII cd03149
Carbonic anhydrase alpha, CA isozyme VII_like subgroup. Carbonic anhydrases (CAs) are ...
 60-300 1.89e-30

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


Pssm-ID: 239402  Cd Length: 236  Bit Score: 121.10  E-value: 1.89e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078   60 KQSPINIDEDLTQVNVNLKKLKFQgWEKASLENtfIHNTGKTVEINLtNDY----YLSGGLSEKVFKASKITFHWGKCNv 135
Cdd:cd03149     3 RQSPIDIVSSEAVYDPKLKPLSLS-YDPCTSLS--ISNNGHSVMVEF-DDSddktVITGGPLENPYRLKQFHFHWGAKH- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  136 sSEGSEHSLEGQKFPLEMQVYCFDADRFSSFEEAVKGKGRLRALSILFEVGvEENLDYKAIIDGTESVSRFGKQAALDPF 215
Cdd:cd03149    78 -GSGSEHTVDGKTFPSELHLVHWNAKKYKSFGEAAAAPDGLAVLGVFLETG-DEHPGLNRLTDALYMVRFKGTKAQFLDF 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  216 VLQNLLPNSTDkYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLAVFCEVLTMQQSGYVMLMdylQNNFREQQYKFSRQ 295
Cdd:cd03149   156 NPKCLLPKSLD-YWTYPGSLTTPPLNESVTWIVLKEPIPVSEKQMGKFRELLFTSEEDQRNHM---VNNFRPPQPLKGRT 231


                  ....*
gi 901694078  296 VFSSY 300
Cdd:cd03149   232 VRASF 236
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 1225-1428 1.90e-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: 120.01  E-value: 1.90e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1225 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIP--DGQNMAEDEFVYWPnkdEPINCesfKVTLMSE 1302
Cdd:cd14637     1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNqlNQSNSAWPCLQYWP---EPGLQ---QYGPMEV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1303 EHKCLSNEEKLIVQDFILE--ATQDDYVLEVRHFQCPKWP----NPDSPISKTFELISIIKEEAANRDGPMIVHDEHGGV 1376
Cdd:cd14637    75 EFVSGSADEDIVTRLFRVQniTRLQEGHLMVRHFQFLRWSayrdTPDSKKAFLHLLASVEKWQRESGEGRTVVHCLNGGG 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 901694078 1377 TAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVVL 1428
Cdd:cd14637   155 RSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIAL 206
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 930-1139 2.28e-30

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


Pssm-ID: 350482 [Multi-domain]  Cd Length: 206  Bit Score: 119.74  E-value: 2.28e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  930 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLveKGRRKCDQYWPTDGSEEYGSFLVNQKSVQV 1009
Cdd:cd14634     1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEM--DAAQLCMQYWPEKTSCCYGPIQVEFVSADI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1010 LAYYTVRNFTLRNTKlkkgsqKGRSSGRLVTQYHYTQWPDM-GVPEYSLPVLAFVRKAAQAKRH---AVGPVVVHCSAGV 1085
Cdd:cd14634    79 DEDIISRIFRICNMA------RPQDGYRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLEKWQEQydgREGRTVVHCLNGG 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 901694078 1086 GRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVE 1139
Cdd:cd14634   153 GRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 1225-1424 4.54e-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: 119.28  E-value: 4.54e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1225 YINASYI-MGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMI-PDGQNMAEDEFVYWPNKDEPINCESFKVTLMSE 1302
Cdd:cd18533     1 YINASYItLPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLtPLVENGREKCDQYWPSGEYEGEYGDLTVELVSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1303 EHKclsNEEKLIVQDFILeATQDDYVLEVRHFQCPKWPN---PDSPISkTFELISIIKE--EAANRDGPMIVHDEHG-GV 1376
Cdd:cd18533    81 EEN---DDGGFIVREFEL-SKEDGKVKKVYHIQYKSWPDfgvPDSPED-LLTLIKLKRElnDSASLDPPIIVHCSAGvGR 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 901694078 1377 TaGTFCALTTLMHQLEK------ENAMDVYQVAKMINLM---RPGVFTDIEQYQFLY 1424
Cdd:cd18533   156 T-GTFIALDSLLDELKRglsdsqDLEDSEDPVYEIVNQLrkqRMSMVQTLRQYIFLY 211
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 1188-1430 1.18e-29

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


Pssm-ID: 350452 [Multi-domain]  Cd Length: 297  Bit Score: 120.81  E-value: 1.18e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1188 YSTAL--KQCNREKNRTSSIIPVERSRVGIS-SLSGEGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQ 1264
Cdd:cd14604    47 YPTATgeKEENVKKNRYKDILPFDHSRVKLTlKTSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVA 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1265 LVVMIPDGQNMAEDEFV-YWPN-KDEPINCESFKVTLMSEEHKclsneEKLIVQDFILEATQDDYVLEVRHFQcpKWPNP 1342
Cdd:cd14604   127 IIVMACREFEMGRKKCErYWPLyGEEPMTFGPFRISCEAEQAR-----TDYFIRTLLLEFQNETRRLYQFHYV--NWPDH 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1343 DSPIS--KTFELISIIKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDI--- 1417
Cdd:cd14604   200 DVPSSfdSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVqtk 279

                         250
                  ....*....|...
gi 901694078 1418 EQYQFLYKVVLSL 1430
Cdd:cd14604   280 EQYELVHRAIAQL 292
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 1194-1432 1.21e-29

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


Pssm-ID: 350474 [Multi-domain]  Cd Length: 276  Bit Score: 120.14  E-value: 1.21e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1194 QCNREKNRTSSIIPVERSRVGISSLSG-EGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIpdg 1272
Cdd:cd14626    39 EVNKPKNRYANVIAYDHSRVILTSVDGvPGSDYINANYIDGYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMM--- 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1273 QNMAEDEFV----YWPNKDEPiNCESFKVTLMSEEHKCLSNeekliVQDFILEATQDDYVLEVRHFQCPKWPNPDSPISK 1348
Cdd:cd14626   116 TRLEEKSRVkcdqYWPIRGTE-TYGMIQVTLLDTVELATYS-----VRTFALYKNGSSEKREVRQFQFMAWPDHGVPEYP 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1349 TFELISIIKEEAAN--RDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKV 1426
Cdd:cd14626   190 TPILAFLRRVKACNppDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEA 269


                  ....*.
gi 901694078 1427 VLSLVS 1432
Cdd:cd14626   270 LLEAAT 275
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 1200-1425 2.45e-29

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


Pssm-ID: 350465 [Multi-domain]  Cd Length: 228  Bit Score: 117.71  E-value: 2.45e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1200 NRTSSIIPVERSRVGISSLSGEG-TDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPD--GQNMA 1276
Cdd:cd14617     1 NRYNNILPYDSTRVKLSNVDDDPcSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQcvEKGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1277 EDEFvYWPNKDEPINCESFKVTLMSEehkclSNEEKLIVQDF-ILEATQDDYVLEVRHFQCPKWPNPDSPiSKTFELISI 1355
Cdd:cd14617    81 KCDH-YWPADQDSLYYGDLIVQMLSE-----SVLPEWTIREFkICSEEQLDAPRLVRHFHYTVWPDHGVP-ETTQSLIQF 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 901694078 1356 IK--EEAANRD---GPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYK 1425
Cdd:cd14617   154 VRtvRDYINRTpgsGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228
alpha_CA_prokaryotic_like cd03124
Carbonic anhydrase alpha, prokaryotic-like subfamily. Carbonic anhydrases (CAs) are ...
 45-263 2.95e-29

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


Pssm-ID: 239398 [Multi-domain]  Cd Length: 216  Bit Score: 116.99  E-value: 2.95e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078   45 NQKNWG---KKYPICNS-PKQSPINIDEDLTQVNVnLKKLKFQgWEKASLEntfIHNTGKTVEINLTNDyylSGGLS--E 118
Cdd:cd03124     1 GPEHWGnldPEFALCATgKNQSPIDITTKAVVSDK-LPPLNYN-YKPTSAT---LVNNGHTIQVNFEGN---GGTLTidG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  119 KVFKASKITFHwgkcnvssEGSEHSLEGQKFPLEMQ-VYcfdadrfssfeeaVKGKGRLRALSILFEVGvEENLDYKAII 197
Cdd:cd03124    73 ETYQLLQFHFH--------SPSEHLINGKRYPLEAHlVH-------------KSKDGQLAVVAVLFEEG-KENPFLKKIL 130

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 901694078  198 DGTESvsRFGKQAALDPFV-LQNLLPNSTDkYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLAVF 263
Cdd:cd03124   131 DNMPK--KEGTEVNLPAILdPNELLPESRS-YYRYEGSLTTPPCSEGVRWIVLKQPITISKEQLAKF 194
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 1225-1428 3.18e-29

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


Pssm-ID: 350482 [Multi-domain]  Cd Length: 206  Bit Score: 116.66  E-value: 3.18e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1225 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDgQNMAEDEFVYWPNKDE----PINCESFKVTLm 1300
Cdd:cd14634     1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNE-MDAAQLCMQYWPEKTSccygPIQVEFVSADI- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1301 seehkclsnEEKLIVQDFI---LEATQDDYVLeVRHFQCPKWPN-PDSPISKTfELISIIK------EEAANRDGPMIVH 1370
Cdd:cd14634    79 ---------DEDIISRIFRicnMARPQDGYRI-VQHLQYIGWPAyRDTPPSKR-SILKVVRrlekwqEQYDGREGRTVVH 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 901694078 1371 DEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVVL 1428
Cdd:cd14634   148 CLNGGGRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVAL 205
alpha_CARP_X_XI_like cd03121
Carbonic anhydrase alpha related protein: groups X, XI and related proteins. This subgroup ...
 49-296 3.49e-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: 117.90  E-value: 3.49e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078   49 WGKKYP---ICNSPK-QSPINIDEDLTQVNVNLKKLKFQGWEKASLEntfIHNTGKTVEINLTNDY--YLSGGLSEKVFK 122
Cdd:cd03121     5 WGLVNSawnLCSKGRrQSPVDIEPSRLLFDPFLTPLRIDTGRKVSGT---FYNTGRHVSFRPDKDPvvNISGGPLSYRYR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  123 ASKITFHWGKCNvsSEGSEHSLEGQKFPLEMQVYCFDADRFSSFEEAVKGKGRLRALSILFEVGVEENLDYKAIIDGTES 202
Cdd:cd03121    82 LEEIRLHFGRED--EQGSEHTVNGQAFPGEVQLIHYNSELYPNFSEASKSPNGLVIVSLFVKIGETSNPELRRLTNRDTI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  203 VS-RFGKQAA-LDPFVLQNLLPNsTDKYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLAvfcEVLTMQQSGYVMLMDY 280
Cdd:cd03121   160 TSiRYKGDAYfLQDLSIELLLPE-TDHYITYEGSLTSPGCHETVTWIILNKPIYITKEQMH---SLRLLSQNSPSQEKAP 235

                         250
                  ....*....|....*.
gi 901694078  281 LQNNFREQQYKFSRQV 296
Cdd:cd03121   236 MSPNFRPVQPLNNRPV 251
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 1200-1425 4.44e-29

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


Pssm-ID: 350464 [Multi-domain]  Cd Length: 224  Bit Score: 116.54  E-value: 4.44e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1200 NRTSSIIPVERSRVGISSLSG-EGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPD----GQN 1274
Cdd:cd14616     1 NRFPNIKPYNNNRVKLIADAGvPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQcfekGRI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1275 MAEDefvYWPNKDEPINCES-FKVTLMSEEhkclsNEEKLIVQDFILEaTQDDYVLeVRHFQCPKWPNPDSPISkTFELI 1353
Cdd:cd14616    81 RCHQ---YWPEDNKPVTVFGdIVITKLMED-----VQIDWTIRDLKIE-RHGDYMM-VRQCNFTSWPEHGVPES-SAPLI 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 901694078 1354 SIIKEEAANRDG---PMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYK 1425
Cdd:cd14616   150 HFVKLVRASRAHdntPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLHQ 224
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 1225-1424 1.02e-28

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


Pssm-ID: 350397 [Multi-domain]  Cd Length: 204  Bit Score: 115.14  E-value: 1.02e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1225 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIpdgQNMAE------DEfvYWPNKDEPiNCESFKVT 1298
Cdd:cd14549     1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMI---TNLVErgrrkcDQ--YWPKEGTE-TYGNIQVT 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1299 LMSEEHkcLSNeekLIVQDFILEATQ------DDYVLEVRHFQCPKWPN---PDSPISktfeLISII-KEEAANRD--GP 1366
Cdd:cd14549    75 LLSTEV--LAT---YTVRTFSLKNLKlkkvkgRSSERVVYQYHYTQWPDhgvPDYTLP----VLSFVrKSSAANPPgaGP 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 901694078 1367 MIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMI----NLMrpgVFTDiEQYQFLY 1424
Cdd:cd14549   146 IVVHCSAGVGRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIrtqrNYL---VQTE-EQYIFIH 203
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 1188-1432 3.16e-28

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 117.02  E-value: 3.16e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1188 YSTALKQCNREKNRTSSIIPVERSRVGISSLSGEGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVV 1267
Cdd:PHA02747   43 IANFEKPENQPKNRYWDIPCWDHNRVILDSGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIV 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1268 MI--PDGQNMAEDEFVYW-PNKDEPINCESFKVTLMSEEHKCLSNEEKLIVQDFILEATQddyvlEVRHFQCPKWPNPDS 1344
Cdd:PHA02747  123 MLtpTKGTNGEEKCYQYWcLNEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILKDSR-----KISHFQCSEWFEDET 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1345 PiSKTFELISIIKEEAANRD-------------GPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRP 1411
Cdd:PHA02747  198 P-SDHPDFIKFIKIIDINRKksgklfnpkdallCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRH 276

                         250       260
                  ....*....|....*....|....
gi 901694078 1412 GVFTDIEQYQFL---YKVVLSLVS 1432
Cdd:PHA02747  277 AGIMNFDDYLFIqpgYEVLHYFLS 300
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 1204-1428 3.57e-28

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


Pssm-ID: 350468 [Multi-domain]  Cd Length: 229  Bit Score: 114.27  E-value: 3.57e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1204 SIIPVERSRVGISSLSG-EGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAEDE-FV 1281
Cdd:cd14620     3 NILPYDHSRVILSQLDGiPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKcYQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1282 YWPNKdepiNCESF-KVTLMSEEHKCLSNeekLIVQDFILEATQDDYVLEVR-----HFQcpKWPN---PDSPISkTFEL 1352
Cdd:cd14620    83 YWPDQ----GCWTYgNIRVAVEDCVVLVD---YTIRKFCIQPQLPDGCKAPRlvtqlHFT--SWPDfgvPFTPIG-MLKF 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 901694078 1353 ISIIKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVVL 1428
Cdd:cd14620   153 LKKVKSVNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALL 228
alpha_CARP_VIII cd03120
Carbonic anhydrase alpha related protein, group VIII. Carbonic anhydrase related proteins ...
 49-289 4.44e-28

Carbonic anhydrase alpha related protein, group VIII. Carbonic anhydrase related proteins (CARPs) are sequence similar to carbonic anhydrases. Carbonic anhydrases are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism. CARPs have lost conserved histidines involved in zinc binding and consequently their catalytic activity. CARP VIII may play roles in various biological processes of the central nervous system, and could be involved in protein-protein interactions. CARP VIII has been shown to bind inositol 1,4,5-triphosphate (IP3) receptor type I (IP3RI), reducing the affinity of the receptor for IP3. IP3RI is an intracellular IP3-gated Ca2+ channel located on intracellular Ca2+ stores. IP3RI converts IP3 signaling into Ca2+ signaling thereby participating in a variety of cell functions.


Pssm-ID: 239394  Cd Length: 256  Bit Score: 114.95  E-value: 4.44e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078   49 WGKKYPICNSPKQSPINI-------DEDLTQVNVNLKKLKFQGWEkaslentfIHNTGKTVEINLTNDYYLSGGL--SEK 119
Cdd:cd03120     4 WGLLFPEANGEYQSPINLnsrearyDPSLLEVRLSPNYVVCRDCE--------VINDGHTIQIILKSKSVLSGGPlpQGH 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  120 VFKASKITFHWGKCNvsSEGSEHSLEGQKFPLEMQVYCFDADRFSSFEEAVKGKGRLRALSILFEVGvEENLDYKAIIDG 199
Cdd:cd03120    76 EFELAEVRFHWGREN--QRGSEHTVNFKAFPMELHLIHWNSTLYSSLEEAMGKPHGIAIIALFVQIG-KEHVGLKAVTEI 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  200 TESVSRFGKQAALDPFVLQNLLPNSTDK-YYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLAVFCEvLTMQQSGYVMLM 278
Cdd:cd03120   153 LQDIQYKGKSKTIPCFNPNTLLPDPLLRdYWVYEGSLTTPPCSEGVTWILFRYPLTISQSQIEEFRR-LRTHVKGAELVE 231

                         250
                  ....*....|....
gi 901694078  279 --DY-LQNNFREQQ 289
Cdd:cd03120   232 gcDGlLGDNFRPTQ 245
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 1225-1425 5.03e-28

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


Pssm-ID: 350390 [Multi-domain]  Cd Length: 202  Bit Score: 112.90  E-value: 5.03e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1225 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVM----IPDGQNMAEDefvYWPNK-DEPINCESFKVTL 1299
Cdd:cd14542     1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMacreFEMGKKKCER---YWPEEgEEQLQFGPFKISL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1300 MSEEHKClsneeklivQDFI---LEATQDDYVLEVRHFQCPKWPNPDSPISKT--FELISIIKEEAANRDGPMIVHDEHG 1374
Cdd:cd14542    78 EKEKRVG---------PDFLirtLKVTFQKESRTVYQFHYTAWPDHGVPSSVDpiLDLVRLVRDYQGSEDVPICVHCSAG 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 901694078 1375 GVTAGTFCALT---TLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYK 1425
Cdd:cd14542   149 CGRTGTICAIDyvwNLLKTGKIPEEFSLFDLVREMRKQRPAMVQTKEQYELVYR 202
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 1189-1427 5.81e-28

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 116.28  E-value: 5.81e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1189 STALKQCNREKNRTSSIIPVERSRVGISS------------------LSGEGTD--YINASYIMGYYQSNEFIITQHPLL 1248
Cdd:PHA02746   44 NHFLKKENLKKNRFHDIPCWDHSRVVINAheslkmfdvgdsdgkkieVTSEDNAenYIHANFVDGFKEANKFICAQGPKE 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1249 HTIKDFWRMIWDHNAQLVVMIPDGQNMAEDEFVYWPN-KDEPINCESFKVTLMSEEHKCLSNEEKLIVQDFILEATQddy 1327
Cdd:PHA02746  124 DTSEDFFKLISEHESQVIVSLTDIDDDDEKCFELWTKeEDSELAFGRFVAKILDIIEELSFTKTRLMITDKISDTSR--- 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1328 vlEVRHFQCPKWP---NPDSPiSKTFELISIIKEEAA----------NRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKE 1394
Cdd:PHA02746  201 --EIHHFWFPDWPdngIPTGM-AEFLELINKVNEEQAelikqadndpQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKE 277

                         250       260       270
                  ....*....|....*....|....*....|...
gi 901694078 1395 NAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVV 1427
Cdd:PHA02746  278 KEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 1225-1428 9.51e-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: 112.32  E-value: 9.51e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1225 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIpdgQNMAEDEFV----YWPNKDEPINceSFKVTLM 1300
Cdd:cd14555     1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMV---TNLVEVGRVkcsrYWPDDTEVYG--DIKVTLV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1301 SEEHKClsneeKLIVQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKT--FELISIIKEEAANRDGPMIVHDEHGGVTA 1378
Cdd:cd14555    76 ETEPLA-----EYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATglLGFIRRVKASNPPSAGPIVVHCSAGAGRT 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 901694078 1379 GTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVVL 1428
Cdd:cd14555   151 GCYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAIL 200
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 930-1139 1.42e-27

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: 111.92  E-value: 1.42e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  930 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRR-KCDQYWPTDGSEEYGSFLVNQKSVQ 1008
Cdd:cd14637     1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWPEPGLQQYGPMEVEFVSGS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1009 VLAYYTVRNFTLRN-TKLKKGSQkgrssgrLVTQYHYTQW-PDMGVPEYS---LPVLAFVRKAAQAKRHavGPVVVHCSA 1083
Cdd:cd14637    81 ADEDIVTRLFRVQNiTRLQEGHL-------MVRHFQFLRWsAYRDTPDSKkafLHLLASVEKWQRESGE--GRTVVHCLN 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 901694078 1084 GVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVE 1139
Cdd:cd14637   152 GGGRSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 1184-1428 1.86e-27

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


Pssm-ID: 350469 [Multi-domain]  Cd Length: 296  Bit Score: 114.35  E-value: 1.86e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1184 LQSDYSTALKQCNREKNRTSSIIPVERSRVGISSLSG-EGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHN 1262
Cdd:cd14621    40 IQATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGvPDSDYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQN 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1263 AQLVVMIPDGQNMAEDEFV-YWPNKdepiNCESFKVTLMSEEHKCLSNE---EKLIVQDfILEATQDDYVLEVRHFQCPK 1338
Cdd:cd14621   120 TATIVMVTNLKERKECKCAqYWPDQ----GCWTYGNIRVSVEDVTVLVDytvRKFCIQQ-VGDVTNKKPQRLITQFHFTS 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1339 WPN---PDSPISkTFELISIIKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFT 1415
Cdd:cd14621   195 WPDfgvPFTPIG-MLKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQ 273

                         250
                  ....*....|...
gi 901694078 1416 DIEQYQFLYKVVL 1428
Cdd:cd14621   274 TDMQYVFIYQALL 286
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 1196-1431 4.19e-27

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


Pssm-ID: 350505 [Multi-domain]  Cd Length: 274  Bit Score: 112.44  E-value: 4.19e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1196 NREKNRTSSIIPVERSRVGISSLSGEGT---DYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIpdg 1272
Cdd:cd17667    27 NKHKNRYINILAYDHSRVKLRPLPGKDSkhsDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMI--- 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1273 QNMAE------DEfvYWPNKdepiNCESFK---VTLMSEE-HKCLSneekliVQDFILEATQDDYVLE-----------V 1331
Cdd:cd17667   104 TNLVEkgrrkcDQ--YWPTE----NSEEYGniiVTLKSTKiHACYT------VRRFSIRNTKVKKGQKgnpkgrqnertV 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1332 RHFQCPKWPNPDSPiSKTFELISIIKEEAANRD---GPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINL 1408
Cdd:cd17667   172 IQYHYTQWPDMGVP-EYALPVLTFVRRSSAARTpemGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRT 250

                         250       260
                  ....*....|....*....|...
gi 901694078 1409 MRPGVFTDIEQYQFLYKVVLSLV 1431
Cdd:cd17667   251 QRNYLVQTEEQYIFIHDALLEAI 273
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 1196-1427 5.51e-27

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


Pssm-ID: 350392 [Multi-domain]  Cd Length: 251  Bit Score: 111.40  E-value: 5.51e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1196 NREKNRTSSIIPVERSRVGISSL--SGEGTDYINASYIM-------GYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLV 1266
Cdd:cd14544     1 NKGKNRYKNILPFDHTRVILKDRdpNVPGSDYINANYIRnenegptTDENAKTYIATQGCLENTVSDFWSMVWQENSRVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1267 VMIPDGQNMAEDEFV-YWPNKDEPINCESFKVTLMSEehkclSNEEKLIVQDFILEAT-QDDYVLEVRHFQCPKWPNPDS 1344
Cdd:cd14544    81 VMTTKEVERGKNKCVrYWPDEGMQKQYGPYRVQNVSE-----HDTTDYTLRELQVSKLdQGDPIREIWHYQYLSWPDHGV 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1345 PiSKTFELISII-----KEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKEN---AMDVYQVAKMINLMRPGVFTD 1416
Cdd:cd14544   156 P-SDPGGVLNFLedvnqRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGldcDIDIQKTIQMVRSQRSGMVQT 234

                         250
                  ....*....|.
gi 901694078 1417 IEQYQFLYKVV 1427
Cdd:cd14544   235 EAQYKFIYVAV 245
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 1197-1425 5.86e-27

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


Pssm-ID: 350393 [Multi-domain]  Cd Length: 231  Bit Score: 110.94  E-value: 5.86e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1197 REKNRTSSIIPVERSRVgisSLSGEGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVM----IPDG 1272
Cdd:cd14545     1 LNRYRDRDPYDHDRSRV---KLKQGDNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMlnklMEKG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1273 QNMAEDefvYWPNKDEPINC---ESFKVTLMSEEHKclsneEKLIVQDFILEATQDDYVLEVRHFQCPKWPN---PDSPI 1346
Cdd:cd14545    78 QIKCAQ---YWPQGEGNAMIfedTGLKVTLLSEEDK-----SYYTVRTLELENLKTQETREVLHFHYTTWPDfgvPESPA 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1347 SKTFELISIIKEEAANRD-GPMIVHDEHGGVTAGTFCALTTLMHQLEKEN--AMDVYQVAKMINLMRPGVFTDIEQYQFL 1423
Cdd:cd14545   150 AFLNFLQKVRESGSLSSDvGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNpsSVDVKKVLLEMRKYRMGLIQTPDQLRFS 229


                  ..
gi 901694078 1424 YK 1425
Cdd:cd14545   230 YL 231
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 1223-1428 8.44e-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: 110.11  E-value: 8.44e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1223 TDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAEDE-FVYWPNKDEPINceSFKVTLMS 1301
Cdd:cd14631    13 SDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKcYKYWPDDTEVYG--DFKVTCVE 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1302 EEHKClsneeKLIVQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTFELISIIKEEAAN--RDGPMIVHDEHGGVTAG 1379
Cdd:cd14631    91 MEPLA-----EYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNppSAGPIVVHCSAGAGRTG 165

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 901694078 1380 TFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVVL 1428
Cdd:cd14631   166 CYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAIL 214
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 930-1139 8.47e-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: 109.39  E-value: 8.47e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  930 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLveKGRRKCDQYWPTDGSEEYGSFLVNQKSVQV 1009
Cdd:cd14635     1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDV--DPAQLCPQYWPENGVHRHGPIQVEFVSADL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1010 LAYYTVRNFTLRNtklkkgSQKGRSSGRLVTQYHYTQWP---DMGVPEYS-LPVLAFVRKAAQAKRHAVGPVVVHCSAGV 1085
Cdd:cd14635    79 EEDIISRIFRIYN------AARPQDGYRMVQQFQFLGWPmyrDTPVSKRSfLKLIRQVDKWQEEYNGGEGRTVVHCLNGG 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 901694078 1086 GRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVE 1139
Cdd:cd14635   153 GRSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 1168-1427 1.02e-26

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


Pssm-ID: 350458 [Multi-domain]  Cd Length: 283  Bit Score: 111.69  E-value: 1.02e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1168 KTKLEKQFQLLSQSNILQSDYSTALKQCNREKNRTSSIIPVERSRVGISSL-SGEGTDYINASYIMGYYQSN-EFIITQH 1245
Cdd:cd14610    16 KNRLEKEWEALCAYQAEPNATNVAQREENVQKNRSLAVLPYDHSRIILKAEnSHSHSDYINASPIMDHDPRNpAYIATQG 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1246 PLLHTIKDFWRMIWDHNAQLVVMI-PDGQNMAEDEFVYWPnkDEPINC-ESFKVTLMSEEHKClsneEKLIVQDFILEAT 1323
Cdd:cd14610    96 PLPATVADFWQMVWESGCVVIVMLtPLAENGVKQCYHYWP--DEGSNLyHIYEVNLVSEHIWC----EDFLVRSFYLKNL 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1324 QDDYVLEVRHFQCPKWPNPDSPIS--KTFELISIIKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEK-ENAMDVY 1400
Cdd:cd14610   170 QTNETRTVTQFHFLSWNDQGVPAStrSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLNKMAKgAKEIDIA 249

                         250       260
                  ....*....|....*....|....*..
gi 901694078 1401 QVAKMINLMRPGVFTDIEQYQFLYKVV 1427
Cdd:cd14610   250 ATLEHLRDQRPGMVQTKEQFEFALTAV 276
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 1196-1428 1.29e-26

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


Pssm-ID: 350456 [Multi-domain]  Cd Length: 277  Bit Score: 111.27  E-value: 1.29e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1196 NREKNRTSSIIPVERSRVgisSLSGEGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIpdgQNM 1275
Cdd:cd14608    25 NKNRNRYRDVSPFDHSRI---KLHQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVML---NRV 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1276 AEDEFV----YWPNKDEP---INCESFKVTLMSEEHKCLSNEEKLIVQDFILEATQddyvlEVRHFQCPKWPN---PDSP 1345
Cdd:cd14608    99 MEKGSLkcaqYWPQKEEKemiFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETR-----EILHFHYTTWPDfgvPESP 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1346 ISKTFELISIIKEEAANRD-GPMIVHDEHGGVTAGTFCALTT---LMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQ 1421
Cdd:cd14608   174 ASFLNFLFKVRESGSLSPEhGPVVVHCSAGIGRSGTFCLADTcllLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLR 253


                  ....*..
gi 901694078 1422 FLYKVVL 1428
Cdd:cd14608   254 FSYLAVI 260
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 1194-1432 1.31e-26

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


Pssm-ID: 350472 [Multi-domain]  Cd Length: 284  Bit Score: 111.36  E-value: 1.31e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1194 QCNREKNRTSSIIPVERSRVGISSLSG-EGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDG 1272
Cdd:cd14624    45 EVNKPKNRYANVIAYDHSRVLLSAIEGiPGSDYINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKL 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1273 QNMAE---DEfvYWPNKDEPINcESFKVTLMSEEHKClsneeKLIVQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKT 1349
Cdd:cd14624   125 EERSRvkcDQ--YWPSRGTETY-GLIQVTLLDTVELA-----TYCVRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPT 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1350 FELISIIKEEAAN--RDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVV 1427
Cdd:cd14624   197 PFLAFLRRVKTCNppDAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDAL 276


                  ....*
gi 901694078 1428 LSLVS 1432
Cdd:cd14624   277 LEAVT 281
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 1225-1428 1.32e-26

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


Pssm-ID: 350483 [Multi-domain]  Cd Length: 206  Bit Score: 109.01  E-value: 1.32e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1225 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDgQNMAEDEFVYWP----NKDEPINCESFKVTLm 1300
Cdd:cd14635     1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLND-VDPAQLCPQYWPengvHRHGPIQVEFVSADL- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1301 seehkclsnEEKLIVQDF-ILEAT--QDDYVLeVRHFQCPKWP-NPDSPISKT--FELISII---KEEAANRDGPMIVHD 1371
Cdd:cd14635    79 ---------EEDIISRIFrIYNAArpQDGYRM-VQQFQFLGWPmYRDTPVSKRsfLKLIRQVdkwQEEYNGGEGRTVVHC 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 901694078 1372 EHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVVL 1428
Cdd:cd14635   149 LNGGGRSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVAL 205
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 930-1139 2.10e-26

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


Pssm-ID: 350484 [Multi-domain]  Cd Length: 206  Bit Score: 108.57  E-value: 2.10e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  930 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNL-VEKGrrkCDQYWPTDGSEEYGSFLVNQKSVQ 1008
Cdd:cd14636     1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVdLAQG---CPQYWPEEGMLRYGPIQVECMSCS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1009 VLAYYTVRNFTLRN-TKLKKGSQkgrssgrLVTQYHYTQWPD-MGVPEYS---LPVLAFVRKAAQAKRHAVGPVVVHCSA 1083
Cdd:cd14636    78 MDCDVISRIFRICNlTRPQEGYL-------MVQQFQYLGWAShREVPGSKrsfLKLILQVEKWQEECDEGEGRTIIHCLN 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 901694078 1084 GVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVE 1139
Cdd:cd14636   151 GGGRSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 1170-1432 3.02e-26

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


Pssm-ID: 350473 [Multi-domain]  Cd Length: 282  Bit Score: 110.18  E-value: 3.02e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1170 KLEKQFQLLSQSNILQSDYSTAlkQCNREKNRTSSIIPVERSRVGISSLSG-EGTDYINASYIMGYYQSNEFIITQHPLL 1248
Cdd:cd14625    23 KLSQEYESIDPGQQFTWEHSNL--EVNKPKNRYANVIAYDHSRVILQPIEGiMGSDYINANYIDGYRKQNAYIATQGPLP 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1249 HTIKDFWRMIWDHNAQLVVM---IPDGQNMAEDEfvYWPNKdepiNCESF---KVTLMSEEHKClsneeKLIVQDFILEA 1322
Cdd:cd14625   101 ETFGDFWRMVWEQRSATVVMmtkLEEKSRIKCDQ--YWPSR----GTETYgmiQVTLLDTIELA-----TFCVRTFSLHK 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1323 TQDDYVLEVRHFQCPKWPNPDSPISKTFELISIIKEEAAN--RDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVY 1400
Cdd:cd14625   170 NGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNppDAGPIVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIY 249

                         250       260       270
                  ....*....|....*....|....*....|..
gi 901694078 1401 QVAKMINLMRPGVFTDIEQYQFLYKVVLSLVS 1432
Cdd:cd14625   250 GHVTLMRSQRNYMVQTEDQYSFIHDALLEAVA 281
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 1168-1427 1.09e-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: 1.09e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1168 KTKLEKQFQLLSQSNILQSDYSTALKQCNREKNRTSSIIPVERSRVGI-SSLSGEGTDYINASYIMGY-YQSNEFIITQH 1245
Cdd:cd14609    14 RDRLAKEWQALCAYQAEPNTCSTAQGEANVKKNRNPDFVPYDHARIKLkAESNPSRSDYINASPIIEHdPRMPAYIATQG 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1246 PLLHTIKDFWRMIWDHNAQLVVM----IPDGQNMAEDefvYWPNKDEPINcESFKVTLMSEEHKClsneEKLIVQDFILE 1321
Cdd:cd14609    94 PLSHTIADFWQMVWENGCTVIVMltplVEDGVKQCDR---YWPDEGSSLY-HIYEVNLVSEHIWC----EDFLVRSFYLK 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1322 ATQDDYVLEVRHFQCPKWPNPDSPiSKTFELISI---IKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKE-NAM 1397
Cdd:cd14609   166 NVQTQETRTLTQFHFLSWPAEGIP-SSTRPLLDFrrkVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKGvKEI 244

                         250       260       270
                  ....*....|....*....|....*....|
gi 901694078 1398 DVYQVAKMINLMRPGVFTDIEQYQFLYKVV 1427
Cdd:cd14609   245 DIAATLEHVRDQRPGMVRTKDQFEFALTAV 274
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 1225-1428 2.16e-25

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


Pssm-ID: 350480 [Multi-domain]  Cd Length: 205  Bit Score: 105.52  E-value: 2.16e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1225 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIpdgQNMAEDEFV----YWPNKDEPINceSFKVTLM 1300
Cdd:cd14632     1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMI---TKLVEVGRVkcskYWPDDSDTYG--DIKITLL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1301 SEEhkclsNEEKLIVQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKT--FELISIIKEEAANRDGPMIVHDEHGGVTA 1378
Cdd:cd14632    76 KTE-----TLAEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATglLAFIRRVKASTPPDAGPVVVHCSAGAGRT 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 901694078 1379 GTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVVL 1428
Cdd:cd14632   151 GCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAIL 200
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 1199-1424 8.15e-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: 104.61  E-value: 8.15e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1199 KNRTSSIIPVERSRVGI--SSLSGEGTDYINASYIMGYY-QSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNM 1275
Cdd:cd14611     2 KNRYKTILPNPHSRVCLkpKNSNDSLSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1276 AEDEFVYWPNKDEPINcesfKVTLMSeehKCLSNEEKLIVQDFILEatQDDYVLEVRHFQCPKWPNPDSPISKT--FELI 1353
Cdd:cd14611    82 NEKCVLYWPEKRGIYG----KVEVLV---NSVKECDNYTIRNLTLK--QGSQSRSVKHYWYTSWPDHKTPDSAQplLQLM 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 901694078 1354 SIIKEE--AANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLY 1424
Cdd:cd14611   153 LDVEEDrlASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 1225-1428 8.43e-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: 103.95  E-value: 8.43e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1225 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDgQNMAEDEFVYWPnKDEPINCESFKVTLMSEEH 1304
Cdd:cd14636     1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNE-VDLAQGCPQYWP-EEGMLRYGPIQVECMSCSM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1305 KClsneeKLIVQDFI---LEATQDDYVLeVRHFQCPKWP-NPDSPISKTFELISII-----KEEAANRDGPMIVHDEHGG 1375
Cdd:cd14636    79 DC-----DVISRIFRicnLTRPQEGYLM-VQQFQYLGWAsHREVPGSKRSFLKLILqvekwQEECDEGEGRTIIHCLNGG 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 901694078 1376 VTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVVL 1428
Cdd:cd14636   153 GRSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVAL 205
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 1196-1428 1.34e-24

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: 104.14  E-value: 1.34e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1196 NREKNRTSSIIPVERSRVgissLSGEGTDYINASYIMGYYQSNEF--IITQHPLLHTIKDFWRMIWDHNAQLVVMIpdgQ 1273
Cdd:cd14597     3 NRKKNRYKNILPYDTTRV----PLGDEGGYINASFIKMPVGDEEFvyIACQGPLPTTVADFWQMVWEQKSTVIAMM---T 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1274 NMAEDEFV----YWP---NKDEPINcESFKVTLMSEEHkclsnEEKLIVQDFILEATQDDYVLEVRHFQCPKWPNPDSPi 1346
Cdd:cd14597    76 QEVEGGKIkcqrYWPeilGKTTMVD-NRLQLTLVRMQQ-----LKNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTP- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1347 SKTFELISIIK-EEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYK 1425
Cdd:cd14597   149 SQPEQLLTFISyMRHIHKSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQ 228


                  ...
gi 901694078 1426 VVL 1428
Cdd:cd14597   229 VIL 231
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 1225-1425 8.17e-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: 100.76  E-value: 8.17e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1225 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAEDEFV-YWPNKdepiNCESFkvtlmSEE 1303
Cdd:cd14551     1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSqYWPDQ----GCWTY-----GNL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1304 HKCLSNEEKLI---VQDFILEATQDDY----VLEVRHFQCPKWPN---PDSPISkTFELISIIKEEAANRDGPMIVHDEH 1373
Cdd:cd14551    72 RVRVEDTVVLVdytTRKFCIQKVNRGIgekrVRLVTQFHFTSWPDfgvPFTPIG-MLKFLKKVKSANPPRAGPIVVHCSA 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 901694078 1374 GGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYK 1425
Cdd:cd14551   151 GVGRTGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 1330-1429 1.38e-23

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


Pssm-ID: 214469 [Multi-domain]  Cd Length: 105  Bit Score: 96.66  E-value: 1.38e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078   1330 EVRHFQCPKWPNPDSPISKT--FELISIIKEE--AANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKE-NAMDVYQVAK 1404
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDsiLELLRAVKKNlnQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 901694078   1405 MINLMRPGVFTDIEQYQFLYKVVLS 1429
Cdd:smart00012   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1330-1429 1.38e-23

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 96.66  E-value: 1.38e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078   1330 EVRHFQCPKWPNPDSPISKT--FELISIIKEE--AANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKE-NAMDVYQVAK 1404
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDsiLELLRAVKKNlnQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 901694078   1405 MINLMRPGVFTDIEQYQFLYKVVLS 1429
Cdd:smart00404   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 892-1137 2.98e-23

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 101.97  E-value: 2.98e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  892 SSNHPDNKHK--NRYVNIVAYDHSRVKLtqlaEKDGKLTDyinANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVE 969
Cdd:PHA02740   45 ACAQAENKAKdeNLALHITRLLHRRIKL----FNDEKVLD---ARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQ 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  970 VIVMITNLVEKgrrKC-DQYWptdGSEEYGSFLVNQKSVQVLAYYTVRNFTLrnTKLKKGSQKGRSsgRLVTQYHYTQWP 1048
Cdd:PHA02740  118 IIVLISRHADK---KCfNQFW---SLKEGCVITSDKFQIETLEIIIKPHFNL--TLLSLTDKFGQA--QKISHFQYTAWP 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1049 DMGVPEYSLPVLAFVRKA----AQAKRHA----VGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQR 1120
Cdd:PHA02740  188 ADGFSHDPDAFIDFFCNIddlcADLEKHKadgkIAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKK 267

                         250
                  ....*....|....*..
gi 901694078 1121 NYLVQTEEQYVFIHDTL 1137
Cdd:PHA02740  268 YGCMNCLDDYVFCYHLI 284
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 1225-1428 6.82e-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: 98.22  E-value: 6.82e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1225 YINASYIMGYYQSNEF--IITQHPLLHTIKDFWRMIWDHNAQLVVMIPdgQNMaEDEFV----YWPnkdepincESFKVT 1298
Cdd:cd14538     1 YINASHIRIPVGGDTYhyIACQGPLPNTTGDFWQMVWEQKSEVIAMVT--QDV-EGGKVkchrYWP--------DSLNKP 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1299 LMSEEHKCLSNEEKLIVQDFI-----LEATQDDYVLEVRHFQCPKWPNPDSPISkTFELISIIKE-EAANRDGPMIVHDE 1372
Cdd:cd14538    70 LICGGRLEVSLEKYQSLQDFVirrisLRDKETGEVHHITHLNFTTWPDHGTPQS-ADPLLRFIRYmRRIHNSGPIVVHCS 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 901694078 1373 HGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVVL 1428
Cdd:cd14538   149 AGIGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACL 204
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 1225-1424 3.28e-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: 96.20  E-value: 3.28e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1225 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIpdgQNMAE------DEfvYWPNKDEPiNCESFKVT 1298
Cdd:cd17668     1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMI---TNLVEkgrrkcDQ--YWPADGSE-EYGNFLVT 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1299 LMSEEHKCLSNEEKLIVQDF-ILEATQDDYVLE--VRHFQCPKWPNPDSPiSKTFELISIIKEEAANRD---GPMIVHDE 1372
Cdd:cd17668    75 QKSVQVLAYYTVRNFTLRNTkIKKGSQKGRPSGrvVTQYHYTQWPDMGVP-EYTLPVLTFVRKASYAKRhavGPVVVHCS 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 901694078 1373 HGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLY 1424
Cdd:cd17668   154 AGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIH 205
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 930-1138 4.44e-22

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


Pssm-ID: 350508 [Multi-domain]  Cd Length: 205  Bit Score: 95.90  E-value: 4.44e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  930 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITN---LVEkgrrkcDQ--YWPTD----GSEEYGSF 1000
Cdd:cd17670     1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDnqgLAE------DEfvYWPSReesmNCEAFTVT 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1001 LVNQKSV------QVLayytVRNFTLRNTKLKKGSQkgrssgrlVTQYHYTQWPDMGVPEYSLPVLAFVRKAAQAKRHav 1074
Cdd:cd17670    75 LISKDRLclsneeQII----IHDFILEATQDDYVLE--------VRHFQCPKWPNPDAPISSTFELINVIKEEALTRD-- 140

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 901694078 1075 GPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLV 1138
Cdd:cd17670   141 GPTIVHDEFGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 1225-1428 4.79e-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: 95.97  E-value: 4.79e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1225 YINASYIMGYYQSNE--FIITQHPLLHTIKDFWRMIWDHNAQLVVMIPD----GQNMAEDefvYWPNK-DEPINCESFKV 1297
Cdd:cd14596     1 YINASYITMPVGEEElfYIATQGPLPSTIDDFWQMVWENRSDVIAMMTReverGKVKCHR---YWPETlQEPMELENYQL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1298 TLmsEEHKCLsneEKLIVQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTFELISIIKEEAANRDGPMIVHDEHGGVT 1377
Cdd:cd14596    78 RL--ENYQAL---QYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHNTGPIVVHCSAGIGR 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 901694078 1378 AGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVVL 1428
Cdd:cd14596   153 AGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVL 203
PHA02738 PHA02738
hypothetical protein; Provisional
 1196-1427 4.97e-22

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 98.84  E-value: 4.97e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1196 NREKNRTSSIIPVERSRVGISSLSGEGtDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMI-PDGQN 1274
Cdd:PHA02738   49 NRKLNRYLDAVCFDHSRVILPAERNRG-DYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLcKKKEN 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1275 MAEDEFVYWPNKDE-PINCESFKVTLMSEEHKCLSNEEKLIVQDFIlEATQddyvlEVRHFQCPKWPNPDSPiSKTFELI 1353
Cdd:PHA02738  128 GREKCFPYWSDVEQgSIRFGKFKITTTQVETHPHYVKSTLLLTDGT-SATQ-----TVTHFNFTAWPDHDVP-KNTSEFL 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1354 SII-------KEEAANR---------DGPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDI 1417
Cdd:PHA02738  201 NFVlevrqcqKELAQESlqighnrlqPPPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIP 280

                         250
                  ....*....|
gi 901694078 1418 EQYQFLYKVV 1427
Cdd:PHA02738  281 FQYFFCYRAV 290
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 930-1138 6.73e-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: 95.45  E-value: 6.73e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  930 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCdQYWPT-DGSEEYGSFLVNQKSVQ 1008
Cdd:cd17669     1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEF-VYWPNkDEPINCETFKVTLIAEE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1009 VLAYYTVRNFTLRNTKLKKGSQKGRSSgrlVTQYHYTQWPDMGVP-EYSLPVLAFVRKAAQAKRhavGPVVVHCSAGVGR 1087
Cdd:cd17669    80 HKCLSNEEKLIIQDFILEATQDDYVLE---VRHFQCPKWPNPDSPiSKTFELISIIKEEAANRD---GPMIVHDEHGGVT 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 901694078 1088 TGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLV 1138
Cdd:cd17669   154 AGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 1225-1425 2.64e-21

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


Pssm-ID: 350405 [Multi-domain]  Cd Length: 201  Bit Score: 93.35  E-value: 2.64e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1225 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAEDE-FVYWPNKDEPINC-ESFKVTLMSE 1302
Cdd:cd14557     1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKcAQYWPSMEEGSRAfGDVVVKINEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1303 EHkClsneEKLIVQDFILEATQDDY-VLEVRHFQCPKWPN---PDSPiSKTFELISIIKEEAANRDGPMIVHDEHGGVTA 1378
Cdd:cd14557    81 KI-C----PDYIIRKLNINNKKEKGsGREVTHIQFTSWPDhgvPEDP-HLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRT 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 901694078 1379 GTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYK 1425
Cdd:cd14557   155 GTYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 1196-1427 5.96e-21

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


Pssm-ID: 350455 [Multi-domain]  Cd Length: 257  Bit Score: 94.26  E-value: 5.96e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1196 NREKNRTSSIIPVERSRVgisSLSGEGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIpdgQNM 1275
Cdd:cd14607    24 NRNRNRYRDVSPYDHSRV---KLQNTENDYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVML---NRI 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1276 AEDEFV----YWPNKDEPINCES---FKVTLMSEEHKCLSNEEKLIVQDFILEATQDdyvleVRHFQCPKWPN---PDSP 1345
Cdd:cd14607    98 VEKDSVkcaqYWPTDEEEVLSFKetgFSVKLLSEDVKSYYTVHLLQLENINSGETRT-----ISHFHYTTWPDfgvPESP 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1346 ISKTFELISIIKEEAANRD-GPMIVHDEHGGVTAGTFCALTTLMHQLEKEN--AMDVYQVAKMINLMRPGVFTDIEQYQF 1422
Cdd:cd14607   173 ASFLNFLFKVRESGSLSPEhGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDIKQVLLDMRKYRMGLIQTPDQLRF 252


                  ....*
gi 901694078 1423 LYKVV 1427
Cdd:cd14607   253 SYMAV 257
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 1196-1428 1.64e-20

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


Pssm-ID: 350448 [Multi-domain]  Cd Length: 274  Bit Score: 93.38  E-value: 1.64e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1196 NREKNRTSSIIPVERSRVgissLSGEGTDYINASY----IMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPD 1271
Cdd:cd14600    40 NMDKNRYKDVLPYDATRV----VLQGNEDYINASYvnmeIPSANIVNKYIATQGPLPHTCAQFWQVVWEQKLSLIVMLTT 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1272 ----GQNMAEDefvYWPNKDEPINCESFKVTLMSEEHKClsneeKLIVQDFILEATQDDYVLEVRHFQCPKWPN---PDS 1344
Cdd:cd14600   116 lterGRTKCHQ---YWPDPPDVMEYGGFRVQCHSEDCTI-----AYVFREMLLTNTQTGEERTVTHLQYVAWPDhgvPDD 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1345 PiSKTFELISIIKEEAANRDgPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLY 1424
Cdd:cd14600   188 S-SDFLEFVNYVRSKRVENE-PVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKFVC 265


                  ....
gi 901694078 1425 KVVL 1428
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 ...
 1225-1427 3.05e-20

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


Pssm-ID: 350394 [Multi-domain]  Cd Length: 208  Bit Score: 90.58  E-value: 3.05e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1225 YINASYIMGYYQSNE-FIITQHPLLHTIKDFWRMIWDHNAQLVVMI-PDGQNMAEDEFVYWPNKDEPINcESFKVTLMSE 1302
Cdd:cd14546     1 YINASTIYDHDPRNPaYIATQGPLPHTIADFWQMIWEQGCVVIVMLtRLQENGVKQCARYWPEEGSEVY-HIYEVHLVSE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1303 EHKClsneEKLIVQDFILEATQDDYVLEVRHFQCPKWPNPDSPIS-KTF-ELISIIKEEAANRDGPMIVHDEHGGVTAGT 1380
Cdd:cd14546    80 HIWC----DDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASaKPLlEFRRKVNKSYRGRSCPIVVHCSDGAGRTGT 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 901694078 1381 FCALTTLMHQLEK-ENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVV 1427
Cdd:cd14546   156 YILIDMVLNRMAKgAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAV 203
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 1225-1425 9.52e-20

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


Pssm-ID: 350387 [Multi-domain]  Cd Length: 205  Bit Score: 88.98  E-value: 9.52e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1225 YINASYIMGYYQ-SNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAEDEFV-YWP-NKDEPINCESFKVTLMS 1301
Cdd:cd14539     1 YINASLIEDLTPyCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHrYWPtERGQALVYGAITVSLQS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1302 EEhkclsneekliVQDF----ILEATQDDYVLE--VRHFQCPKWPNPDSPISKTfELISIIKE------EAANRDGPMIV 1369
Cdd:cd14539    81 VR-----------TTPThverIISIQHKDTRLSrsVVHLQFTTWPELGLPDSPN-PLLRFIEEvhshylQQRSLQTPIVV 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 901694078 1370 HDEHGGVTAGTFCALTTLMHQLEKENAM-DVYQVAKMINLMRPGVFTDIEQYQFLYK 1425
Cdd:cd14539   149 HCSSGVGRTGAFCLLYAAVQEIEAGNGIpDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 1196-1433 1.16e-19

catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein phosphatase non-receptor type 11 (PTPN11), also called SH2 domain-containing tyrosine phosphatase 2 (SHP-2 or SHP2), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN11 promotes the activation of the RAS/Mitogen-Activated Protein Kinases (MAPK) Extracellular-Regulated Kinases 1/2 (ERK1/2) pathway, a canonical signaling cascade that plays key roles in various cellular processes, including proliferation, survival, differentiation, migration, or metabolism. It also regulates the phosphoinositide 3-kinase (PI3K)/AKT pathway, a fundamental cascade that functions in cell survival, proliferation, migration, morphogenesis, and metabolism. PTPN11 dysregulation is associated with several developmental diseases and malignancies, such as Noonan syndrome and juvenile myelomonocytic leukemia. It contains two tandem SH2 domains, a catalytic PTP domain, and a C-terminal tail with regulatory properties.


Pssm-ID: 350453 [Multi-domain]  Cd Length: 253  Bit Score: 90.08  E-value: 1.16e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1196 NREKNRTSSIIPVERSRVGISS--LSGEGTDYINASYIMGYYQSN--------EFIITQHPLLHTIKDFWRMIWDHNAQL 1265
Cdd:cd14605     2 NKNKNRYKNILPFDHTRVVLHDgdPNEPVSDYINANIIMPEFETKcnnskpkkSYIATQGCLQNTVNDFWRMVFQENSRV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1266 VVMIPDGQNMAEDEFV-YWPNKDEPINCESFKVTLMSEE--HKCLSNEEKLIvqdfilEATQDDYVLEVRHFQCPKWPN- 1341
Cdd:cd14605    82 IVMTTKEVERGKSKCVkYWPDEYALKEYGVMRVRNVKESaaHDYILRELKLS------KVGQGNTERTVWQYHFRTWPDh 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1342 --PDSP--ISKTFELISiIKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENA---MDVYQVAKMINLMRPGVF 1414
Cdd:cd14605   156 gvPSDPggVLDFLEEVH-HKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRSGMV 234

                         250
                  ....*....|....*....
gi 901694078 1415 TDIEQYQFLYKVVLSLVST 1433
Cdd:cd14605   235 QTEAQYRFIYMAVQHYIET 253
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 1171-1434 2.46e-19

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 90.45  E-value: 2.46e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1171 LEKQFQLLSQSNILQSDYsTALKQCNREKNRTSSIIPVERSRVGISSLSGeGTDYINASYIMGYYQSNEFIITQHPLLHT 1250
Cdd:PHA02742   28 LKEEHEHIMQEIVAFSCN-ESLELKNMKKCRYPDAPCFDRNRVILKIEDG-GDDFINASYVDGHNAKGRFICTQAPLEET 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1251 IKDFWRMIWDHNAQLVVMIP----DGQnmaEDEFVYWpNKDEPINCESFKVTLMSEEHKCLSNEEkliVQDFILEATQDD 1326
Cdd:PHA02742  106 ALDFWQAIFQDQVRVIVMITkimeDGK---EACYPYW-MPHERGKATHGEFKIKTKKIKSFRNYA---VTNLCLTDTNTG 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1327 YVLEVRHFQCPKWPNPDSP--ISKTFELISIIKE-----------EAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEK 1393
Cdd:PHA02742  179 ASLDIKHFAYEDWPHGGLPrdPNKFLDFVLAVREadlkadvdikgENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNE 258

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 901694078 1394 ENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVVL---SLVSTR 1434
Cdd:PHA02742  259 RAIIPLLSIVRDLRKQRHNCLSLPQQYIFCYFIVLifaKLMADK 302
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 1196-1433 8.12e-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: 8.12e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1196 NREKNRTSSIIPVERSRVGISSLSGE--GTDYINASYIMGYYQSNE-----FIITQHPLLHTIKDFWRMIWDHNAQLVVM 1268
Cdd:cd14606    18 NKSKNRYKNILPFDHSRVILQGRDSNipGSDYINANYVKNQLLGPDenaktYIASQGCLEATVNDFWQMAWQENSRVIVM 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1269 ----IPDGQNMAedeFVYWPNKDEPINCESFKVTLMSEEHkclSNEEKL-IVQDFILEATqdDYVLEVRHFQCPKWPNPD 1343
Cdd:cd14606    98 ttreVEKGRNKC---VPYWPEVGMQRAYGPYSVTNCGEHD---TTEYKLrTLQVSPLDNG--ELIREIWHYQYLSWPDHG 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1344 SPiSKTFELISII-----KEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENA---MDVYQVAKMINLMRPGVFT 1415
Cdd:cd14606   170 VP-SEPGGVLSFLdqinqRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVRAQRSGMVQ 248

                         250
                  ....*....|....*...
gi 901694078 1416 DIEQYQFLYKVVLSLVST 1433
Cdd:cd14606   249 TEAQYKFIYVAIAQFIET 266
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 1188-1431 2.58e-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: 86.97  E-value: 2.58e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1188 YSTALKQCNREKNRTSSIIPVERSRVGISSLSGEGTDYINASYIMGYYQSNE--FIITQHPLLHTIKDFWRMIWDHNAQL 1265
Cdd:cd14599    30 FTTATLPENAERNRIREVVPYEENRVELVPTKENNTGYINASHIKVTVGGEEwhYIATQGPLPHTCHDFWQMVWEQGVNV 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1266 VVMIpdgqnMAEDE------FVYWPNKDEPINCES---FKVTLMSEEHKCLSNEEKLIVQDFIleATQDDYVLevrHFQC 1336
Cdd:cd14599   110 IAMV-----TAEEEggrsksHRYWPKLGSKHSSATygkFKVTTKFRTDSGCYATTGLKVKHLL--SGQERTVW---HLQY 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1337 PKWPNPDSP------ISKTFELISI------IKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAK 1404
Cdd:cd14599   180 TDWPDHGCPeevqgfLSYLEEIQSVrrhtnsMLDSTKNCNPPIVVHCSAGVGRTGVVILTELMIGCLEHNEKVEVPVMLR 259

                         250       260
                  ....*....|....*....|....*..
gi 901694078 1405 MINLMRPGVFTDIEQYQFLYKVVLSLV 1431
Cdd:cd14599   260 HLREQRMFMIQTIAQYKFVYQVLIQFL 286
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1224-1370 9.84e-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: 83.53  E-value: 9.84e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1224 DYINASY----IMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVM----IPDGQNMAEDefvYWPNKDEPINCESF 1295
Cdd:cd14541     1 DYINANYvnmeIPGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMlttlVERGRVKCHQ---YWPDLGETMQFGNL 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 901694078 1296 KVTLMSEEhkclsNEEKLIVQDFILEATQDDYVLEVRHFQCPKWPNPDSPiSKTFELISIIKEEAANRDG---PMIVH 1370
Cdd:cd14541    78 QITCVSEE-----VTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVP-DDSSDFLDFVKRVRQNRVGmvePTVVH 149
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 1224-1428 3.33e-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: 3.33e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1224 DYINASYIMGYYQS----NEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIpdgQNMAEDEFV----YWPNKDEPINCESF 1295
Cdd:cd14601     1 DYINANYINMEIPSssiiNRYIACQGPLPNTCSDFWQMTWEQGSSMVVML---TTQVERGRVkchqYWPEPSGSSSYGGF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1296 KVTLMSEEhkclsNEEKLIVQDFILEATQDDYVLEVRHFQCPKWPN---PDSPiSKTFELISIIKEEAANRDGPMIVHDE 1372
Cdd:cd14601    78 QVTCHSEE-----GNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDhgvPDDS-SDFLDFVCLVRNKRAGKDEPVVVHCS 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 901694078 1373 HGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVVL 1428
Cdd:cd14601   152 AGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAIL 207
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1225-1428 7.92e-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: 80.96  E-value: 7.92e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1225 YINASYIMGYYQSNE--FIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQ-NMAEDEFVYWPNkdepincesfkvtlMS 1301
Cdd:cd14540     1 YINASHITATVGGKQrfYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEeGGREKCFRYWPT--------------LG 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1302 EEHKCLSNEEKLIVQDF------------ILEATQDDYVLEVRHFQCPKWPN---PDSPisKTF-----ELISI---IKE 1358
Cdd:cd14540    67 GEHDALTFGEYKVSTKFsvssgcytttglRVKHTLSGQSRTVWHLQYTDWPDhgcPEDV--SGFldfleEINSVrrhTNQ 144

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 901694078 1359 EAA--NRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVVL 1428
Cdd:cd14540   145 DVAghNRNPPTLVHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLI 216
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 1225-1424 1.16e-16

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


Pssm-ID: 350496 [Multi-domain]  Cd Length: 206  Bit Score: 80.20  E-value: 1.16e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1225 YINASYIMGYYQSN--EFIITQHPLLHTIKDFWRMIWDHNAQLVVMIP---DGQNMAEDEFVYWPNKDEPINCESFKVTL 1299
Cdd:cd17658     1 YINASLVETPASESlpKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTrlvDNYSTAKCADYFPAEENESREFGRISVTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1300 MSEEHKCLSNEEK-LIVQDFILEatqdDYVLEVRHFQCPKWPN---PDS--PISKTFELISIIKEEAanrdGPMIVHDEH 1373
Cdd:cd17658    81 KKLKHSQHSITLRvLEVQYIESE----EPPLSVLHIQYPEWPDhgvPKDtrSVRELLKRLYGIPPSA----GPIVVHCSA 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 901694078 1374 GGVTAGTFCALTTLMHQLEKEN--AMDVYQVAKMINLMRPGVFTDIEQYQFLY 1424
Cdd:cd17658   153 GIGRTGAYCTIHNTIRRILEGDmsAVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 902-1139 6.25e-14

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


Pssm-ID: 350407 [Multi-domain]  Cd Length: 227  Bit Score: 72.82  E-value: 6.25e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  902 NRYVNIvaydHSRVKltqlaEKDGKLtdyINANYVDGYNRPKAyIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKG 981
Cdd:cd14559     1 NRFTNI----QTRVS-----TPVGKN---LNANRVQIGNKNVA-IACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQ 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  982 RRKCDQYWPTDGSeeYGSFLVNQKsvQVLAYYTVRNFTLRNTKLK-KGSQKGRSsgrlVTQYHYTQWPDMG-VPEYSLPV 1059
Cdd:cd14559    68 RKGLPPYFRQSGT--YGSVTVKSK--KTGKDELVDGLKADMYNLKiTDGNKTIT----IPVVHVTNWPDHTaISSEGLKE 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1060 LA-FVRKAAQAKRHAVGPV-------------VVHCSAGVGRTGTYIvldSMLQQIQHEGTVNIFGFLKHIRSQRN-YLV 1124
Cdd:cd14559   140 LAdLVNKSAEEKRNFYKSKgssaindknkllpVIHCRAGVGRTGQLA---AAMELNKSPNNLSVEDIVSDMRTSRNgKMV 216

                         250
                  ....*....|....*
gi 901694078 1125 QTEEQYvfihDTLVE 1139
Cdd:cd14559   217 QKDEQL----DTLKE 227
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 1225-1431 3.82e-13

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


Pssm-ID: 350446 [Multi-domain]  Cd Length: 220  Bit Score: 70.39  E-value: 3.82e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1225 YINASYIMGYYQSNE--FIITQHPLLHTIKDFWRMIWDHNAQLVVMIP-DGQNMAEDEFVYWP---NKDEPINCESFKVT 1298
Cdd:cd14598     1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTaEEEGGREKSFRYWPrlgSRHNTVTYGRFKIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1299 L-MSEEHKCLSNEEKLIVQdfiLEATQDDYVLevrHFQCPKWPNPDSP------ISKTFELISIIKEEAANRD-----GP 1366
Cdd:cd14598    81 TrFRTDSGCYATTGLKIKH---LLTGQERTVW---HLQYTDWPEHGCPedlkgfLSYLEEIQSVRRHTNSTIDpkspnPP 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 901694078 1367 MIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVVLSLV 1431
Cdd:cd14598   155 VLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFL 219
fn3 pfam00041
Fibronectin type III domain;
313-401 1.83e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 58.58  E-value: 1.83e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078   313 SEPENVQADPENYTSLLVTWERPRVVyDAMIEKFAVLYQPLaGNDQAKHEFLTDGYQDlGAILNNLLPNMSYVLQIVAVC 392
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDG-NGPITGYEVEYRPK-NSGEPWNEITVPGTTT-SVTLTGLKPGTEYEVRVQAVN 77


                   ....*....
gi 901694078   393 SNGlYGKYS 401
Cdd:pfam00041   78 GGG-EGPPS 85
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
1041-1135 3.01e-09

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 56.90  E-value: 3.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1041 QYHYTQWPDMGVPEYS--LPVLAFVRKAAQAKRhavgPVVVHCSAGVGRTGT----YIVLDSM-LQQIqhegtvnifgfL 1113
Cdd:COG2453    49 EYLHLPIPDFGAPDDEqlQEAVDFIDEALREGK----KVLVHCRGGIGRTGTvaaaYLVLLGLsAEEA-----------L 113

                          90       100
                  ....*....|....*....|..
gi 901694078 1114 KHIRSQRNYLVQTEEQYVFIHD 1135
Cdd:COG2453   114 ARVRAARPGAVETPAQRAFLER 135
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 1193-1432 6.95e-09

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 58.82  E-value: 6.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1193 KQCNREKNRT---SSIIPVER---SRVGISSlsgeGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLV 1266
Cdd:PHA02740   44 KACAQAENKAkdeNLALHITRllhRRIKLFN----DEKVLDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQII 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1267 VMI---PDGQNMAEdefvYWPNKDEP-INCESFKVTLMSEEHKCLSNEEKLIVQDfileatQDDYVLEVRHFQCPKWP-- 1340
Cdd:PHA02740  120 VLIsrhADKKCFNQ----FWSLKEGCvITSDKFQIETLEIIIKPHFNLTLLSLTD------KFGQAQKISHFQYTAWPad 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1341 ----NPDSPISKTFELISII----KEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPG 1412
Cdd:PHA02740  190 gfshDPDAFIDFFCNIDDLCadleKHKADGKIAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYG 269

                         250       260
                  ....*....|....*....|
gi 901694078 1413 VFTDIEQYQFLYKVVLSLVS 1432
Cdd:PHA02740  270 CMNCLDDYVFCYHLIAAYLK 289
PLN02179 PLN02179
carbonic anhydrase
 49-253 1.39e-08

carbonic anhydrase


Pssm-ID: 177835  Cd Length: 235  Bit Score: 57.30  E-value: 1.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078   49 WGKKYP---ICNSPK-QSPInideDLTQVNVNLkkLKFQGWEKA-SLENTFIHNTGKTVEINLTNDyylsgglsekvfkA 123
Cdd:PLN02179   50 WGKLNPqwkVCSTGKyQSPI----DLTDERVSL--IHDQALSRHyKPAPAVIQSRGHDVMVSWKGD-------------A 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  124 SKITFHWG-----KCNVSSEgSEHSLEGQKFPLEMQVYCFDAdrfssfeeavkgKGRLRALSILFEVGvEENLDYKAIID 198
Cdd:PLN02179  111 GKITIHQTdyklvQCHWHSP-SEHTINGTSYDLELHMVHTSA------------SGKTAVVGVLYKLG-EPDEFLTKLLN 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 901694078  199 GTESVsrfGKQ----AALDPFVLQNllpnSTDKYYIYNGSLTSPPCTDTVEWIVFKDTV 253
Cdd:PLN02179  177 GIKGV---GKKeinlGIVDPRDIRF----ETNNFYRYIGSLTIPPCTEGVIWTVVKRVV 228
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 1059-1135 7.36e-08

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


Pssm-ID: 350344 [Multi-domain]  Cd Length: 113  Bit Score: 51.97  E-value: 7.36e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 901694078 1059 VLAFVRKAAQAKRHAvGPVVVHCSAGVGRTGTYIVLDSMLQQIqhegtVNIFGFLKHIRSQR-NYLVQTEEQYVFIHD 1135
Cdd:cd14494    42 VDRFLEVLDQAEKPG-EPVLVHCKAGVGRTGTLVACYLVLLGG-----MSAEEAVRIVRLIRpGGIPQTIEQLDFLIK 113
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 313-406 1.46e-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: 47.88  E-value: 1.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078  313 SEPENVQADPENYTSLLVTWERPRvVYDAMIEKFAVLYQPLAGNDQakHEFLTDGYQDLGAILNNLLPNMSYVLQIVAVC 392
Cdd:cd00063     2 SPPTNLRVTDVTSTSVTLSWTPPE-DDGGPITGYVVEYREKGSGDW--KEVEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78

                          90
                  ....*....|....
gi 901694078  393 SNGlYGKYSDQLIV 406
Cdd:cd00063    79 GGG-ESPPSESVTV 91
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 1042-1135 6.60e-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: 48.50  E-value: 6.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1042 YHYT-QWPDMGVPEYSLpVLAFVRKAAQAKRHAvGPVVVHCSAGVGRTG----TYIVldsMLQQIQHEGTVnifgflKHI 1116
Cdd:cd14506    78 YFYNfGWKDYGVPSLTT-ILDIVKVMAFALQEG-GKVAVHCHAGLGRTGvliaCYLV---YALRMSADQAI------RLV 146

                          90
                  ....*....|....*....
gi 901694078 1117 RSQRNYLVQTEEQYVFIHD 1135
Cdd:cd14506   147 RSKRPNSIQTRGQVLCVRE 165
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 313-395 8.96e-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: 45.30  E-value: 8.96e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078    313 SEPENVQADPENYTSLLVTWERPRvvyDAMIEKFAVLYQPLAGNDQAKHEFLTDGYQDLGAILNNLLPNMSYVLQIVAVC 392
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPP---DDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78


                    ...
gi 901694078    393 SNG 395
Cdd:smart00060   79 GAG 81
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 1040-1135 1.60e-05

cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of eukaryotic cyclin-dependent kinase inhibitor 3 (CDKN3) and related archaeal and bacterial proteins. CDKN3 is also known as kinase-associated phosphatase (KAP), CDK2-associated dual-specificity phosphatase, cyclin-dependent kinase interactor 1 (CDI1), or cyclin-dependent kinase-interacting protein 2 (CIP2). It has been characterized as dual-specificity phosphatase, which function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and protein-tyrosine-phosphatase (EC 3.1.3.48). It dephosphorylates CDK2 at a threonine residue in a cyclin-dependent manner, resulting in the inhibition of G1/S cell cycle progression. It also interacts with CDK1 and controls progression through mitosis by dephosphorylating CDC2. CDKN3 may also function as a tumor suppressor; its loss of function was found in a variety of cancers including glioblastoma and hepatocellular carcinoma. However, it has also been found over-expressed in many cancers such as breast, cervical, lung and prostate cancers, and may also have an oncogenic function.


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 46.87  E-value: 1.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1040 TQYHYTqWPDMGVP---EYSLPVLAFVRKAAQAKRHavgpVVVHCSAGVGRTGTyiVLDSMLQQIQ----HEGTVNIfgf 1112
Cdd:cd14505    74 TWHHLP-IPDGGVPsdiAQWQELLEELLSALENGKK----VLIHCKGGLGRTGL--IAACLLLELGdtldPEQAIAA--- 143

                          90       100
                  ....*....|....*....|...
gi 901694078 1113 lkhIRSQRNYLVQTEEQYVFIHD 1135
Cdd:cd14505   144 ---VRALRPGAIQTPKQENFLHQ 163
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 1041-1133 4.00e-05

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


Pssm-ID: 350354 [Multi-domain]  Cd Length: 142  Bit Score: 44.96  E-value: 4.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694078 1041 QYHYTQWPDMGVPEYSL--PVLAFVRKAaqakrHAVG-PVVVHCSAGVGRTGT----YIVLDSMLQQIQHegtvnifgfL 1113
Cdd:cd14504    51 RYHHIPIEDYTPPTLEQidEFLDIVEEA-----NAKNeAVLVHCLAGKGRTGTmlacYLVKTGKISAVDA---------I 116

                          90       100
                  ....*....|....*....|
gi 901694078 1114 KHIRSQRNYLVQTEEQYVFI 1133
Cdd:cd14504   117 NEIRRIRPGSIETSEQEKFV 136
PLN02202 PLN02202
carbonate dehydratase
 225-263 1.97e-03

carbonate dehydratase


Pssm-ID: 177853 [Multi-domain]  Cd Length: 284  Bit Score: 41.97  E-value: 1.97e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 901694078  225 TDKYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLAVF 263
Cdd:PLN02202  201 TRKYFRYIGSLTTPPCSENVSWTILGKVRSMSKEQVELL 239
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
1059-1119 2.61e-03

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 39.57  E-value: 2.61e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 901694078   1059 VLAFVRKAAQAKrhavGPVVVHCSAGVGRTGTYIVldSMLQQIQHEGTVNIFGFLKHIRSQ 1119
Cdd:smart00195   67 AVEFIEDAESKG----GKVLVHCQAGVSRSATLII--AYLMKTRNMSLNDAYDFVKDRRPI 121
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 1043-1092 5.95e-03

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


Pssm-ID: 350349 [Multi-domain]  Cd Length: 174  Bit Score: 39.36  E-value: 5.95e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 901694078 1043 HYtqwpDMGVPEYSLPVLAFVRKAAQAKRHAVGPVVVHCSAGVGRTGTYI 1092
Cdd:cd14499    82 HY----DLYFPDGSTPSDDIVKKFLDICENEKGAIAVHCKAGLGRTGTLI 127
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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