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Conserved domains on  [gi|515108943|ref|WP_016738030|]
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phosphoribosyltransferase [Gluconobacter thailandicus]

Protein Classification

type I phosphoribosyltransferase( domain architecture ID 27)

type I phosphoribosyltransferase similar to phosphoribosyltransferases with specificities for hypoxanthine, guanine, and/or xanthine

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRTases_typeI super family cl00309
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
1-214 1.31e-80

Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The type I PRTases are identified by a conserved PRPP binding motif which features two adjacent acidic residues surrounded by one or more hydrophobic residue. PRTases catalyze the displacement of the alpha-1'-pyrophosphate of 5-phosphoribosyl-alpha1-pyrophosphate (PRPP) by a nitrogen-containing nucleophile. The reaction products are an alpha-1 substituted ribose-5'-phosphate and a free pyrophosphate (PP). PRPP, an activated form of ribose-5-phosphate, is a key metabolite connecting nucleotide synthesis and salvage pathways. The type I PRTase family includes a range of diverse phosphoribosyl transferase enzymes and regulatory proteins of the nucleotide synthesis and salvage pathways, including adenine phosphoribosyltransferase EC:2.4.2.7., hypoxanthine-guanine-xanthine phosphoribosyltransferase, hypoxanthine phosphoribosyltransferase EC:2.4.2.8., ribose-phosphate pyrophosphokinase EC:2.7.6.1., amidophosphoribosyltransferase EC:2.4.2.14., orotate phosphoribosyltransferase EC:2.4.2.10., uracil phosphoribosyltransferase EC:2.4.2.9., and xanthine-guanine phosphoribosyltransferase EC:2.4.2.22.


The actual alignment was detected with superfamily member PRK06031:

Pssm-ID: 444823  Cd Length: 233  Bit Score: 240.43  E-value: 1.31e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515108943   1 MSTVPFWQHFAPDEDL--SAPYTDRFRVRFGAHR-LDLPLRVLPDGQKAVSSLLVNQASFPVMDALSENLTEIARSLAPD 77
Cdd:PRK06031   7 MAPHDFWQEIHPPGTFagDGPFRSSYPATLPDGRqLLLPIRGLPDGDRALASLIVNQASFEVLDALAEHLAEKARAFDPD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515108943  78 LIVGMPTLGLGLAATIARACGLERYVPLSTSRKFWYDERLSAPLSSITSPDKTKRLYLDPNLLPLLEaAKRIVIVDDVVS 157
Cdd:PRK06031  87 VVAGLPTLGLTLAAAVARKLGHTRYVPLGTSRKFWYRDELSVPLSSITTPDQGKRLYIDPRMLPLLE-GRRVALIDDVIS 165
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515108943 158 TGVSLEAGVRVLAATGVSPCAALCVMTQSKRWQ-------GKFSFPVMSCFSSPLFKRVGGGWV 214
Cdd:PRK06031 166 SGASIVAGLRLLAACGIEPAGIGAAMLQSERWReslaaagPQWPARVVGVFATPILERTAAGWW 229
 
Name Accession Description Interval E-value
PRK06031 PRK06031
phosphoribosyltransferase; Provisional
1-214 1.31e-80

phosphoribosyltransferase; Provisional


Pssm-ID: 235678  Cd Length: 233  Bit Score: 240.43  E-value: 1.31e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515108943   1 MSTVPFWQHFAPDEDL--SAPYTDRFRVRFGAHR-LDLPLRVLPDGQKAVSSLLVNQASFPVMDALSENLTEIARSLAPD 77
Cdd:PRK06031   7 MAPHDFWQEIHPPGTFagDGPFRSSYPATLPDGRqLLLPIRGLPDGDRALASLIVNQASFEVLDALAEHLAEKARAFDPD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515108943  78 LIVGMPTLGLGLAATIARACGLERYVPLSTSRKFWYDERLSAPLSSITSPDKTKRLYLDPNLLPLLEaAKRIVIVDDVVS 157
Cdd:PRK06031  87 VVAGLPTLGLTLAAAVARKLGHTRYVPLGTSRKFWYRDELSVPLSSITTPDQGKRLYIDPRMLPLLE-GRRVALIDDVIS 165
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515108943 158 TGVSLEAGVRVLAATGVSPCAALCVMTQSKRWQ-------GKFSFPVMSCFSSPLFKRVGGGWV 214
Cdd:PRK06031 166 SGASIVAGLRLLAACGIEPAGIGAAMLQSERWReslaaagPQWPARVVGVFATPILERTAAGWW 229
Apt COG0503
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ...
33-186 3.14e-20

Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide transport and metabolism]; Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein is part of the Pathway/BioSystem: Purine salvage


Pssm-ID: 440269  Cd Length: 171  Bit Score: 83.59  E-value: 3.14e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515108943  33 LDLPlRVLPDGQ--KAVSSLLVNqasFPVMDALSENLTEIARSLAPDLIVGMPTLGLGLAATIARACGLeRYVPLSTSRK 110
Cdd:COG0503    8 RDIP-DFPKPGIlfRDITPLLGD---PELFRAAGDELAERFADKGIDKVVGIEARGFILAAALAYALGV-PFVPARKPGK 82
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515108943 111 FWYDErLSAPLSSITSPDKTkrLYLDPNLLPlleAAKRIVIVDDVVSTGVSLEAGVRVLAATGVSPCAALCVMTQS 186
Cdd:COG0503   83 LPGET-VSEEYDLEYGTGDT--LELHKDALK---PGDRVLIVDDLLATGGTAKAAIKLVEEAGAEVVGIAFLIELG 152
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
76-202 2.16e-11

Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The type I PRTases are identified by a conserved PRPP binding motif which features two adjacent acidic residues surrounded by one or more hydrophobic residue. PRTases catalyze the displacement of the alpha-1'-pyrophosphate of 5-phosphoribosyl-alpha1-pyrophosphate (PRPP) by a nitrogen-containing nucleophile. The reaction products are an alpha-1 substituted ribose-5'-phosphate and a free pyrophosphate (PP). PRPP, an activated form of ribose-5-phosphate, is a key metabolite connecting nucleotide synthesis and salvage pathways. The type I PRTase family includes a range of diverse phosphoribosyl transferase enzymes and regulatory proteins of the nucleotide synthesis and salvage pathways, including adenine phosphoribosyltransferase EC:2.4.2.7., hypoxanthine-guanine-xanthine phosphoribosyltransferase, hypoxanthine phosphoribosyltransferase EC:2.4.2.8., ribose-phosphate pyrophosphokinase EC:2.7.6.1., amidophosphoribosyltransferase EC:2.4.2.14., orotate phosphoribosyltransferase EC:2.4.2.10., uracil phosphoribosyltransferase EC:2.4.2.9., and xanthine-guanine phosphoribosyltransferase EC:2.4.2.22.


Pssm-ID: 206754 [Multi-domain]  Cd Length: 130  Bit Score: 59.33  E-value: 2.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515108943  76 PDLIVGMPTLGLGLAATIARACGLeRYVPLSTSRKfwyderlsaplssiTSPDKTKRLYLDPNLLPLLEAAKRIVIVDDV 155
Cdd:cd06223   16 PDVVVGILRGGLPLAAALARALGL-PLAFIRKERK--------------GPGRTPSEPYGLELPLGGDVKGKRVLLVDDV 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 515108943 156 VSTGVSLEAGVRVLAATGVSPCAALCVMTQSKRWQGKFSFPVMSCFS 202
Cdd:cd06223   81 IATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGGARELASPGDPVYS 127
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
76-182 6.43e-08

Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl transferase enzymes. This family includes: Adenine phosphoribosyl-transferase EC:2.4.2.7. Hypoxanthine-guanine-xanthine phosphoribosyl-transferase. Hypoxanthine phosphoribosyl-transferase EC:2.4.2.8. Ribose-phosphate pyrophosphokinase i EC:2.7.6.1. Amidophosphoribosyltransferase EC:2.4.2.14. Orotate phosphoribosyl-transferase EC:2.4.2.10. Uracil phosphoribosyl-transferase EC:2.4.2.9. Xanthine-guanine phosphoribosyl-transferase EC:2.4.2.22. In Arabidopsis, At the very N-terminus of this domain is the P-Loop NTPase domain.


Pssm-ID: 425489 [Multi-domain]  Cd Length: 150  Bit Score: 50.06  E-value: 6.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515108943   76 PDLIVGMPTLGLGLAATIARacglERYVPLSTSRKFWYDERLSAPLssitspdktkrlyLDPNLLPLLEAaKRIVIVDDV 155
Cdd:pfam00156  30 PDVVVGILRGGLPFAGILAR----RLDVPLAFVRKVSYNPDTSEVM-------------KTSSALPDLKG-KTVLIVDDI 91
                          90       100
                  ....*....|....*....|....*..
gi 515108943  156 VSTGVSLEAGVRVLAATGVSpCAALCV 182
Cdd:pfam00156  92 LDTGGTLLKVLELLKNVGPK-EVKIAV 117
 
Name Accession Description Interval E-value
PRK06031 PRK06031
phosphoribosyltransferase; Provisional
1-214 1.31e-80

phosphoribosyltransferase; Provisional


Pssm-ID: 235678  Cd Length: 233  Bit Score: 240.43  E-value: 1.31e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515108943   1 MSTVPFWQHFAPDEDL--SAPYTDRFRVRFGAHR-LDLPLRVLPDGQKAVSSLLVNQASFPVMDALSENLTEIARSLAPD 77
Cdd:PRK06031   7 MAPHDFWQEIHPPGTFagDGPFRSSYPATLPDGRqLLLPIRGLPDGDRALASLIVNQASFEVLDALAEHLAEKARAFDPD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515108943  78 LIVGMPTLGLGLAATIARACGLERYVPLSTSRKFWYDERLSAPLSSITSPDKTKRLYLDPNLLPLLEaAKRIVIVDDVVS 157
Cdd:PRK06031  87 VVAGLPTLGLTLAAAVARKLGHTRYVPLGTSRKFWYRDELSVPLSSITTPDQGKRLYIDPRMLPLLE-GRRVALIDDVIS 165
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515108943 158 TGVSLEAGVRVLAATGVSPCAALCVMTQSKRWQ-------GKFSFPVMSCFSSPLFKRVGGGWV 214
Cdd:PRK06031 166 SGASIVAGLRLLAACGIEPAGIGAAMLQSERWReslaaagPQWPARVVGVFATPILERTAAGWW 229
Apt COG0503
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ...
33-186 3.14e-20

Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide transport and metabolism]; Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein is part of the Pathway/BioSystem: Purine salvage


Pssm-ID: 440269  Cd Length: 171  Bit Score: 83.59  E-value: 3.14e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515108943  33 LDLPlRVLPDGQ--KAVSSLLVNqasFPVMDALSENLTEIARSLAPDLIVGMPTLGLGLAATIARACGLeRYVPLSTSRK 110
Cdd:COG0503    8 RDIP-DFPKPGIlfRDITPLLGD---PELFRAAGDELAERFADKGIDKVVGIEARGFILAAALAYALGV-PFVPARKPGK 82
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515108943 111 FWYDErLSAPLSSITSPDKTkrLYLDPNLLPlleAAKRIVIVDDVVSTGVSLEAGVRVLAATGVSPCAALCVMTQS 186
Cdd:COG0503   83 LPGET-VSEEYDLEYGTGDT--LELHKDALK---PGDRVLIVDDLLATGGTAKAAIKLVEEAGAEVVGIAFLIELG 152
PRK07322 PRK07322
adenine phosphoribosyltransferase; Provisional
21-207 4.25e-13

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 180928  Cd Length: 178  Bit Score: 65.00  E-value: 4.25e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515108943  21 TDRFRVRFGAHRLDLPL-RVLPDGqkAVssllvnqASFpVMDALSENLTEIARSLAP------DLIVGMPTLGLGLAATI 93
Cdd:PRK07322   1 METYPLTVGGVTRELPLiRVGPDL--AI-------ALF-VILGDTELTEAAAEALAKrlptevDVLVTPETKGIPLAHAL 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515108943  94 ARACGLErYVPLSTSRKFWYDERLSAPLSSITSpDKTKRLYLDPNLLPLLEAaKRIVIVDDVVSTGVSLEAGVRVLAATG 173
Cdd:PRK07322  71 SRRLGKP-YVVARKSRKPYMQDPIIQEVVSITT-GKPQLLVLDGADAEKLKG-KRVAIVDDVVSTGGTLTALERLVERAG 147
                        170       180       190
                 ....*....|....*....|....*....|....
gi 515108943 174 VSPCAALCVMTQSKRWQGKfsfPVMSCFSSPLFK 207
Cdd:PRK07322 148 GQVVAKAAIFAEGDASNRL---DVIYLAHLPLFP 178
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
76-202 2.16e-11

Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The type I PRTases are identified by a conserved PRPP binding motif which features two adjacent acidic residues surrounded by one or more hydrophobic residue. PRTases catalyze the displacement of the alpha-1'-pyrophosphate of 5-phosphoribosyl-alpha1-pyrophosphate (PRPP) by a nitrogen-containing nucleophile. The reaction products are an alpha-1 substituted ribose-5'-phosphate and a free pyrophosphate (PP). PRPP, an activated form of ribose-5-phosphate, is a key metabolite connecting nucleotide synthesis and salvage pathways. The type I PRTase family includes a range of diverse phosphoribosyl transferase enzymes and regulatory proteins of the nucleotide synthesis and salvage pathways, including adenine phosphoribosyltransferase EC:2.4.2.7., hypoxanthine-guanine-xanthine phosphoribosyltransferase, hypoxanthine phosphoribosyltransferase EC:2.4.2.8., ribose-phosphate pyrophosphokinase EC:2.7.6.1., amidophosphoribosyltransferase EC:2.4.2.14., orotate phosphoribosyltransferase EC:2.4.2.10., uracil phosphoribosyltransferase EC:2.4.2.9., and xanthine-guanine phosphoribosyltransferase EC:2.4.2.22.


Pssm-ID: 206754 [Multi-domain]  Cd Length: 130  Bit Score: 59.33  E-value: 2.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515108943  76 PDLIVGMPTLGLGLAATIARACGLeRYVPLSTSRKfwyderlsaplssiTSPDKTKRLYLDPNLLPLLEAAKRIVIVDDV 155
Cdd:cd06223   16 PDVVVGILRGGLPLAAALARALGL-PLAFIRKERK--------------GPGRTPSEPYGLELPLGGDVKGKRVLLVDDV 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 515108943 156 VSTGVSLEAGVRVLAATGVSPCAALCVMTQSKRWQGKFSFPVMSCFS 202
Cdd:cd06223   81 IATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGGARELASPGDPVYS 127
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
76-182 6.43e-08

Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl transferase enzymes. This family includes: Adenine phosphoribosyl-transferase EC:2.4.2.7. Hypoxanthine-guanine-xanthine phosphoribosyl-transferase. Hypoxanthine phosphoribosyl-transferase EC:2.4.2.8. Ribose-phosphate pyrophosphokinase i EC:2.7.6.1. Amidophosphoribosyltransferase EC:2.4.2.14. Orotate phosphoribosyl-transferase EC:2.4.2.10. Uracil phosphoribosyl-transferase EC:2.4.2.9. Xanthine-guanine phosphoribosyl-transferase EC:2.4.2.22. In Arabidopsis, At the very N-terminus of this domain is the P-Loop NTPase domain.


Pssm-ID: 425489 [Multi-domain]  Cd Length: 150  Bit Score: 50.06  E-value: 6.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515108943   76 PDLIVGMPTLGLGLAATIARacglERYVPLSTSRKFWYDERLSAPLssitspdktkrlyLDPNLLPLLEAaKRIVIVDDV 155
Cdd:pfam00156  30 PDVVVGILRGGLPFAGILAR----RLDVPLAFVRKVSYNPDTSEVM-------------KTSSALPDLKG-KTVLIVDDI 91
                          90       100
                  ....*....|....*....|....*..
gi 515108943  156 VSTGVSLEAGVRVLAATGVSpCAALCV 182
Cdd:pfam00156  92 LDTGGTLLKVLELLKNVGPK-EVKIAV 117
PyrE COG0461
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ...
67-182 2.02e-05

Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate phosphoribosyltransferase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 440229  Cd Length: 201  Bit Score: 43.60  E-value: 2.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515108943  67 LTEIARSLA---------PDLIVGMPTLGLGLAATIARACGLeryvPLSTSRKfwyderlsaplssitSPDK--TKRLyl 135
Cdd:COG0461   46 LELLGEALAelikelgpeFDAVAGPATGGIPLAAAVARALGL----PAIFVRK---------------EAKDhgTGGQ-- 104
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 515108943 136 dpnLLPLLEAAKRIVIVDDVVSTGVSLEAGVRVLAATGVSPCAALCV 182
Cdd:COG0461  105 ---IEGGLLPGERVLVVEDVITTGGSVLEAVEALREAGAEVVGVAVI 148
Hpt1 COG2236
Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism]; Hypoxanthine ...
61-173 4.27e-05

Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism]; Hypoxanthine phosphoribosyltransferase is part of the Pathway/BioSystem: Purine salvage


Pssm-ID: 441837 [Multi-domain]  Cd Length: 153  Bit Score: 42.14  E-value: 4.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515108943  61 DALSENLTE-IARS-LAPDLIVGMPTLGLGLAATIARACGLERYVPLSTSrkFWYDERLSAPLSSITSPdktkrlyldpn 138
Cdd:COG2236   15 HELSRRLAEqILESgFRPDVIVAIARGGLVPARILADALGVPDLASIRVS--SYTGTAKRLEEPVVKGP----------- 81
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 515108943 139 lLPLLEAAKRIVIVDDVVSTGVSLEAGVRVLAATG 173
Cdd:COG2236   82 -LDEDLAGKRVLIVDDVADTGRTLEAVRDLLKEAG 115
ComFC COG1040
DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General ...
145-182 1.74e-04

DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General function prediction only];


Pssm-ID: 440662 [Multi-domain]  Cd Length: 196  Bit Score: 40.96  E-value: 1.74e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 515108943 145 AAKRIVIVDDVVSTGVSLEAGVRVLAATGVSPCAALCV 182
Cdd:COG1040  154 AGKHVLLVDDVLTTGATLAEAARALKAAGAARVDVLVL 191
PRK02277 PRK02277
orotate phosphoribosyltransferase-like protein; Provisional
64-188 1.86e-04

orotate phosphoribosyltransferase-like protein; Provisional


Pssm-ID: 235023 [Multi-domain]  Cd Length: 200  Bit Score: 41.01  E-value: 1.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515108943  64 SENLTEIARSLA---------PDLIVGMPTLGLGLAATIARACGLER--YVPlstsRKFWYDER------LSAPLSSIts 126
Cdd:PRK02277  65 SSRLRYIASAMAdmlekedeeVDVVVGIAKSGVPLATLVADELGKDLaiYHP----KKWDHGEGekktgsFSRNFASV-- 138
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515108943 127 pdktkrlyldpnllplleAAKRIVIVDDVVSTGVSLEAGVRVLAATGVSPCAalCVMTQSKR 188
Cdd:PRK02277 139 ------------------EGKRCVIVDDVITSGTTMKETIEYLKEHGGKPVA--VVVLIDKS 180
pyrE PRK00455
orotate phosphoribosyltransferase; Validated
59-182 2.41e-04

orotate phosphoribosyltransferase; Validated


Pssm-ID: 234771  Cd Length: 202  Bit Score: 40.53  E-value: 2.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515108943  59 VMDALSENLTEIArsLAPDLIVGMPTLGLGLAATIARACGLeryvplstsrKFWYDERlsaplssitspdKTKRLYLDPN 138
Cdd:PRK00455  50 LGRFLAEAIKDSG--IEFDVVAGPATGGIPLAAAVARALDL----------PAIFVRK------------EAKDHGEGGQ 105
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 515108943 139 LLPLLEAAKRIVIVDDVVSTGVS-LEAgVRVLAATGVSPCAALCV 182
Cdd:PRK00455 106 IEGRRLFGKRVLVVEDVITTGGSvLEA-VEAIRAAGAEVVGVAVI 149
 
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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