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Conserved domains on  [gi|6323927|ref|NP_013998|]
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orotate phosphoribosyltransferase URA10 [Saccharomyces cerevisiae S288C]

Protein Classification

type I phosphoribosyltransferase; uracil phosphoribosyltransferase( domain architecture ID 10794514)

type I phosphoribosyltransferase similar to phosphoribosyltransferases with specificities for hypoxanthine, guanine, and/or xanthine; uracil phosphoribosyltransferase catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
pyrE TIGR00336
orotate phosphoribosyltransferase; Orotate phosphoribosyltransferase (OPRTase) is involved in ...
 17-202 5.20e-83

orotate phosphoribosyltransferase; Orotate phosphoribosyltransferase (OPRTase) is involved in the biosynthesis of pyrimidine nucleotides. Alpha-D-ribosyldiphosphate 5-phosphate (PRPP) and orotate are utilized to form pyrophosphate and orotidine 5'-monophosphate (OMP) in the presence of divalent cations, preferably Mg2+. In a number of eukaryotes, this protein is fused to a domain that catalyses the reaction (EC 4.1.1.23). The combined activity of EC 2.4.2.10 and EC 4.1.1.23 is termed uridine 5'-monophosphate synthase. The conserved Lys (K) residue at position 101 of the seed alignment has been proposed as the active site for the enzyme. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


:

Pssm-ID: 129436 [Multi-domain]  Cd Length: 173  Bit Score: 244.64  E-value: 5.20e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323927     17 ELGLECKALRFGSFKLNSGRQSPYFFNLSLFNSGKLLANLATAYATAIIQSELKFDVIFGPAYKGIPLAAIVCVKLAEIG 96
Cdd:TIGR00336   1 ELLLEVQALKFGEFTLSSGRKSPYYFNIKLFNTGPELANLIARYAAAIIKSHLEFDVIAGPALGGIPIATAVSVKLAKPG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323927     97 GtkfqGIQYAFNRKKVKDHGEGGIIVGASLEDKRVLIIDDVMTAGTAINEAFEIISIAQGRVVGCIVALDRQEVihesdp 176
Cdd:TIGR00336  81 G----DIPLCFNRKEAKDHGEGGNIEGELLEGDKVVVVEDVITTGTSILEAVEIIQAAGGQVAGVIIAVDRQER------ 150

                         170       180
                  ....*....|....*....|....*.
gi 6323927    177 ertSATQSVSKRYNVPVLSIVSLTQV 202
Cdd:TIGR00336 151 ---SAGQEFEKEYGLPVISLITLKDL 173
 
Name Accession Description Interval E-value
pyrE TIGR00336
orotate phosphoribosyltransferase; Orotate phosphoribosyltransferase (OPRTase) is involved in ...
 17-202 5.20e-83

orotate phosphoribosyltransferase; Orotate phosphoribosyltransferase (OPRTase) is involved in the biosynthesis of pyrimidine nucleotides. Alpha-D-ribosyldiphosphate 5-phosphate (PRPP) and orotate are utilized to form pyrophosphate and orotidine 5'-monophosphate (OMP) in the presence of divalent cations, preferably Mg2+. In a number of eukaryotes, this protein is fused to a domain that catalyses the reaction (EC 4.1.1.23). The combined activity of EC 2.4.2.10 and EC 4.1.1.23 is termed uridine 5'-monophosphate synthase. The conserved Lys (K) residue at position 101 of the seed alignment has been proposed as the active site for the enzyme. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 129436 [Multi-domain]  Cd Length: 173  Bit Score: 244.64  E-value: 5.20e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323927     17 ELGLECKALRFGSFKLNSGRQSPYFFNLSLFNSGKLLANLATAYATAIIQSELKFDVIFGPAYKGIPLAAIVCVKLAEIG 96
Cdd:TIGR00336   1 ELLLEVQALKFGEFTLSSGRKSPYYFNIKLFNTGPELANLIARYAAAIIKSHLEFDVIAGPALGGIPIATAVSVKLAKPG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323927     97 GtkfqGIQYAFNRKKVKDHGEGGIIVGASLEDKRVLIIDDVMTAGTAINEAFEIISIAQGRVVGCIVALDRQEVihesdp 176
Cdd:TIGR00336  81 G----DIPLCFNRKEAKDHGEGGNIEGELLEGDKVVVVEDVITTGTSILEAVEIIQAAGGQVAGVIIAVDRQER------ 150

                         170       180
                  ....*....|....*....|....*.
gi 6323927    177 ertSATQSVSKRYNVPVLSIVSLTQV 202
Cdd:TIGR00336 151 ---SAGQEFEKEYGLPVISLITLKDL 173
pyrE PRK00455
orotate phosphoribosyltransferase; Validated
 9-227 2.01e-67

orotate phosphoribosyltransferase; Validated


Pssm-ID: 234771  Cd Length: 202  Bit Score: 206.16  E-value: 2.01e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323927     9 EEYQKTFLELGLECKALRFGSFKLNSGRQSPYFFNL-SLFNSGKLLANLATAYATAIIQSELKFDVIFGPAYKGIPLAAI 87
Cdd:PRK00455   2 KMYAREFIEFLLEIGALLFGHFTLSSGRKSPYYFDCrKLLSYPEALALLGRFLAEAIKDSGIEFDVVAGPATGGIPLAAA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323927    88 VCVKLaeiggtkfqGIQYAFNRKKVKDHGEGGIIVGASLEDKRVLIIDDVMTAGTAINEAFEIISIAQGRVVGCIVALDR 167
Cdd:PRK00455  82 VARAL---------DLPAIFVRKEAKDHGEGGQIEGRRLFGKRVLVVEDVITTGGSVLEAVEAIRAAGAEVVGVAVIVDR 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6323927   168 QevihesdpertSATQSVSKRYNVPVLSIVSLTQVVQF-MGNRLSPEQKSAIENYRKAYGI 227
Cdd:PRK00455 153 Q-----------SAAQEVFADAGVPLISLITLDDLLEYaEEGPLCKEGLPAVKAYRRNYGV 202
PyrE COG0461
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ...
 10-226 3.40e-61

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


Pssm-ID: 440229  Cd Length: 201  Bit Score: 190.37  E-value: 3.40e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323927   10 EYQKTFLELGLECKALRFGSFKLNSGRQSPYFFNLSLFNS-GKLLANLATAYATAIIQSELKFDVIFGPAYKGIPLAAIV 88
Cdd:COG0461   2 SYKEELAELLLEIGALLFGHFTLSSGRHSPYYIDCRLVLSyPEALELLGEALAELIKELGPEFDAVAGPATGGIPLAAAV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323927   89 CVKLaeiggtkfqGIQYAFNRKKVKDHGEGGIIVGASLEDKRVLIIDDVMTAGTAINEAFEIISIAQGRVVGCIVALDRQ 168
Cdd:COG0461  82 ARAL---------GLPAIFVRKEAKDHGTGGQIEGGLLPGERVLVVEDVITTGGSVLEAVEALREAGAEVVGVAVIVDRE 152

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323927  169 EvihesdpertSATQSVsKRYNVPVLSIVSLTQVVQFM--GNRLSPEQKSAIENYRKAYG 226
Cdd:COG0461 153 E----------GAAENL-EEAGVPLHSLLTLDDLLELLkeKGYIDPEELEALEAYREKPG 201
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 56-169 2.19e-18

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: 77.82  E-value: 2.19e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323927   56 LATAYATAIIQSELKFDVIFGPAYKGIPLAAIVCVKLaeiggtkfqGIQYAFNRKKVKDHGEGGI-------IVGASLED 128
Cdd:cd06223   1 AGRLLAEEIREDLLEPDVVVGILRGGLPLAAALARAL---------GLPLAFIRKERKGPGRTPSepyglelPLGGDVKG 71

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 6323927  129 KRVLIIDDVMTAGTAINEAFEIISIAQGRVVGCIVALDRQE 169
Cdd:cd06223  72 KRVLLVDDVIATGGTLLAAIELLKEAGAKVVGVAVLLDKPE 112
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 70-167 5.79e-10

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: 55.83  E-value: 5.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323927     70 KFDVIFGPAYKGIPLAAIVC----VKLAEIGGTKFQGIQYAfnrkkvkdhGEGGIIVGASLEDKRVLIIDDVMTAGTAIN 145
Cdd:pfam00156  29 KPDVVVGILRGGLPFAGILArrldVPLAFVRKVSYNPDTSE---------VMKTSSALPDLKGKTVLIVDDILDTGGTLL 99

                          90       100
                  ....*....|....*....|..
gi 6323927    146 EAFEIISIAQGRVVGCIVALDR 167
Cdd:pfam00156 100 KVLELLKNVGPKEVKIAVLIDK 121
 
Name Accession Description Interval E-value
pyrE TIGR00336
orotate phosphoribosyltransferase; Orotate phosphoribosyltransferase (OPRTase) is involved in ...
 17-202 5.20e-83

orotate phosphoribosyltransferase; Orotate phosphoribosyltransferase (OPRTase) is involved in the biosynthesis of pyrimidine nucleotides. Alpha-D-ribosyldiphosphate 5-phosphate (PRPP) and orotate are utilized to form pyrophosphate and orotidine 5'-monophosphate (OMP) in the presence of divalent cations, preferably Mg2+. In a number of eukaryotes, this protein is fused to a domain that catalyses the reaction (EC 4.1.1.23). The combined activity of EC 2.4.2.10 and EC 4.1.1.23 is termed uridine 5'-monophosphate synthase. The conserved Lys (K) residue at position 101 of the seed alignment has been proposed as the active site for the enzyme. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 129436 [Multi-domain]  Cd Length: 173  Bit Score: 244.64  E-value: 5.20e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323927     17 ELGLECKALRFGSFKLNSGRQSPYFFNLSLFNSGKLLANLATAYATAIIQSELKFDVIFGPAYKGIPLAAIVCVKLAEIG 96
Cdd:TIGR00336   1 ELLLEVQALKFGEFTLSSGRKSPYYFNIKLFNTGPELANLIARYAAAIIKSHLEFDVIAGPALGGIPIATAVSVKLAKPG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323927     97 GtkfqGIQYAFNRKKVKDHGEGGIIVGASLEDKRVLIIDDVMTAGTAINEAFEIISIAQGRVVGCIVALDRQEVihesdp 176
Cdd:TIGR00336  81 G----DIPLCFNRKEAKDHGEGGNIEGELLEGDKVVVVEDVITTGTSILEAVEIIQAAGGQVAGVIIAVDRQER------ 150

                         170       180
                  ....*....|....*....|....*.
gi 6323927    177 ertSATQSVSKRYNVPVLSIVSLTQV 202
Cdd:TIGR00336 151 ---SAGQEFEKEYGLPVISLITLKDL 173
pyrE PRK00455
orotate phosphoribosyltransferase; Validated
 9-227 2.01e-67

orotate phosphoribosyltransferase; Validated


Pssm-ID: 234771  Cd Length: 202  Bit Score: 206.16  E-value: 2.01e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323927     9 EEYQKTFLELGLECKALRFGSFKLNSGRQSPYFFNL-SLFNSGKLLANLATAYATAIIQSELKFDVIFGPAYKGIPLAAI 87
Cdd:PRK00455   2 KMYAREFIEFLLEIGALLFGHFTLSSGRKSPYYFDCrKLLSYPEALALLGRFLAEAIKDSGIEFDVVAGPATGGIPLAAA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323927    88 VCVKLaeiggtkfqGIQYAFNRKKVKDHGEGGIIVGASLEDKRVLIIDDVMTAGTAINEAFEIISIAQGRVVGCIVALDR 167
Cdd:PRK00455  82 VARAL---------DLPAIFVRKEAKDHGEGGQIEGRRLFGKRVLVVEDVITTGGSVLEAVEAIRAAGAEVVGVAVIVDR 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6323927   168 QevihesdpertSATQSVSKRYNVPVLSIVSLTQVVQF-MGNRLSPEQKSAIENYRKAYGI 227
Cdd:PRK00455 153 Q-----------SAAQEVFADAGVPLISLITLDDLLEYaEEGPLCKEGLPAVKAYRRNYGV 202
PyrE COG0461
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ...
 10-226 3.40e-61

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


Pssm-ID: 440229  Cd Length: 201  Bit Score: 190.37  E-value: 3.40e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323927   10 EYQKTFLELGLECKALRFGSFKLNSGRQSPYFFNLSLFNS-GKLLANLATAYATAIIQSELKFDVIFGPAYKGIPLAAIV 88
Cdd:COG0461   2 SYKEELAELLLEIGALLFGHFTLSSGRHSPYYIDCRLVLSyPEALELLGEALAELIKELGPEFDAVAGPATGGIPLAAAV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323927   89 CVKLaeiggtkfqGIQYAFNRKKVKDHGEGGIIVGASLEDKRVLIIDDVMTAGTAINEAFEIISIAQGRVVGCIVALDRQ 168
Cdd:COG0461  82 ARAL---------GLPAIFVRKEAKDHGTGGQIEGGLLPGERVLVVEDVITTGGSVLEAVEALREAGAEVVGVAVIVDRE 152

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323927  169 EvihesdpertSATQSVsKRYNVPVLSIVSLTQVVQFM--GNRLSPEQKSAIENYRKAYG 226
Cdd:COG0461 153 E----------GAAENL-EEAGVPLHSLLTLDDLLELLkeKGYIDPEELEALEAYREKPG 201
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 56-169 2.19e-18

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: 77.82  E-value: 2.19e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323927   56 LATAYATAIIQSELKFDVIFGPAYKGIPLAAIVCVKLaeiggtkfqGIQYAFNRKKVKDHGEGGI-------IVGASLED 128
Cdd:cd06223   1 AGRLLAEEIREDLLEPDVVVGILRGGLPLAAALARAL---------GLPLAFIRKERKGPGRTPSepyglelPLGGDVKG 71

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 6323927  129 KRVLIIDDVMTAGTAINEAFEIISIAQGRVVGCIVALDRQE 169
Cdd:cd06223  72 KRVLLVDDVIATGGTLLAAIELLKEAGAKVVGVAVLLDKPE 112
PRK02277 PRK02277
orotate phosphoribosyltransferase-like protein; Provisional
 49-168 8.01e-13

orotate phosphoribosyltransferase-like protein; Provisional


Pssm-ID: 235023 [Multi-domain]  Cd Length: 200  Bit Score: 64.89  E-value: 8.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323927    49 SGKLLANLATAYATAIIQSELKFDVIFGPAYKGIPLAAIVcvklAEIGGTKFqGIQYAFNRKKVKDHGEGGIIVG--ASL 126
Cdd:PRK02277  64 SSSRLRYIASAMADMLEKEDEEVDVVVGIAKSGVPLATLV----ADELGKDL-AIYHPKKWDHGEGEKKTGSFSRnfASV 138

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 6323927   127 EDKRVLIIDDVMTAGTAINEAFEIISIAQGRVVGCIVALDRQ 168
Cdd:PRK02277 139 EGKRCVIVDDVITSGTTMKETIEYLKEHGGKPVAVVVLIDKS 180
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 70-167 5.79e-10

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: 55.83  E-value: 5.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323927     70 KFDVIFGPAYKGIPLAAIVC----VKLAEIGGTKFQGIQYAfnrkkvkdhGEGGIIVGASLEDKRVLIIDDVMTAGTAIN 145
Cdd:pfam00156  29 KPDVVVGILRGGLPFAGILArrldVPLAFVRKVSYNPDTSE---------VMKTSSALPDLKGKTVLIVDDILDTGGTLL 99

                          90       100
                  ....*....|....*....|..
gi 6323927    146 EAFEIISIAQGRVVGCIVALDR 167
Cdd:pfam00156 100 KVLELLKNVGPKEVKIAVLIDK 121
Apt COG0503
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ...
 45-166 1.32e-09

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: 55.47  E-value: 1.32e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323927   45 SLFNSGKLLANLATAYATAIiqSELKFDVIFGPAYKGIPLAAIVCVKLaeiggtkfqGIQYAFNRKKVK----------- 113
Cdd:COG0503  25 PLLGDPELFRAAGDELAERF--ADKGIDKVVGIEARGFILAAALAYAL---------GVPFVPARKPGKlpgetvseeyd 93

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 6323927  114 -DHGEGGIIV---GASLEDKRVLIIDDVMTAGTAINEAFEIISIAQGRVVGCIVALD 166
Cdd:COG0503  94 lEYGTGDTLElhkDALKPGDRVLIVDDLLATGGTAKAAIKLVEEAGAEVVGIAFLIE 150
PRK05500 PRK05500
bifunctional orotidine-5'-phosphate decarboxylase/orotate phosphoribosyltransferase;
25-220 2.72e-08

bifunctional orotidine-5'-phosphate decarboxylase/orotate phosphoribosyltransferase;


Pssm-ID: 180119 [Multi-domain]  Cd Length: 477  Bit Score: 53.53  E-value: 2.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323927    25 LRFGSFKLNSGRQSPYFFNL-SLFNSGKLLANLATAYAtAIIQSeLKFDVIFGPAYKGIPLAAIVCVKLAEiggtkfqgi 103
Cdd:PRK05500 300 LLFGEYVQASGATFSYYIDLrKIISNPQLFHQVLSAYA-EILKN-LTFDRIAGIPYGSLPTATGLALHLHH--------- 368

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323927   104 QYAFNRKKVKDHGEGGIIVGASLEDKRVLIIDDVMTAGTAINEAFEIISIAqGRVVGCIVALdrqeVIHE---SDPERTS 180
Cdd:PRK05500 369 PMIFPRKEVKAHGTRRLIEGNFHPGETVVVVDDILITGKSVMEGAEKLKSA-GLNVRDIVVF----IDHEqgvKDKLQSH 443

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 6323927   181 ATQSVSkrynvpVLSIVSLTQVVqFMGNRLSPEQKSAIEN 220
Cdd:PRK05500 444 GYQAYS------VLTISEITETL-YQAGRINEEQYQALTE 476
PRK13809 PRK13809
orotate phosphoribosyltransferase; Provisional
 24-168 2.31e-05

orotate phosphoribosyltransferase; Provisional


Pssm-ID: 184340  Cd Length: 206  Bit Score: 43.67  E-value: 2.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323927    24 ALRFGSFKLNSGRQSPYFFNLSLFNSgklLANLATAYATAI--IQSELKFDVIFGPAYKGIPLAAivCVKLaeiggtKFQ 101
Cdd:PRK13809  22 AIKFGKFILASGEETPIYVDMRLVIS---SPEVLQTIATLIwrLRPSFNSSLLCGVPYTALTLAT--SISL------KYN 90

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6323927   102 gIQYAFNRKKVKDHGEGGIIVGASL--EDKRVLIIDDVMTAGTAINEAFEIISIAQGRVVGCIVALDRQ 168
Cdd:PRK13809  91 -IPMVLRRKELKNVDPSDAIKVEGLftPGQTCLVINDMVSSGKSIIETAVALEEEGLVVREALVFLDRQ 158
PRK07322 PRK07322
adenine phosphoribosyltransferase; Provisional
 70-171 5.37e-05

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 180928  Cd Length: 178  Bit Score: 42.27  E-value: 5.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323927    70 KFDVIFGPAYKGIPLAAIVCVKLaeiggtkfqGIQYAFNRKKVKDH--------------GEGGIIV-----GASLEDKR 130
Cdd:PRK07322  52 EVDVLVTPETKGIPLAHALSRRL---------GKPYVVARKSRKPYmqdpiiqevvsittGKPQLLVldgadAEKLKGKR 122

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 6323927   131 VLIIDDVMTAGTAINEAFEIISIAQGRVVGCIVAL------DRQEVI 171
Cdd:PRK07322 123 VAIVDDVVSTGGTLTALERLVERAGGQVVAKAAIFaegdasNRLDVI 169
ComFC COG1040
DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General ...
 123-163 9.94e-04

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


Pssm-ID: 440662 [Multi-domain]  Cd Length: 196  Bit Score: 38.65  E-value: 9.94e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 6323927  123 GASLEDKRVLIIDDVMTAGTAINEAFEIISIAQGRVVGCIV 163
Cdd:COG1040 150 PARLAGKHVLLVDDVLTTGATLAEAARALKAAGAARVDVLV 190
PRK02304 PRK02304
adenine phosphoribosyltransferase; Provisional
 52-169 2.49e-03

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 235028  Cd Length: 175  Bit Score: 37.36  E-value: 2.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323927    52 LLANlATAYATAIIQ-----SELKFDVIFGPAYKGIPLAAIVCVKLaeiggtkfqGIQYAFNRKKVK------------- 113
Cdd:PRK02304  29 LLAD-PEAFREVIDAlveryKDADIDKIVGIEARGFIFGAALAYKL---------GIGFVPVRKPGKlpretisesyele 98

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323927   114 ---DHGEggIIVGASLEDKRVLIIDDVM-TAGTAiNEAFEIISIAQGRVVGCIVALDRQE 169
Cdd:PRK02304  99 ygtDTLE--IHKDAIKPGDRVLIVDDLLaTGGTL-EAAIKLLERLGAEVVGAAFVIELPD 155
Hpt1 COG2236
Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism]; Hypoxanthine ...
 61-137 5.79e-03

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: 35.98  E-value: 5.79e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323927   61 ATAIIQSELKFDVIFGPAYKGIPLAAIVC----VKLAEIGGTKF-QGIQYAFNRKKVKDHgeggiiVGASLEDKRVLIID 135
Cdd:COG2236  22 AEQILESGFRPDVIVAIARGGLVPARILAdalgVPDLASIRVSSyTGTAKRLEEPVVKGP------LDEDLAGKRVLIVD 95


                ..
gi 6323927  136 DV 137
Cdd:COG2236  96 DV 97
 
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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