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Conserved domains on  [gi|489054474|ref|WP_002964645|]
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MULTISPECIES: adenine phosphoribosyltransferase [Brucella]

Protein Classification

purine phosphoribosyltransferase family protein( domain architecture ID 10011795)

purine phosphoribosyltransferase family protein similar to adenine phosphoribosyltransferase and hypoxanthine/guanine phosphoribosyltransferase

EC:  2.4.2.-
Gene Ontology:  GO:0106130|GO:0016757
PubMed:  11751055|7030616

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PRK02304 PRK02304
adenine phosphoribosyltransferase; Provisional
 9-180 9.41e-85

adenine phosphoribosyltransferase; Provisional


:

Pssm-ID: 235028  Cd Length: 175  Bit Score: 247.30  E-value: 9.41e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054474   9 LKDAIRTIPDYPKPGVQFRDVTTLMGNAQAFRRAVDELVYPYAGNRIDKVAGIEARGFILGGAIAHQLSAGFVPIRKKGK 88
Cdd:PRK02304   6 LKSSIRTIPDFPKPGILFRDITPLLADPEAFREVIDALVERYKDADIDKIVGIEARGFIFGAALAYKLGIGFVPVRKPGK 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054474  89 LPRDTVRIAYSLEYGVDEMEMHRDAIEKGERVVLVDDLIATGGTAEAAAKLLLQMGAEIVAACFIIDLPDLGGRKKLEal 168
Cdd:PRK02304  86 LPRETISESYELEYGTDTLEIHKDAIKPGDRVLIVDDLLATGGTLEAAIKLLERLGAEVVGAAFVIELPDLGGREKLE-- 163

                        170
                 ....*....|..
gi 489054474 169 GLPVRTLVAFEG 180
Cdd:PRK02304 164 GYPVKSLVKFDG 175
 
Name Accession Description Interval E-value
PRK02304 PRK02304
adenine phosphoribosyltransferase; Provisional
 9-180 9.41e-85

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 235028  Cd Length: 175  Bit Score: 247.30  E-value: 9.41e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054474   9 LKDAIRTIPDYPKPGVQFRDVTTLMGNAQAFRRAVDELVYPYAGNRIDKVAGIEARGFILGGAIAHQLSAGFVPIRKKGK 88
Cdd:PRK02304   6 LKSSIRTIPDFPKPGILFRDITPLLADPEAFREVIDALVERYKDADIDKIVGIEARGFIFGAALAYKLGIGFVPVRKPGK 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054474  89 LPRDTVRIAYSLEYGVDEMEMHRDAIEKGERVVLVDDLIATGGTAEAAAKLLLQMGAEIVAACFIIDLPDLGGRKKLEal 168
Cdd:PRK02304  86 LPRETISESYELEYGTDTLEIHKDAIKPGDRVLIVDDLLATGGTLEAAIKLLERLGAEVVGAAFVIELPDLGGREKLE-- 163

                        170
                 ....*....|..
gi 489054474 169 GLPVRTLVAFEG 180
Cdd:PRK02304 164 GYPVKSLVKFDG 175
apt TIGR01090
adenine phosphoribosyltransferase; A phylogenetic analysis suggested omitting the ...
 9-178 1.85e-72

adenine phosphoribosyltransferase; A phylogenetic analysis suggested omitting the bi-directional best hit homologs from the spirochetes from the seed for this model and making only tentative predictions of adenine phosphoribosyltransferase function for this lineage. The trusted cutoff score is made high for this reason. Most proteins scoring between the trusted and noise cutoffs are likely to act as adenine phosphotransferase. [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 273437  Cd Length: 169  Bit Score: 215.99  E-value: 1.85e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054474    9 LKDAIRTIPDYPKPGVQFRDVTTLMGNAQAFRRAVDELVYPYAGNRIDKVAGIEARGFILGGAIAHQLSAGFVPIRKKGK 88
Cdd:TIGR01090   1 LKQAIRSIPDFPKKGILFRDITPLLNNPELFRFLIDLLVERYKDANIDYIVGPEARGFIFGAALAYKLGVGFVPVRKPGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054474   89 LPRDTVRIAYSLEYGVDEMEMHRDAIEKGERVVLVDDLIATGGTAEAAAKLLLQMGAEIVAACFIIDLPDLGGRKKLEAL 168
Cdd:TIGR01090  81 LPGETISASYDLEYGKDVLEIHKDAIKPGQRVLIVDDLLATGGTAAATDELIKKLGGEVVEAAFLIELKDLNGRAKLEPN 160

                         170
                  ....*....|
gi 489054474  169 gLPVRTLVAF 178
Cdd:TIGR01090 161 -VPVFSLLEY 169
Apt COG0503
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ...
 8-178 1.02e-69

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: 208.78  E-value: 1.02e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054474   8 TLKDAIRTIPDYPKPGVQFRDVTTLMGNAQAFRRAVDELVYPYAGNRIDKVAGIEARGFILGGAIAHQLSAGFVPIRKKG 87
Cdd:COG0503    2 DLKDLIRDIPDFPKPGILFRDITPLLGDPELFRAAGDELAERFADKGIDKVVGIEARGFILAAALAYALGVPFVPARKPG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054474  88 KLPRDTVRIAYSLEYG-VDEMEMHRDAIEKGERVVLVDDLIATGGTAEAAAKLLLQMGAEIVAACFIIDLPDLGGRKKLE 166
Cdd:COG0503   82 KLPGETVSEEYDLEYGtGDTLELHKDALKPGDRVLIVDDLLATGGTAKAAIKLVEEAGAEVVGIAFLIELGFLGGREKLR 161

                        170
                 ....*....|..
gi 489054474 167 alGLPVRTLVAF 178
Cdd:COG0503  162 --DYPVESLLTL 171
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 52-175 2.62e-15

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: 68.58  E-value: 2.62e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054474  52 GNRIDKVAGIEARGFILGGAIAHQLSAGFVPIRKKGKLPRDTVRIAYsleygvdEMEMHRDAIEKGERVVLVDDLIATGG 131
Cdd:cd06223   13 LLEPDVVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPSEPY-------GLELPLGGDVKGKRVLLVDDVIATGG 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 489054474 132 TAEAAAKLLLQMGAEIVAACFIIDLPDlGGRKKLEALGLPVRTL 175
Cdd:cd06223   86 TLLAAIELLKEAGAKVVGVAVLLDKPE-GGARELASPGDPVYSL 128
HPT_Archaea NF040646
hypoxanthine/guanine phosphoribosyltransferase;
40-176 1.62e-11

hypoxanthine/guanine phosphoribosyltransferase;


Pssm-ID: 468613  Cd Length: 184  Bit Score: 59.93  E-value: 1.62e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054474  40 RRAVDELVyPYAGNRIDKVAGIEARGFILGGAIAHQLSAGFVPIRK-KGKLPRDtvrIAYSLEYGVDEMEMHRDAIEKGE 118
Cdd:NF040646  40 REIADRII-KIADLDVDKIVTVEAMGIPIATALSLKTDIPLVIIRKrKYGLPGE---VEVHQSTGYSKGELYINGINKGD 115

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489054474 119 RVVLVDDLIATGGTAEAAAKLLLQMGAEIVAACFIIDLPDlgGRKKLE-ALGLPVRTLV 176
Cdd:NF040646 116 RVLIVDDVISTGGTLIAVIKALEKAGAEIKDVVVVIERGE--GKKIVEeKTGYKVKTLV 172
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 35-155 3.38e-07

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: 47.36  E-value: 3.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054474   35 NAQAFRRAVDEL---VYPYAGNRIDKVAGIEARGFILGGAIAHQLSAGFVPIRKKGKLPRDTVRIAYSleygvdememHR 111
Cdd:pfam00156   7 DNPAILKAVARLaaqINEDYGGKPDVVVGILRGGLPFAGILARRLDVPLAFVRKVSYNPDTSEVMKTS----------SA 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 489054474  112 DAIEKGERVVLVDDLIATGGTAEAAAKLLLQMGAEIVAACFIID 155
Cdd:pfam00156  77 LPDLKGKTVLIVDDILDTGGTLLKVLELLKNVGPKEVKIAVLID 120
 
Name Accession Description Interval E-value
PRK02304 PRK02304
adenine phosphoribosyltransferase; Provisional
 9-180 9.41e-85

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 235028  Cd Length: 175  Bit Score: 247.30  E-value: 9.41e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054474   9 LKDAIRTIPDYPKPGVQFRDVTTLMGNAQAFRRAVDELVYPYAGNRIDKVAGIEARGFILGGAIAHQLSAGFVPIRKKGK 88
Cdd:PRK02304   6 LKSSIRTIPDFPKPGILFRDITPLLADPEAFREVIDALVERYKDADIDKIVGIEARGFIFGAALAYKLGIGFVPVRKPGK 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054474  89 LPRDTVRIAYSLEYGVDEMEMHRDAIEKGERVVLVDDLIATGGTAEAAAKLLLQMGAEIVAACFIIDLPDLGGRKKLEal 168
Cdd:PRK02304  86 LPRETISESYELEYGTDTLEIHKDAIKPGDRVLIVDDLLATGGTLEAAIKLLERLGAEVVGAAFVIELPDLGGREKLE-- 163

                        170
                 ....*....|..
gi 489054474 169 GLPVRTLVAFEG 180
Cdd:PRK02304 164 GYPVKSLVKFDG 175
apt TIGR01090
adenine phosphoribosyltransferase; A phylogenetic analysis suggested omitting the ...
 9-178 1.85e-72

adenine phosphoribosyltransferase; A phylogenetic analysis suggested omitting the bi-directional best hit homologs from the spirochetes from the seed for this model and making only tentative predictions of adenine phosphoribosyltransferase function for this lineage. The trusted cutoff score is made high for this reason. Most proteins scoring between the trusted and noise cutoffs are likely to act as adenine phosphotransferase. [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 273437  Cd Length: 169  Bit Score: 215.99  E-value: 1.85e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054474    9 LKDAIRTIPDYPKPGVQFRDVTTLMGNAQAFRRAVDELVYPYAGNRIDKVAGIEARGFILGGAIAHQLSAGFVPIRKKGK 88
Cdd:TIGR01090   1 LKQAIRSIPDFPKKGILFRDITPLLNNPELFRFLIDLLVERYKDANIDYIVGPEARGFIFGAALAYKLGVGFVPVRKPGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054474   89 LPRDTVRIAYSLEYGVDEMEMHRDAIEKGERVVLVDDLIATGGTAEAAAKLLLQMGAEIVAACFIIDLPDLGGRKKLEAL 168
Cdd:TIGR01090  81 LPGETISASYDLEYGKDVLEIHKDAIKPGQRVLIVDDLLATGGTAAATDELIKKLGGEVVEAAFLIELKDLNGRAKLEPN 160

                         170
                  ....*....|
gi 489054474  169 gLPVRTLVAF 178
Cdd:TIGR01090 161 -VPVFSLLEY 169
Apt COG0503
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ...
 8-178 1.02e-69

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: 208.78  E-value: 1.02e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054474   8 TLKDAIRTIPDYPKPGVQFRDVTTLMGNAQAFRRAVDELVYPYAGNRIDKVAGIEARGFILGGAIAHQLSAGFVPIRKKG 87
Cdd:COG0503    2 DLKDLIRDIPDFPKPGILFRDITPLLGDPELFRAAGDELAERFADKGIDKVVGIEARGFILAAALAYALGVPFVPARKPG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054474  88 KLPRDTVRIAYSLEYG-VDEMEMHRDAIEKGERVVLVDDLIATGGTAEAAAKLLLQMGAEIVAACFIIDLPDLGGRKKLE 166
Cdd:COG0503   82 KLPGETVSEEYDLEYGtGDTLELHKDALKPGDRVLIVDDLLATGGTAKAAIKLVEEAGAEVVGIAFLIELGFLGGREKLR 161

                        170
                 ....*....|..
gi 489054474 167 alGLPVRTLVAF 178
Cdd:COG0503  162 --DYPVESLLTL 171
PLN02293 PLN02293
adenine phosphoribosyltransferase
 9-181 1.66e-59

adenine phosphoribosyltransferase


Pssm-ID: 177930  Cd Length: 187  Bit Score: 183.72  E-value: 1.66e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054474   9 LKDAIRTIPDYPKPGVQFRDVTTLMGNAQAFRRAVDELVYPYAGNRIDKVAGIEARGFILGGAIAHQLSAGFVPIRKKGK 88
Cdd:PLN02293  17 ISSAIRVVPDFPKPGIMFQDITTLLLDPKAFKDTIDLFVERYRDMGISVVAGIEARGFIFGPPIALAIGAKFVPLRKPGK 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054474  89 LPRDTVRIAYSLEYGVDEMEMHRDAIEKGERVVLVDDLIATGGTAEAAAKLLLQMGAEIVAACFIIDLPDLGGRKKLEal 168
Cdd:PLN02293  97 LPGEVISEEYVLEYGTDCLEMHVGAVEPGERALVIDDLIATGGTLCAAINLLERAGAEVVECACVIELPELKGREKLN-- 174

                        170
                 ....*....|...
gi 489054474 169 GLPVRTLVAFEGD 181
Cdd:PLN02293 175 GKPLFVLVESRGI 187
PRK12560 PRK12560
adenine phosphoribosyltransferase; Provisional
 9-176 1.80e-24

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 183595  Cd Length: 187  Bit Score: 94.08  E-value: 1.80e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054474   9 LKDAIRTIPDYPKPGV--QFRDVTTLMgNAQAFRRAVDElVYPYAGNRIDKVAGIEARGFILGGAIAHqlsAGFVPIRKK 86
Cdd:PRK12560   6 LYKNARVVNSGKALTTvnEFTDQLPAL-RPKVLKETAKE-IIKYIDKDIDKIVTEEDKGAPLATPVSL---LSGKPLAMA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054474  87 GKLPRDTVRIAYS-LEYGVDEME--MHRDAIEKGERVVLVDDLIATGGTAEAAAKLLLQMGAEIVAACFIIDLPDLGGRK 163
Cdd:PRK12560  81 RWYPYSLSELNYNvVEIGSEYFEgvVYLNGIEKGDRVAIIDDTLSTGGTVIALIKAIENSGGIVSDVICVIEKTQNNGRK 160

                        170
                 ....*....|....
gi 489054474 164 KL-EALGLPVRTLV 176
Cdd:PRK12560 161 KLfTQTGINVKSLV 174
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 52-175 2.62e-15

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: 68.58  E-value: 2.62e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054474  52 GNRIDKVAGIEARGFILGGAIAHQLSAGFVPIRKKGKLPRDTVRIAYsleygvdEMEMHRDAIEKGERVVLVDDLIATGG 131
Cdd:cd06223   13 LLEPDVVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPSEPY-------GLELPLGGDVKGKRVLLVDDVIATGG 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 489054474 132 TAEAAAKLLLQMGAEIVAACFIIDLPDlGGRKKLEALGLPVRTL 175
Cdd:cd06223   86 TLLAAIELLKEAGAKVVGVAVLLDKPE-GGARELASPGDPVYSL 128
HPT_Archaea NF040646
hypoxanthine/guanine phosphoribosyltransferase;
40-176 1.62e-11

hypoxanthine/guanine phosphoribosyltransferase;


Pssm-ID: 468613  Cd Length: 184  Bit Score: 59.93  E-value: 1.62e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054474  40 RRAVDELVyPYAGNRIDKVAGIEARGFILGGAIAHQLSAGFVPIRK-KGKLPRDtvrIAYSLEYGVDEMEMHRDAIEKGE 118
Cdd:NF040646  40 REIADRII-KIADLDVDKIVTVEAMGIPIATALSLKTDIPLVIIRKrKYGLPGE---VEVHQSTGYSKGELYINGINKGD 115

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489054474 119 RVVLVDDLIATGGTAEAAAKLLLQMGAEIVAACFIIDLPDlgGRKKLE-ALGLPVRTLV 176
Cdd:NF040646 116 RVLIVDDVISTGGTLIAVIKALEKAGAEIKDVVVVIERGE--GKKIVEeKTGYKVKTLV 172
PyrE COG0461
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ...
 32-176 1.99e-10

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


Pssm-ID: 440229  Cd Length: 201  Bit Score: 57.09  E-value: 1.99e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054474  32 LMGNAQAFRRAVDELV--YPYAGNRIDKVAGIEARGFILGGAIAHQLSAGFVPIRKKGKlprdtvriayslEYGvdEMEM 109
Cdd:COG0461   39 VLSYPEALELLGEALAelIKELGPEFDAVAGPATGGIPLAAAVARALGLPAIFVRKEAK------------DHG--TGGQ 104

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489054474 110 HRDAIEKGERVVLVDDLIATGGTAEAAAKLLLQMGAEIVAACFIIDLPDlGGRKKLEALGLPVRTLV 176
Cdd:COG0461  105 IEGGLLPGERVLVVEDVITTGGSVLEAVEALREAGAEVVGVAVIVDREE-GAAENLEEAGVPLHSLL 170
PRK08558 PRK08558
adenine phosphoribosyltransferase; Provisional
 37-179 5.44e-08

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 181466 [Multi-domain]  Cd Length: 238  Bit Score: 50.76  E-value: 5.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054474  37 QAFRRAVDELVY-PYAGNRIDKVAGIEARGFILGGAIAHQLSAGFVPIRKKgklpRDTVRIAYSLEYGVDE------MEM 109
Cdd:PRK08558  93 PSFLRLIAPVVAeRFMGLRVDVVLTAATDGIPLAVAIASYFGADLVYAKKS----KETGVEKFYEEYQRLAsgievtLYL 168

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054474 110 HRDAIEKGERVVLVDDLIATGGTAEAAAKLLLQMGAEIVAACFIIDLPDLGGRKKLEALGLPVRTLVAFE 179
Cdd:PRK08558 169 PASALKKGDRVLIVDDIIRSGETQRALLDLARQAGADVVGVFFLIAVGEVGIDRAREETDAPVDALYTLE 238
purR_Bsub TIGR01743
pur operon repressor, Bacillus subtilis type; This model represents the puring operon ...
 9-155 8.16e-08

pur operon repressor, Bacillus subtilis type; This model represents the puring operon repressor PurR of low-GC Gram-positive bacteria. This homodimeric repressor contains a large region homologous to phosphoribosyltransferases and is inhibited by 5-phosphoribosyl 1-pyrophosphate. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis, Regulatory functions, DNA interactions]


Pssm-ID: 130804 [Multi-domain]  Cd Length: 268  Bit Score: 50.55  E-value: 8.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054474    9 LKDAIRTIPDypkpgvQFRDVTTLMGNAQAFRRAVDELVYPYAGNRIDKVAGIEARGFILGGAIAHQLSAGFVPIRKKGK 88
Cdd:TIGR01743  89 LSEPERILPG------GYLYLTDILGKPSILSKIGKILASVFAEREIDAVMTVATKGIPLAYAVASVLNVPLVIVRKDSK 162

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054474   89 LPR-DTVRIAY--SLEYGVDEMEMHRDAIEKGERVVLVDDLIATGGTAEAAAKLLLQMGAEIVAACFIID 155
Cdd:TIGR01743 163 VTEgSTVSINYvsGSSNRIQTMSLAKRSLKTGSKVLIIDDFMKAGGTINGMINLLDEFDAEVAGIGVLID 232
pyrE PRK00455
orotate phosphoribosyltransferase; Validated
 51-179 1.04e-07

orotate phosphoribosyltransferase; Validated


Pssm-ID: 234771  Cd Length: 202  Bit Score: 49.77  E-value: 1.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054474  51 AGNRIDKVAGIEARGFILGGAIAHQLSAGFVPIRKKGKlprdtvriayslEYGVD-EMEMHRdaiEKGERVVLVDDLIAT 129
Cdd:PRK00455  61 SGIEFDVVAGPATGGIPLAAAVARALDLPAIFVRKEAK------------DHGEGgQIEGRR---LFGKRVLVVEDVITT 125

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 489054474 130 GGTAEAAAKLLLQMGAEIVAACFIIDLPDlGGRKKLEALGLPVRTLVAFE 179
Cdd:PRK00455 126 GGSVLEAVEAIRAAGAEVVGVAVIVDRQS-AAQEVFADAGVPLISLITLD 174
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 35-155 3.38e-07

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: 47.36  E-value: 3.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054474   35 NAQAFRRAVDEL---VYPYAGNRIDKVAGIEARGFILGGAIAHQLSAGFVPIRKKGKLPRDTVRIAYSleygvdememHR 111
Cdd:pfam00156   7 DNPAILKAVARLaaqINEDYGGKPDVVVGILRGGLPFAGILARRLDVPLAFVRKVSYNPDTSEVMKTS----------SA 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 489054474  112 DAIEKGERVVLVDDLIATGGTAEAAAKLLLQMGAEIVAACFIID 155
Cdd:pfam00156  77 LPDLKGKTVLIVDDILDTGGTLLKVLELLKNVGPKEVKIAVLID 120
PRK09219 PRK09219
xanthine phosphoribosyltransferase; Validated
 50-175 3.17e-03

xanthine phosphoribosyltransferase; Validated


Pssm-ID: 181705  Cd Length: 189  Bit Score: 36.69  E-value: 3.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054474  50 YAGNRIDKVAGIEARGFILGGAIAHQLSAGFVPIRKK------GKLPRDTVriaYSLEYGVD-EMEMHRDAIEKGERVVL 122
Cdd:PRK09219  46 FKDEGITKILTIEASGIAPAVMAALALGVPVVFAKKKksltltDDVYTATV---YSFTKQVTsTVSVSKKFLSEGDRVLI 122

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489054474 123 VDDLIATGGTAEAAAKLLLQMGAEIVAACFIIDLPDLGGRKKLEALGLPVRTL 175
Cdd:PRK09219 123 IDDFLANGQAALGLIDIIEQAGAKVAGIGIVIEKSFQDGRKLLEEKGYRVESL 175
PRK07322 PRK07322
adenine phosphoribosyltransferase; Provisional
 32-174 8.67e-03

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 180928  Cd Length: 178  Bit Score: 35.34  E-value: 8.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054474  32 LMGNAQAFRRAVDELVyPYAGNRIDKVAGIEARGFILGGAIAHQLSAGFVPIRKKGK------LPRDTVriaySLEYGVD 105
Cdd:PRK07322  31 ILGDTELTEAAAEALA-KRLPTEVDVLVTPETKGIPLAHALSRRLGKPYVVARKSRKpymqdpIIQEVV----SITTGKP 105

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489054474 106 EM----EMHRDAIeKGERVVLVDDLIATGGTAEAAAKLLLQMGAEIVAACFIIDLPDLGGRKKLEALG-LPVRT 174
Cdd:PRK07322 106 QLlvldGADAEKL-KGKRVAIVDDVVSTGGTLTALERLVERAGGQVVAKAAIFAEGDASNRLDVIYLAhLPLFP 178
 
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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