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Conserved domains on  [gi|15596740|ref|NP_250234|]
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adenine phosphoribosyltransferase [Pseudomonas aeruginosa PAO1]

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

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List of domain hits

Name Accession Description Interval E-value
PRK02304 PRK02304
adenine phosphoribosyltransferase; Provisional
8-177 2.72e-85

adenine phosphoribosyltransferase; Provisional


:

Pssm-ID: 235028  Cd Length: 175  Bit Score: 248.45  E-value: 2.72e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596740    8 LKSQIRAVPDFPKPGVVFRDITPLFQSPRALRMTVDSFVQRYIEADFSHIGAMDARGFLIGSAVAYALNKPLVLFRKQGK 87
Cdd:PRK02304   6 LKSSIRTIPDFPKPGILFRDITPLLADPEAFREVIDALVERYKDADIDKIVGIEARGFIFGAALAYKLGIGFVPVRKPGK 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596740   88 LPADVLAEGYQTEYGEAFLEVHADSLCEGDSVLIFDDLIATGGTLLAAASLVRRLGARVFEAAAIIDLPELGGSTRLQda 167
Cdd:PRK02304  86 LPRETISESYELEYGTDTLEIHKDAIKPGDRVLIVDDLLATGGTLEAAIKLLERLGAEVVGAAFVIELPDLGGREKLE-- 163
                        170
                 ....*....|
gi 15596740  168 GISTFSLTAF 177
Cdd:PRK02304 164 GYPVKSLVKF 173
 
Name Accession Description Interval E-value
PRK02304 PRK02304
adenine phosphoribosyltransferase; Provisional
8-177 2.72e-85

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 235028  Cd Length: 175  Bit Score: 248.45  E-value: 2.72e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596740    8 LKSQIRAVPDFPKPGVVFRDITPLFQSPRALRMTVDSFVQRYIEADFSHIGAMDARGFLIGSAVAYALNKPLVLFRKQGK 87
Cdd:PRK02304   6 LKSSIRTIPDFPKPGILFRDITPLLADPEAFREVIDALVERYKDADIDKIVGIEARGFIFGAALAYKLGIGFVPVRKPGK 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596740   88 LPADVLAEGYQTEYGEAFLEVHADSLCEGDSVLIFDDLIATGGTLLAAASLVRRLGARVFEAAAIIDLPELGGSTRLQda 167
Cdd:PRK02304  86 LPRETISESYELEYGTDTLEIHKDAIKPGDRVLIVDDLLATGGTLEAAIKLLERLGAEVVGAAFVIELPDLGGREKLE-- 163
                        170
                 ....*....|
gi 15596740  168 GISTFSLTAF 177
Cdd:PRK02304 164 GYPVKSLVKF 173
apt TIGR01090
adenine phosphoribosyltransferase; A phylogenetic analysis suggested omitting the ...
8-174 1.43e-68

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: 205.97  E-value: 1.43e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596740     8 LKSQIRAVPDFPKPGVVFRDITPLFQSPRALRMTVDSFVQRYIEADFSHIGAMDARGFLIGSAVAYALNKPLVLFRKQGK 87
Cdd:TIGR01090   1 LKQAIRSIPDFPKKGILFRDITPLLNNPELFRFLIDLLVERYKDANIDYIVGPEARGFIFGAALAYKLGVGFVPVRKPGK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596740    88 LPADVLAEGYQTEYGEAFLEVHADSLCEGDSVLIFDDLIATGGTLLAAASLVRRLGARVFEAAAIIDLPELGGSTRLQDA 167
Cdd:TIGR01090  81 LPGETISASYDLEYGKDVLEIHKDAIKPGQRVLIVDDLLATGGTAAATDELIKKLGGEVVEAAFLIELKDLNGRAKLEPN 160

                  ....*..
gi 15596740   168 gISTFSL 174
Cdd:TIGR01090 161 -VPVFSL 166
Apt COG0503
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ...
7-177 1.38e-66

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: 201.07  E-value: 1.38e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596740   7 TLKSQIRAVPDFPKPGVVFRDITPLFQSPRALRMTVDSFVQRYIEADFSHIGAMDARGFLIGSAVAYALNKPLVLFRKQG 86
Cdd:COG0503   2 DLKDLIRDIPDFPKPGILFRDITPLLGDPELFRAAGDELAERFADKGIDKVVGIEARGFILAAALAYALGVPFVPARKPG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596740  87 KLPADVLAEGYQTEYGE-AFLEVHADSLCEGDSVLIFDDLIATGGTLLAAASLVRRLGARVFEAAAIIDLPELGGSTRLQ 165
Cdd:COG0503  82 KLPGETVSEEYDLEYGTgDTLELHKDALKPGDRVLIVDDLLATGGTAKAAIKLVEEAGAEVVGIAFLIELGFLGGREKLR 161
                       170
                ....*....|..
gi 15596740 166 DAGIstFSLTAF 177
Cdd:COG0503 162 DYPV--ESLLTL 171
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
53-160 1.86e-20

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: 82.06  E-value: 1.86e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596740  53 DFSHIGAMDARGFLIGSAVAYALNKPLVLFRKQGKLPADVLAEGYQteygeafLEVHADSLCEGDSVLIFDDLIATGGTL 132
Cdd:cd06223  15 EPDVVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPSEPYG-------LELPLGGDVKGKRVLLVDDVIATGGTL 87
                        90       100
                ....*....|....*....|....*...
gi 15596740 133 LAAASLVRRLGARVFEAAAIIDLPELGG 160
Cdd:cd06223  88 LAAIELLKEAGAKVVGVAVLLDKPEGGA 115
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
56-157 6.19e-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: 55.06  E-value: 6.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596740    56 HIGAMDARGFLIGSAVAYALNKPLVLFRKQGKLPADVLAEGYqteygeafleVHADSLCEGDSVLIFDDLIATGGTLLAA 135
Cdd:pfam00156  32 VVVGILRGGLPFAGILARRLDVPLAFVRKVSYNPDTSEVMKT----------SSALPDLKGKTVLIVDDILDTGGTLLKV 101
                          90       100
                  ....*....|....*....|..
gi 15596740   136 ASLVRRLGARVFEAAAIIDLPE 157
Cdd:pfam00156 102 LELLKNVGPKEVKIAVLIDKPA 123
 
Name Accession Description Interval E-value
PRK02304 PRK02304
adenine phosphoribosyltransferase; Provisional
8-177 2.72e-85

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 235028  Cd Length: 175  Bit Score: 248.45  E-value: 2.72e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596740    8 LKSQIRAVPDFPKPGVVFRDITPLFQSPRALRMTVDSFVQRYIEADFSHIGAMDARGFLIGSAVAYALNKPLVLFRKQGK 87
Cdd:PRK02304   6 LKSSIRTIPDFPKPGILFRDITPLLADPEAFREVIDALVERYKDADIDKIVGIEARGFIFGAALAYKLGIGFVPVRKPGK 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596740   88 LPADVLAEGYQTEYGEAFLEVHADSLCEGDSVLIFDDLIATGGTLLAAASLVRRLGARVFEAAAIIDLPELGGSTRLQda 167
Cdd:PRK02304  86 LPRETISESYELEYGTDTLEIHKDAIKPGDRVLIVDDLLATGGTLEAAIKLLERLGAEVVGAAFVIELPDLGGREKLE-- 163
                        170
                 ....*....|
gi 15596740  168 GISTFSLTAF 177
Cdd:PRK02304 164 GYPVKSLVKF 173
apt TIGR01090
adenine phosphoribosyltransferase; A phylogenetic analysis suggested omitting the ...
8-174 1.43e-68

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: 205.97  E-value: 1.43e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596740     8 LKSQIRAVPDFPKPGVVFRDITPLFQSPRALRMTVDSFVQRYIEADFSHIGAMDARGFLIGSAVAYALNKPLVLFRKQGK 87
Cdd:TIGR01090   1 LKQAIRSIPDFPKKGILFRDITPLLNNPELFRFLIDLLVERYKDANIDYIVGPEARGFIFGAALAYKLGVGFVPVRKPGK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596740    88 LPADVLAEGYQTEYGEAFLEVHADSLCEGDSVLIFDDLIATGGTLLAAASLVRRLGARVFEAAAIIDLPELGGSTRLQDA 167
Cdd:TIGR01090  81 LPGETISASYDLEYGKDVLEIHKDAIKPGQRVLIVDDLLATGGTAAATDELIKKLGGEVVEAAFLIELKDLNGRAKLEPN 160

                  ....*..
gi 15596740   168 gISTFSL 174
Cdd:TIGR01090 161 -VPVFSL 166
Apt COG0503
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ...
7-177 1.38e-66

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: 201.07  E-value: 1.38e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596740   7 TLKSQIRAVPDFPKPGVVFRDITPLFQSPRALRMTVDSFVQRYIEADFSHIGAMDARGFLIGSAVAYALNKPLVLFRKQG 86
Cdd:COG0503   2 DLKDLIRDIPDFPKPGILFRDITPLLGDPELFRAAGDELAERFADKGIDKVVGIEARGFILAAALAYALGVPFVPARKPG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596740  87 KLPADVLAEGYQTEYGE-AFLEVHADSLCEGDSVLIFDDLIATGGTLLAAASLVRRLGARVFEAAAIIDLPELGGSTRLQ 165
Cdd:COG0503  82 KLPGETVSEEYDLEYGTgDTLELHKDALKPGDRVLIVDDLLATGGTAKAAIKLVEEAGAEVVGIAFLIELGFLGGREKLR 161
                       170
                ....*....|..
gi 15596740 166 DAGIstFSLTAF 177
Cdd:COG0503 162 DYPV--ESLLTL 171
PLN02293 PLN02293
adenine phosphoribosyltransferase
8-166 2.52e-61

adenine phosphoribosyltransferase


Pssm-ID: 177930  Cd Length: 187  Bit Score: 188.34  E-value: 2.52e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596740    8 LKSQIRAVPDFPKPGVVFRDITPLFQSPRALRMTVDSFVQRYIEADFSHIGAMDARGFLIGSAVAYALNKPLVLFRKQGK 87
Cdd:PLN02293  17 ISSAIRVVPDFPKPGIMFQDITTLLLDPKAFKDTIDLFVERYRDMGISVVAGIEARGFIFGPPIALAIGAKFVPLRKPGK 96
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596740   88 LPADVLAEGYQTEYGEAFLEVHADSLCEGDSVLIFDDLIATGGTLLAAASLVRRLGARVFEAAAIIDLPELGGSTRLQD 166
Cdd:PLN02293  97 LPGEVISEEYVLEYGTDCLEMHVGAVEPGERALVIDDLIATGGTLCAAINLLERAGAEVVECACVIELPELKGREKLNG 175
PRK12560 PRK12560
adenine phosphoribosyltransferase; Provisional
8-181 1.28e-25

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 183595  Cd Length: 187  Bit Score: 97.16  E-value: 1.28e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596740    8 LKSQIRAVPDFPKPGVV--FRDITPLFQsPRALRMTVDSFVQrYIEADFSHIGAMDARGFLIGSAVAYALNKPLvlfRKQ 85
Cdd:PRK12560   6 LYKNARVVNSGKALTTVneFTDQLPALR-PKVLKETAKEIIK-YIDKDIDKIVTEEDKGAPLATPVSLLSGKPL---AMA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596740   86 GKLPADVLAEGYQT-EYGEAFLE--VHADSLCEGDSVLIFDDLIATGGTLLAAASLVRRLGARVFEAAAIIDLPELGGST 162
Cdd:PRK12560  81 RWYPYSLSELNYNVvEIGSEYFEgvVYLNGIEKGDRVAIIDDTLSTGGTVIALIKAIENSGGIVSDVICVIEKTQNNGRK 160
                        170       180
                 ....*....|....*....|
gi 15596740  163 RLQDA-GISTFSLTAFALDE 181
Cdd:PRK12560 161 KLFTQtGINVKSLVKIDVKP 180
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
53-160 1.86e-20

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: 82.06  E-value: 1.86e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596740  53 DFSHIGAMDARGFLIGSAVAYALNKPLVLFRKQGKLPADVLAEGYQteygeafLEVHADSLCEGDSVLIFDDLIATGGTL 132
Cdd:cd06223  15 EPDVVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPSEPYG-------LELPLGGDVKGKRVLLVDDVIATGGTL 87
                        90       100
                ....*....|....*....|....*...
gi 15596740 133 LAAASLVRRLGARVFEAAAIIDLPELGG 160
Cdd:cd06223  88 LAAIELLKEAGAKVVGVAVLLDKPEGGA 115
PyrE COG0461
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ...
3-175 2.53e-14

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


Pssm-ID: 440229  Cd Length: 201  Bit Score: 67.87  E-value: 2.53e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596740   3 FDEFTLKSQIRAvpdfpkPgvVFRDITPLFQSPRALRMTVDSFVQRYIEA--DFSHIGAMDARGFLIGSAVAYALNKPLV 80
Cdd:COG0461  19 FGHFTLSSGRHS------P--YYIDCRLVLSYPEALELLGEALAELIKELgpEFDAVAGPATGGIPLAAAVARALGLPAI 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596740  81 LFRKQGKlpadvlaegyqtEYGE-AFLEVHadsLCEGDSVLIFDDLIATGGTLLAAASLVRRLGARVFEAAAIIDLPElG 159
Cdd:COG0461  91 FVRKEAK------------DHGTgGQIEGG---LLPGERVLVVEDVITTGGSVLEAVEALREAGAEVVGVAVIVDREE-G 154
                       170
                ....*....|....*.
gi 15596740 160 GSTRLQDAGISTFSLT 175
Cdd:COG0461 155 AAENLEEAGVPLHSLL 170
pyrE PRK00455
orotate phosphoribosyltransferase; Validated
3-175 8.63e-12

orotate phosphoribosyltransferase; Validated


Pssm-ID: 234771  Cd Length: 202  Bit Score: 60.94  E-value: 8.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596740    3 FDEFTLKSQIRAvpdfpkPgvVFRDITPLFQSPRALRMTVDSFVQRYIEA--DFSHIGAMDARGFLIGSAVAYALNKPLV 80
Cdd:PRK00455  20 FGHFTLSSGRKS------P--YYFDCRKLLSYPEALALLGRFLAEAIKDSgiEFDVVAGPATGGIPLAAAVARALDLPAI 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596740   81 LFRKQGKlpadvlaegyqtEYGE-AFLEVhadSLCEGDSVLIFDDLIATGGTLLAAASLVRRLGARVFEAAAIIDLPElG 159
Cdd:PRK00455  92 FVRKEAK------------DHGEgGQIEG---RRLFGKRVLVVEDVITTGGSVLEAVEAIRAAGAEVVGVAVIVDRQS-A 155
                        170
                 ....*....|....*.
gi 15596740  160 GSTRLQDAGISTFSLT 175
Cdd:PRK00455 156 AQEVFADAGVPLISLI 171
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
56-157 6.19e-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: 55.06  E-value: 6.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596740    56 HIGAMDARGFLIGSAVAYALNKPLVLFRKQGKLPADVLAEGYqteygeafleVHADSLCEGDSVLIFDDLIATGGTLLAA 135
Cdd:pfam00156  32 VVVGILRGGLPFAGILARRLDVPLAFVRKVSYNPDTSEVMKT----------SSALPDLKGKTVLIVDDILDTGGTLLKV 101
                          90       100
                  ....*....|....*....|..
gi 15596740   136 ASLVRRLGARVFEAAAIIDLPE 157
Cdd:pfam00156 102 LELLKNVGPKEVKIAVLIDKPA 123
ribP_PPkin TIGR01251
ribose-phosphate pyrophosphokinase; Alternate name: phosphoribosylpyrophosphate synthetase In ...
48-150 4.30e-07

ribose-phosphate pyrophosphokinase; Alternate name: phosphoribosylpyrophosphate synthetase In some systems, close homologs lacking enzymatic activity exist and perform regulatory functions. The model is designated subfamily rather than equivalog for this reason. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 273523 [Multi-domain]  Cd Length: 308  Bit Score: 48.43  E-value: 4.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596740    48 RYIEADFSH---IGAMDARGFLIGSAVAYALNKPLVLFRKQgKLPADVLAEgyqteygeaflEVHADSLCEGDSVLIFDD 124
Cdd:TIGR01251 151 EYLKKKILDnpvVVSPDAGGVERAKKVADALGCPLAIIDKR-RISATNEVE-----------VMNLVGDVEGKDVVIVDD 218
                          90       100
                  ....*....|....*....|....*..
gi 15596740   125 LIATGGTLLAAASLVRRLGA-RVFEAA 150
Cdd:TIGR01251 219 IIDTGGTIAKAAEILKSAGAkRVIAAA 245
PRK08558 PRK08558
adenine phosphoribosyltransferase; Provisional
64-153 1.33e-06

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 181466 [Multi-domain]  Cd Length: 238  Bit Score: 46.91  E-value: 1.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596740   64 GFLIGSAVAYALNKPLVlFRKQGKLPA--------DVLAEGYqteygEAFLEVHADSLCEGDSVLIFDDLIATGGTLLAA 135
Cdd:PRK08558 122 GIPLAVAIASYFGADLV-YAKKSKETGvekfyeeyQRLASGI-----EVTLYLPASALKKGDRVLIVDDIIRSGETQRAL 195
                         90
                 ....*....|....*...
gi 15596740  136 ASLVRRLGARVFEAAAII 153
Cdd:PRK08558 196 LDLARQAGADVVGVFFLI 213
PRK09219 PRK09219
xanthine phosphoribosyltransferase; Validated
42-174 1.42e-06

xanthine phosphoribosyltransferase; Validated


Pssm-ID: 181705  Cd Length: 189  Bit Score: 46.32  E-value: 1.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596740   42 VDSFVQRYIEAD-FSHIGAMDARGFL--------------IGSAV--AYALNKPLVLFRKQ-------GKLPADVLAEGY 97
Cdd:PRK09219  22 VDSFLNHQVDPKlMNEIGKEFARRFKdegitkiltieasgIAPAVmaALALGVPVVFAKKKksltltdDVYTATVYSFTK 101
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15596740   98 QTEYGeafLEVHADSLCEGDSVLIFDDLIATGGTLLAAASLVRRLGARVFEAAAIIDLPELGGSTRLQDAGISTFSL 174
Cdd:PRK09219 102 QVTST---VSVSKKFLSEGDRVLIIDDFLANGQAALGLIDIIEQAGAKVAGIGIVIEKSFQDGRKLLEEKGYRVESL 175
ComFC COG1040
DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General ...
55-152 3.25e-06

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


Pssm-ID: 440662 [Multi-domain]  Cd Length: 196  Bit Score: 45.20  E-value: 3.25e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596740  55 SHIGAMDARGF----LIGSAVAYALNKPL---VLFR-----KQGKLPAD---VLAEGyqteygeAFlEVHADSLCEGDSV 119
Cdd:COG1040  87 LHRRRLRRRGFnqaeLLARALARALGIPVlpdLLRRvratpSQAGLSRAerrRNLRG-------AF-AVRPPARLAGKHV 158
                        90       100       110
                ....*....|....*....|....*....|...
gi 15596740 120 LIFDDLIATGGTLLAAASLVRRLGARVFEAAAI 152
Cdd:COG1040 159 LLVDDVLTTGATLAEAARALKAAGAARVDVLVL 191
PRK00934 PRK00934
ribose-phosphate pyrophosphokinase; Provisional
46-169 3.69e-06

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 234868 [Multi-domain]  Cd Length: 285  Bit Score: 45.67  E-value: 3.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596740   46 VQRYIEADFSHIGAMDArgflIGSAVAYALNKPLVLFRKQGKLP-ADVLAEGYQTEYgeAFLE-------------VHAD 111
Cdd:PRK00934 128 ILEFFPIPFINLDAAPL----IAEYIGDKLDDPLVLAPDKGALElAKEAAEILGCEY--DYLEktrispteveiapKNLD 201
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15596740  112 SlcEGDSVLIFDDLIATGGTLLAAASLVRRLGARVFEAAAIIDLPELGGSTRLQDAGI 169
Cdd:PRK00934 202 V--KGKDVLIVDDIISTGGTMATAIKILKEQGAKKVYVACVHPVLVGDAILKLYNAGV 257
PrsA COG0462
Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; ...
115-145 2.29e-05

Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; Phosphoribosylpyrophosphate synthetase is part of the Pathway/BioSystem: Histidine biosynthesis, Purine biosynthesis


Pssm-ID: 440230 [Multi-domain]  Cd Length: 311  Bit Score: 43.51  E-value: 2.29e-05
                        10        20        30
                ....*....|....*....|....*....|.
gi 15596740 115 EGDSVLIFDDLIATGGTLLAAASLVRRLGAR 145
Cdd:COG0462 210 EGKTCIIVDDMIDTGGTLVEAAEALKEAGAK 240
PRK06827 PRK06827
phosphoribosylpyrophosphate synthetase; Provisional
18-150 3.69e-05

phosphoribosylpyrophosphate synthetase; Provisional


Pssm-ID: 180714 [Multi-domain]  Cd Length: 382  Bit Score: 43.02  E-value: 3.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596740   18 FPKPGvvFRDITPLFQSPRALRMTVDSfvqryIEADFSHI-------GAMDargfligSAVAYA--LNKPLVLFRK---- 84
Cdd:PRK06827 177 IPLMG--FENLYPSYQIIKALLKNEKD-----LEIDKDHLmvispdtGAMD-------RAKYYAsvLGVDLGLFYKrrdy 242
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15596740   85 ----QGKLPAdvlaegYQTEY-GEAFlevhadslcEGDSVLIFDDLIATGGTLLAAASLVRRLGAR-VFEAA 150
Cdd:PRK06827 243 srvvNGRNPI------VAHEFlGRDV---------EGKDVLIVDDMIASGGSMIDAAKELKSRGAKkIIVAA 299
PRK07322 PRK07322
adenine phosphoribosyltransferase; Provisional
115-164 7.59e-05

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 180928  Cd Length: 178  Bit Score: 41.50  E-value: 7.59e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 15596740  115 EGDSVLIFDDLIATGGTLLAAASLVRRLGARVFEAAAIidLPELGGSTRL 164
Cdd:PRK07322 119 KGKRVAIVDDVVSTGGTLTALERLVERAGGQVVAKAAI--FAEGDASNRL 166
Hpt1 COG2236
Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism]; Hypoxanthine ...
62-152 1.76e-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: 37.13  E-value: 1.76e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596740  62 ARGFLI-GSAVAYALNKPLVLFrkqgklpadVLAEGYQTEYG---EAFLEVHADSLCEGDSVLIFDDLIATGGTLLAAAS 137
Cdd:COG2236  39 ARGGLVpARILADALGVPDLAS---------IRVSSYTGTAKrleEPVVKGPLDEDLAGKRVLIVDDVADTGRTLEAVRD 109
                        90
                ....*....|....*
gi 15596740 138 LVRRLGARVFEAAAI 152
Cdd:COG2236 110 LLKEAGPAEVRTAVL 124
PRK01259 PRK01259
ribose-phosphate diphosphokinase;
115-150 3.44e-03

ribose-phosphate diphosphokinase;


Pssm-ID: 234929 [Multi-domain]  Cd Length: 309  Bit Score: 37.02  E-value: 3.44e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 15596740  115 EGDSVLIFDDLIATGGTLLAAASLVRRLGA-RVFEAA 150
Cdd:PRK01259 207 EGRDCILVDDMIDTAGTLCKAAEALKERGAkSVYAYA 243
upp PRK00129
uracil phosphoribosyltransferase; Reviewed
115-182 7.67e-03

uracil phosphoribosyltransferase; Reviewed


Pssm-ID: 234653  Cd Length: 209  Bit Score: 35.83  E-value: 7.67e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15596740  115 EGDSVLIFDDLIATGGTLLAAASLVRRLGARVFEAAAIIDLPElgGSTRLQDAGISTFSLTAfALDER 182
Cdd:PRK00129 123 DERTVIVVDPMLATGGSAIAAIDLLKKRGAKNIKVLCLVAAPE--GIKALEEAHPDVEIYTA-AIDEK 187
 
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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