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Conserved domains on  [gi|665409664|ref|NP_001286908|]
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adenine phosphoribosyltransferase, isoform C [Drosophila melanogaster]

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
 9-182 1.55e-66

adenine phosphoribosyltransferase; Provisional


:

Pssm-ID: 235028  Cd Length: 175  Bit Score: 201.07  E-value: 1.55e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409664   9 DKLDYVKSKIGEYPNFPKEGILFRDIFGALTDPKACVYLRDLLVDHIRESapEAEVIVGLDSRGFLFNLLIATELGLGCA 88
Cdd:PRK02304   1 MMLEDLKSSIRTIPDFPKPGILFRDITPLLADPEAFREVIDALVERYKDA--DIDKIVGIEARGFIFGAALAYKLGIGFV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409664  89 PIRKKGKLAGEVVSVEYKLEYGIDTFELQKSAIKPGQKVVVVDDLLATGGSLVAATELIGKVGGVVVESLVVMELVGLEG 168
Cdd:PRK02304  79 PVRKPGKLPRETISESYELEYGTDTLEIHKDAIKPGDRVLIVDDLLATGGTLEAAIKLLERLGAEVVGAAFVIELPDLGG 158

                        170
                 ....*....|....*
gi 665409664 169 RKRLDG-KVHSLIKY 182
Cdd:PRK02304 159 REKLEGyPVKSLVKF 173
 
Name Accession Description Interval E-value
PRK02304 PRK02304
adenine phosphoribosyltransferase; Provisional
 9-182 1.55e-66

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 235028  Cd Length: 175  Bit Score: 201.07  E-value: 1.55e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409664   9 DKLDYVKSKIGEYPNFPKEGILFRDIFGALTDPKACVYLRDLLVDHIRESapEAEVIVGLDSRGFLFNLLIATELGLGCA 88
Cdd:PRK02304   1 MMLEDLKSSIRTIPDFPKPGILFRDITPLLADPEAFREVIDALVERYKDA--DIDKIVGIEARGFIFGAALAYKLGIGFV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409664  89 PIRKKGKLAGEVVSVEYKLEYGIDTFELQKSAIKPGQKVVVVDDLLATGGSLVAATELIGKVGGVVVESLVVMELVGLEG 168
Cdd:PRK02304  79 PVRKPGKLPRETISESYELEYGTDTLEIHKDAIKPGDRVLIVDDLLATGGTLEAAIKLLERLGAEVVGAAFVIELPDLGG 158

                        170
                 ....*....|....*
gi 665409664 169 RKRLDG-KVHSLIKY 182
Cdd:PRK02304 159 REKLEGyPVKSLVKF 173
apt TIGR01090
adenine phosphoribosyltransferase; A phylogenetic analysis suggested omitting the ...
 14-182 7.46e-63

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: 191.72  E-value: 7.46e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409664   14 VKSKIGEYPNFPKEGILFRDIFGALTDPKACVYLRDLLVDHIRESAPEAevIVGLDSRGFLFNLLIATELGLGCAPIRKK 93
Cdd:TIGR01090   1 LKQAIRSIPDFPKKGILFRDITPLLNNPELFRFLIDLLVERYKDANIDY--IVGPEARGFIFGAALAYKLGVGFVPVRKP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409664   94 GKLAGEVVSVEYKLEYGIDTFELQKSAIKPGQKVVVVDDLLATGGSLVAATELIGKVGGVVVESLVVMELVGLEGRKRLD 173
Cdd:TIGR01090  79 GKLPGETISASYDLEYGKDVLEIHKDAIKPGQRVLIVDDLLATGGTAAATDELIKKLGGEVVEAAFLIELKDLNGRAKLE 158

                         170
                  ....*....|.
gi 665409664  174 GK--VHSLIKY 182
Cdd:TIGR01090 159 PNvpVFSLLEY 169
Apt COG0503
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ...
 12-182 4.35e-59

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: 181.81  E-value: 4.35e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409664  12 DYVKSKIGEYPNFPKEGILFRDIFGALTDPKACVYLRDLLVDHIRESapEAEVIVGLDSRGFLFNLLIATELGLGCAPIR 91
Cdd:COG0503    1 EDLKDLIRDIPDFPKPGILFRDITPLLGDPELFRAAGDELAERFADK--GIDKVVGIEARGFILAAALAYALGVPFVPAR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409664  92 KKGKLAGEVVSVEYKLEYG-IDTFELQKSAIKPGQKVVVVDDLLATGGSLVAATELIGKVGGVVVESLVVMELVGLEGRK 170
Cdd:COG0503   79 KPGKLPGETVSEEYDLEYGtGDTLELHKDALKPGDRVLIVDDLLATGGTAKAAIKLVEEAGAEVVGIAFLIELGFLGGRE 158

                        170
                 ....*....|...
gi 665409664 171 RLDGK-VHSLIKY 182
Cdd:COG0503  159 KLRDYpVESLLTL 171
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 49-176 1.47e-22

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: 87.45  E-value: 1.47e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409664  49 DLLVDHIRESAPEAEVIVGLDSRGFLFNLLIATELGLGCAPIRKKGKLAGEVVSVEYKLEYGIDtfelqksAIKPGQKVV 128
Cdd:cd06223    3 RLLAEEIREDLLEPDVVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPSEPYGLELPLG-------GDVKGKRVL 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 665409664 129 VVDDLLATGGSLVAATELIGKVGGVVVESLVVMELVGLEGRKRLDGKV 176
Cdd:cd06223   76 LVDDVIATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGGARELASPGD 123
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 47-176 2.04e-11

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: 58.92  E-value: 2.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409664   47 LRDLLVDHIRESAPEAEVIVGLDSRGFLFNLLIATELGLGCAPIRKKGKLAGEVVSVEYkleygidtfeLQKSAIKPGQK 126
Cdd:pfam00156  15 VARLAAQINEDYGGKPDVVVGILRGGLPFAGILARRLDVPLAFVRKVSYNPDTSEVMKT----------SSALPDLKGKT 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 665409664  127 VVVVDDLLATGGSLVAATELIGKVGGVVVESLVVMElvGLEGRKRLDGKV 176
Cdd:pfam00156  85 VLIVDDILDTGGTLLKVLELLKNVGPKEVKIAVLID--KPAGTEPKDKYD 132
HPT_Archaea NF040646
hypoxanthine/guanine phosphoribosyltransferase;
90-181 9.43e-05

hypoxanthine/guanine phosphoribosyltransferase;


Pssm-ID: 468613  Cd Length: 184  Bit Score: 41.06  E-value: 9.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409664  90 IRK-KGKLAGEVvsvEYKLEYGIDTFELQKSAIKPGQKVVVVDDLLATGGSLVAATELIGKVGGVVVESLVVMELVglEG 168
Cdd:NF040646  82 IRKrKYGLPGEV---EVHQSTGYSKGELYINGINKGDRVLIVDDVISTGGTLIAVIKALEKAGAEIKDVVVVIERG--EG 156

                         90
                 ....*....|....*..
gi 665409664 169 RKRLDGK----VHSLIK 181
Cdd:NF040646 157 KKIVEEKtgykVKTLVK 173
 
Name Accession Description Interval E-value
PRK02304 PRK02304
adenine phosphoribosyltransferase; Provisional
 9-182 1.55e-66

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 235028  Cd Length: 175  Bit Score: 201.07  E-value: 1.55e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409664   9 DKLDYVKSKIGEYPNFPKEGILFRDIFGALTDPKACVYLRDLLVDHIRESapEAEVIVGLDSRGFLFNLLIATELGLGCA 88
Cdd:PRK02304   1 MMLEDLKSSIRTIPDFPKPGILFRDITPLLADPEAFREVIDALVERYKDA--DIDKIVGIEARGFIFGAALAYKLGIGFV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409664  89 PIRKKGKLAGEVVSVEYKLEYGIDTFELQKSAIKPGQKVVVVDDLLATGGSLVAATELIGKVGGVVVESLVVMELVGLEG 168
Cdd:PRK02304  79 PVRKPGKLPRETISESYELEYGTDTLEIHKDAIKPGDRVLIVDDLLATGGTLEAAIKLLERLGAEVVGAAFVIELPDLGG 158

                        170
                 ....*....|....*
gi 665409664 169 RKRLDG-KVHSLIKY 182
Cdd:PRK02304 159 REKLEGyPVKSLVKF 173
apt TIGR01090
adenine phosphoribosyltransferase; A phylogenetic analysis suggested omitting the ...
 14-182 7.46e-63

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: 191.72  E-value: 7.46e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409664   14 VKSKIGEYPNFPKEGILFRDIFGALTDPKACVYLRDLLVDHIRESAPEAevIVGLDSRGFLFNLLIATELGLGCAPIRKK 93
Cdd:TIGR01090   1 LKQAIRSIPDFPKKGILFRDITPLLNNPELFRFLIDLLVERYKDANIDY--IVGPEARGFIFGAALAYKLGVGFVPVRKP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409664   94 GKLAGEVVSVEYKLEYGIDTFELQKSAIKPGQKVVVVDDLLATGGSLVAATELIGKVGGVVVESLVVMELVGLEGRKRLD 173
Cdd:TIGR01090  79 GKLPGETISASYDLEYGKDVLEIHKDAIKPGQRVLIVDDLLATGGTAAATDELIKKLGGEVVEAAFLIELKDLNGRAKLE 158

                         170
                  ....*....|.
gi 665409664  174 GK--VHSLIKY 182
Cdd:TIGR01090 159 PNvpVFSLLEY 169
Apt COG0503
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ...
 12-182 4.35e-59

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: 181.81  E-value: 4.35e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409664  12 DYVKSKIGEYPNFPKEGILFRDIFGALTDPKACVYLRDLLVDHIRESapEAEVIVGLDSRGFLFNLLIATELGLGCAPIR 91
Cdd:COG0503    1 EDLKDLIRDIPDFPKPGILFRDITPLLGDPELFRAAGDELAERFADK--GIDKVVGIEARGFILAAALAYALGVPFVPAR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409664  92 KKGKLAGEVVSVEYKLEYG-IDTFELQKSAIKPGQKVVVVDDLLATGGSLVAATELIGKVGGVVVESLVVMELVGLEGRK 170
Cdd:COG0503   79 KPGKLPGETVSEEYDLEYGtGDTLELHKDALKPGDRVLIVDDLLATGGTAKAAIKLVEEAGAEVVGIAFLIELGFLGGRE 158

                        170
                 ....*....|...
gi 665409664 171 RLDGK-VHSLIKY 182
Cdd:COG0503  159 KLRDYpVESLLTL 171
PLN02293 PLN02293
adenine phosphoribosyltransferase
 1-175 1.06e-54

adenine phosphoribosyltransferase


Pssm-ID: 177930  Cd Length: 187  Bit Score: 171.40  E-value: 1.06e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409664   1 MSPSISAEDKLDYVKSKIGEYPNFPKEGILFRDIFGALTDPKACVYLRDLLVDHIRESAPEaeVIVGLDSRGFLFNLLIA 80
Cdd:PLN02293   4 MENGDQGDPRLQGISSAIRVVPDFPKPGIMFQDITTLLLDPKAFKDTIDLFVERYRDMGIS--VVAGIEARGFIFGPPIA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409664  81 TELGLGCAPIRKKGKLAGEVVSVEYKLEYGIDTFELQKSAIKPGQKVVVVDDLLATGGSLVAATELIGKVGGVVVESLVV 160
Cdd:PLN02293  82 LAIGAKFVPLRKPGKLPGEVISEEYVLEYGTDCLEMHVGAVEPGERALVIDDLIATGGTLCAAINLLERAGAEVVECACV 161

                        170
                 ....*....|....*
gi 665409664 161 MELVGLEGRKRLDGK 175
Cdd:PLN02293 162 IELPELKGREKLNGK 176
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 49-176 1.47e-22

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: 87.45  E-value: 1.47e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409664  49 DLLVDHIRESAPEAEVIVGLDSRGFLFNLLIATELGLGCAPIRKKGKLAGEVVSVEYKLEYGIDtfelqksAIKPGQKVV 128
Cdd:cd06223    3 RLLAEEIREDLLEPDVVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPSEPYGLELPLG-------GDVKGKRVL 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 665409664 129 VVDDLLATGGSLVAATELIGKVGGVVVESLVVMELVGLEGRKRLDGKV 176
Cdd:cd06223   76 LVDDVIATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGGARELASPGD 123
PRK12560 PRK12560
adenine phosphoribosyltransferase; Provisional
 10-182 1.62e-22

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 183595  Cd Length: 187  Bit Score: 89.07  E-value: 1.62e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409664  10 KLDYVKSKIGEYPNFPKEGIL--FRDIFGALTdPKACVYLRDLLVDHIRESApeaEVIVGLDSRGFLFNLLIATelgLGC 87
Cdd:PRK12560   2 LLKNLYKNARVVNSGKALTTVneFTDQLPALR-PKVLKETAKEIIKYIDKDI---DKIVTEEDKGAPLATPVSL---LSG 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409664  88 APIRKKGKLAGEVVSVEY-KLEYGIDTFE--LQKSAIKPGQKVVVVDDLLATGGSLVAATELIGKVGGVVVESLVVMELV 164
Cdd:PRK12560  75 KPLAMARWYPYSLSELNYnVVEIGSEYFEgvVYLNGIEKGDRVAIIDDTLSTGGTVIALIKAIENSGGIVSDVICVIEKT 154

                        170       180
                 ....*....|....*....|..
gi 665409664 165 GLEGRKRLDGK----VHSLIKY 182
Cdd:PRK12560 155 QNNGRKKLFTQtginVKSLVKI 176
PyrE COG0461
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ...
 38-182 1.27e-13

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


Pssm-ID: 440229  Cd Length: 201  Bit Score: 65.95  E-value: 1.27e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409664  38 LTDPKACVYLRDLLVDHIRESAPEAEVIVGLDSRGFLFNLLIATELGLGCAPIRKKGKLAGEVVSVEykleygidtfelq 117
Cdd:COG0461   40 LSYPEALELLGEALAELIKELGPEFDAVAGPATGGIPLAAAVARALGLPAIFVRKEAKDHGTGGQIE------------- 106

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665409664 118 kSAIKPGQKVVVVDDLLATGGSLVAATELIGKVGGVVVESLVV---MElvglEGRKRLDG---KVHSLIKY 182
Cdd:COG0461  107 -GGLLPGERVLVVEDVITTGGSVLEAVEALREAGAEVVGVAVIvdrEE----GAAENLEEagvPLHSLLTL 172
pyrE PRK00455
orotate phosphoribosyltransferase; Validated
 37-182 8.72e-12

orotate phosphoribosyltransferase; Validated


Pssm-ID: 234771  Cd Length: 202  Bit Score: 60.94  E-value: 8.72e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409664  37 ALTDPKACVYLRDLLVDHIRESAPEAEVIVGLDSRGFLFNLLIATELGLGCAPIRKKGKlagevvsveyklEYGID-TFE 115
Cdd:PRK00455  40 LLSYPEALALLGRFLAEAIKDSGIEFDVVAGPATGGIPLAAAVARALDLPAIFVRKEAK------------DHGEGgQIE 107

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665409664 116 LqksAIKPGQKVVVVDDLLATGGSLVAATELIGKVGGVVVESLVVM--ELVGLEGRKRLDGKVHSLIKY 182
Cdd:PRK00455 108 G---RRLFGKRVLVVEDVITTGGSVLEAVEAIRAAGAEVVGVAVIVdrQSAAQEVFADAGVPLISLITL 173
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 47-176 2.04e-11

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: 58.92  E-value: 2.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409664   47 LRDLLVDHIRESAPEAEVIVGLDSRGFLFNLLIATELGLGCAPIRKKGKLAGEVVSVEYkleygidtfeLQKSAIKPGQK 126
Cdd:pfam00156  15 VARLAAQINEDYGGKPDVVVGILRGGLPFAGILARRLDVPLAFVRKVSYNPDTSEVMKT----------SSALPDLKGKT 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 665409664  127 VVVVDDLLATGGSLVAATELIGKVGGVVVESLVVMElvGLEGRKRLDGKV 176
Cdd:pfam00156  85 VLIVDDILDTGGTLLKVLELLKNVGPKEVKIAVLID--KPAGTEPKDKYD 132
pyrE_Therm TIGR01367
orotate phosphoribosyltransferase, Thermus family; This model represents a distinct clade of ...
 38-155 4.21e-08

orotate phosphoribosyltransferase, Thermus family; This model represents a distinct clade of orotate phosphoribosyltransferases. Members include the experimentally determined example from Thermus aquaticus and additional examples from Caulobacter crescentus, Helicobacter pylori, Mesorhizobium loti, and related species. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273579  Cd Length: 187  Bit Score: 50.56  E-value: 4.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409664   38 LTDPKACVYLRDLLVDHIRESAPEAEVIVGLDSRGFLFNLLIATELglgcapirKKGKLAGEVVSVEYKLEYGIdtfelq 117
Cdd:TIGR01367  35 LEHPEALMELGGELAQKILDYGLKVDFIVGPAMGGVILGYEVARQL--------SVRSIFAEREGGGMKLRRGF------ 100

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 665409664  118 ksAIKPGQKVVVVDDLLATGGSLVAATELIGKVGGVVV 155
Cdd:TIGR01367 101 --AVKPGEKFVAVEDVVTTGGSLLEAIRAIEGQGGQVV 136
PRK07322 PRK07322
adenine phosphoribosyltransferase; Provisional
 60-160 1.84e-07

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 180928  Cd Length: 178  Bit Score: 48.82  E-value: 1.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409664  60 PEAEVIVGLDSRGFLFNLLIATELGLGCAPIRKKGK------LAGEVVSVEYKLEYGI--DTFELQKsaIKpGQKVVVVD 131
Cdd:PRK07322  51 TEVDVLVTPETKGIPLAHALSRRLGKPYVVARKSRKpymqdpIIQEVVSITTGKPQLLvlDGADAEK--LK-GKRVAIVD 127

                         90       100
                 ....*....|....*....|....*....
gi 665409664 132 DLLATGGSLVAATELIGKVGGVVVESLVV 160
Cdd:PRK07322 128 DVVSTGGTLTALERLVERAGGQVVAKAAI 156
ribP_PPkin TIGR01251
ribose-phosphate pyrophosphokinase; Alternate name: phosphoribosylpyrophosphate synthetase In ...
 50-151 3.62e-06

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: 45.73  E-value: 3.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409664   50 LLVDHIRESAPEAEVIVGLDSRGFLFNLLIATELGLGCAPIRKKGKLAGEVVSVEYKLeygIDTfelqksaikPGQKVVV 129
Cdd:TIGR01251 148 VLAEYLKKKILDNPVVVSPDAGGVERAKKVADALGCPLAIIDKRRISATNEVEVMNLV---GDV---------EGKDVVI 215

                          90       100
                  ....*....|....*....|..
gi 665409664  130 VDDLLATGGSLVAATELIGKVG 151
Cdd:TIGR01251 216 VDDIIDTGGTIAKAAEILKSAG 237
PRK05500 PRK05500
bifunctional orotidine-5'-phosphate decarboxylase/orotate phosphoribosyltransferase;
122-160 5.98e-05

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


Pssm-ID: 180119 [Multi-domain]  Cd Length: 477  Bit Score: 42.36  E-value: 5.98e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 665409664 122 KPGQKVVVVDDLLATGGSLVAATELIgKVGGVVVESLVV 160
Cdd:PRK05500 391 HPGETVVVVDDILITGKSVMEGAEKL-KSAGLNVRDIVV 428
PRK02277 PRK02277
orotate phosphoribosyltransferase-like protein; Provisional
 51-181 8.53e-05

orotate phosphoribosyltransferase-like protein; Provisional


Pssm-ID: 235023 [Multi-domain]  Cd Length: 200  Bit Score: 41.39  E-value: 8.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409664  51 LVDHIRESAPEAEVIVGLDSRGFLFNLLIATELGLGCAPIRKKGKLAGEVVSVEykleygiDTFELQKSAIKpGQKVVVV 130
Cdd:PRK02277  75 MADMLEKEDEEVDVVVGIAKSGVPLATLVADELGKDLAIYHPKKWDHGEGEKKT-------GSFSRNFASVE-GKRCVIV 146

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 665409664 131 DDLLATGGSLVAATELIGKVGGVVVESLVVMELVGLEgrkRLDG-KVHSLIK 181
Cdd:PRK02277 147 DDVITSGTTMKETIEYLKEHGGKPVAVVVLIDKSGID---EIDGvPVYSLIR 195
HPT_Archaea NF040646
hypoxanthine/guanine phosphoribosyltransferase;
90-181 9.43e-05

hypoxanthine/guanine phosphoribosyltransferase;


Pssm-ID: 468613  Cd Length: 184  Bit Score: 41.06  E-value: 9.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409664  90 IRK-KGKLAGEVvsvEYKLEYGIDTFELQKSAIKPGQKVVVVDDLLATGGSLVAATELIGKVGGVVVESLVVMELVglEG 168
Cdd:NF040646  82 IRKrKYGLPGEV---EVHQSTGYSKGELYINGINKGDRVLIVDDVISTGGTLIAVIKALEKAGAEIKDVVVVIERG--EG 156

                         90
                 ....*....|....*..
gi 665409664 169 RKRLDGK----VHSLIK 181
Cdd:NF040646 157 KKIVEEKtgykVKTLVK 173
pyrE TIGR00336
orotate phosphoribosyltransferase; Orotate phosphoribosyltransferase (OPRTase) is involved in ...
 120-162 1.03e-04

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: 40.87  E-value: 1.03e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 665409664  120 AIKPGQKVVVVDDLLATGGSLVAATELIGKVGGVVVESLVVME 162
Cdd:TIGR00336 104 ELLEGDKVVVVEDVITTGTSILEAVEIIQAAGGQVAGVIIAVD 146
PRK06031 PRK06031
phosphoribosyltransferase; Provisional
 49-162 3.01e-04

phosphoribosyltransferase; Provisional


Pssm-ID: 235678  Cd Length: 233  Bit Score: 40.12  E-value: 3.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409664  49 DLLVDHIRE--SAPEAEVIVGLDSRGFLFNLLIATELG------LGCApiRK---KGKLAGEVVSveykleygIDTFELQ 117
Cdd:PRK06031  70 DALAEHLAEkaRAFDPDVVAGLPTLGLTLAAAVARKLGhtryvpLGTS--RKfwyRDELSVPLSS--------ITTPDQG 139

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 665409664 118 KSA-IKP-------GQKVVVVDDLLATGGSLVAATELIGKVGGVVVESLVVME 162
Cdd:PRK06031 140 KRLyIDPrmlplleGRRVALIDDVISSGASIVAGLRLLAACGIEPAGIGAAML 192
PRK08558 PRK08558
adenine phosphoribosyltransferase; Provisional
 79-182 3.98e-04

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 181466 [Multi-domain]  Cd Length: 238  Bit Score: 39.59  E-value: 3.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409664  79 IATELGLGCAPIRKKGKLAGEVVSVEY-KLEYGID-TFELQKSAIKPGQKVVVVDDLLATGGSLVAATELIGKVGGVVVE 156
Cdd:PRK08558 129 IASYFGADLVYAKKSKETGVEKFYEEYqRLASGIEvTLYLPASALKKGDRVLIVDDIIRSGETQRALLDLARQAGADVVG 208

                         90       100       110
                 ....*....|....*....|....*....|
gi 665409664 157 SLVVMElVGLEGRKRLDGK----VHSLIKY 182
Cdd:PRK08558 209 VFFLIA-VGEVGIDRAREEtdapVDALYTL 237
PLN02541 PLN02541
uracil phosphoribosyltransferase
 121-160 2.46e-03

uracil phosphoribosyltransferase


Pssm-ID: 215297  Cd Length: 244  Bit Score: 37.46  E-value: 2.46e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 665409664 121 IKPGQKVVVVDDLLATGGSLVAATELIGKVGGVVVESLVV 160
Cdd:PLN02541 154 FPEGSRVLVVDPMLATGGTIVAAIDELVSRGASVEQIRVV 193
PrsA COG0462
Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; ...
 50-147 6.46e-03

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: 36.19  E-value: 6.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409664  50 LLVDHIRESAPEAEVIVGLDSRGFLFNLLIATELGLGCAPIRKKGKLAGEVVS------VEykleygidtfelqksaikp 123
Cdd:COG0462  150 LLADYIKSKDLEDLVVVSPDVGGVKRARAFAKRLGAPLAIIDKRRPGANEVEVmniigdVE------------------- 210

                         90       100
                 ....*....|....*....|....
gi 665409664 124 GQKVVVVDDLLATGGSLVAATELI 147
Cdd:COG0462  211 GKTCIIVDDMIDTGGTLVEAAEAL 234
 
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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