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Conserved domains on  [gi|502909665|ref|WP_013144641|]
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MULTISPECIES: adenine phosphoribosyltransferase [Bacillaceae]

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
1-170 3.41e-102

adenine phosphoribosyltransferase; Provisional


:

Pssm-ID: 235028  Cd Length: 175  Bit Score: 290.82  E-value: 3.41e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502909665   1 MDLKQYITIVPDFPKPGIMFKDITTLMDNGPAYKYATDQIVQYAREKQIDIVVGPEARGFIIGCPVAYALGVGFAPVRKE 80
Cdd:PRK02304   4 EDLKSSIRTIPDFPKPGILFRDITPLLADPEAFREVIDALVERYKDADIDKIVGIEARGFIFGAALAYKLGIGFVPVRKP 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502909665  81 GKLPREVVRVEYGLEYGTDVLTMHKDAIKPGQRVLITDDLLATGGTMRATIDLVEQLGGVVAGLAFLIELTELGGRKKLE 160
Cdd:PRK02304  84 GKLPRETISESYELEYGTDTLEIHKDAIKPGDRVLIVDDLLATGGTLEAAIKLLERLGAEVVGAAFVIELPDLGGREKLE 163
                        170
                 ....*....|
gi 502909665 161 GYDILTLMQF 170
Cdd:PRK02304 164 GYPVKSLVKF 173
 
Name Accession Description Interval E-value
PRK02304 PRK02304
adenine phosphoribosyltransferase; Provisional
1-170 3.41e-102

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 235028  Cd Length: 175  Bit Score: 290.82  E-value: 3.41e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502909665   1 MDLKQYITIVPDFPKPGIMFKDITTLMDNGPAYKYATDQIVQYAREKQIDIVVGPEARGFIIGCPVAYALGVGFAPVRKE 80
Cdd:PRK02304   4 EDLKSSIRTIPDFPKPGILFRDITPLLADPEAFREVIDALVERYKDADIDKIVGIEARGFIFGAALAYKLGIGFVPVRKP 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502909665  81 GKLPREVVRVEYGLEYGTDVLTMHKDAIKPGQRVLITDDLLATGGTMRATIDLVEQLGGVVAGLAFLIELTELGGRKKLE 160
Cdd:PRK02304  84 GKLPRETISESYELEYGTDTLEIHKDAIKPGDRVLIVDDLLATGGTLEAAIKLLERLGAEVVGAAFVIELPDLGGREKLE 163
                        170
                 ....*....|
gi 502909665 161 GYDILTLMQF 170
Cdd:PRK02304 164 GYPVKSLVKF 173
apt TIGR01090
adenine phosphoribosyltransferase; A phylogenetic analysis suggested omitting the ...
3-170 3.44e-94

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: 270.30  E-value: 3.44e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502909665    3 LKQYITIVPDFPKPGIMFKDITTLMDNGPAYKYATDQIVQYAREKQIDIVVGPEARGFIIGCPVAYALGVGFAPVRKEGK 82
Cdd:TIGR01090   1 LKQAIRSIPDFPKKGILFRDITPLLNNPELFRFLIDLLVERYKDANIDYIVGPEARGFIFGAALAYKLGVGFVPVRKPGK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502909665   83 LPREVVRVEYGLEYGTDVLTMHKDAIKPGQRVLITDDLLATGGTMRATIDLVEQLGGVVAGLAFLIELTELGGRKKLEG- 161
Cdd:TIGR01090  81 LPGETISASYDLEYGKDVLEIHKDAIKPGQRVLIVDDLLATGGTAAATDELIKKLGGEVVEAAFLIELKDLNGRAKLEPn 160

                  ....*....
gi 502909665  162 YDILTLMQF 170
Cdd:TIGR01090 161 VPVFSLLEY 169
Apt COG0503
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ...
1-170 5.41e-87

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: 252.30  E-value: 5.41e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502909665   1 MDLKQYITIVPDFPKPGIMFKDITTLMDNGPAYKYATDQIVQYAREKQIDIVVGPEARGFIIGCPVAYALGVGFAPVRKE 80
Cdd:COG0503    1 EDLKDLIRDIPDFPKPGILFRDITPLLGDPELFRAAGDELAERFADKGIDKVVGIEARGFILAAALAYALGVPFVPARKP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502909665  81 GKLPREVVRVEYGLEYGT-DVLTMHKDAIKPGQRVLITDDLLATGGTMRATIDLVEQLGGVVAGLAFLIELTELGGRKKL 159
Cdd:COG0503   81 GKLPGETVSEEYDLEYGTgDTLELHKDALKPGDRVLIVDDLLATGGTAKAAIKLVEEAGAEVVGIAFLIELGFLGGREKL 160
                        170
                 ....*....|.
gi 502909665 160 EGYDILTLMQF 170
Cdd:COG0503  161 RDYPVESLLTL 171
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
36-165 1.17e-26

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: 97.85  E-value: 1.17e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502909665  36 ATDQIVQYAREK--QIDIVVGPEARGFIIGCPVAYALGVGFAPVRKEGKLPREVVRVEYGLEygtdvltMHKDAIKPGQR 113
Cdd:cd06223    1 AGRLLAEEIREDllEPDVVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPSEPYGLE-------LPLGGDVKGKR 73
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 502909665 114 VLITDDLLATGGTMRATIDLVEQLGGVVAGLAFLIELTELGGRKKLEGYDIL 165
Cdd:cd06223   74 VLLVDDVIATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGGARELASPGDPV 125
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
39-149 1.84e-13

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: 63.92  E-value: 1.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502909665   39 QIVQYAREKQiDIVVGPEARGFIIGCPVAYALGVGFAPVRKEGKLPrevvrveyglEYGTDVLTMHKDAIKPGQRVLITD 118
Cdd:pfam00156  21 QINEDYGGKP-DVVVGILRGGLPFAGILARRLDVPLAFVRKVSYNP----------DTSEVMKTSSALPDLKGKTVLIVD 89
                          90       100       110
                  ....*....|....*....|....*....|.
gi 502909665  119 DLLATGGTMRATIDLVEQLGGVVAGLAFLIE 149
Cdd:pfam00156  90 DILDTGGTLLKVLELLKNVGPKEVKIAVLID 120
 
Name Accession Description Interval E-value
PRK02304 PRK02304
adenine phosphoribosyltransferase; Provisional
1-170 3.41e-102

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 235028  Cd Length: 175  Bit Score: 290.82  E-value: 3.41e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502909665   1 MDLKQYITIVPDFPKPGIMFKDITTLMDNGPAYKYATDQIVQYAREKQIDIVVGPEARGFIIGCPVAYALGVGFAPVRKE 80
Cdd:PRK02304   4 EDLKSSIRTIPDFPKPGILFRDITPLLADPEAFREVIDALVERYKDADIDKIVGIEARGFIFGAALAYKLGIGFVPVRKP 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502909665  81 GKLPREVVRVEYGLEYGTDVLTMHKDAIKPGQRVLITDDLLATGGTMRATIDLVEQLGGVVAGLAFLIELTELGGRKKLE 160
Cdd:PRK02304  84 GKLPRETISESYELEYGTDTLEIHKDAIKPGDRVLIVDDLLATGGTLEAAIKLLERLGAEVVGAAFVIELPDLGGREKLE 163
                        170
                 ....*....|
gi 502909665 161 GYDILTLMQF 170
Cdd:PRK02304 164 GYPVKSLVKF 173
apt TIGR01090
adenine phosphoribosyltransferase; A phylogenetic analysis suggested omitting the ...
3-170 3.44e-94

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: 270.30  E-value: 3.44e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502909665    3 LKQYITIVPDFPKPGIMFKDITTLMDNGPAYKYATDQIVQYAREKQIDIVVGPEARGFIIGCPVAYALGVGFAPVRKEGK 82
Cdd:TIGR01090   1 LKQAIRSIPDFPKKGILFRDITPLLNNPELFRFLIDLLVERYKDANIDYIVGPEARGFIFGAALAYKLGVGFVPVRKPGK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502909665   83 LPREVVRVEYGLEYGTDVLTMHKDAIKPGQRVLITDDLLATGGTMRATIDLVEQLGGVVAGLAFLIELTELGGRKKLEG- 161
Cdd:TIGR01090  81 LPGETISASYDLEYGKDVLEIHKDAIKPGQRVLIVDDLLATGGTAAATDELIKKLGGEVVEAAFLIELKDLNGRAKLEPn 160

                  ....*....
gi 502909665  162 YDILTLMQF 170
Cdd:TIGR01090 161 VPVFSLLEY 169
Apt COG0503
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ...
1-170 5.41e-87

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: 252.30  E-value: 5.41e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502909665   1 MDLKQYITIVPDFPKPGIMFKDITTLMDNGPAYKYATDQIVQYAREKQIDIVVGPEARGFIIGCPVAYALGVGFAPVRKE 80
Cdd:COG0503    1 EDLKDLIRDIPDFPKPGILFRDITPLLGDPELFRAAGDELAERFADKGIDKVVGIEARGFILAAALAYALGVPFVPARKP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502909665  81 GKLPREVVRVEYGLEYGT-DVLTMHKDAIKPGQRVLITDDLLATGGTMRATIDLVEQLGGVVAGLAFLIELTELGGRKKL 159
Cdd:COG0503   81 GKLPGETVSEEYDLEYGTgDTLELHKDALKPGDRVLIVDDLLATGGTAKAAIKLVEEAGAEVVGIAFLIELGFLGGREKL 160
                        170
                 ....*....|.
gi 502909665 160 EGYDILTLMQF 170
Cdd:COG0503  161 RDYPVESLLTL 171
PLN02293 PLN02293
adenine phosphoribosyltransferase
7-167 4.03e-66

adenine phosphoribosyltransferase


Pssm-ID: 177930  Cd Length: 187  Bit Score: 199.90  E-value: 4.03e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502909665   7 ITIVPDFPKPGIMFKDITTLMDNGPAYKYATDQIVQYAREKQIDIVVGPEARGFIIGCPVAYALGVGFAPVRKEGKLPRE 86
Cdd:PLN02293  21 IRVVPDFPKPGIMFQDITTLLLDPKAFKDTIDLFVERYRDMGISVVAGIEARGFIFGPPIALAIGAKFVPLRKPGKLPGE 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502909665  87 VVRVEYGLEYGTDVLTMHKDAIKPGQRVLITDDLLATGGTMRATIDLVEQLGGVVAGLAFLIELTELGGRKKLEGYDILT 166
Cdd:PLN02293 101 VISEEYVLEYGTDCLEMHVGAVEPGERALVIDDLIATGGTLCAAINLLERAGAEVVECACVIELPELKGREKLNGKPLFV 180

                 .
gi 502909665 167 L 167
Cdd:PLN02293 181 L 181
PRK12560 PRK12560
adenine phosphoribosyltransferase; Provisional
1-170 1.85e-41

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 183595  Cd Length: 187  Bit Score: 137.22  E-value: 1.85e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502909665   1 MDLKQYITIVPDFPKPGIM--FKDITTLMdNGPAYKYATDQIVQYArEKQIDIVVGPEARGFIIGCPVAYalgVGFAPVR 78
Cdd:PRK12560   4 KNLYKNARVVNSGKALTTVneFTDQLPAL-RPKVLKETAKEIIKYI-DKDIDKIVTEEDKGAPLATPVSL---LSGKPLA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502909665  79 KEGKLPREVVRVEY-GLEYGTDVL--TMHKDAIKPGQRVLITDDLLATGGTMRATIDLVEQLGGVVAGLAFLIELTELGG 155
Cdd:PRK12560  79 MARWYPYSLSELNYnVVEIGSEYFegVVYLNGIEKGDRVAIIDDTLSTGGTVIALIKAIENSGGIVSDVICVIEKTQNNG 158
                        170
                 ....*....|....*...
gi 502909665 156 RKKLE---GYDILTLMQF 170
Cdd:PRK12560 159 RKKLFtqtGINVKSLVKI 176
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
36-165 1.17e-26

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: 97.85  E-value: 1.17e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502909665  36 ATDQIVQYAREK--QIDIVVGPEARGFIIGCPVAYALGVGFAPVRKEGKLPREVVRVEYGLEygtdvltMHKDAIKPGQR 113
Cdd:cd06223    1 AGRLLAEEIREDllEPDVVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPSEPYGLE-------LPLGGDVKGKR 73
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 502909665 114 VLITDDLLATGGTMRATIDLVEQLGGVVAGLAFLIELTELGGRKKLEGYDIL 165
Cdd:cd06223   74 VLLVDDVIATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGGARELASPGDPV 125
PyrE COG0461
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ...
44-164 1.54e-15

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


Pssm-ID: 440229  Cd Length: 201  Bit Score: 70.57  E-value: 1.54e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502909665  44 AREKQIDIVVGPEARGFIIGCPVAYALGVGFAPVRKEGKlprevvrveyglEYGTDVLTmhKDAIKPGQRVLITDDLLAT 123
Cdd:COG0461   59 ELGPEFDAVAGPATGGIPLAAAVARALGLPAIFVRKEAK------------DHGTGGQI--EGGLLPGERVLVVEDVITT 124
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 502909665 124 GGTMRATIDLVEQLGGVVAGLAFLIELTElGGRKKLEGYDI 164
Cdd:COG0461  125 GGSVLEAVEALREAGAEVVGVAVIVDREE-GAAENLEEAGV 164
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
39-149 1.84e-13

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: 63.92  E-value: 1.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502909665   39 QIVQYAREKQiDIVVGPEARGFIIGCPVAYALGVGFAPVRKEGKLPrevvrveyglEYGTDVLTMHKDAIKPGQRVLITD 118
Cdd:pfam00156  21 QINEDYGGKP-DVVVGILRGGLPFAGILARRLDVPLAFVRKVSYNP----------DTSEVMKTSSALPDLKGKTVLIVD 89
                          90       100       110
                  ....*....|....*....|....*....|.
gi 502909665  119 DLLATGGTMRATIDLVEQLGGVVAGLAFLIE 149
Cdd:pfam00156  90 DILDTGGTLLKVLELLKNVGPKEVKIAVLID 120
PRK09219 PRK09219
xanthine phosphoribosyltransferase; Validated
45-167 5.14e-13

xanthine phosphoribosyltransferase; Validated


Pssm-ID: 181705  Cd Length: 189  Bit Score: 63.65  E-value: 5.14e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502909665  45 REKQIDIVVGPEARGFIIGCPVAYALGVG--FAPVRKEGKLPREVvrveygleYGTDV----------LTMHKDAIKPGQ 112
Cdd:PRK09219  47 KDEGITKILTIEASGIAPAVMAALALGVPvvFAKKKKSLTLTDDV--------YTATVysftkqvtstVSVSKKFLSEGD 118
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 502909665 113 RVLITDDLLATGGTMRATIDLVEQLGGVVAGLAFLIELTELGGRKKLE--GYDILTL 167
Cdd:PRK09219 119 RVLIIDDFLANGQAALGLIDIIEQAGAKVAGIGIVIEKSFQDGRKLLEekGYRVESL 175
pyrE_Therm TIGR01367
orotate phosphoribosyltransferase, Thermus family; This model represents a distinct clade of ...
48-170 1.40e-11

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: 59.80  E-value: 1.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502909665   48 QIDIVVGPEARGFIIGCPVAYALGVGFAPVRKEGKlpreVVRVEYGLEygtdvltmhkdaIKPGQRVLITDDLLATGGTM 127
Cdd:TIGR01367  58 KVDFIVGPAMGGVILGYEVARQLSVRSIFAEREGG----GMKLRRGFA------------VKPGEKFVAVEDVVTTGGSL 121
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 502909665  128 RATIDLVEQLGGVVAGLAFLIELTElgGRKKLEGYDILTLMQF 170
Cdd:TIGR01367 122 LEAIRAIEGQGGQVVGLACIIDRSQ--GGKPDSGVPLMSLKEL 162
pyrE PRK00455
orotate phosphoribosyltransferase; Validated
27-145 2.49e-11

orotate phosphoribosyltransferase; Validated


Pssm-ID: 234771  Cd Length: 202  Bit Score: 59.40  E-value: 2.49e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502909665  27 MDNGPAYKY--ATDQIVQYAREK------QIDIVVGPEARGFIIGCPVAYALGVGFAPVRKEGKlprevvrveyglEYGT 98
Cdd:PRK00455  35 FDCRKLLSYpeALALLGRFLAEAikdsgiEFDVVAGPATGGIPLAAAVARALDLPAIFVRKEAK------------DHGE 102
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 502909665  99 D---VLtmhkdAIKPGQRVLITDDLLATGGTMRATIDLVEQLGGVVAGLA 145
Cdd:PRK00455 103 GgqiEG-----RRLFGKRVLVVEDVITTGGSVLEAVEAIRAAGAEVVGVA 147
PRK08558 PRK08558
adenine phosphoribosyltransferase; Provisional
47-164 3.11e-11

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 181466 [Multi-domain]  Cd Length: 238  Bit Score: 59.62  E-value: 3.11e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502909665  47 KQIDIVVGPEARGFIIGCPVAYALGVGFAPVRKEgklpREVVRVEYGLEY-----GTDV-LTMHKDAIKPGQRVLITDDL 120
Cdd:PRK08558 110 LRVDVVLTAATDGIPLAVAIASYFGADLVYAKKS----KETGVEKFYEEYqrlasGIEVtLYLPASALKKGDRVLIVDDI 185
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 502909665 121 LATGGTMRATIDLVEQLGGVVAGLAFLIELTELGGRKKLEGYDI 164
Cdd:PRK08558 186 IRSGETQRALLDLARQAGADVVGVFFLIAVGEVGIDRAREETDA 229
PRK07322 PRK07322
adenine phosphoribosyltransferase; Provisional
49-149 1.70e-08

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 180928  Cd Length: 178  Bit Score: 51.13  E-value: 1.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502909665  49 IDIVVGPEARGFIIGCPVAYALGVGFAPVRKEGK------LPREVVRVEYGLEY-----GTDVltmhkDAIKpGQRVLIT 117
Cdd:PRK07322  53 VDVLVTPETKGIPLAHALSRRLGKPYVVARKSRKpymqdpIIQEVVSITTGKPQllvldGADA-----EKLK-GKRVAIV 126
                         90       100       110
                 ....*....|....*....|....*....|...
gi 502909665 118 DDLLATGGTMRATIDLVEQLGG-VVAGLAFLIE 149
Cdd:PRK07322 127 DDVVSTGGTLTALERLVERAGGqVVAKAAIFAE 159
ribP_PPkin TIGR01251
ribose-phosphate pyrophosphokinase; Alternate name: phosphoribosylpyrophosphate synthetase In ...
35-138 3.83e-05

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: 42.65  E-value: 3.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502909665   35 YATDQIVQYAREKQID--IVVGPEARGFIIGCPVAYALGVGFAPVRKEGKLPREVVRVeygleygtdvltMHKDAIKPGQ 112
Cdd:TIGR01251 144 YASPVLAEYLKKKILDnpVVVSPDAGGVERAKKVADALGCPLAIIDKRRISATNEVEV------------MNLVGDVEGK 211
                          90       100
                  ....*....|....*....|....*.
gi 502909665  113 RVLITDDLLATGGTMRATIDLVEQLG 138
Cdd:TIGR01251 212 DVVIVDDIIDTGGTIAKAAEILKSAG 237
Hpt1 COG2236
Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism]; Hypoxanthine ...
27-138 2.00e-04

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: 39.44  E-value: 2.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502909665  27 MDNGPAYKYATDQIVQYARE--KQI-------DIVVGPeAR-GFIIGCPVAYALGV-GFAPVR----KEGKLPREVVRVE 91
Cdd:COG2236    1 MDKFKKEYLSWDEIHELSRRlaEQIlesgfrpDVIVAI-ARgGLVPARILADALGVpDLASIRvssyTGTAKRLEEPVVK 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 502909665  92 YGLeygTDVLTmhkdaikpGQRVLITDDLLATGGTMRATIDLVEQLG 138
Cdd:COG2236   80 GPL---DEDLA--------GKRVLIVDDVADTGRTLEAVRDLLKEAG 115
PLN02541 PLN02541
uracil phosphoribosyltransferase
106-141 2.39e-04

uracil phosphoribosyltransferase


Pssm-ID: 215297  Cd Length: 244  Bit Score: 40.15  E-value: 2.39e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 502909665 106 DAIKPGQRVLITDDLLATGGTMRATIDLVEQLGGVV 141
Cdd:PLN02541 152 DKFPEGSRVLVVDPMLATGGTIVAAIDELVSRGASV 187
PrsA COG0462
Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; ...
35-138 4.30e-04

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: 39.66  E-value: 4.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502909665  35 YATDQIVQYAREKQID--IVVGPE------ARGFiigcpvAYALGVGFAPVRKEGKLPREVVrveygleygtdvlTMHKD 106
Cdd:COG0462  146 YAAPLLADYIKSKDLEdlVVVSPDvggvkrARAF------AKRLGAPLAIIDKRRPGANEVE-------------VMNII 206
                         90       100       110
                 ....*....|....*....|....*....|...
gi 502909665 107 -AIKpGQRVLITDDLLATGGTMRATIDLVEQLG 138
Cdd:COG0462  207 gDVE-GKTCIIVDDMIDTGGTLVEAAEALKEAG 238
upp PRK00129
uracil phosphoribosyltransferase; Reviewed
111-138 2.82e-03

uracil phosphoribosyltransferase; Reviewed


Pssm-ID: 234653  Cd Length: 209  Bit Score: 36.60  E-value: 2.82e-03
                         10        20
                 ....*....|....*....|....*...
gi 502909665 111 GQRVLITDDLLATGGTMRATIDLVEQLG 138
Cdd:PRK00129 124 ERTVIVVDPMLATGGSAIAAIDLLKKRG 151
PRK02277 PRK02277
orotate phosphoribosyltransferase-like protein; Provisional
45-148 5.75e-03

orotate phosphoribosyltransferase-like protein; Provisional


Pssm-ID: 235023 [Multi-domain]  Cd Length: 200  Bit Score: 36.00  E-value: 5.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502909665  45 REKQIDIVVGPEARGFIIGCPVAYALGVGFA-----------PVRKEGKLPREVVRVEygleygtdvltmhkdaikpGQR 113
Cdd:PRK02277  82 EDEEVDVVVGIAKSGVPLATLVADELGKDLAiyhpkkwdhgeGEKKTGSFSRNFASVE-------------------GKR 142
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 502909665 114 VLITDDLLATGGTMRATIDLVEQLGGVVAGLAFLI 148
Cdd:PRK02277 143 CVIVDDVITSGTTMKETIEYLKEHGGKPVAVVVLI 177
COG1926 COG1926
Predicted phosphoribosyltransferase [General function prediction only];
111-138 8.81e-03

Predicted phosphoribosyltransferase [General function prediction only];


Pssm-ID: 441529  Cd Length: 209  Bit Score: 35.43  E-value: 8.81e-03
                         10        20
                 ....*....|....*....|....*...
gi 502909665 111 GQRVLITDDLLATGGTMRATIDLVEQLG 138
Cdd:COG1926  121 GRTVILVDDGIATGATMRAALRALRRQG 148
 
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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