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Conserved domains on  [gi|490589613|ref|WP_004454633|]
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xanthine phosphoribosyltransferase [Clostridioides difficile]

Protein Classification

xanthine phosphoribosyltransferase( domain architecture ID 10013152)

xanthine phosphoribosyltransferase converts the preformed base xanthine, a product of nucleic acid breakdown, to xanthosine 5'-monophosphate (XMP), so it can be reused for RNA or DNA synthesis

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK09219 PRK09219
xanthine phosphoribosyltransferase; Validated
1-190 7.53e-104

xanthine phosphoribosyltransferase; Validated


:

Pssm-ID: 181705  Cd Length: 189  Bit Score: 296.31  E-value: 7.53e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589613   1 MKALQEKILREGSVSGNDILKVDSFLNHQIDVAFLNEIGREFKERFKGEKVDKIFTIEASGIAIASIVSQYFDnAPVVFA 80
Cdd:PRK09219   1 MKLLEERILKDGKVLSGNILKVDSFLNHQVDPKLMNEIGKEFARRFKDEGITKILTIEASGIAPAVMAALALG-VPVVFA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589613  81 KKSESKNLDKDVYETNVYSFTKAREYSVKVSKKYINKGENILIVDDFLANGRAALGLKDLIEQAEANLVGVGIVIEKGFQ 160
Cdd:PRK09219  80 KKKKSLTLTDDVYTATVYSFTKQVTSTVSVSKKFLSEGDRVLIIDDFLANGQAALGLIDIIEQAGAKVAGIGIVIEKSFQ 159
                        170       180       190
                 ....*....|....*....|....*....|
gi 490589613 161 AGGALLKANDVRLESLAVVESIDNGTVKFR 190
Cdd:PRK09219 160 DGRKLLEEKGYRVESLARIASLENGKVTFV 189
 
Name Accession Description Interval E-value
PRK09219 PRK09219
xanthine phosphoribosyltransferase; Validated
1-190 7.53e-104

xanthine phosphoribosyltransferase; Validated


Pssm-ID: 181705  Cd Length: 189  Bit Score: 296.31  E-value: 7.53e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589613   1 MKALQEKILREGSVSGNDILKVDSFLNHQIDVAFLNEIGREFKERFKGEKVDKIFTIEASGIAIASIVSQYFDnAPVVFA 80
Cdd:PRK09219   1 MKLLEERILKDGKVLSGNILKVDSFLNHQVDPKLMNEIGKEFARRFKDEGITKILTIEASGIAPAVMAALALG-VPVVFA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589613  81 KKSESKNLDKDVYETNVYSFTKAREYSVKVSKKYINKGENILIVDDFLANGRAALGLKDLIEQAEANLVGVGIVIEKGFQ 160
Cdd:PRK09219  80 KKKKSLTLTDDVYTATVYSFTKQVTSTVSVSKKFLSEGDRVLIIDDFLANGQAALGLIDIIEQAGAKVAGIGIVIEKSFQ 159
                        170       180       190
                 ....*....|....*....|....*....|
gi 490589613 161 AGGALLKANDVRLESLAVVESIDNGTVKFR 190
Cdd:PRK09219 160 DGRKLLEEKGYRVESLARIASLENGKVTFV 189
XPRTase TIGR01744
xanthine phosphoribosyltransferase; This model represent a xanthine-specific ...
1-189 2.44e-65

xanthine phosphoribosyltransferase; This model represent a xanthine-specific phosphoribosyltransferase of Bacillus subtilis and closely related proteins from other species, mostly from other Gram-positive bacteria. The adjacent gene is a xanthine transporter; B. subtilis can import xanthine for the purine salvage pathway or for catabolism to obtain nitrogen. [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 130805  Cd Length: 191  Bit Score: 198.88  E-value: 2.44e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589613    1 MKALQEKILREGSVSGNDILKVDSFLNHQIDVAFLNEIGREFKERFKGEKVDKIFTIEASGIAIAsIVSQYFDNAPVVFA 80
Cdd:TIGR01744   1 MELLKQKIKEEGVVLPGGILKVDSFLNHQIDPKLMQEVGEEFARRFADDGITKIVTIEASGIAPA-IMTGLKLGVPVVFA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589613   81 KKSESKNLDKDVYETNVYSFTKAREYSVKVSKKYINKGENILIVDDFLANGRAALGLKDLIEQAEANLVGVGIVIEKGFQ 160
Cdd:TIGR01744  80 RKKKPLTLTDNLLTASVHSFTKQTTSTVAVSGEFLSDQDRVLIIDDFLANGQAAHGLVDIAKQAGAKIAGIGIVIEKSFQ 159
                         170       180
                  ....*....|....*....|....*....
gi 490589613  161 AGGALLKANDVRLESLAVVESIDNGTVKF 189
Cdd:TIGR01744 160 NGRQELVELGYRVESLARIQSLEEGKVTF 188
Apt COG0503
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ...
2-179 1.14e-46

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: 150.61  E-value: 1.14e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589613   2 KALQEKILREGSV--SGNDILKVDSFLnhqIDVAFLNEIGREFKERFKGEKVDKIFTIEASGIAIASIVSQYFdNAPVVF 79
Cdd:COG0503    1 EDLKDLIRDIPDFpkPGILFRDITPLL---GDPELFRAAGDELAERFADKGIDKVVGIEARGFILAAALAYAL-GVPFVP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589613  80 AKKSESKNLDkdVYETNVYS-FTKarEYSVKVSKKYINKGENILIVDDFLANGRAALGLKDLIEQAEANLVGVGIVIEKG 158
Cdd:COG0503   77 ARKPGKLPGE--TVSEEYDLeYGT--GDTLELHKDALKPGDRVLIVDDLLATGGTAKAAIKLVEEAGAEVVGIAFLIELG 152
                        170       180
                 ....*....|....*....|.
gi 490589613 159 FQAGGALLKanDVRLESLAVV 179
Cdd:COG0503  153 FLGGREKLR--DYPVESLLTL 171
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
38-178 1.14e-11

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: 59.33  E-value: 1.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589613  38 IGREFKERFK--GEKVDKIFTIEASGIAIASIVSQYFdNAPVVFAKKsesknldkdvyETNVYSFTKAREYSVKVSKKYI 115
Cdd:cd06223    1 AGRLLAEEIRedLLEPDVVVGILRGGLPLAAALARAL-GLPLAFIRK-----------ERKGPGRTPSEPYGLELPLGGD 68
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490589613 116 NKGENILIVDDFLANGRAALGLKDLIEQAEANLVGVGIVIEKgFQAGGALLKANDVRLESLAV 178
Cdd:cd06223   69 VKGKRVLLVDDVIATGGTLLAAIELLKEAGAKVVGVAVLLDK-PEGGARELASPGDPVYSLFT 130
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
22-158 8.07e-06

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: 43.89  E-value: 8.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589613   22 VDSFLNHQidvAFLNEIGREFKERF--KGEKVDKIFTIEASGIAIASIVSQYFDNAPVVFAKKSesknldkdvYETNVYS 99
Cdd:pfam00156   2 VDEILDNP---AILKAVARLAAQINedYGGKPDVVVGILRGGLPFAGILARRLDVPLAFVRKVS---------YNPDTSE 69
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 490589613  100 FTKAreysvkVSKKYINKGENILIVDDFLANGRAALGLKDLIEQAEANLVGVGIVIEKG 158
Cdd:pfam00156  70 VMKT------SSALPDLKGKTVLIVDDILDTGGTLLKVLELLKNVGPKEVKIAVLIDKP 122
 
Name Accession Description Interval E-value
PRK09219 PRK09219
xanthine phosphoribosyltransferase; Validated
1-190 7.53e-104

xanthine phosphoribosyltransferase; Validated


Pssm-ID: 181705  Cd Length: 189  Bit Score: 296.31  E-value: 7.53e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589613   1 MKALQEKILREGSVSGNDILKVDSFLNHQIDVAFLNEIGREFKERFKGEKVDKIFTIEASGIAIASIVSQYFDnAPVVFA 80
Cdd:PRK09219   1 MKLLEERILKDGKVLSGNILKVDSFLNHQVDPKLMNEIGKEFARRFKDEGITKILTIEASGIAPAVMAALALG-VPVVFA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589613  81 KKSESKNLDKDVYETNVYSFTKAREYSVKVSKKYINKGENILIVDDFLANGRAALGLKDLIEQAEANLVGVGIVIEKGFQ 160
Cdd:PRK09219  80 KKKKSLTLTDDVYTATVYSFTKQVTSTVSVSKKFLSEGDRVLIIDDFLANGQAALGLIDIIEQAGAKVAGIGIVIEKSFQ 159
                        170       180       190
                 ....*....|....*....|....*....|
gi 490589613 161 AGGALLKANDVRLESLAVVESIDNGTVKFR 190
Cdd:PRK09219 160 DGRKLLEEKGYRVESLARIASLENGKVTFV 189
XPRTase TIGR01744
xanthine phosphoribosyltransferase; This model represent a xanthine-specific ...
1-189 2.44e-65

xanthine phosphoribosyltransferase; This model represent a xanthine-specific phosphoribosyltransferase of Bacillus subtilis and closely related proteins from other species, mostly from other Gram-positive bacteria. The adjacent gene is a xanthine transporter; B. subtilis can import xanthine for the purine salvage pathway or for catabolism to obtain nitrogen. [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 130805  Cd Length: 191  Bit Score: 198.88  E-value: 2.44e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589613    1 MKALQEKILREGSVSGNDILKVDSFLNHQIDVAFLNEIGREFKERFKGEKVDKIFTIEASGIAIAsIVSQYFDNAPVVFA 80
Cdd:TIGR01744   1 MELLKQKIKEEGVVLPGGILKVDSFLNHQIDPKLMQEVGEEFARRFADDGITKIVTIEASGIAPA-IMTGLKLGVPVVFA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589613   81 KKSESKNLDKDVYETNVYSFTKAREYSVKVSKKYINKGENILIVDDFLANGRAALGLKDLIEQAEANLVGVGIVIEKGFQ 160
Cdd:TIGR01744  80 RKKKPLTLTDNLLTASVHSFTKQTTSTVAVSGEFLSDQDRVLIIDDFLANGQAAHGLVDIAKQAGAKIAGIGIVIEKSFQ 159
                         170       180
                  ....*....|....*....|....*....
gi 490589613  161 AGGALLKANDVRLESLAVVESIDNGTVKF 189
Cdd:TIGR01744 160 NGRQELVELGYRVESLARIQSLEEGKVTF 188
Apt COG0503
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ...
2-179 1.14e-46

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: 150.61  E-value: 1.14e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589613   2 KALQEKILREGSV--SGNDILKVDSFLnhqIDVAFLNEIGREFKERFKGEKVDKIFTIEASGIAIASIVSQYFdNAPVVF 79
Cdd:COG0503    1 EDLKDLIRDIPDFpkPGILFRDITPLL---GDPELFRAAGDELAERFADKGIDKVVGIEARGFILAAALAYAL-GVPFVP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589613  80 AKKSESKNLDkdVYETNVYS-FTKarEYSVKVSKKYINKGENILIVDDFLANGRAALGLKDLIEQAEANLVGVGIVIEKG 158
Cdd:COG0503   77 ARKPGKLPGE--TVSEEYDLeYGT--GDTLELHKDALKPGDRVLIVDDLLATGGTAKAAIKLVEEAGAEVVGIAFLIELG 152
                        170       180
                 ....*....|....*....|.
gi 490589613 159 FQAGGALLKanDVRLESLAVV 179
Cdd:COG0503  153 FLGGREKLR--DYPVESLLTL 171
PRK08558 PRK08558
adenine phosphoribosyltransferase; Provisional
31-180 4.25e-20

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 181466 [Multi-domain]  Cd Length: 238  Bit Score: 84.27  E-value: 4.25e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589613  31 DVAFLNEIGREFKERFKGEKVDKIFTIEASGIAIASIVSQYFDnAPVVFAKKSESKNLDKdVYETNVYSfTKAREYSVKV 110
Cdd:PRK08558  92 DPSFLRLIAPVVAERFMGLRVDVVLTAATDGIPLAVAIASYFG-ADLVYAKKSKETGVEK-FYEEYQRL-ASGIEVTLYL 168
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589613 111 SKKYINKGENILIVDDFLANGRAALGLKDLIEQAEANLVGVGIVIEKGFQAGGALLKANDVRLESLAVVE 180
Cdd:PRK08558 169 PASALKKGDRVLIVDDIIRSGETQRALLDLARQAGADVVGVFFLIAVGEVGIDRAREETDAPVDALYTLE 238
PRK02304 PRK02304
adenine phosphoribosyltransferase; Provisional
35-176 2.55e-16

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 235028  Cd Length: 175  Bit Score: 72.80  E-value: 2.55e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589613  35 LNEIGREFKERFKGEKVDKIFTIEASGIAIASIVSqYFDNAPVVFAKKSEsknldKDVYETnvYSFTKAREYS---VKVS 111
Cdd:PRK02304  36 FREVIDALVERYKDADIDKIVGIEARGFIFGAALA-YKLGIGFVPVRKPG-----KLPRET--ISESYELEYGtdtLEIH 107
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490589613 112 KKYINKGENILIVDDFLANGRAALGLKDLIEQAEANLVGVGIVIEKGFQAGGALLKanDVRLESL 176
Cdd:PRK02304 108 KDAIKPGDRVLIVDDLLATGGTLEAAIKLLERLGAEVVGAAFVIELPDLGGREKLE--GYPVKSL 170
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
38-178 1.14e-11

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: 59.33  E-value: 1.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589613  38 IGREFKERFK--GEKVDKIFTIEASGIAIASIVSQYFdNAPVVFAKKsesknldkdvyETNVYSFTKAREYSVKVSKKYI 115
Cdd:cd06223    1 AGRLLAEEIRedLLEPDVVVGILRGGLPLAAALARAL-GLPLAFIRK-----------ERKGPGRTPSEPYGLELPLGGD 68
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490589613 116 NKGENILIVDDFLANGRAALGLKDLIEQAEANLVGVGIVIEKgFQAGGALLKANDVRLESLAV 178
Cdd:cd06223   69 VKGKRVLLVDDVIATGGTLLAAIELLKEAGAKVVGVAVLLDK-PEGGARELASPGDPVYSLFT 130
PRK12560 PRK12560
adenine phosphoribosyltransferase; Provisional
50-157 3.12e-07

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 183595  Cd Length: 187  Bit Score: 48.24  E-value: 3.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589613  50 KVDKIFTIEASGIAIASIVSQyFDNAPVVFAKKSESK--NLDKDVYETNVYSFtkareySVKVSKKYINKGENILIVDDF 127
Cdd:PRK12560  51 DIDKIVTEEDKGAPLATPVSL-LSGKPLAMARWYPYSlsELNYNVVEIGSEYF------EGVVYLNGIEKGDRVAIIDDT 123
                         90       100       110
                 ....*....|....*....|....*....|
gi 490589613 128 LANGRAALGLKDLIEQAEANLVGVGIVIEK 157
Cdd:PRK12560 124 LSTGGTVIALIKAIENSGGIVSDVICVIEK 153
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
22-158 8.07e-06

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: 43.89  E-value: 8.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589613   22 VDSFLNHQidvAFLNEIGREFKERF--KGEKVDKIFTIEASGIAIASIVSQYFDNAPVVFAKKSesknldkdvYETNVYS 99
Cdd:pfam00156   2 VDEILDNP---AILKAVARLAAQINedYGGKPDVVVGILRGGLPFAGILARRLDVPLAFVRKVS---------YNPDTSE 69
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 490589613  100 FTKAreysvkVSKKYINKGENILIVDDFLANGRAALGLKDLIEQAEANLVGVGIVIEKG 158
Cdd:pfam00156  70 VMKT------SSALPDLKGKTVLIVDDILDTGGTLLKVLELLKNVGPKEVKIAVLIDKP 122
PLN02293 PLN02293
adenine phosphoribosyltransferase
42-162 1.69e-04

adenine phosphoribosyltransferase


Pssm-ID: 177930  Cd Length: 187  Bit Score: 40.43  E-value: 1.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589613  42 FKERFKGEKVDKIFTIEASG------IAIASivsqyfdNAPVVFAKKSesKNLDKDV----YETnvysftkarEYS---V 108
Cdd:PLN02293  54 FVERYRDMGISVVAGIEARGfifgppIALAI-------GAKFVPLRKP--GKLPGEViseeYVL---------EYGtdcL 115
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 490589613 109 KVSKKYINKGENILIVDDFLANGRAALGLKDLIEQAEANLVGVGIVIEKGFQAG 162
Cdd:PLN02293 116 EMHVGAVEPGERALVIDDLIATGGTLCAAINLLERAGAEVVECACVIELPELKG 169
pyrE PRK00455
orotate phosphoribosyltransferase; Validated
35-177 1.69e-03

orotate phosphoribosyltransferase; Validated


Pssm-ID: 234771  Cd Length: 202  Bit Score: 37.83  E-value: 1.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589613  35 LNEIGREFKERFK--GEKVDKIFTIEASGIAIASIVSQYFdNAPVVFAKKSEsknldKDVYETNVysFTKAREysvkvsk 112
Cdd:PRK00455  47 LALLGRFLAEAIKdsGIEFDVVAGPATGGIPLAAAVARAL-DLPAIFVRKEA-----KDHGEGGQ--IEGRRL------- 111
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490589613 113 kyinKGENILIVDDFLANGRAALGLKDLIEQAEANLVGVGIVIEKGfQAGGALLKANDVRLESLA 177
Cdd:PRK00455 112 ----FGKRVLVVEDVITTGGSVLEAVEAIRAAGAEVVGVAVIVDRQ-SAAQEVFADAGVPLISLI 171
 
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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