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Conserved domains on  [gi|1081348499|gb|OFU86743|]
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xanthine phosphoribosyltransferase [Streptococcus sp. HMSC10E12]

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

EC:  2.4.2.22
Gene Ontology:  GO:0016763|GO:0046110|GO:0043101|GO:0000310
PubMed:  16716072|9100006|11933250

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK09219 PRK09219
xanthine phosphoribosyltransferase; Validated
 1-189 4.84e-125

xanthine phosphoribosyltransferase; Validated


:

Pssm-ID: 181705  Cd Length: 189  Bit Score: 350.24  E-value: 4.84e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348499   1 MKLLEDRILKDGNVLGENILKVDSFLTHQVDFDLMREIGKVFAEKFKDAGITKVVTIEASGIAPALYAAEALDVPMIFAK 80
Cdd:PRK09219    1 MKLLEERILKDGKVLSGNILKVDSFLNHQVDPKLMNEIGKEFARRFKDEGITKILTIEASGIAPAVMAALALGVPVVFAK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348499  81 KAKNITMNEGILTAEVYSFTKQVTSTVSIASKFLTPEDKVLIVDDFLANGQAAKGLIQIIEEAGAHVEAVGIVIEKSFQD 160
Cdd:PRK09219   81 KKKSLTLTDDVYTATVYSFTKQVTSTVSVSKKFLSEGDRVLIIDDFLANGQAALGLIDIIEQAGAKVAGIGIVIEKSFQD 160

                         170       180
                  ....*....|....*....|....*....
gi 1081348499 161 GRALLEEAGYPVVSLARLDRFENGQVVFK 189
Cdd:PRK09219  161 GRKLLEEKGYRVESLARIASLENGKVTFV 189
 
Name Accession Description Interval E-value
PRK09219 PRK09219
xanthine phosphoribosyltransferase; Validated
 1-189 4.84e-125

xanthine phosphoribosyltransferase; Validated


Pssm-ID: 181705  Cd Length: 189  Bit Score: 350.24  E-value: 4.84e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348499   1 MKLLEDRILKDGNVLGENILKVDSFLTHQVDFDLMREIGKVFAEKFKDAGITKVVTIEASGIAPALYAAEALDVPMIFAK 80
Cdd:PRK09219    1 MKLLEERILKDGKVLSGNILKVDSFLNHQVDPKLMNEIGKEFARRFKDEGITKILTIEASGIAPAVMAALALGVPVVFAK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348499  81 KAKNITMNEGILTAEVYSFTKQVTSTVSIASKFLTPEDKVLIVDDFLANGQAAKGLIQIIEEAGAHVEAVGIVIEKSFQD 160
Cdd:PRK09219   81 KKKSLTLTDDVYTATVYSFTKQVTSTVSVSKKFLSEGDRVLIIDDFLANGQAALGLIDIIEQAGAKVAGIGIVIEKSFQD 160

                         170       180
                  ....*....|....*....|....*....
gi 1081348499 161 GRALLEEAGYPVVSLARLDRFENGQVVFK 189
Cdd:PRK09219  161 GRKLLEEKGYRVESLARIASLENGKVTFV 189
XPRTase TIGR01744
xanthine phosphoribosyltransferase; This model represent a xanthine-specific ...
 1-191 1.16e-81

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: 240.48  E-value: 1.16e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348499   1 MKLLEDRILKDGNVLGENILKVDSFLTHQVDFDLMREIGKVFAEKFKDAGITKVVTIEASGIAPALYAAEALDVPMIFAK 80
Cdd:TIGR01744   1 MELLKQKIKEEGVVLPGGILKVDSFLNHQIDPKLMQEVGEEFARRFADDGITKIVTIEASGIAPAIMTGLKLGVPVVFAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348499  81 KAKNITMNEGILTAEVYSFTKQVTSTVSIASKFLTPEDKVLIVDDFLANGQAAKGLIQIIEEAGAHVEAVGIVIEKSFQD 160
Cdd:TIGR01744  81 KKKPLTLTDNLLTASVHSFTKQTTSTVAVSGEFLSDQDRVLIIDDFLANGQAAHGLVDIAKQAGAKIAGIGIVIEKSFQN 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1081348499 161 GRALLEEAGYPVVSLARLDRFENGQVVFKEA 191
Cdd:TIGR01744 161 GRQELVELGYRVESLARIQSLEEGKVTFVQE 191
Apt COG0503
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ...
 2-178 2.86e-53

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: 167.56  E-value: 2.86e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348499   2 KLLEDRILKDGNVLGENIL--KVDSFLthqVDFDLMREIGKVFAEKFKDAGITKVVTIEASGIAPALYAAEALDVPMIFA 79
Cdd:COG0503     1 EDLKDLIRDIPDFPKPGILfrDITPLL---GDPELFRAAGDELAERFADKGIDKVVGIEARGFILAAALAYALGVPFVPA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348499  80 KKAKNITMNegILTAEVYS-FTKQvtSTVSIASKFLTPEDKVLIVDDFLANGQAAKGLIQIIEEAGAHVEAVGIVIEKSF 158
Cdd:COG0503    78 RKPGKLPGE--TVSEEYDLeYGTG--DTLELHKDALKPGDRVLIVDDLLATGGTAKAAIKLVEEAGAEVVGIAFLIELGF 153

                         170       180
                  ....*....|....*....|
gi 1081348499 159 QDGRALLEEagYPVVSLARL 178
Cdd:COG0503   154 LGGREKLRD--YPVESLLTL 171
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 38-176 6.97e-14

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: 65.11  E-value: 6.97e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348499  38 IGKVFAEKFKDAG--ITKVVTIEASGIAPALYAAEALDVPMIFAKKAKNITMNEGILTAEVYsftkqvtstvsIASKFLT 115
Cdd:cd06223     1 AGRLLAEEIREDLlePDVVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPSEPYGLE-----------LPLGGDV 69

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1081348499 116 PEDKVLIVDDFLANGQAAKGLIQIIEEAGAHVEAVGIVIEKsFQDGRALLEEAGYPVVSLA 176
Cdd:cd06223    70 KGKRVLLVDDVIATGGTLLAAIELLKEAGAKVVGVAVLLDK-PEGGARELASPGDPVYSLF 129
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 36-154 2.77e-04

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: 39.66  E-value: 2.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348499  36 REIGKVFAEKFKDAG--ITKVVTIEASGIAPALYAAEALDVPMIFAKKAKnitmnegiltaevySFTKQVTSTVSIASKF 113
Cdd:pfam00156  13 KAVARLAAQINEDYGgkPDVVVGILRGGLPFAGILARRLDVPLAFVRKVS--------------YNPDTSEVMKTSSALP 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1081348499 114 LTPEDKVLIVDDFLANGQAAKGLIQIIEEAGAhvEAVGIVI 154
Cdd:pfam00156  79 DLKGKTVLIVDDILDTGGTLLKVLELLKNVGP--KEVKIAV 117
 
Name Accession Description Interval E-value
PRK09219 PRK09219
xanthine phosphoribosyltransferase; Validated
 1-189 4.84e-125

xanthine phosphoribosyltransferase; Validated


Pssm-ID: 181705  Cd Length: 189  Bit Score: 350.24  E-value: 4.84e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348499   1 MKLLEDRILKDGNVLGENILKVDSFLTHQVDFDLMREIGKVFAEKFKDAGITKVVTIEASGIAPALYAAEALDVPMIFAK 80
Cdd:PRK09219    1 MKLLEERILKDGKVLSGNILKVDSFLNHQVDPKLMNEIGKEFARRFKDEGITKILTIEASGIAPAVMAALALGVPVVFAK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348499  81 KAKNITMNEGILTAEVYSFTKQVTSTVSIASKFLTPEDKVLIVDDFLANGQAAKGLIQIIEEAGAHVEAVGIVIEKSFQD 160
Cdd:PRK09219   81 KKKSLTLTDDVYTATVYSFTKQVTSTVSVSKKFLSEGDRVLIIDDFLANGQAALGLIDIIEQAGAKVAGIGIVIEKSFQD 160

                         170       180
                  ....*....|....*....|....*....
gi 1081348499 161 GRALLEEAGYPVVSLARLDRFENGQVVFK 189
Cdd:PRK09219  161 GRKLLEEKGYRVESLARIASLENGKVTFV 189
XPRTase TIGR01744
xanthine phosphoribosyltransferase; This model represent a xanthine-specific ...
 1-191 1.16e-81

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: 240.48  E-value: 1.16e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348499   1 MKLLEDRILKDGNVLGENILKVDSFLTHQVDFDLMREIGKVFAEKFKDAGITKVVTIEASGIAPALYAAEALDVPMIFAK 80
Cdd:TIGR01744   1 MELLKQKIKEEGVVLPGGILKVDSFLNHQIDPKLMQEVGEEFARRFADDGITKIVTIEASGIAPAIMTGLKLGVPVVFAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348499  81 KAKNITMNEGILTAEVYSFTKQVTSTVSIASKFLTPEDKVLIVDDFLANGQAAKGLIQIIEEAGAHVEAVGIVIEKSFQD 160
Cdd:TIGR01744  81 KKKPLTLTDNLLTASVHSFTKQTTSTVAVSGEFLSDQDRVLIIDDFLANGQAAHGLVDIAKQAGAKIAGIGIVIEKSFQN 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1081348499 161 GRALLEEAGYPVVSLARLDRFENGQVVFKEA 191
Cdd:TIGR01744 161 GRQELVELGYRVESLARIQSLEEGKVTFVQE 191
Apt COG0503
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ...
 2-178 2.86e-53

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: 167.56  E-value: 2.86e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348499   2 KLLEDRILKDGNVLGENIL--KVDSFLthqVDFDLMREIGKVFAEKFKDAGITKVVTIEASGIAPALYAAEALDVPMIFA 79
Cdd:COG0503     1 EDLKDLIRDIPDFPKPGILfrDITPLL---GDPELFRAAGDELAERFADKGIDKVVGIEARGFILAAALAYALGVPFVPA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348499  80 KKAKNITMNegILTAEVYS-FTKQvtSTVSIASKFLTPEDKVLIVDDFLANGQAAKGLIQIIEEAGAHVEAVGIVIEKSF 158
Cdd:COG0503    78 RKPGKLPGE--TVSEEYDLeYGTG--DTLELHKDALKPGDRVLIVDDLLATGGTAKAAIKLVEEAGAEVVGIAFLIELGF 153

                         170       180
                  ....*....|....*....|
gi 1081348499 159 QDGRALLEEagYPVVSLARL 178
Cdd:COG0503   154 LGGREKLRD--YPVESLLTL 171
PRK02304 PRK02304
adenine phosphoribosyltransferase; Provisional
 33-175 1.82e-21

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 235028  Cd Length: 175  Bit Score: 86.28  E-value: 1.82e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348499  33 DLMREIGKVFAEKFKDAGITKVVTIEASG--IAPALyaAEALDVPMIFAKKAknitmneGILTAEVYSFTKQV---TSTV 107
Cdd:PRK02304   34 EAFREVIDALVERYKDADIDKIVGIEARGfiFGAAL--AYKLGIGFVPVRKP-------GKLPRETISESYELeygTDTL 104

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1081348499 108 SIASKFLTPEDKVLIVDDFLANGQAAKGLIQIIEEAGAHVEAVGIVIEKSFQDGRALLEeaGYPVVSL 175
Cdd:PRK02304  105 EIHKDAIKPGDRVLIVDDLLATGGTLEAAIKLLERLGAEVVGAAFVIELPDLGGREKLE--GYPVKSL 170
PRK08558 PRK08558
adenine phosphoribosyltransferase; Provisional
 31-179 1.13e-16

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 181466 [Multi-domain]  Cd Length: 238  Bit Score: 75.03  E-value: 1.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348499  31 DFDLMREIGKVFAEKFKDAGITKVVTIEASGIAPALYAAEALDVPMIFAKKAKNITMNEGILTAEVYSFTKQVTstVSIA 110
Cdd:PRK08558   92 DPSFLRLIAPVVAERFMGLRVDVVLTAATDGIPLAVAIASYFGADLVYAKKSKETGVEKFYEEYQRLASGIEVT--LYLP 169

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1081348499 111 SKFLTPEDKVLIVDDFLANGQAAKGLIQIIEEAGAHVEAVGIVIEKSFQDGRALLEEAGYPVVSLARLD 179
Cdd:PRK08558  170 ASALKKGDRVLIVDDIIRSGETQRALLDLARQAGADVVGVFFLIAVGEVGIDRAREETDAPVDALYTLE 238
PyrE COG0461
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ...
 33-179 9.38e-16

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


Pssm-ID: 440229  Cd Length: 201  Bit Score: 71.72  E-value: 9.38e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348499  33 DLMREIGKVFAEKFKDAG--ITKVVTIEASGIAPALYAAEALDVPMIFA-KKAKNI-TMN--EGiltaevysftkqvtst 106
Cdd:COG0461    44 EALELLGEALAELIKELGpeFDAVAGPATGGIPLAAAVARALGLPAIFVrKEAKDHgTGGqiEG---------------- 107

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1081348499 107 vsiaskFLTPEDKVLIVDDFLANGQAAKGLIQIIEEAGAHVEAVGIVIEKSfQDGRALLEEAGYPVVSLARLD 179
Cdd:COG0461   108 ------GLLPGERVLVVEDVITTGGSVLEAVEALREAGAEVVGVAVIVDRE-EGAAENLEEAGVPLHSLLTLD 173
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 38-176 6.97e-14

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: 65.11  E-value: 6.97e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348499  38 IGKVFAEKFKDAG--ITKVVTIEASGIAPALYAAEALDVPMIFAKKAKNITMNEGILTAEVYsftkqvtstvsIASKFLT 115
Cdd:cd06223     1 AGRLLAEEIREDLlePDVVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPSEPYGLE-----------LPLGGDV 69

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1081348499 116 PEDKVLIVDDFLANGQAAKGLIQIIEEAGAHVEAVGIVIEKsFQDGRALLEEAGYPVVSLA 176
Cdd:cd06223    70 KGKRVLLVDDVIATGGTLLAAIELLKEAGAKVVGVAVLLDK-PEGGARELASPGDPVYSLF 129
pyrE PRK00455
orotate phosphoribosyltransferase; Validated
 36-179 4.20e-11

orotate phosphoribosyltransferase; Validated


Pssm-ID: 234771  Cd Length: 202  Bit Score: 59.40  E-value: 4.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348499  36 REIGKVFAEKFKDAG--ITKVVTIEASGIAPALYAAEALDVPMIFA-KKAKNITMNEGILTAEVysftkqvtstvsiask 112
Cdd:PRK00455   48 ALLGRFLAEAIKDSGieFDVVAGPATGGIPLAAAVARALDLPAIFVrKEAKDHGEGGQIEGRRL---------------- 111

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1081348499 113 fltPEDKVLIVDDFLANGQAAKGLIQIIEEAGAHVEAVGIVIEKSfQDGRALLEEAGYPVVSLARLD 179
Cdd:PRK00455  112 ---FGKRVLVVEDVITTGGSVLEAVEAIRAAGAEVVGVAVIVDRQ-SAAQEVFADAGVPLISLITLD 174
PRK12560 PRK12560
adenine phosphoribosyltransferase; Provisional
 118-189 3.15e-10

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 183595  Cd Length: 187  Bit Score: 56.72  E-value: 3.15e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1081348499 118 DKVLIVDDFLANGQAAKGLIQIIEEAGAHVEAVGIVIEKSFQDGR-ALLEEAGYPVVSLARLDRFENGQVVFK 189
Cdd:PRK12560  115 DRVAIIDDTLSTGGTVIALIKAIENSGGIVSDVICVIEKTQNNGRkKLFTQTGINVKSLVKIDVKPHGVDIIE 187
PLN02293 PLN02293
adenine phosphoribosyltransferase
 41-162 9.99e-09

adenine phosphoribosyltransferase


Pssm-ID: 177930  Cd Length: 187  Bit Score: 52.37  E-value: 9.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348499  41 VFAEKFKDAGITKVVTIEASG--IAPALyaAEALDVPMIFAKKAKNITmneGILTAEVYSfTKQVTSTVSIASKFLTPED 118
Cdd:PLN02293   53 LFVERYRDMGISVVAGIEARGfiFGPPI--ALAIGAKFVPLRKPGKLP---GEVISEEYV-LEYGTDCLEMHVGAVEPGE 126

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1081348499 119 KVLIVDDFLANGQAAKGLIQIIEEAGAHVEAVGIVIEKSFQDGR 162
Cdd:PLN02293  127 RALVIDDLIATGGTLCAAINLLERAGAEVVECACVIELPELKGR 170
PRK07322 PRK07322
adenine phosphoribosyltransferase; Provisional
 31-181 1.25e-06

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 180928  Cd Length: 178  Bit Score: 46.51  E-value: 1.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348499  31 DFDLMREIGKVFAEKFKDaGITKVVTIEASGIAPALYAAEALDVPMIFAKKAKNITMNEGILTaEVYSFTKQVTSTVSIA 110
Cdd:PRK07322   34 DTELTEAAAEALAKRLPT-EVDVLVTPETKGIPLAHALSRRLGKPYVVARKSRKPYMQDPIIQ-EVVSITTGKPQLLVLD 111

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1081348499 111 SKF--LTPEDKVLIVDDFLANGQAAKGLIQIIEEAGAHVEAVGIVieksfqdgraLLEEAGY---PVVSLARLDRF 181
Cdd:PRK07322  112 GADaeKLKGKRVAIVDDVVSTGGTLTALERLVERAGGQVVAKAAI----------FAEGDASnrlDVIYLAHLPLF 177
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 36-154 2.77e-04

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: 39.66  E-value: 2.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348499  36 REIGKVFAEKFKDAG--ITKVVTIEASGIAPALYAAEALDVPMIFAKKAKnitmnegiltaevySFTKQVTSTVSIASKF 113
Cdd:pfam00156  13 KAVARLAAQINEDYGgkPDVVVGILRGGLPFAGILARRLDVPLAFVRKVS--------------YNPDTSEVMKTSSALP 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1081348499 114 LTPEDKVLIVDDFLANGQAAKGLIQIIEEAGAhvEAVGIVI 154
Cdd:pfam00156  79 DLKGKTVLIVDDILDTGGTLLKVLELLKNVGP--KEVKIAV 117
 
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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