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Conserved domains on  [gi|507042493|ref|WP_016114144|]
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MULTISPECIES: xanthine phosphoribosyltransferase [Bacillus]

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 1.65e-122

xanthine phosphoribosyltransferase; Validated


:

Pssm-ID: 181705  Cd Length: 189  Bit Score: 343.69  E-value: 1.65e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507042493   1 MKVLQEKILNEGKVLSGDVLKVDAFLNHQIDPVLMQKIGKEFAQRFKEDNITKIVTIESSGIAPAVMAGLELGVKVVFAR 80
Cdd:PRK09219   1 MKLLEERILKDGKVLSGNILKVDSFLNHQVDPKLMNEIGKEFARRFKDEGITKILTIEASGIAPAVMAALALGVPVVFAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507042493  81 KRKSLTLQDNMYVAKVYSFTKQETNEISLSRNHIHENDRVLIIDDFLANGQAALGLMSLVEQAGASIAGIGIVIEKAFQD 160
Cdd:PRK09219  81 KKKSLTLTDDVYTATVYSFTKQVTSTVSVSKKFLSEGDRVLIIDDFLANGQAALGLIDIIEQAGAKVAGIGIVIEKSFQD 160

                        170       180
                 ....*....|....*....|....*....
gi 507042493 161 GGKKLRENGVRVESLAEIASLDNGTVTFV 189
Cdd:PRK09219 161 GRKLLEEKGYRVESLARIASLENGKVTFV 189
 
Name Accession Description Interval E-value
PRK09219 PRK09219
xanthine phosphoribosyltransferase; Validated
 1-189 1.65e-122

xanthine phosphoribosyltransferase; Validated


Pssm-ID: 181705  Cd Length: 189  Bit Score: 343.69  E-value: 1.65e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507042493   1 MKVLQEKILNEGKVLSGDVLKVDAFLNHQIDPVLMQKIGKEFAQRFKEDNITKIVTIESSGIAPAVMAGLELGVKVVFAR 80
Cdd:PRK09219   1 MKLLEERILKDGKVLSGNILKVDSFLNHQVDPKLMNEIGKEFARRFKDEGITKILTIEASGIAPAVMAALALGVPVVFAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507042493  81 KRKSLTLQDNMYVAKVYSFTKQETNEISLSRNHIHENDRVLIIDDFLANGQAALGLMSLVEQAGASIAGIGIVIEKAFQD 160
Cdd:PRK09219  81 KKKSLTLTDDVYTATVYSFTKQVTSTVSVSKKFLSEGDRVLIIDDFLANGQAALGLIDIIEQAGAKVAGIGIVIEKSFQD 160

                        170       180
                 ....*....|....*....|....*....
gi 507042493 161 GGKKLRENGVRVESLAEIASLDNGTVTFV 189
Cdd:PRK09219 161 GRKLLEEKGYRVESLARIASLENGKVTFV 189
XPRTase TIGR01744
xanthine phosphoribosyltransferase; This model represent a xanthine-specific ...
 1-190 1.37e-91

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: 265.90  E-value: 1.37e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507042493    1 MKVLQEKILNEGKVLSGDVLKVDAFLNHQIDPVLMQKIGKEFAQRFKEDNITKIVTIESSGIAPAVMAGLELGVKVVFAR 80
Cdd:TIGR01744   1 MELLKQKIKEEGVVLPGGILKVDSFLNHQIDPKLMQEVGEEFARRFADDGITKIVTIEASGIAPAIMTGLKLGVPVVFAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507042493   81 KRKSLTLQDNMYVAKVYSFTKQETNEISLSRNHIHENDRVLIIDDFLANGQAALGLMSLVEQAGASIAGIGIVIEKAFQD 160
Cdd:TIGR01744  81 KKKPLTLTDNLLTASVHSFTKQTTSTVAVSGEFLSDQDRVLIIDDFLANGQAAHGLVDIAKQAGAKIAGIGIVIEKSFQN 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 507042493  161 GGKKLRENGVRVESLAEIASLDNGTVTFVQ 190
Cdd:TIGR01744 161 GRQELVELGYRVESLARIQSLEEGKVTFVQ 190
Apt COG0503
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ...
 2-178 9.08e-57

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: 176.80  E-value: 9.08e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507042493   2 KVLQEKILNEGKVLSGDVL--KVDAFLnhqIDPVLMQKIGKEFAQRFKEDNITKIVTIESSGIAPAVMAGLELGVKVVFA 79
Cdd:COG0503    1 EDLKDLIRDIPDFPKPGILfrDITPLL---GDPELFRAAGDELAERFADKGIDKVVGIEARGFILAAALAYALGVPFVPA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507042493  80 RKRKSLTLqdNMYVAKVYS-FTKQETneISLSRNHIHENDRVLIIDDFLANGQAALGLMSLVEQAGASIAGIGIVIEKAF 158
Cdd:COG0503   78 RKPGKLPG--ETVSEEYDLeYGTGDT--LELHKDALKPGDRVLIVDDLLATGGTAKAAIKLVEEAGAEVVGIAFLIELGF 153

                        170       180
                 ....*....|....*....|
gi 507042493 159 QDGGKKLREngVRVESLAEI 178
Cdd:COG0503  154 LGGREKLRD--YPVESLLTL 171
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 38-177 1.90e-15

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: 69.35  E-value: 1.90e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507042493  38 IGKEFAQRFKED--NITKIVTIESSGIAPAVMAGLELGVKVVFARKRKsltlqdnmyvaKVYSFTKQETNEISLSRNHIH 115
Cdd:cd06223    1 AGRLLAEEIREDllEPDVVVGILRGGLPLAAALARALGLPLAFIRKER-----------KGPGRTPSEPYGLELPLGGDV 69

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 507042493 116 ENDRVLIIDDFLANGQAALGLMSLVEQAGASIAGIGIVIEKaFQDGGKKLRENGVRVESLAE 177
Cdd:cd06223   70 KGKRVLLVDDVIATGGTLLAAIELLKEAGAKVVGVAVLLDK-PEGGARELASPGDPVYSLFT 130
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 22-156 6.94e-07

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: 46.97  E-value: 6.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507042493   22 VDAFLNHqidPVLMQKIGKEFAQRFKEDN--ITKIVTIESSGIAPAVMAGLELGVKVVFARKRKSltlqdnmyvakvysF 99
Cdd:pfam00156   2 VDEILDN---PAILKAVARLAAQINEDYGgkPDVVVGILRGGLPFAGILARRLDVPLAFVRKVSY--------------N 64

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 507042493  100 TKQETNEISLSRNHIHENDRVLIIDDFLANGQAALGLMSLVEQAGASIAGIGIVIEK 156
Cdd:pfam00156  65 PDTSEVMKTSSALPDLKGKTVLIVDDILDTGGTLLKVLELLKNVGPKEVKIAVLIDK 121
 
Name Accession Description Interval E-value
PRK09219 PRK09219
xanthine phosphoribosyltransferase; Validated
 1-189 1.65e-122

xanthine phosphoribosyltransferase; Validated


Pssm-ID: 181705  Cd Length: 189  Bit Score: 343.69  E-value: 1.65e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507042493   1 MKVLQEKILNEGKVLSGDVLKVDAFLNHQIDPVLMQKIGKEFAQRFKEDNITKIVTIESSGIAPAVMAGLELGVKVVFAR 80
Cdd:PRK09219   1 MKLLEERILKDGKVLSGNILKVDSFLNHQVDPKLMNEIGKEFARRFKDEGITKILTIEASGIAPAVMAALALGVPVVFAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507042493  81 KRKSLTLQDNMYVAKVYSFTKQETNEISLSRNHIHENDRVLIIDDFLANGQAALGLMSLVEQAGASIAGIGIVIEKAFQD 160
Cdd:PRK09219  81 KKKSLTLTDDVYTATVYSFTKQVTSTVSVSKKFLSEGDRVLIIDDFLANGQAALGLIDIIEQAGAKVAGIGIVIEKSFQD 160

                        170       180
                 ....*....|....*....|....*....
gi 507042493 161 GGKKLRENGVRVESLAEIASLDNGTVTFV 189
Cdd:PRK09219 161 GRKLLEEKGYRVESLARIASLENGKVTFV 189
XPRTase TIGR01744
xanthine phosphoribosyltransferase; This model represent a xanthine-specific ...
 1-190 1.37e-91

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: 265.90  E-value: 1.37e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507042493    1 MKVLQEKILNEGKVLSGDVLKVDAFLNHQIDPVLMQKIGKEFAQRFKEDNITKIVTIESSGIAPAVMAGLELGVKVVFAR 80
Cdd:TIGR01744   1 MELLKQKIKEEGVVLPGGILKVDSFLNHQIDPKLMQEVGEEFARRFADDGITKIVTIEASGIAPAIMTGLKLGVPVVFAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507042493   81 KRKSLTLQDNMYVAKVYSFTKQETNEISLSRNHIHENDRVLIIDDFLANGQAALGLMSLVEQAGASIAGIGIVIEKAFQD 160
Cdd:TIGR01744  81 KKKPLTLTDNLLTASVHSFTKQTTSTVAVSGEFLSDQDRVLIIDDFLANGQAAHGLVDIAKQAGAKIAGIGIVIEKSFQN 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 507042493  161 GGKKLRENGVRVESLAEIASLDNGTVTFVQ 190
Cdd:TIGR01744 161 GRQELVELGYRVESLARIQSLEEGKVTFVQ 190
Apt COG0503
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ...
 2-178 9.08e-57

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: 176.80  E-value: 9.08e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507042493   2 KVLQEKILNEGKVLSGDVL--KVDAFLnhqIDPVLMQKIGKEFAQRFKEDNITKIVTIESSGIAPAVMAGLELGVKVVFA 79
Cdd:COG0503    1 EDLKDLIRDIPDFPKPGILfrDITPLL---GDPELFRAAGDELAERFADKGIDKVVGIEARGFILAAALAYALGVPFVPA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507042493  80 RKRKSLTLqdNMYVAKVYS-FTKQETneISLSRNHIHENDRVLIIDDFLANGQAALGLMSLVEQAGASIAGIGIVIEKAF 158
Cdd:COG0503   78 RKPGKLPG--ETVSEEYDLeYGTGDT--LELHKDALKPGDRVLIVDDLLATGGTAKAAIKLVEEAGAEVVGIAFLIELGF 153

                        170       180
                 ....*....|....*....|
gi 507042493 159 QDGGKKLREngVRVESLAEI 178
Cdd:COG0503  154 LGGREKLRD--YPVESLLTL 171
PRK02304 PRK02304
adenine phosphoribosyltransferase; Provisional
 31-178 5.26e-23

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 235028  Cd Length: 175  Bit Score: 90.52  E-value: 5.26e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507042493  31 DPVLMQKIGKEFAQRFKEDNITKIVTIESSG--IAPAVmaGLELGVKVVFARKRKSLTlqdnmyvAKVYSFTKQ-E--TN 105
Cdd:PRK02304  32 DPEAFREVIDALVERYKDADIDKIVGIEARGfiFGAAL--AYKLGIGFVPVRKPGKLP-------RETISESYElEygTD 102

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 507042493 106 EISLSRNHIHENDRVLIIDDFLANGQAALGLMSLVEQAGASIAGIGIVIEKAFQDGGKKLRenGVRVESLAEI 178
Cdd:PRK02304 103 TLEIHKDAIKPGDRVLIVDDLLATGGTLEAAIKLLERLGAEVVGAAFVIELPDLGGREKLE--GYPVKSLVKF 173
PRK08558 PRK08558
adenine phosphoribosyltransferase; Provisional
 31-179 8.29e-20

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 181466 [Multi-domain]  Cd Length: 238  Bit Score: 83.50  E-value: 8.29e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507042493  31 DPVLMQKIGKEFAQRFKEDNITKIVTIESSGIAPAVMAGLELGVKVVFARKRKSlTLQDNMYVAKVYSFTKQETNeISLS 110
Cdd:PRK08558  92 DPSFLRLIAPVVAERFMGLRVDVVLTAATDGIPLAVAIASYFGADLVYAKKSKE-TGVEKFYEEYQRLASGIEVT-LYLP 169

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507042493 111 RNHIHENDRVLIIDDFLANGQAALGLMSLVEQAGASIAGIGIVIEKAfQDGGKKLREN-GVRVESLAEIA 179
Cdd:PRK08558 170 ASALKKGDRVLIVDDIIRSGETQRALLDLARQAGADVVGVFFLIAVG-EVGIDRAREEtDAPVDALYTLE 238
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 38-177 1.90e-15

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: 69.35  E-value: 1.90e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507042493  38 IGKEFAQRFKED--NITKIVTIESSGIAPAVMAGLELGVKVVFARKRKsltlqdnmyvaKVYSFTKQETNEISLSRNHIH 115
Cdd:cd06223    1 AGRLLAEEIREDllEPDVVVGILRGGLPLAAALARALGLPLAFIRKER-----------KGPGRTPSEPYGLELPLGGDV 69

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 507042493 116 ENDRVLIIDDFLANGQAALGLMSLVEQAGASIAGIGIVIEKaFQDGGKKLRENGVRVESLAE 177
Cdd:cd06223   70 KGKRVLLVDDVIATGGTLLAAIELLKEAGAKVVGVAVLLDK-PEGGARELASPGDPVYSLFT 130
PLN02293 PLN02293
adenine phosphoribosyltransferase
 31-181 8.74e-15

adenine phosphoribosyltransferase


Pssm-ID: 177930  Cd Length: 187  Bit Score: 68.93  E-value: 8.74e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507042493  31 DPVLMQKIGKEFAQRFKEDNITKIVTIESSG--IAPAVmaGLELGVKVVFARKRKSLTlqdNMYVAKVYSfTKQETNEIS 108
Cdd:PLN02293  43 DPKAFKDTIDLFVERYRDMGISVVAGIEARGfiFGPPI--ALAIGAKFVPLRKPGKLP---GEVISEEYV-LEYGTDCLE 116

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 507042493 109 LSRNHIHENDRVLIIDDFLANGQAALGLMSLVEQAGASIAGIGIVIEKAFQDGGKKLreNGVRVESLAEIASL 181
Cdd:PLN02293 117 MHVGAVEPGERALVIDDLIATGGTLCAAINLLERAGAEVVECACVIELPELKGREKL--NGKPLFVLVESRGI 187
PRK12560 PRK12560
adenine phosphoribosyltransferase; Provisional
 32-184 1.51e-13

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 183595  Cd Length: 187  Bit Score: 65.96  E-value: 1.51e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507042493  32 PVLMQKIGKEFAQrFKEDNITKIVTIESSGIAPAVMAGLELGVKVVFARKRKSLTLQDNMYVAKVYSftkqETNEISLSR 111
Cdd:PRK12560  34 PKVLKETAKEIIK-YIDKDIDKIVTEEDKGAPLATPVSLLSGKPLAMARWYPYSLSELNYNVVEIGS----EYFEGVVYL 108

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 507042493 112 NHIHENDRVLIIDDFLANGQAALGLMSLVEQAGASIAGIGIVIEKAFQDGGKKLREN-GVRVESLAEIASLDNG 184
Cdd:PRK12560 109 NGIEKGDRVAIIDDTLSTGGTVIALIKAIENSGGIVSDVICVIEKTQNNGRKKLFTQtGINVKSLVKIDVKPHG 182
PyrE COG0461
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ...
 31-181 1.24e-12

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


Pssm-ID: 440229  Cd Length: 201  Bit Score: 63.63  E-value: 1.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507042493  31 DPVLMQKIGKEFAQRFKE--DNITKIVTIESSGIAPAVMAGLELGVKVVFARKrksltlqdnmyVAKVYSftkqETNEIs 108
Cdd:COG0461   42 YPEALELLGEALAELIKElgPEFDAVAGPATGGIPLAAAVARALGLPAIFVRK-----------EAKDHG----TGGQI- 105

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 507042493 109 lsRNHIHENDRVLIIDDFLANGQAALGLMSLVEQAGASIAGIGIVIEkaFQDGGKK-LRENGVRVESLAEIASL 181
Cdd:COG0461  106 --EGGLLPGERVLVVEDVITTGGSVLEAVEALREAGAEVVGVAVIVD--REEGAAEnLEEAGVPLHSLLTLDDL 175
PRK07322 PRK07322
adenine phosphoribosyltransferase; Provisional
 31-149 6.56e-08

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 180928  Cd Length: 178  Bit Score: 50.36  E-value: 6.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507042493  31 DPVLMQKIGKEFAQRFKEDnITKIVTIESSGIAPAVMAGLELGVKVVFARKRKSLTLQDNmYVAKVYSFTKQETNEISLS 110
Cdd:PRK07322  34 DTELTEAAAEALAKRLPTE-VDVLVTPETKGIPLAHALSRRLGKPYVVARKSRKPYMQDP-IIQEVVSITTGKPQLLVLD 111

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 507042493 111 RNHIH--ENDRVLIIDDFLANGQAALGLMSLVEQAGASIAG 149
Cdd:PRK07322 112 GADAEklKGKRVAIVDDVVSTGGTLTALERLVERAGGQVVA 152
pyrE PRK00455
orotate phosphoribosyltransferase; Validated
 31-181 1.07e-07

orotate phosphoribosyltransferase; Validated


Pssm-ID: 234771  Cd Length: 202  Bit Score: 49.77  E-value: 1.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507042493  31 DPVLMQKIGKEFAQRFKED--NITKIVTIESSGIAPAVMAGLELGVKVVFARKrksltlqdnmyVAKVYSftkqETNEIS 108
Cdd:PRK00455  43 YPEALALLGRFLAEAIKDSgiEFDVVAGPATGGIPLAAAVARALDLPAIFVRK-----------EAKDHG----EGGQIE 107

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 507042493 109 LSRNhihENDRVLIIDDFLANGQAALGLMSLVEQAGASIAGIGIVI--EKAFQDggkKLRENGVRVESLAEIASL 181
Cdd:PRK00455 108 GRRL---FGKRVLVVEDVITTGGSVLEAVEAIRAAGAEVVGVAVIVdrQSAAQE---VFADAGVPLISLITLDDL 176
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 22-156 6.94e-07

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: 46.97  E-value: 6.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507042493   22 VDAFLNHqidPVLMQKIGKEFAQRFKEDN--ITKIVTIESSGIAPAVMAGLELGVKVVFARKRKSltlqdnmyvakvysF 99
Cdd:pfam00156   2 VDEILDN---PAILKAVARLAAQINEDYGgkPDVVVGILRGGLPFAGILARRLDVPLAFVRKVSY--------------N 64

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 507042493  100 TKQETNEISLSRNHIHENDRVLIIDDFLANGQAALGLMSLVEQAGASIAGIGIVIEK 156
Cdd:pfam00156  65 PDTSEVMKTSSALPDLKGKTVLIVDDILDTGGTLLKVLELLKNVGPKEVKIAVLIDK 121
 
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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