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Conserved domains on  [gi|488015172|ref|WP_002086571|]
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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 6.01e-124

xanthine phosphoribosyltransferase; Validated


:

Pssm-ID: 181705  Cd Length: 189  Bit Score: 347.54  E-value: 6.01e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488015172   1 MKVLQEKILNEGKVLSGDVLKVDAFLNHQIDPVLMQEIGKEFAKRFKEENITKIVTIESSGIAPAVMAALELGVKVVFAR 80
Cdd:PRK09219   1 MKLLEERILKDGKVLSGNILKVDSFLNHQVDPKLMNEIGKEFARRFKDEGITKILTIEASGIAPAVMAALALGVPVVFAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488015172  81 KRKSLTLQDNMYVANVYSFTKQETNEISLSRNHIDENDHVLIIDDFLANGQAALGLMSLVEQAGASIAGIGIVIEKAFQD 160
Cdd:PRK09219  81 KKKSLTLTDDVYTATVYSFTKQVTSTVSVSKKFLSEGDRVLIIDDFLANGQAALGLIDIIEQAGAKVAGIGIVIEKSFQD 160

                        170       180
                 ....*....|....*....|....*....
gi 488015172 161 GGKKLREQGVRVESLAEIASLDNGTVTFV 189
Cdd:PRK09219 161 GRKLLEEKGYRVESLARIASLENGKVTFV 189
 
Name Accession Description Interval E-value
PRK09219 PRK09219
xanthine phosphoribosyltransferase; Validated
 1-189 6.01e-124

xanthine phosphoribosyltransferase; Validated


Pssm-ID: 181705  Cd Length: 189  Bit Score: 347.54  E-value: 6.01e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488015172   1 MKVLQEKILNEGKVLSGDVLKVDAFLNHQIDPVLMQEIGKEFAKRFKEENITKIVTIESSGIAPAVMAALELGVKVVFAR 80
Cdd:PRK09219   1 MKLLEERILKDGKVLSGNILKVDSFLNHQVDPKLMNEIGKEFARRFKDEGITKILTIEASGIAPAVMAALALGVPVVFAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488015172  81 KRKSLTLQDNMYVANVYSFTKQETNEISLSRNHIDENDHVLIIDDFLANGQAALGLMSLVEQAGASIAGIGIVIEKAFQD 160
Cdd:PRK09219  81 KKKSLTLTDDVYTATVYSFTKQVTSTVSVSKKFLSEGDRVLIIDDFLANGQAALGLIDIIEQAGAKVAGIGIVIEKSFQD 160

                        170       180
                 ....*....|....*....|....*....
gi 488015172 161 GGKKLREQGVRVESLAEIASLDNGTVTFV 189
Cdd:PRK09219 161 GRKLLEEKGYRVESLARIASLENGKVTFV 189
XPRTase TIGR01744
xanthine phosphoribosyltransferase; This model represent a xanthine-specific ...
 1-191 7.44e-92

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: 266.67  E-value: 7.44e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488015172    1 MKVLQEKILNEGKVLSGDVLKVDAFLNHQIDPVLMQEIGKEFAKRFKEENITKIVTIESSGIAPAVMAALELGVKVVFAR 80
Cdd:TIGR01744   1 MELLKQKIKEEGVVLPGGILKVDSFLNHQIDPKLMQEVGEEFARRFADDGITKIVTIEASGIAPAIMTGLKLGVPVVFAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488015172   81 KRKSLTLQDNMYVANVYSFTKQETNEISLSRNHIDENDHVLIIDDFLANGQAALGLMSLVEQAGASIAGIGIVIEKAFQD 160
Cdd:TIGR01744  81 KKKPLTLTDNLLTASVHSFTKQTTSTVAVSGEFLSDQDRVLIIDDFLANGQAAHGLVDIAKQAGAKIAGIGIVIEKSFQN 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 488015172  161 GGKKLREQGVRVESLAEIASLDNGTVTFVQQ 191
Cdd:TIGR01744 161 GRQELVELGYRVESLARIQSLEEGKVTFVQE 191
Apt COG0503
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ...
 2-178 3.83e-58

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: 180.27  E-value: 3.83e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488015172   2 KVLQEKILNEGKVLSGDVL--KVDAFLnhqIDPVLMQEIGKEFAKRFKEENITKIVTIESSGIAPAVMAALELGVKVVFA 79
Cdd:COG0503    1 EDLKDLIRDIPDFPKPGILfrDITPLL---GDPELFRAAGDELAERFADKGIDKVVGIEARGFILAAALAYALGVPFVPA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488015172  80 RKRKSLTLqdNMYVANVYS-FTKQETneISLSRNHIDENDHVLIIDDFLANGQAALGLMSLVEQAGASIAGIGIVIEKAF 158
Cdd:COG0503   78 RKPGKLPG--ETVSEEYDLeYGTGDT--LELHKDALKPGDRVLIVDDLLATGGTAKAAIKLVEEAGAEVVGIAFLIELGF 153

                        170       180
                 ....*....|....*....|
gi 488015172 159 QDGGKKLREQgvRVESLAEI 178
Cdd:COG0503  154 LGGREKLRDY--PVESLLTL 171
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 38-177 1.06e-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: 70.12  E-value: 1.06e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488015172  38 IGKEFAKRFKEE--NITKIVTIESSGIAPAVMAALELGVKVVFARKRKsltlqdnmyvaNVYSFTKQETNEISLSRNHID 115
Cdd:cd06223    1 AGRLLAEEIREDllEPDVVVGILRGGLPLAAALARALGLPLAFIRKER-----------KGPGRTPSEPYGLELPLGGDV 69

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488015172 116 ENDHVLIIDDFLANGQAALGLMSLVEQAGASIAGIGIVIEKaFQDGGKKLREQGVRVESLAE 177
Cdd:cd06223   70 KGKRVLLVDDVIATGGTLLAAIELLKEAGAKVVGVAVLLDK-PEGGARELASPGDPVYSLFT 130
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 22-156 1.18e-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: 48.90  E-value: 1.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488015172   22 VDAFLNHqidPVLMQEIGKEFAKRFKE--ENITKIVTIESSGIAPAVMAALELGVKVVFARKRKSltlqdnmyvanvysF 99
Cdd:pfam00156   2 VDEILDN---PAILKAVARLAAQINEDygGKPDVVVGILRGGLPFAGILARRLDVPLAFVRKVSY--------------N 64

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 488015172  100 TKQETNEISLSRNHIDENDHVLIIDDFLANGQAALGLMSLVEQAGASIAGIGIVIEK 156
Cdd:pfam00156  65 PDTSEVMKTSSALPDLKGKTVLIVDDILDTGGTLLKVLELLKNVGPKEVKIAVLIDK 121
 
Name Accession Description Interval E-value
PRK09219 PRK09219
xanthine phosphoribosyltransferase; Validated
 1-189 6.01e-124

xanthine phosphoribosyltransferase; Validated


Pssm-ID: 181705  Cd Length: 189  Bit Score: 347.54  E-value: 6.01e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488015172   1 MKVLQEKILNEGKVLSGDVLKVDAFLNHQIDPVLMQEIGKEFAKRFKEENITKIVTIESSGIAPAVMAALELGVKVVFAR 80
Cdd:PRK09219   1 MKLLEERILKDGKVLSGNILKVDSFLNHQVDPKLMNEIGKEFARRFKDEGITKILTIEASGIAPAVMAALALGVPVVFAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488015172  81 KRKSLTLQDNMYVANVYSFTKQETNEISLSRNHIDENDHVLIIDDFLANGQAALGLMSLVEQAGASIAGIGIVIEKAFQD 160
Cdd:PRK09219  81 KKKSLTLTDDVYTATVYSFTKQVTSTVSVSKKFLSEGDRVLIIDDFLANGQAALGLIDIIEQAGAKVAGIGIVIEKSFQD 160

                        170       180
                 ....*....|....*....|....*....
gi 488015172 161 GGKKLREQGVRVESLAEIASLDNGTVTFV 189
Cdd:PRK09219 161 GRKLLEEKGYRVESLARIASLENGKVTFV 189
XPRTase TIGR01744
xanthine phosphoribosyltransferase; This model represent a xanthine-specific ...
 1-191 7.44e-92

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: 266.67  E-value: 7.44e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488015172    1 MKVLQEKILNEGKVLSGDVLKVDAFLNHQIDPVLMQEIGKEFAKRFKEENITKIVTIESSGIAPAVMAALELGVKVVFAR 80
Cdd:TIGR01744   1 MELLKQKIKEEGVVLPGGILKVDSFLNHQIDPKLMQEVGEEFARRFADDGITKIVTIEASGIAPAIMTGLKLGVPVVFAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488015172   81 KRKSLTLQDNMYVANVYSFTKQETNEISLSRNHIDENDHVLIIDDFLANGQAALGLMSLVEQAGASIAGIGIVIEKAFQD 160
Cdd:TIGR01744  81 KKKPLTLTDNLLTASVHSFTKQTTSTVAVSGEFLSDQDRVLIIDDFLANGQAAHGLVDIAKQAGAKIAGIGIVIEKSFQN 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 488015172  161 GGKKLREQGVRVESLAEIASLDNGTVTFVQQ 191
Cdd:TIGR01744 161 GRQELVELGYRVESLARIQSLEEGKVTFVQE 191
Apt COG0503
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ...
 2-178 3.83e-58

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: 180.27  E-value: 3.83e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488015172   2 KVLQEKILNEGKVLSGDVL--KVDAFLnhqIDPVLMQEIGKEFAKRFKEENITKIVTIESSGIAPAVMAALELGVKVVFA 79
Cdd:COG0503    1 EDLKDLIRDIPDFPKPGILfrDITPLL---GDPELFRAAGDELAERFADKGIDKVVGIEARGFILAAALAYALGVPFVPA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488015172  80 RKRKSLTLqdNMYVANVYS-FTKQETneISLSRNHIDENDHVLIIDDFLANGQAALGLMSLVEQAGASIAGIGIVIEKAF 158
Cdd:COG0503   78 RKPGKLPG--ETVSEEYDLeYGTGDT--LELHKDALKPGDRVLIVDDLLATGGTAKAAIKLVEEAGAEVVGIAFLIELGF 153

                        170       180
                 ....*....|....*....|
gi 488015172 159 QDGGKKLREQgvRVESLAEI 178
Cdd:COG0503  154 LGGREKLRDY--PVESLLTL 171
PRK02304 PRK02304
adenine phosphoribosyltransferase; Provisional
 31-178 1.77e-23

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 235028  Cd Length: 175  Bit Score: 91.68  E-value: 1.77e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488015172  31 DPVLMQEIGKEFAKRFKEENITKIVTIESSG--IAPAVmaALELGVKVVFARKRKSLTlqdnmyvANVYSFTKQ-E--TN 105
Cdd:PRK02304  32 DPEAFREVIDALVERYKDADIDKIVGIEARGfiFGAAL--AYKLGIGFVPVRKPGKLP-------RETISESYElEygTD 102

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488015172 106 EISLSRNHIDENDHVLIIDDFLANGQAALGLMSLVEQAGASIAGIGIVIEKAFQDGGKKLReqGVRVESLAEI 178
Cdd:PRK02304 103 TLEIHKDAIKPGDRVLIVDDLLATGGTLEAAIKLLERLGAEVVGAAFVIELPDLGGREKLE--GYPVKSLVKF 173
PRK08558 PRK08558
adenine phosphoribosyltransferase; Provisional
 31-179 8.20e-20

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 181466 [Multi-domain]  Cd Length: 238  Bit Score: 83.50  E-value: 8.20e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488015172  31 DPVLMQEIGKEFAKRFKEENITKIVTIESSGIAPAVMAALELGVKVVFARKRKSlTLQDNMYVANVYSFTKQETNeISLS 110
Cdd:PRK08558  92 DPSFLRLIAPVVAERFMGLRVDVVLTAATDGIPLAVAIASYFGADLVYAKKSKE-TGVEKFYEEYQRLASGIEVT-LYLP 169

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488015172 111 RNHIDENDHVLIIDDFLANGQAALGLMSLVEQAGASIAGIGIVIEKAfQDGGKKLREQ-GVRVESLAEIA 179
Cdd:PRK08558 170 ASALKKGDRVLIVDDIIRSGETQRALLDLARQAGADVVGVFFLIAVG-EVGIDRAREEtDAPVDALYTLE 238
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 38-177 1.06e-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: 70.12  E-value: 1.06e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488015172  38 IGKEFAKRFKEE--NITKIVTIESSGIAPAVMAALELGVKVVFARKRKsltlqdnmyvaNVYSFTKQETNEISLSRNHID 115
Cdd:cd06223    1 AGRLLAEEIREDllEPDVVVGILRGGLPLAAALARALGLPLAFIRKER-----------KGPGRTPSEPYGLELPLGGDV 69

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488015172 116 ENDHVLIIDDFLANGQAALGLMSLVEQAGASIAGIGIVIEKaFQDGGKKLREQGVRVESLAE 177
Cdd:cd06223   70 KGKRVLLVDDVIATGGTLLAAIELLKEAGAKVVGVAVLLDK-PEGGARELASPGDPVYSLFT 130
PRK12560 PRK12560
adenine phosphoribosyltransferase; Provisional
 32-184 2.40e-15

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 183595  Cd Length: 187  Bit Score: 70.58  E-value: 2.40e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488015172  32 PVLMQEIGKEFAKrFKEENITKIVTIESSGIAPAVMAALELGVKVVFARKRKSLTLQDNMYVANVYSftkqETNEISLSR 111
Cdd:PRK12560  34 PKVLKETAKEIIK-YIDKDIDKIVTEEDKGAPLATPVSLLSGKPLAMARWYPYSLSELNYNVVEIGS----EYFEGVVYL 108

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488015172 112 NHIDENDHVLIIDDFLANGQAALGLMSLVEQAGASIAGIGIVIEKAFQDGGKKLREQ-GVRVESLAEIASLDNG 184
Cdd:PRK12560 109 NGIEKGDRVAIIDDTLSTGGTVIALIKAIENSGGIVSDVICVIEKTQNNGRKKLFTQtGINVKSLVKIDVKPHG 182
PLN02293 PLN02293
adenine phosphoribosyltransferase
 31-165 3.19e-14

adenine phosphoribosyltransferase


Pssm-ID: 177930  Cd Length: 187  Bit Score: 67.78  E-value: 3.19e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488015172  31 DPVLMQEIGKEFAKRFKEENITKIVTIESSG--IAPAVmaALELGVKVVFARKRKSLTlqdNMYVANVYSfTKQETNEIS 108
Cdd:PLN02293  43 DPKAFKDTIDLFVERYRDMGISVVAGIEARGfiFGPPI--ALAIGAKFVPLRKPGKLP---GEVISEEYV-LEYGTDCLE 116

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488015172 109 LSRNHIDENDHVLIIDDFLANGQAALGLMSLVEQAGASIAGIGIVIEKAFQDGGKKL 165
Cdd:PLN02293 117 MHVGAVEPGERALVIDDLIATGGTLCAAINLLERAGAEVVECACVIELPELKGREKL 173
PyrE COG0461
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ...
 31-181 2.65e-11

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


Pssm-ID: 440229  Cd Length: 201  Bit Score: 59.78  E-value: 2.65e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488015172  31 DPVLMQEIGKEFAKRFKEE--NITKIVTIESSGIAPAVMAALELGVKVVFARKRKsltlqdnmyvanvysftKQ--ETNE 106
Cdd:COG0461   42 YPEALELLGEALAELIKELgpEFDAVAGPATGGIPLAAAVARALGLPAIFVRKEA-----------------KDhgTGGQ 104

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488015172 107 IslsRNHIDENDHVLIIDDFLANGQAALGLMSLVEQAGASIAGIGIVIEkaFQDGGKK-LREQGVRVESLAEIASL 181
Cdd:COG0461  105 I---EGGLLPGERVLVVEDVITTGGSVLEAVEALREAGAEVVGVAVIVD--REEGAAEnLEEAGVPLHSLLTLDDL 175
PRK07322 PRK07322
adenine phosphoribosyltransferase; Provisional
 31-149 6.43e-08

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 180928  Cd Length: 178  Bit Score: 50.36  E-value: 6.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488015172  31 DPVLMQEIGKEFAKRFKEEnITKIVTIESSGIAPAVMAALELGVKVVFARKRKSLTLQDNmYVANVYSFTKQETNEISLS 110
Cdd:PRK07322  34 DTELTEAAAEALAKRLPTE-VDVLVTPETKGIPLAHALSRRLGKPYVVARKSRKPYMQDP-IIQEVVSITTGKPQLLVLD 111

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 488015172 111 RNHID--ENDHVLIIDDFLANGQAALGLMSLVEQAGASIAG 149
Cdd:PRK07322 112 GADAEklKGKRVAIVDDVVSTGGTLTALERLVERAGGQVVA 152
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 22-156 1.18e-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: 48.90  E-value: 1.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488015172   22 VDAFLNHqidPVLMQEIGKEFAKRFKE--ENITKIVTIESSGIAPAVMAALELGVKVVFARKRKSltlqdnmyvanvysF 99
Cdd:pfam00156   2 VDEILDN---PAILKAVARLAAQINEDygGKPDVVVGILRGGLPFAGILARRLDVPLAFVRKVSY--------------N 64

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 488015172  100 TKQETNEISLSRNHIDENDHVLIIDDFLANGQAALGLMSLVEQAGASIAGIGIVIEK 156
Cdd:pfam00156  65 PDTSEVMKTSSALPDLKGKTVLIVDDILDTGGTLLKVLELLKNVGPKEVKIAVLIDK 121
pyrE PRK00455
orotate phosphoribosyltransferase; Validated
 31-181 5.47e-06

orotate phosphoribosyltransferase; Validated


Pssm-ID: 234771  Cd Length: 202  Bit Score: 45.15  E-value: 5.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488015172  31 DPVLMQEIGKEFAKRFKEE--NITKIVTIESSGIAPAVMAALELGVKVVFARKRKSltlqdnmyvanvysfTKQETNEIS 108
Cdd:PRK00455  43 YPEALALLGRFLAEAIKDSgiEFDVVAGPATGGIPLAAAVARALDLPAIFVRKEAK---------------DHGEGGQIE 107

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488015172 109 LSRNhidENDHVLIIDDFLANGQAALGLMSLVEQAGASIAGIGIVI--EKAFQDggkKLREQGVRVESLAEIASL 181
Cdd:PRK00455 108 GRRL---FGKRVLVVEDVITTGGSVLEAVEAIRAAGAEVVGVAVIVdrQSAAQE---VFADAGVPLISLITLDDL 176
 
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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