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Conserved domains on  [gi|742449024|ref|WP_038905881|]
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MULTISPECIES: DNA utilization protein GntX [Dickeya]

Protein Classification

DNA utilization protein GntX( domain architecture ID 11485422)

DNA utilization protein GntX is required for the use of extracellular DNA as a nutrient and may be involved in gluconate metabolism

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK11595 PRK11595
DNA utilization protein GntX; Provisional
 1-238 1.46e-120

DNA utilization protein GntX; Provisional


:

Pssm-ID: 183221 [Multi-domain]  Cd Length: 227  Bit Score: 342.40  E-value: 1.46e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742449024   1 MLTIMAQCWLCQQPLYHSHHGICSHCRCHLPQPLVCCPRCGLPSASDILPCGRCLQQPPPWQSLLFVSDYQPPLSRLITR 80
Cdd:PRK11595   1 MLTVPGLCWLCRMPLALSHWGICSVCSRALRTLKTCCPQCGLPATHPHLPCGRCLQKPPPWQRLVFVSDYAPPLSGLIHQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742449024  81 FKFQGRIELAPTLARLLLLHWQGCRRATALrlpdayPRPDAIVTVPLHRRRHWRRGFNQTDLIARWLAHWLGCAYDPDTL 160
Cdd:PRK11595  81 LKFSRRSELASVLARLLLLEWLQARRSTGL------QKPDRIISVPLHQRRHWRRGFNQSDLLCRPLARWLGCDYDSEAL 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 742449024 161 IRVRYTVPQQSLGARSRRRNLRGAFRCRQDVISQRVAgkrlvLLDDVVTTGSTVAEVSRTLLRAGAQHVQVWCVCRTL 238
Cdd:PRK11595 155 TRTRATATQHFLSARLRKRNLKNAFRLELPVQGQHMA-----IVDDVVTTGSTVAEIAQLLLRNGAASVQVWCLCRTL 227
 
Name Accession Description Interval E-value
PRK11595 PRK11595
DNA utilization protein GntX; Provisional
 1-238 1.46e-120

DNA utilization protein GntX; Provisional


Pssm-ID: 183221 [Multi-domain]  Cd Length: 227  Bit Score: 342.40  E-value: 1.46e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742449024   1 MLTIMAQCWLCQQPLYHSHHGICSHCRCHLPQPLVCCPRCGLPSASDILPCGRCLQQPPPWQSLLFVSDYQPPLSRLITR 80
Cdd:PRK11595   1 MLTVPGLCWLCRMPLALSHWGICSVCSRALRTLKTCCPQCGLPATHPHLPCGRCLQKPPPWQRLVFVSDYAPPLSGLIHQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742449024  81 FKFQGRIELAPTLARLLLLHWQGCRRATALrlpdayPRPDAIVTVPLHRRRHWRRGFNQTDLIARWLAHWLGCAYDPDTL 160
Cdd:PRK11595  81 LKFSRRSELASVLARLLLLEWLQARRSTGL------QKPDRIISVPLHQRRHWRRGFNQSDLLCRPLARWLGCDYDSEAL 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 742449024 161 IRVRYTVPQQSLGARSRRRNLRGAFRCRQDVISQRVAgkrlvLLDDVVTTGSTVAEVSRTLLRAGAQHVQVWCVCRTL 238
Cdd:PRK11595 155 TRTRATATQHFLSARLRKRNLKNAFRLELPVQGQHMA-----IVDDVVTTGSTVAEIAQLLLRNGAASVQVWCLCRTL 227
ComFC COG1040
DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General ...
 36-239 8.27e-70

DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General function prediction only];


Pssm-ID: 440662 [Multi-domain]  Cd Length: 196  Bit Score: 212.37  E-value: 8.27e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742449024  36 CCPRCGLPSASDIlpCGRCLQQpppwqsllFVSDYQPPLSRLITRFKFQGRIELAPTLARLLLLHWQgcrratalrlPDA 115
Cdd:COG1040   16 RCLLCGAAPGGGL--CPDCRAK--------AAFRYEGPLRRLILALKYRGRLDLARLLARLLARALR----------EAL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742449024 116 YPRPDAIVTVPLHRRRHWRRGFNQTDLIARWLAHWLGCAYDPDTLIRVRYTVPQQSLGARSRRRNLRGAFRCRQDvisQR 195
Cdd:COG1040   76 LPRPDLIVPVPLHRRRLRRRGFNQAELLARALARALGIPVLPDLLRRVRATPSQAGLSRAERRRNLRGAFAVRPP---AR 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 742449024 196 VAGKRLVLLDDVVTTGSTVAEVSRTLLRAGAQHVQVWCVCRTLS 239
Cdd:COG1040  153 LAGKHVLLVDDVLTTGATLAEAARALKAAGAARVDVLVLARTPR 196
comF TIGR00201
comF family protein; This protein is found in species that do (Bacillus subtilis, Haemophilus ...
 23-236 2.39e-45

comF family protein; This protein is found in species that do (Bacillus subtilis, Haemophilus influenzae) or do not (E. coli, Borrelia burgdorferi) have described systems for natural transformation with exogenous DNA. It is involved in competence for transformation in Bacillus subtilis. [Cellular processes, DNA transformation]


Pssm-ID: 272958 [Multi-domain]  Cd Length: 190  Bit Score: 149.98  E-value: 2.39e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742449024   23 CSHCRCHLPQPLVCCPRCGLPSASDILPcgRCLQQPppwqsLLFVSDYQPPLSRLITRFKFQGRIELAPTLARLLllhwq 102
Cdd:TIGR00201   1 CSLCGRPYQSVHALCRQCGSWRTRIRDS--LCLRQN-----LVSVYTYNEPLKELISRFKFRGQAEIIRALASLL----- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742449024  103 gcrratALRLPDAYPR-PDAIVTVPLHRRRHWRRGFNQTDLIARWLAHWLGCAYDPdtLIRVrYTVPQQSLGARSRRRNL 181
Cdd:TIGR00201  69 ------SLTVSKAYRDlPDVIVPVPLSKEREWRRGFNQADLLAQCLSRWLFNYHNI--VIRL-NNETQSKLKATLRFLNL 139

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 742449024  182 RGAFRCRqdviSQRVAGKRLVLLDDVVTTGSTVAEVSRTLLRAGAQHVQVWCVCR 236
Cdd:TIGR00201 140 ENAFDLK----NNSFQGRNIVLVDDVVTTGATLHEIARLLLELGAASVQVWTLAR 190
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 109-234 6.49e-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: 66.27  E-value: 6.49e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742449024 109 ALRLPDAYPRPDAIVTVPlhrrrhwRRGFNqtdlIARWLAHWLGCAYDPdtLIRVRYTVPQQSLGARSRRRNLRGafrcr 188
Cdd:cd06223    6 AEEIREDLLEPDVVVGIL-------RGGLP----LAAALARALGLPLAF--IRKERKGPGRTPSEPYGLELPLGG----- 67

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 742449024 189 qdvisqRVAGKRLVLLDDVVTTGSTVAEVSRTLLRAGAQHVQVWCV 234
Cdd:cd06223   68 ------DVKGKRVLLVDDVIATGGTLLAAIELLKEAGAKVVGVAVL 107
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 102-236 3.70e-05

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: 42.74  E-value: 3.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742449024  102 QGCRRATALRLPDAYPRPDAIVTVPlhrrrhwRRGFnqtdLIARWLAHWLGCAYDpDTLIRVRYTVPQQSLGARSRRRNL 181
Cdd:pfam00156  13 KAVARLAAQINEDYGGKPDVVVGIL-------RGGL----PFAGILARRLDVPLA-FVRKVSYNPDTSEVMKTSSALPDL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 742449024  182 RGafrcrqdvisqrvagKRLVLLDDVVTTGSTVAEVSRTLLRAGAQHVQVWCVCR 236
Cdd:pfam00156  81 KG---------------KTVLIVDDILDTGGTLLKVLELLKNVGPKEVKIAVLID 120
 
Name Accession Description Interval E-value
PRK11595 PRK11595
DNA utilization protein GntX; Provisional
 1-238 1.46e-120

DNA utilization protein GntX; Provisional


Pssm-ID: 183221 [Multi-domain]  Cd Length: 227  Bit Score: 342.40  E-value: 1.46e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742449024   1 MLTIMAQCWLCQQPLYHSHHGICSHCRCHLPQPLVCCPRCGLPSASDILPCGRCLQQPPPWQSLLFVSDYQPPLSRLITR 80
Cdd:PRK11595   1 MLTVPGLCWLCRMPLALSHWGICSVCSRALRTLKTCCPQCGLPATHPHLPCGRCLQKPPPWQRLVFVSDYAPPLSGLIHQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742449024  81 FKFQGRIELAPTLARLLLLHWQGCRRATALrlpdayPRPDAIVTVPLHRRRHWRRGFNQTDLIARWLAHWLGCAYDPDTL 160
Cdd:PRK11595  81 LKFSRRSELASVLARLLLLEWLQARRSTGL------QKPDRIISVPLHQRRHWRRGFNQSDLLCRPLARWLGCDYDSEAL 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 742449024 161 IRVRYTVPQQSLGARSRRRNLRGAFRCRQDVISQRVAgkrlvLLDDVVTTGSTVAEVSRTLLRAGAQHVQVWCVCRTL 238
Cdd:PRK11595 155 TRTRATATQHFLSARLRKRNLKNAFRLELPVQGQHMA-----IVDDVVTTGSTVAEIAQLLLRNGAASVQVWCLCRTL 227
ComFC COG1040
DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General ...
 36-239 8.27e-70

DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General function prediction only];


Pssm-ID: 440662 [Multi-domain]  Cd Length: 196  Bit Score: 212.37  E-value: 8.27e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742449024  36 CCPRCGLPSASDIlpCGRCLQQpppwqsllFVSDYQPPLSRLITRFKFQGRIELAPTLARLLLLHWQgcrratalrlPDA 115
Cdd:COG1040   16 RCLLCGAAPGGGL--CPDCRAK--------AAFRYEGPLRRLILALKYRGRLDLARLLARLLARALR----------EAL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742449024 116 YPRPDAIVTVPLHRRRHWRRGFNQTDLIARWLAHWLGCAYDPDTLIRVRYTVPQQSLGARSRRRNLRGAFRCRQDvisQR 195
Cdd:COG1040   76 LPRPDLIVPVPLHRRRLRRRGFNQAELLARALARALGIPVLPDLLRRVRATPSQAGLSRAERRRNLRGAFAVRPP---AR 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 742449024 196 VAGKRLVLLDDVVTTGSTVAEVSRTLLRAGAQHVQVWCVCRTLS 239
Cdd:COG1040  153 LAGKHVLLVDDVLTTGATLAEAARALKAAGAARVDVLVLARTPR 196
comF TIGR00201
comF family protein; This protein is found in species that do (Bacillus subtilis, Haemophilus ...
 23-236 2.39e-45

comF family protein; This protein is found in species that do (Bacillus subtilis, Haemophilus influenzae) or do not (E. coli, Borrelia burgdorferi) have described systems for natural transformation with exogenous DNA. It is involved in competence for transformation in Bacillus subtilis. [Cellular processes, DNA transformation]


Pssm-ID: 272958 [Multi-domain]  Cd Length: 190  Bit Score: 149.98  E-value: 2.39e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742449024   23 CSHCRCHLPQPLVCCPRCGLPSASDILPcgRCLQQPppwqsLLFVSDYQPPLSRLITRFKFQGRIELAPTLARLLllhwq 102
Cdd:TIGR00201   1 CSLCGRPYQSVHALCRQCGSWRTRIRDS--LCLRQN-----LVSVYTYNEPLKELISRFKFRGQAEIIRALASLL----- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742449024  103 gcrratALRLPDAYPR-PDAIVTVPLHRRRHWRRGFNQTDLIARWLAHWLGCAYDPdtLIRVrYTVPQQSLGARSRRRNL 181
Cdd:TIGR00201  69 ------SLTVSKAYRDlPDVIVPVPLSKEREWRRGFNQADLLAQCLSRWLFNYHNI--VIRL-NNETQSKLKATLRFLNL 139

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 742449024  182 RGAFRCRqdviSQRVAGKRLVLLDDVVTTGSTVAEVSRTLLRAGAQHVQVWCVCR 236
Cdd:TIGR00201 140 ENAFDLK----NNSFQGRNIVLVDDVVTTGATLHEIARLLLELGAASVQVWTLAR 190
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 109-234 6.49e-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: 66.27  E-value: 6.49e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742449024 109 ALRLPDAYPRPDAIVTVPlhrrrhwRRGFNqtdlIARWLAHWLGCAYDPdtLIRVRYTVPQQSLGARSRRRNLRGafrcr 188
Cdd:cd06223    6 AEEIREDLLEPDVVVGIL-------RGGLP----LAAALARALGLPLAF--IRKERKGPGRTPSEPYGLELPLGG----- 67

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 742449024 189 qdvisqRVAGKRLVLLDDVVTTGSTVAEVSRTLLRAGAQHVQVWCV 234
Cdd:cd06223   68 ------DVKGKRVLLVDDVIATGGTLLAAIELLKEAGAKVVGVAVL 107
PRK07322 PRK07322
adenine phosphoribosyltransferase; Provisional
 194-236 1.19e-05

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 180928  Cd Length: 178  Bit Score: 44.58  E-value: 1.19e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 742449024 194 QRVAGKRLVLLDDVVTTGSTVAEVSRTLLRAGAQHVQVWCVCR 236
Cdd:PRK07322 116 EKLKGKRVAIVDDVVSTGGTLTALERLVERAGGQVVAKAAIFA 158
PyrE COG0461
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ...
 94-234 1.86e-05

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


Pssm-ID: 440229  Cd Length: 201  Bit Score: 43.99  E-value: 1.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742449024  94 ARLLLLHWQGCRRATAL---RLPDAYPRPDAIVTVPLhrrrhwrRGfnqtDLIARWLAHWLGcaydpdtlirVRYTVPQQ 170
Cdd:COG0461   36 CRLVLSYPEALELLGEAlaeLIKELGPEFDAVAGPAT-------GG----IPLAAAVARALG----------LPAIFVRK 94

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 742449024 171 SLGARSRRRNLRGAFrcrqdvisqrVAGKRLVLLDDVVTTGSTVAEVSRTLLRAGAQHVQVWCV 234
Cdd:COG0461   95 EAKDHGTGGQIEGGL----------LPGERVLVVEDVITTGGSVLEAVEALREAGAEVVGVAVI 148
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 102-236 3.70e-05

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: 42.74  E-value: 3.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742449024  102 QGCRRATALRLPDAYPRPDAIVTVPlhrrrhwRRGFnqtdLIARWLAHWLGCAYDpDTLIRVRYTVPQQSLGARSRRRNL 181
Cdd:pfam00156  13 KAVARLAAQINEDYGGKPDVVVGIL-------RGGL----PFAGILARRLDVPLA-FVRKVSYNPDTSEVMKTSSALPDL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 742449024  182 RGafrcrqdvisqrvagKRLVLLDDVVTTGSTVAEVSRTLLRAGAQHVQVWCVCR 236
Cdd:pfam00156  81 KG---------------KTVLIVDDILDTGGTLLKVLELLKNVGPKEVKIAVLID 120
PrsA COG0462
Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; ...
 196-234 7.35e-05

Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; Phosphoribosylpyrophosphate synthetase is part of the Pathway/BioSystem: Histidine biosynthesis, Purine biosynthesis


Pssm-ID: 440230 [Multi-domain]  Cd Length: 311  Bit Score: 43.12  E-value: 7.35e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 742449024 196 VAGKRLVLLDDVVTTGSTVAEVSRTLLRAGAQHVQVWCV 234
Cdd:COG0462  209 VEGKTCIIVDDMIDTGGTLVEAAEALKEAGAKSVYAAAT 247
PRK02277 PRK02277
orotate phosphoribosyltransferase-like protein; Provisional
 196-232 9.96e-05

orotate phosphoribosyltransferase-like protein; Provisional


Pssm-ID: 235023 [Multi-domain]  Cd Length: 200  Bit Score: 41.78  E-value: 9.96e-05
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 742449024 196 VAGKRLVLLDDVVTTGSTVAEVSRTLLRAGAQHVQVW 232
Cdd:PRK02277 138 VEGKRCVIVDDVITSGTTMKETIEYLKEHGGKPVAVV 174
PRK02458 PRK02458
ribose-phosphate pyrophosphokinase; Provisional
 196-229 2.27e-04

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 235039 [Multi-domain]  Cd Length: 323  Bit Score: 41.65  E-value: 2.27e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 742449024 196 VAGKRLVLLDDVVTTGSTVAEVSRTLLRAGAQHV 229
Cdd:PRK02458 216 VAGKKAILIDDILNTGKTFAEAAKIVEREGATEI 249
PRK03092 PRK03092
ribose-phosphate diphosphokinase;
196-229 1.02e-03

ribose-phosphate diphosphokinase;


Pssm-ID: 179535 [Multi-domain]  Cd Length: 304  Bit Score: 39.55  E-value: 1.02e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 742449024 196 VAGKRLVLLDDVVTTGSTVAEVSRTLLRAGAQHV 229
Cdd:PRK03092 199 VEGRTCVLVDDMIDTGGTIAGAVRALKEAGAKDV 232
PRK07199 PRK07199
ribose-phosphate diphosphokinase;
120-226 1.21e-03

ribose-phosphate diphosphokinase;


Pssm-ID: 235960 [Multi-domain]  Cd Length: 301  Bit Score: 39.15  E-value: 1.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742449024 120 DAIVTV-P-LHRRRHWRRGF-------NQTDLIARWLAHwlgcaYDPDTLI------------------RVRYTVPQQS- 171
Cdd:PRK07199 119 DRLVTVdPhLHRYPSLSEVYpipavvlSAAPAIAAWIRA-----HVPRPLLigpdeeseqwvaavaeraGAPHAVLRKTr 193

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 742449024 172 LGARSRRRNLRGAfrcrqdvisQRVAGKRLVLLDDVVTTGSTVAEVSRTLLRAGA 226
Cdd:PRK07199 194 HGDRDVEISLPDA---------APWAGRTPVLVDDIVSTGRTLIEAARQLRAAGA 239
pyrE PRK00455
orotate phosphoribosyltransferase; Validated
 195-227 2.53e-03

orotate phosphoribosyltransferase; Validated


Pssm-ID: 234771  Cd Length: 202  Bit Score: 37.83  E-value: 2.53e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 742449024 195 RVAGKRLVLLDDVVTTGSTVAEVSRTLLRAGAQ 227
Cdd:PRK00455 110 RLFGKRVLVVEDVITTGGSVLEAVEAIRAAGAE 142
PRK05793 PRK05793
amidophosphoribosyltransferase; Provisional
 160-231 4.87e-03

amidophosphoribosyltransferase; Provisional


Pssm-ID: 235611 [Multi-domain]  Cd Length: 469  Bit Score: 37.71  E-value: 4.87e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 742449024 160 LIRVRYT-----VPQQSLgaRSRrrnlrgAFRCRQDVISQRVAGKRLVLLDDVVTTGSTVAEVSRTLLRAGAQHVQV 231
Cdd:PRK05793 318 FIKNKYVgrtfiAPSQEL--RER------AVRVKLNPLKVNVEGKRVVLIDDSIVRGTTSKRLVELLRKAGAKEVHF 386
PLN02293 PLN02293
adenine phosphoribosyltransferase
 197-234 8.84e-03

adenine phosphoribosyltransferase


Pssm-ID: 177930  Cd Length: 187  Bit Score: 36.19  E-value: 8.84e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 742449024 197 AGKRLVLLDDVVTTGSTVAEVSRTLLRAGAQHVQVWCV 234
Cdd:PLN02293 124 PGERALVIDDLIATGGTLCAAINLLERAGAEVVECACV 161
PRK02812 PRK02812
ribose-phosphate pyrophosphokinase; Provisional
 196-229 9.71e-03

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 235072 [Multi-domain]  Cd Length: 330  Bit Score: 36.64  E-value: 9.71e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 742449024 196 VAGKRLVLLDDVVTTGSTVAEVSRTLLRAGAQHV 229
Cdd:PRK02812 228 VKGKTAILVDDMIDTGGTICEGARLLRKEGAKQV 261
PLN02238 PLN02238
hypoxanthine phosphoribosyltransferase
 196-231 9.98e-03

hypoxanthine phosphoribosyltransferase


Pssm-ID: 215132  Cd Length: 189  Bit Score: 35.78  E-value: 9.98e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 742449024 196 VAGKRLVLLDDVVTTGSTVAEVSRTLLRAGAQHVQV 231
Cdd:PLN02238  95 VKGKHVLLVEDIVDTGNTLSALVAHLEAKGAASVSV 130
 
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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