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Conserved domains on  [gi|937518419|gb|ALI38905|]
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DNA utilization protein GntX [Escherichia coli str. K-12 substr. MG1655]

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
 1-227 1.42e-135

DNA utilization protein GntX; Provisional


:

Pssm-ID: 183221 [Multi-domain]  Cd Length: 227  Bit Score: 379.77  E-value: 1.42e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937518419   1 MLTVPGLCWLCRMPLALGHWGICSVCSRATRTDKTLCPQCGLPATHSHLPCGRCLQKPPPWQRLVTVADYAPPLSPLIHQ 80
Cdd:PRK11595   1 MLTVPGLCWLCRMPLALSHWGICSVCSRALRTLKTCCPQCGLPATHPHLPCGRCLQKPPPWQRLVFVSDYAPPLSGLIHQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937518419  81 LKFSRRSEIASALSRLLLLEVLHARRTTGLQLPDRIVSVPLWQRRHWRRGFNQSDLLCQPLSRWLHCQWDSEAVTRTRAT 160
Cdd:PRK11595  81 LKFSRRSELASVLARLLLLEWLQARRSTGLQKPDRIISVPLHQRRHWRRGFNQSDLLCRPLARWLGCDYDSEALTRTRAT 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 937518419 161 ATQHFLSARLRKRNLKNAFRLELPVQGRHMVIVDDVVTTGSTVAEIAQLLLRNGAAAVQVWCLCRTL 227
Cdd:PRK11595 161 ATQHFLSARLRKRNLKNAFRLELPVQGQHMAIVDDVVTTGSTVAEIAQLLLRNGAASVQVWCLCRTL 227
 
Name Accession Description Interval E-value
PRK11595 PRK11595
DNA utilization protein GntX; Provisional
 1-227 1.42e-135

DNA utilization protein GntX; Provisional


Pssm-ID: 183221 [Multi-domain]  Cd Length: 227  Bit Score: 379.77  E-value: 1.42e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937518419   1 MLTVPGLCWLCRMPLALGHWGICSVCSRATRTDKTLCPQCGLPATHSHLPCGRCLQKPPPWQRLVTVADYAPPLSPLIHQ 80
Cdd:PRK11595   1 MLTVPGLCWLCRMPLALSHWGICSVCSRALRTLKTCCPQCGLPATHPHLPCGRCLQKPPPWQRLVFVSDYAPPLSGLIHQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937518419  81 LKFSRRSEIASALSRLLLLEVLHARRTTGLQLPDRIVSVPLWQRRHWRRGFNQSDLLCQPLSRWLHCQWDSEAVTRTRAT 160
Cdd:PRK11595  81 LKFSRRSELASVLARLLLLEWLQARRSTGLQKPDRIISVPLHQRRHWRRGFNQSDLLCRPLARWLGCDYDSEALTRTRAT 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 937518419 161 ATQHFLSARLRKRNLKNAFRLELPVQGRHMVIVDDVVTTGSTVAEIAQLLLRNGAAAVQVWCLCRTL 227
Cdd:PRK11595 161 ATQHFLSARLRKRNLKNAFRLELPVQGQHMAIVDDVVTTGSTVAEIAQLLLRNGAASVQVWCLCRTL 227
comF TIGR00201
comF family protein; This protein is found in species that do (Bacillus subtilis, Haemophilus ...
 23-225 6.06e-86

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: 252.83  E-value: 6.06e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937518419   23 CSVCSRATRTDKTLCPQCGLPATHSHLPcgRCLQKPppwqrLVTVADYAPPLSPLIHQLKFSRRSEIASALSRLLLLEVL 102
Cdd:TIGR00201   1 CSLCGRPYQSVHALCRQCGSWRTRIRDS--LCLRQN-----LVSVYTYNEPLKELISRFKFRGQAEIIRALASLLSLTVS 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937518419  103 HARRttglQLPDRIVSVPLWQRRHWRRGFNQSDLLCQPLSRWLhcQWDSEAVTRTRAtATQHFLSARLRKRNLKNAFRLE 182
Cdd:TIGR00201  74 KAYR----DLPDVIVPVPLSKEREWRRGFNQADLLAQCLSRWL--FNYHNIVIRLNN-ETQSKLKATLRFLNLENAFDLK 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 937518419  183 LP-VQGRHMVIVDDVVTTGSTVAEIAQLLLRNGAAAVQVWCLCR 225
Cdd:TIGR00201 147 NNsFQGRNIVLVDDVVTTGATLHEIARLLLELGAASVQVWTLAR 190
ComFC COG1040
DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General ...
 37-227 6.42e-56

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


Pssm-ID: 440662 [Multi-domain]  Cd Length: 196  Bit Score: 176.55  E-value: 6.42e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937518419  37 CPQCGlpATHSHLPCGRCLQKpppwqrlvTVADYAPPLSPLIHQLKFSRRSEIASALSRLLLlevlHARRTTGLQLPDRI 116
Cdd:COG1040   17 CLLCG--AAPGGGLCPDCRAK--------AAFRYEGPLRRLILALKYRGRLDLARLLARLLA----RALREALLPRPDLI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937518419 117 VSVPLWQRRHWRRGFNQSDLLCQPLSRWLHCQWDSEAVTRTRATATQHFLSARLRKRNLKNAFRL--ELPVQGRHMVIVD 194
Cdd:COG1040   83 VPVPLHRRRLRRRGFNQAELLARALARALGIPVLPDLLRRVRATPSQAGLSRAERRRNLRGAFAVrpPARLAGKHVLLVD 162

                        170       180       190
                 ....*....|....*....|....*....|...
gi 937518419 195 DVVTTGSTVAEIAQLLLRNGAAAVQVWCLCRTL 227
Cdd:COG1040  163 DVLTTGATLAEAARALKAAGAARVDVLVLARTP 195
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 113-223 4.65e-11

Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The type I PRTases are identified by a conserved PRPP binding motif which features two adjacent acidic residues surrounded by one or more hydrophobic residue. PRTases catalyze the displacement of the alpha-1'-pyrophosphate of 5-phosphoribosyl-alpha1-pyrophosphate (PRPP) by a nitrogen-containing nucleophile. The reaction products are an alpha-1 substituted ribose-5'-phosphate and a free pyrophosphate (PP). PRPP, an activated form of ribose-5-phosphate, is a key metabolite connecting nucleotide synthesis and salvage pathways. The type I PRTase family includes a range of diverse phosphoribosyl transferase enzymes and regulatory proteins of the nucleotide synthesis and salvage pathways, including adenine phosphoribosyltransferase EC:2.4.2.7., hypoxanthine-guanine-xanthine phosphoribosyltransferase, hypoxanthine phosphoribosyltransferase EC:2.4.2.8., ribose-phosphate pyrophosphokinase EC:2.7.6.1., amidophosphoribosyltransferase EC:2.4.2.14., orotate phosphoribosyltransferase EC:2.4.2.10., uracil phosphoribosyltransferase EC:2.4.2.9., and xanthine-guanine phosphoribosyltransferase EC:2.4.2.22.


Pssm-ID: 206754 [Multi-domain]  Cd Length: 130  Bit Score: 58.56  E-value: 4.65e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937518419 113 PDRIVSVPlwqrrhwRRGFNqsdlLCQPLSRWLHCQWDSEAVTRTRATATQHFLSARLrkrnlknaFRLELPVQGRHMVI 192
Cdd:cd06223   16 PDVVVGIL-------RGGLP----LAAALARALGLPLAFIRKERKGPGRTPSEPYGLE--------LPLGGDVKGKRVLL 76

                         90       100       110
                 ....*....|....*....|....*....|.
gi 937518419 193 VDDVVTTGSTVAEIAQLLLRNGAAAVQVWCL 223
Cdd:cd06223   77 VDDVIATGGTLLAAIELLKEAGAKVVGVAVL 107
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 187-225 6.31e-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: 38.89  E-value: 6.31e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 937518419  187 GRHMVIVDDVVTTGSTVAEIAQLLLRNGAAAVQVWCLCR 225
Cdd:pfam00156  82 GKTVLIVDDILDTGGTLLKVLELLKNVGPKEVKIAVLID 120
 
Name Accession Description Interval E-value
PRK11595 PRK11595
DNA utilization protein GntX; Provisional
 1-227 1.42e-135

DNA utilization protein GntX; Provisional


Pssm-ID: 183221 [Multi-domain]  Cd Length: 227  Bit Score: 379.77  E-value: 1.42e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937518419   1 MLTVPGLCWLCRMPLALGHWGICSVCSRATRTDKTLCPQCGLPATHSHLPCGRCLQKPPPWQRLVTVADYAPPLSPLIHQ 80
Cdd:PRK11595   1 MLTVPGLCWLCRMPLALSHWGICSVCSRALRTLKTCCPQCGLPATHPHLPCGRCLQKPPPWQRLVFVSDYAPPLSGLIHQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937518419  81 LKFSRRSEIASALSRLLLLEVLHARRTTGLQLPDRIVSVPLWQRRHWRRGFNQSDLLCQPLSRWLHCQWDSEAVTRTRAT 160
Cdd:PRK11595  81 LKFSRRSELASVLARLLLLEWLQARRSTGLQKPDRIISVPLHQRRHWRRGFNQSDLLCRPLARWLGCDYDSEALTRTRAT 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 937518419 161 ATQHFLSARLRKRNLKNAFRLELPVQGRHMVIVDDVVTTGSTVAEIAQLLLRNGAAAVQVWCLCRTL 227
Cdd:PRK11595 161 ATQHFLSARLRKRNLKNAFRLELPVQGQHMAIVDDVVTTGSTVAEIAQLLLRNGAASVQVWCLCRTL 227
comF TIGR00201
comF family protein; This protein is found in species that do (Bacillus subtilis, Haemophilus ...
 23-225 6.06e-86

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: 252.83  E-value: 6.06e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937518419   23 CSVCSRATRTDKTLCPQCGLPATHSHLPcgRCLQKPppwqrLVTVADYAPPLSPLIHQLKFSRRSEIASALSRLLLLEVL 102
Cdd:TIGR00201   1 CSLCGRPYQSVHALCRQCGSWRTRIRDS--LCLRQN-----LVSVYTYNEPLKELISRFKFRGQAEIIRALASLLSLTVS 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937518419  103 HARRttglQLPDRIVSVPLWQRRHWRRGFNQSDLLCQPLSRWLhcQWDSEAVTRTRAtATQHFLSARLRKRNLKNAFRLE 182
Cdd:TIGR00201  74 KAYR----DLPDVIVPVPLSKEREWRRGFNQADLLAQCLSRWL--FNYHNIVIRLNN-ETQSKLKATLRFLNLENAFDLK 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 937518419  183 LP-VQGRHMVIVDDVVTTGSTVAEIAQLLLRNGAAAVQVWCLCR 225
Cdd:TIGR00201 147 NNsFQGRNIVLVDDVVTTGATLHEIARLLLELGAASVQVWTLAR 190
ComFC COG1040
DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General ...
 37-227 6.42e-56

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


Pssm-ID: 440662 [Multi-domain]  Cd Length: 196  Bit Score: 176.55  E-value: 6.42e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937518419  37 CPQCGlpATHSHLPCGRCLQKpppwqrlvTVADYAPPLSPLIHQLKFSRRSEIASALSRLLLlevlHARRTTGLQLPDRI 116
Cdd:COG1040   17 CLLCG--AAPGGGLCPDCRAK--------AAFRYEGPLRRLILALKYRGRLDLARLLARLLA----RALREALLPRPDLI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937518419 117 VSVPLWQRRHWRRGFNQSDLLCQPLSRWLHCQWDSEAVTRTRATATQHFLSARLRKRNLKNAFRL--ELPVQGRHMVIVD 194
Cdd:COG1040   83 VPVPLHRRRLRRRGFNQAELLARALARALGIPVLPDLLRRVRATPSQAGLSRAERRRNLRGAFAVrpPARLAGKHVLLVD 162

                        170       180       190
                 ....*....|....*....|....*....|...
gi 937518419 195 DVVTTGSTVAEIAQLLLRNGAAAVQVWCLCRTL 227
Cdd:COG1040  163 DVLTTGATLAEAARALKAAGAARVDVLVLARTP 195
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 113-223 4.65e-11

Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The type I PRTases are identified by a conserved PRPP binding motif which features two adjacent acidic residues surrounded by one or more hydrophobic residue. PRTases catalyze the displacement of the alpha-1'-pyrophosphate of 5-phosphoribosyl-alpha1-pyrophosphate (PRPP) by a nitrogen-containing nucleophile. The reaction products are an alpha-1 substituted ribose-5'-phosphate and a free pyrophosphate (PP). PRPP, an activated form of ribose-5-phosphate, is a key metabolite connecting nucleotide synthesis and salvage pathways. The type I PRTase family includes a range of diverse phosphoribosyl transferase enzymes and regulatory proteins of the nucleotide synthesis and salvage pathways, including adenine phosphoribosyltransferase EC:2.4.2.7., hypoxanthine-guanine-xanthine phosphoribosyltransferase, hypoxanthine phosphoribosyltransferase EC:2.4.2.8., ribose-phosphate pyrophosphokinase EC:2.7.6.1., amidophosphoribosyltransferase EC:2.4.2.14., orotate phosphoribosyltransferase EC:2.4.2.10., uracil phosphoribosyltransferase EC:2.4.2.9., and xanthine-guanine phosphoribosyltransferase EC:2.4.2.22.


Pssm-ID: 206754 [Multi-domain]  Cd Length: 130  Bit Score: 58.56  E-value: 4.65e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937518419 113 PDRIVSVPlwqrrhwRRGFNqsdlLCQPLSRWLHCQWDSEAVTRTRATATQHFLSARLrkrnlknaFRLELPVQGRHMVI 192
Cdd:cd06223   16 PDVVVGIL-------RGGLP----LAAALARALGLPLAFIRKERKGPGRTPSEPYGLE--------LPLGGDVKGKRVLL 76

                         90       100       110
                 ....*....|....*....|....*....|.
gi 937518419 193 VDDVVTTGSTVAEIAQLLLRNGAAAVQVWCL 223
Cdd:cd06223   77 VDDVIATGGTLLAAIELLKEAGAKVVGVAVL 107
HptA COG0634
Hypoxanthine-guanine phosphoribosyltransferase [Nucleotide transport and metabolism]; ...
 181-220 1.84e-06

Hypoxanthine-guanine phosphoribosyltransferase [Nucleotide transport and metabolism]; Hypoxanthine-guanine phosphoribosyltransferase is part of the Pathway/BioSystem: Purine salvage


Pssm-ID: 440399  Cd Length: 176  Bit Score: 46.56  E-value: 1.84e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 937518419 181 LELPVQGRHMVIVDDVVTTGSTVAEIAQLLLRNGAAAVQV 220
Cdd:COG0634   85 LDEDIEGRDVLIVEDIIDTGLTLSYLLELLKSRGPASVKI 124
PLN02297 PLN02297
ribose-phosphate pyrophosphokinase
 186-222 2.51e-06

ribose-phosphate pyrophosphokinase


Pssm-ID: 177934 [Multi-domain]  Cd Length: 326  Bit Score: 47.38  E-value: 2.51e-06
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 937518419 186 QGRHMVIVDDVVTTGSTVAEIAQLLLRNGAAAVQVWC 222
Cdd:PLN02297 229 AGRHVVIVDDLVQSGGTLIECQKVLAAHGAAKVSAYV 265
PRK02277 PRK02277
orotate phosphoribosyltransferase-like protein; Provisional
 184-223 4.94e-06

orotate phosphoribosyltransferase-like protein; Provisional


Pssm-ID: 235023 [Multi-domain]  Cd Length: 200  Bit Score: 45.63  E-value: 4.94e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 937518419 184 PVQGRHMVIVDDVVTTGSTVAEIAQLLLRNGAAAVQVWCL 223
Cdd:PRK02277 137 SVEGKRCVIVDDVITSGTTMKETIEYLKEHGGKPVAVVVL 176
PRK00934 PRK00934
ribose-phosphate pyrophosphokinase; Provisional
 182-222 4.98e-06

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 234868 [Multi-domain]  Cd Length: 285  Bit Score: 46.06  E-value: 4.98e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 937518419 182 ELPVQGRHMVIVDDVVTTGSTVAEIAQLLLRNGAAAVQVWC 222
Cdd:PRK00934 199 NLDVKGKDVLIVDDIISTGGTMATAIKILKEQGAKKVYVAC 239
PLN02238 PLN02238
hypoxanthine phosphoribosyltransferase
 181-220 1.41e-05

hypoxanthine phosphoribosyltransferase


Pssm-ID: 215132  Cd Length: 189  Bit Score: 44.26  E-value: 1.41e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 937518419 181 LELPVQGRHMVIVDDVVTTGSTVAEIAQLLLRNGAAAVQV 220
Cdd:PLN02238  91 LKIDVKGKHVLLVEDIVDTGNTLSALVAHLEAKGAASVSV 130
PRK07199 PRK07199
ribose-phosphate diphosphokinase;
148-218 2.66e-05

ribose-phosphate diphosphokinase;


Pssm-ID: 235960 [Multi-domain]  Cd Length: 301  Bit Score: 44.16  E-value: 2.66e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 937518419 148 QWDSEAVTRTRATatqhflSARLRK-----RNLKNAFRLELPVQGRHMVIVDDVVTTGSTVAEIAQLLLRNGAAAV 218
Cdd:PRK07199 173 QWVAAVAERAGAP------HAVLRKtrhgdRDVEISLPDAAPWAGRTPVLVDDIVSTGRTLIEAARQLRAAGAASP 242
PRK03092 PRK03092
ribose-phosphate diphosphokinase;
185-218 1.62e-04

ribose-phosphate diphosphokinase;


Pssm-ID: 179535 [Multi-domain]  Cd Length: 304  Bit Score: 41.86  E-value: 1.62e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 937518419 185 VQGRHMVIVDDVVTTGSTVAEIAQLLLRNGAAAV 218
Cdd:PRK03092 199 VEGRTCVLVDDMIDTGGTIAGAVRALKEAGAKDV 232
PLN02369 PLN02369
ribose-phosphate pyrophosphokinase
 185-222 1.92e-04

ribose-phosphate pyrophosphokinase


Pssm-ID: 215209 [Multi-domain]  Cd Length: 302  Bit Score: 41.60  E-value: 1.92e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 937518419 185 VQGRHMVIVDDVVTTGSTVAEIAQLLLRNGAAAVQVWC 222
Cdd:PLN02369 200 VKGKVAIMVDDMIDTAGTITKGAALLHQEGAREVYACA 237
PyrE COG0461
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ...
 184-223 2.22e-04

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


Pssm-ID: 440229  Cd Length: 201  Bit Score: 40.91  E-value: 2.22e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 937518419 184 PVQGRHMVIVDDVVTTGSTVAEIAQLLLRNGAAAVQVWCL 223
Cdd:COG0461  109 LLPGERVLVVEDVITTGGSVLEAVEALREAGAEVVGVAVI 148
PRK01259 PRK01259
ribose-phosphate diphosphokinase;
185-222 2.41e-04

ribose-phosphate diphosphokinase;


Pssm-ID: 234929 [Multi-domain]  Cd Length: 309  Bit Score: 41.26  E-value: 2.41e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 937518419 185 VQGRHMVIVDDVVTTGSTVAEIAQLLLRNGAAAVQVWC 222
Cdd:PRK01259 206 VEGRDCILVDDMIDTAGTLCKAAEALKERGAKSVYAYA 243
PRK07322 PRK07322
adenine phosphoribosyltransferase; Provisional
 185-220 3.01e-04

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 180928  Cd Length: 178  Bit Score: 40.35  E-value: 3.01e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 937518419 185 VQGRHMVIVDDVVTTGSTVAEIAQLLLRNGAAAVQV 220
Cdd:PRK07322 118 LKGKRVAIVDDVVSTGGTLTALERLVERAGGQVVAK 153
PRK09162 PRK09162
hypoxanthine-guanine phosphoribosyltransferase; Provisional
 182-218 4.89e-04

hypoxanthine-guanine phosphoribosyltransferase; Provisional


Pssm-ID: 181675  Cd Length: 181  Bit Score: 39.46  E-value: 4.89e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 937518419 182 ELPVQGRHMVIVDDVVTTGSTVAEIAQLLLRNGAAAV 218
Cdd:PRK09162  92 RESLKGRTVLVVDDILDEGHTLAAIRDRCLEMGAAEV 128
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 187-225 6.31e-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: 38.89  E-value: 6.31e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 937518419  187 GRHMVIVDDVVTTGSTVAEIAQLLLRNGAAAVQVWCLCR 225
Cdd:pfam00156  82 GKTVLIVDDILDTGGTLLKVLELLKNVGPKEVKIAVLID 120
pyrE PRK00455
orotate phosphoribosyltransferase; Validated
 180-223 1.28e-03

orotate phosphoribosyltransferase; Validated


Pssm-ID: 234771  Cd Length: 202  Bit Score: 38.60  E-value: 1.28e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 937518419 180 RLEL-PVQGRHMVIVDDVVTTGSTVAEIAQLLLRNGAAAVQVWCL 223
Cdd:PRK00455 105 QIEGrRLFGKRVLVVEDVITTGGSVLEAVEAIRAAGAEVVGVAVI 149
PRK02812 PRK02812
ribose-phosphate pyrophosphokinase; Provisional
 150-218 1.70e-03

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 235072 [Multi-domain]  Cd Length: 330  Bit Score: 38.57  E-value: 1.70e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 937518419 150 DSEAVTRTRATATQ------HFLSARLRKRNLKNAFRLELPVQGRHMVIVDDVVTTGSTVAEIAQLLLRNGAAAV 218
Cdd:PRK02812 187 DVGGVARARAFAKKlndaplAIIDKRRQAHNVAEVLNVIGDVKGKTAILVDDMIDTGGTICEGARLLRKEGAKQV 261
COG1926 COG1926
Predicted phosphoribosyltransferase [General function prediction only];
171-218 3.58e-03

Predicted phosphoribosyltransferase [General function prediction only];


Pssm-ID: 441529  Cd Length: 209  Bit Score: 37.36  E-value: 3.58e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 937518419 171 RKRNLKNAFRLELPVQGRHMVIVDDVVTTGSTVAEIAQLLLRNGAAAV 218
Cdd:COG1926  105 RRRRRYRGGRPPPDLKGRTVILVDDGIATGATMRAALRALRRQGPARI 152
PRK02458 PRK02458
ribose-phosphate pyrophosphokinase; Provisional
 185-215 5.71e-03

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 235039 [Multi-domain]  Cd Length: 323  Bit Score: 37.03  E-value: 5.71e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 937518419 185 VQGRHMVIVDDVVTTGSTVAEIAQLLLRNGA 215
Cdd:PRK02458 216 VAGKKAILIDDILNTGKTFAEAAKIVEREGA 246
PRK04923 PRK04923
ribose-phosphate diphosphokinase;
103-222 6.19e-03

ribose-phosphate diphosphokinase;


Pssm-ID: 179893 [Multi-domain]  Cd Length: 319  Bit Score: 37.22  E-value: 6.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937518419 103 HARRTTGL-QLP-DRIVSVPLWQRRHWRRGFNQSDLLCQPlsrwlhcqwDSEAVTRTRATATQ------HFLSARLRKRN 174
Cdd:PRK04923 134 HADQIQGFfDVPvDNVYASPLLLADIWRAYGTDNLIVVSP---------DVGGVVRARAVAKRlddadlAIIDKRRPRAN 204

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 937518419 175 LKNAFRLELPVQGRHMVIVDDVVTTGSTVAEIAQLLLRNGAAAVQVWC 222
Cdd:PRK04923 205 VATVMNIIGDVQGKTCVLVDDLVDTAGTLCAAAAALKQRGALKVVAYI 252
 
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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