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Conserved domains on  [gi|489958296|ref|WP_003861603|]
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MULTISPECIES: DNA utilization protein GntX [Enterobacter]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK11595 super family cl30474
DNA utilization protein GntX; Provisional
 1-226 9.62e-119

DNA utilization protein GntX; Provisional


The actual alignment was detected with superfamily member PRK11595:

Pssm-ID: 183221 [Multi-domain]  Cd Length: 227  Bit Score: 337.01  E-value: 9.62e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958296   1 MLTVPGLCWLCRMPLAMSAWGVCSVCTRALGYLKG-CPQCGLPAVSQTLPCGRCLKKAPPWSALVAVDDYVLPLSRLVHQ 79
Cdd:PRK11595   1 MLTVPGLCWLCRMPLALSHWGICSVCSRALRTLKTcCPQCGLPATHPHLPCGRCLQKPPPWQRLVFVSDYAPPLSGLIHQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958296  80 FKFSSQIALAQPLARLLLLAVLQARRTRGLPPVDTLVNVPLFQRRHWRRGYNQSDLLCRPLAHWLGCRYPASALKRTHAT 159
Cdd:PRK11595  81 LKFSRRSELASVLARLLLLEWLQARRSTGLQKPDRIISVPLHQRRHWRRGFNQSDLLCRPLARWLGCDYDSEALTRTRAT 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489958296 160 AVQHRLNARSRKRNLKNAFRLELPVNGLHIAIVDDVVTTGSTVAELSRLLLQSGAASVQVWCLCRTL 226
Cdd:PRK11595 161 ATQHFLSARLRKRNLKNAFRLELPVQGQHMAIVDDVVTTGSTVAEIAQLLLRNGAASVQVWCLCRTL 227
 
Name Accession Description Interval E-value
PRK11595 PRK11595
DNA utilization protein GntX; Provisional
 1-226 9.62e-119

DNA utilization protein GntX; Provisional


Pssm-ID: 183221 [Multi-domain]  Cd Length: 227  Bit Score: 337.01  E-value: 9.62e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958296   1 MLTVPGLCWLCRMPLAMSAWGVCSVCTRALGYLKG-CPQCGLPAVSQTLPCGRCLKKAPPWSALVAVDDYVLPLSRLVHQ 79
Cdd:PRK11595   1 MLTVPGLCWLCRMPLALSHWGICSVCSRALRTLKTcCPQCGLPATHPHLPCGRCLQKPPPWQRLVFVSDYAPPLSGLIHQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958296  80 FKFSSQIALAQPLARLLLLAVLQARRTRGLPPVDTLVNVPLFQRRHWRRGYNQSDLLCRPLAHWLGCRYPASALKRTHAT 159
Cdd:PRK11595  81 LKFSRRSELASVLARLLLLEWLQARRSTGLQKPDRIISVPLHQRRHWRRGFNQSDLLCRPLARWLGCDYDSEALTRTRAT 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489958296 160 AVQHRLNARSRKRNLKNAFRLELPVNGLHIAIVDDVVTTGSTVAELSRLLLQSGAASVQVWCLCRTL 226
Cdd:PRK11595 161 ATQHFLSARLRKRNLKNAFRLELPVQGQHMAIVDDVVTTGSTVAEIAQLLLRNGAASVQVWCLCRTL 227
ComFC COG1040
DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General ...
 36-226 7.59e-51

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


Pssm-ID: 440662 [Multi-domain]  Cd Length: 196  Bit Score: 163.45  E-value: 7.59e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958296  36 CPQCGlpAVSQTLPCGRCLKKAppwsalvaVDDYVLPLSRLVHQFKFSSQialaQPLARLLLLAVLQARRTRGLPPVDTL 115
Cdd:COG1040   17 CLLCG--AAPGGGLCPDCRAKA--------AFRYEGPLRRLILALKYRGR----LDLARLLARLLARALREALLPRPDLI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958296 116 VNVPLFQRRHWRRGYNQSDLLCRPLAHWLGCRYPASALKRTHATAVQHRLNARSRKRNLKNAFRL--ELPVNGLHIAIVD 193
Cdd:COG1040   83 VPVPLHRRRLRRRGFNQAELLARALARALGIPVLPDLLRRVRATPSQAGLSRAERRRNLRGAFAVrpPARLAGKHVLLVD 162

                        170       180       190
                 ....*....|....*....|....*....|...
gi 489958296 194 DVVTTGSTVAELSRLLLQSGAASVQVWCLCRTL 226
Cdd:COG1040  163 DVLTTGATLAEAARALKAAGAARVDVLVLARTP 195
comF TIGR00201
comF family protein; This protein is found in species that do (Bacillus subtilis, Haemophilus ...
 23-224 5.31e-49

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: 158.84  E-value: 5.31e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958296   23 CSVCTRALGYLKG-CPQCGLPAVSQTLPcgRCLKKAppwsaLVAVDDYVLPLSRLVHQFKFSSQIALAQPLARLLLLAVL 101
Cdd:TIGR00201   1 CSLCGRPYQSVHAlCRQCGSWRTRIRDS--LCLRQN-----LVSVYTYNEPLKELISRFKFRGQAEIIRALASLLSLTVS 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958296  102 QARRTrgLPpvDTLVNVPLFQRRHWRRGYNQSDLLCRPLAHWLgcRYPASALKRTHAtAVQHRLNARSRKRNLKNAFRLE 181
Cdd:TIGR00201  74 KAYRD--LP--DVIVPVPLSKEREWRRGFNQADLLAQCLSRWL--FNYHNIVIRLNN-ETQSKLKATLRFLNLENAFDLK 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 489958296  182 LP-VNGLHIAIVDDVVTTGSTVAELSRLLLQSGAASVQVWCLCR 224
Cdd:TIGR00201 147 NNsFQGRNIVLVDDVVTTGATLHEIARLLLELGAASVQVWTLAR 190
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 139-222 1.24e-09

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: 54.71  E-value: 1.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958296 139 PLAHWLgcrypASALKRTHATA-VQHRLNARSRKRNLKNAFRLELPVNGLHIAIVDDVVTTGSTVAELSRLLLQSGAASV 217
Cdd:cd06223   28 PLAAAL-----ARALGLPLAFIrKERKGPGRTPSEPYGLELPLGGDVKGKRVLLVDDVIATGGTLLAAIELLKEAGAKVV 102


                 ....*
gi 489958296 218 QVWCL 222
Cdd:cd06223  103 GVAVL 107
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 186-224 9.55e-03

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: 35.42  E-value: 9.55e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 489958296  186 GLHIAIVDDVVTTGSTVAELSRLLLQSGAASVQVWCLCR 224
Cdd:pfam00156  82 GKTVLIVDDILDTGGTLLKVLELLKNVGPKEVKIAVLID 120
 
Name Accession Description Interval E-value
PRK11595 PRK11595
DNA utilization protein GntX; Provisional
 1-226 9.62e-119

DNA utilization protein GntX; Provisional


Pssm-ID: 183221 [Multi-domain]  Cd Length: 227  Bit Score: 337.01  E-value: 9.62e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958296   1 MLTVPGLCWLCRMPLAMSAWGVCSVCTRALGYLKG-CPQCGLPAVSQTLPCGRCLKKAPPWSALVAVDDYVLPLSRLVHQ 79
Cdd:PRK11595   1 MLTVPGLCWLCRMPLALSHWGICSVCSRALRTLKTcCPQCGLPATHPHLPCGRCLQKPPPWQRLVFVSDYAPPLSGLIHQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958296  80 FKFSSQIALAQPLARLLLLAVLQARRTRGLPPVDTLVNVPLFQRRHWRRGYNQSDLLCRPLAHWLGCRYPASALKRTHAT 159
Cdd:PRK11595  81 LKFSRRSELASVLARLLLLEWLQARRSTGLQKPDRIISVPLHQRRHWRRGFNQSDLLCRPLARWLGCDYDSEALTRTRAT 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489958296 160 AVQHRLNARSRKRNLKNAFRLELPVNGLHIAIVDDVVTTGSTVAELSRLLLQSGAASVQVWCLCRTL 226
Cdd:PRK11595 161 ATQHFLSARLRKRNLKNAFRLELPVQGQHMAIVDDVVTTGSTVAEIAQLLLRNGAASVQVWCLCRTL 227
ComFC COG1040
DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General ...
 36-226 7.59e-51

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


Pssm-ID: 440662 [Multi-domain]  Cd Length: 196  Bit Score: 163.45  E-value: 7.59e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958296  36 CPQCGlpAVSQTLPCGRCLKKAppwsalvaVDDYVLPLSRLVHQFKFSSQialaQPLARLLLLAVLQARRTRGLPPVDTL 115
Cdd:COG1040   17 CLLCG--AAPGGGLCPDCRAKA--------AFRYEGPLRRLILALKYRGR----LDLARLLARLLARALREALLPRPDLI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958296 116 VNVPLFQRRHWRRGYNQSDLLCRPLAHWLGCRYPASALKRTHATAVQHRLNARSRKRNLKNAFRL--ELPVNGLHIAIVD 193
Cdd:COG1040   83 VPVPLHRRRLRRRGFNQAELLARALARALGIPVLPDLLRRVRATPSQAGLSRAERRRNLRGAFAVrpPARLAGKHVLLVD 162

                        170       180       190
                 ....*....|....*....|....*....|...
gi 489958296 194 DVVTTGSTVAELSRLLLQSGAASVQVWCLCRTL 226
Cdd:COG1040  163 DVLTTGATLAEAARALKAAGAARVDVLVLARTP 195
comF TIGR00201
comF family protein; This protein is found in species that do (Bacillus subtilis, Haemophilus ...
 23-224 5.31e-49

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: 158.84  E-value: 5.31e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958296   23 CSVCTRALGYLKG-CPQCGLPAVSQTLPcgRCLKKAppwsaLVAVDDYVLPLSRLVHQFKFSSQIALAQPLARLLLLAVL 101
Cdd:TIGR00201   1 CSLCGRPYQSVHAlCRQCGSWRTRIRDS--LCLRQN-----LVSVYTYNEPLKELISRFKFRGQAEIIRALASLLSLTVS 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958296  102 QARRTrgLPpvDTLVNVPLFQRRHWRRGYNQSDLLCRPLAHWLgcRYPASALKRTHAtAVQHRLNARSRKRNLKNAFRLE 181
Cdd:TIGR00201  74 KAYRD--LP--DVIVPVPLSKEREWRRGFNQADLLAQCLSRWL--FNYHNIVIRLNN-ETQSKLKATLRFLNLENAFDLK 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 489958296  182 LP-VNGLHIAIVDDVVTTGSTVAELSRLLLQSGAASVQVWCLCR 224
Cdd:TIGR00201 147 NNsFQGRNIVLVDDVVTTGATLHEIARLLLELGAASVQVWTLAR 190
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 139-222 1.24e-09

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: 54.71  E-value: 1.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958296 139 PLAHWLgcrypASALKRTHATA-VQHRLNARSRKRNLKNAFRLELPVNGLHIAIVDDVVTTGSTVAELSRLLLQSGAASV 217
Cdd:cd06223   28 PLAAAL-----ARALGLPLAFIrKERKGPGRTPSEPYGLELPLGGDVKGKRVLLVDDVIATGGTLLAAIELLKEAGAKVV 102


                 ....*
gi 489958296 218 QVWCL 222
Cdd:cd06223  103 GVAVL 107
PRK00934 PRK00934
ribose-phosphate pyrophosphokinase; Provisional
 181-221 4.36e-06

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 234868 [Multi-domain]  Cd Length: 285  Bit Score: 46.44  E-value: 4.36e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 489958296 181 ELPVNGLHIAIVDDVVTTGSTVAELSRLLLQSGAASVQVWC 221
Cdd:PRK00934 199 NLDVKGKDVLIVDDIISTGGTMATAIKILKEQGAKKVYVAC 239
PLN02238 PLN02238
hypoxanthine phosphoribosyltransferase
 180-219 2.66e-05

hypoxanthine phosphoribosyltransferase


Pssm-ID: 215132  Cd Length: 189  Bit Score: 43.49  E-value: 2.66e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 489958296 180 LELPVNGLHIAIVDDVVTTGSTVAELSRLLLQSGAASVQV 219
Cdd:PLN02238  91 LKIDVKGKHVLLVEDIVDTGNTLSALVAHLEAKGAASVSV 130
HptA COG0634
Hypoxanthine-guanine phosphoribosyltransferase [Nucleotide transport and metabolism]; ...
 180-219 2.81e-05

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: 43.09  E-value: 2.81e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 489958296 180 LELPVNGLHIAIVDDVVTTGSTVAELSRLLLQSGAASVQV 219
Cdd:COG0634   85 LDEDIEGRDVLIVEDIIDTGLTLSYLLELLKSRGPASVKI 124
PRK07322 PRK07322
adenine phosphoribosyltransferase; Provisional
 184-219 1.46e-04

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 180928  Cd Length: 178  Bit Score: 41.12  E-value: 1.46e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 489958296 184 VNGLHIAIVDDVVTTGSTVAELSRLLLQSGAASVQV 219
Cdd:PRK07322 118 LKGKRVAIVDDVVSTGGTLTALERLVERAGGQVVAK 153
PLN02297 PLN02297
ribose-phosphate pyrophosphokinase
 186-221 5.79e-04

ribose-phosphate pyrophosphokinase


Pssm-ID: 177934 [Multi-domain]  Cd Length: 326  Bit Score: 40.06  E-value: 5.79e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 489958296 186 GLHIAIVDDVVTTGSTVAELSRLLLQSGAASVQVWC 221
Cdd:PLN02297 230 GRHVVIVDDLVQSGGTLIECQKVLAAHGAAKVSAYV 265
PRK02277 PRK02277
orotate phosphoribosyltransferase-like protein; Provisional
 183-222 9.17e-04

orotate phosphoribosyltransferase-like protein; Provisional


Pssm-ID: 235023 [Multi-domain]  Cd Length: 200  Bit Score: 39.08  E-value: 9.17e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 489958296 183 PVNGLHIAIVDDVVTTGSTVAELSRLLLQSGAASVQVWCL 222
Cdd:PRK02277 137 SVEGKRCVIVDDVITSGTTMKETIEYLKEHGGKPVAVVVL 176
PyrE COG0461
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ...
 157-222 3.94e-03

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


Pssm-ID: 440229  Cd Length: 201  Bit Score: 37.06  E-value: 3.94e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489958296 157 HATAVQHRLNARS---RKRNlKN---AFRLE-LPVNGLHIAIVDDVVTTGSTVAELSRLLLQSGAASVQVWCL 222
Cdd:COG0461   77 LAAAVARALGLPAifvRKEA-KDhgtGGQIEgGLLPGERVLVVEDVITTGGSVLEAVEALREAGAEVVGVAVI 148
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 186-224 9.55e-03

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: 35.42  E-value: 9.55e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 489958296  186 GLHIAIVDDVVTTGSTVAELSRLLLQSGAASVQVWCLCR 224
Cdd:pfam00156  82 GKTVLIVDDILDTGGTLLKVLELLKNVGPKEVKIAVLID 120
 
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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