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Conserved domains on  [gi|492308484|ref|WP_005804600|]
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MULTISPECIES: ComF family protein [Acinetobacter]

Protein Classification

ComF family protein( domain architecture ID 11437133)

ComF family protein is a predicted amidophosphoribosyltransferase; similar to Haemophilus influenzae competence protein F, which is involved in DNA transformation

Gene Ontology:  GO:0030420
PubMed:  8412657|8901420

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ComFC COG1040
DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General ...
 7-208 2.35e-55

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


:

Pssm-ID: 440662 [Multi-domain]  Cd Length: 196  Bit Score: 174.63  E-value: 2.35e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492308484   7 FKHLIQLFSP--CSLCelDTREKYSLCKDCWEQlpwlkqtiqrnnqsvlVACNYAYPVNRIIQQFKYEQKLHYQILLGEI 84
Cdd:COG1040    5 LRALLDLLFPprCLLC--GAAPGGGLCPDCRAK----------------AAFRYEGPLRRLILALKYRGRLDLARLLARL 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492308484  85 L----KQLKFPKVQAIVPMPISNQRLIERGFNQSLLLANILSRHLKIPVWQPI-QRL-NEHSQKGLTRLERFENIEQQFL 158
Cdd:COG1040   67 LaralREALLPRPDLIVPVPLHRRRLRRRGFNQAELLARALARALGIPVLPDLlRRVrATPSQAGLSRAERRRNLRGAFA 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 492308484 159 PHHQEKRRYRRVLIIDDVITTGSSVHALSQALKQLGCTSIHTACLAATPK 208
Cdd:COG1040  147 VRPPARLAGKHVLLVDDVLTTGATLAEAARALKAAGAARVDVLVLARTPR 196
 
Name Accession Description Interval E-value
ComFC COG1040
DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General ...
 7-208 2.35e-55

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


Pssm-ID: 440662 [Multi-domain]  Cd Length: 196  Bit Score: 174.63  E-value: 2.35e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492308484   7 FKHLIQLFSP--CSLCelDTREKYSLCKDCWEQlpwlkqtiqrnnqsvlVACNYAYPVNRIIQQFKYEQKLHYQILLGEI 84
Cdd:COG1040    5 LRALLDLLFPprCLLC--GAAPGGGLCPDCRAK----------------AAFRYEGPLRRLILALKYRGRLDLARLLARL 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492308484  85 L----KQLKFPKVQAIVPMPISNQRLIERGFNQSLLLANILSRHLKIPVWQPI-QRL-NEHSQKGLTRLERFENIEQQFL 158
Cdd:COG1040   67 LaralREALLPRPDLIVPVPLHRRRLRRRGFNQAELLARALARALGIPVLPDLlRRVrATPSQAGLSRAERRRNLRGAFA 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 492308484 159 PHHQEKRRYRRVLIIDDVITTGSSVHALSQALKQLGCTSIHTACLAATPK 208
Cdd:COG1040  147 VRPPARLAGKHVLLVDDVLTTGATLAEAARALKAAGAARVDVLVLARTPR 196
comF TIGR00201
comF family protein; This protein is found in species that do (Bacillus subtilis, Haemophilus ...
 17-204 1.03e-26

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: 101.06  E-value: 1.03e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492308484   17 CSLCELDTREKYSLCKDCWEQLPWLKQTIQRNNQSVLVAcNYAYPVNRIIQQFKYEQKLH----YQILLGEILKQLKFPK 92
Cdd:TIGR00201   1 CSLCGRPYQSVHALCRQCGSWRTRIRDSLCLRQNLVSVY-TYNEPLKELISRFKFRGQAEiiraLASLLSLTVSKAYRDL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492308484   93 VQAIVPMPISNQRLIERGFNQSLLLANILSRHLKIPVwQPIQRLNEHSQKGLTRLERFENIEQQF---LPHHQekrrYRR 169
Cdd:TIGR00201  80 PDVIVPVPLSKEREWRRGFNQADLLAQCLSRWLFNYH-NIVIRLNNETQSKLKATLRFLNLENAFdlkNNSFQ----GRN 154

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 492308484  170 VLIIDDVITTGSSVHALSQALKQLGCTSIHTACLA 204
Cdd:TIGR00201 155 IVLVDDVVTTGATLHEIARLLLELGAASVQVWTLA 189
PRK11595 PRK11595
DNA utilization protein GntX; Provisional
 8-206 3.13e-18

DNA utilization protein GntX; Provisional


Pssm-ID: 183221 [Multi-domain]  Cd Length: 227  Bit Score: 79.31  E-value: 3.13e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492308484   8 KHLIQLFSPCSLCELDTREKYSLCKDCWEQLP-WlkqtiqrnnQSVLVACNYAYPVNRIIQQFKYEQKLHYQILLGEIL- 85
Cdd:PRK11595  28 RALRTLKTCCPQCGLPATHPHLPCGRCLQKPPpW---------QRLVFVSDYAPPLSGLIHQLKFSRRSELASVLARLLl 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492308484  86 -------KQLKFPKVQAIVPMPISNQRLIERGFNQSLLLANILSRHLKIPvWQP--IQRLNEH-SQKGLTRLERFENIEQ 155
Cdd:PRK11595  99 lewlqarRSTGLQKPDRIISVPLHQRRHWRRGFNQSDLLCRPLARWLGCD-YDSeaLTRTRATaTQHFLSARLRKRNLKN 177

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 492308484 156 QFlpHHQEKRRYRRVLIIDDVITTGSSVHALSQALKQLGCTSIHTACLAAT 206
Cdd:PRK11595 178 AF--RLELPVQGQHMAIVDDVVTTGSTVAEIAQLLLRNGAASVQVWCLCRT 226
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 78-207 5.29e-13

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: 63.18  E-value: 5.29e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492308484  78 QILLGEILKQLkfPKVQAIVPMPisnqrliERGFNqsllLANILSRHLKIPVWQPIQRLNEHSQKGLTRLERFENIEqqf 157
Cdd:cd06223    3 RLLAEEIREDL--LEPDVVVGIL-------RGGLP----LAAALARALGLPLAFIRKERKGPGRTPSEPYGLELPLG--- 66

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 492308484 158 lphhqEKRRYRRVLIIDDVITTGSSVHALSQALKQLGCTSIHTACLAATP 207
Cdd:cd06223   67 -----GDVKGKRVLLVDDVIATGGTLLAAIELLKEAGAKVVGVAVLLDKP 111
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 107-209 1.95e-08

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: 51.21  E-value: 1.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492308484  107 IERGfnqSLLLANILSRHLKIPVwqpiqrlnehsqkGLTRLERFEN--IEQQFLPHHQEKRRYRRVLIIDDVITTGSSVH 184
Cdd:pfam00156  36 ILRG---GLPFAGILARRLDVPL-------------AFVRKVSYNPdtSEVMKTSSALPDLKGKTVLIVDDILDTGGTLL 99

                          90       100
                  ....*....|....*....|....*
gi 492308484  185 ALSQALKQLGCTSIHTACLAATPKS 209
Cdd:pfam00156 100 KVLELLKNVGPKEVKIAVLIDKPAG 124
 
Name Accession Description Interval E-value
ComFC COG1040
DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General ...
 7-208 2.35e-55

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


Pssm-ID: 440662 [Multi-domain]  Cd Length: 196  Bit Score: 174.63  E-value: 2.35e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492308484   7 FKHLIQLFSP--CSLCelDTREKYSLCKDCWEQlpwlkqtiqrnnqsvlVACNYAYPVNRIIQQFKYEQKLHYQILLGEI 84
Cdd:COG1040    5 LRALLDLLFPprCLLC--GAAPGGGLCPDCRAK----------------AAFRYEGPLRRLILALKYRGRLDLARLLARL 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492308484  85 L----KQLKFPKVQAIVPMPISNQRLIERGFNQSLLLANILSRHLKIPVWQPI-QRL-NEHSQKGLTRLERFENIEQQFL 158
Cdd:COG1040   67 LaralREALLPRPDLIVPVPLHRRRLRRRGFNQAELLARALARALGIPVLPDLlRRVrATPSQAGLSRAERRRNLRGAFA 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 492308484 159 PHHQEKRRYRRVLIIDDVITTGSSVHALSQALKQLGCTSIHTACLAATPK 208
Cdd:COG1040  147 VRPPARLAGKHVLLVDDVLTTGATLAEAARALKAAGAARVDVLVLARTPR 196
comF TIGR00201
comF family protein; This protein is found in species that do (Bacillus subtilis, Haemophilus ...
 17-204 1.03e-26

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: 101.06  E-value: 1.03e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492308484   17 CSLCELDTREKYSLCKDCWEQLPWLKQTIQRNNQSVLVAcNYAYPVNRIIQQFKYEQKLH----YQILLGEILKQLKFPK 92
Cdd:TIGR00201   1 CSLCGRPYQSVHALCRQCGSWRTRIRDSLCLRQNLVSVY-TYNEPLKELISRFKFRGQAEiiraLASLLSLTVSKAYRDL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492308484   93 VQAIVPMPISNQRLIERGFNQSLLLANILSRHLKIPVwQPIQRLNEHSQKGLTRLERFENIEQQF---LPHHQekrrYRR 169
Cdd:TIGR00201  80 PDVIVPVPLSKEREWRRGFNQADLLAQCLSRWLFNYH-NIVIRLNNETQSKLKATLRFLNLENAFdlkNNSFQ----GRN 154

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 492308484  170 VLIIDDVITTGSSVHALSQALKQLGCTSIHTACLA 204
Cdd:TIGR00201 155 IVLVDDVVTTGATLHEIARLLLELGAASVQVWTLA 189
PRK11595 PRK11595
DNA utilization protein GntX; Provisional
 8-206 3.13e-18

DNA utilization protein GntX; Provisional


Pssm-ID: 183221 [Multi-domain]  Cd Length: 227  Bit Score: 79.31  E-value: 3.13e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492308484   8 KHLIQLFSPCSLCELDTREKYSLCKDCWEQLP-WlkqtiqrnnQSVLVACNYAYPVNRIIQQFKYEQKLHYQILLGEIL- 85
Cdd:PRK11595  28 RALRTLKTCCPQCGLPATHPHLPCGRCLQKPPpW---------QRLVFVSDYAPPLSGLIHQLKFSRRSELASVLARLLl 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492308484  86 -------KQLKFPKVQAIVPMPISNQRLIERGFNQSLLLANILSRHLKIPvWQP--IQRLNEH-SQKGLTRLERFENIEQ 155
Cdd:PRK11595  99 lewlqarRSTGLQKPDRIISVPLHQRRHWRRGFNQSDLLCRPLARWLGCD-YDSeaLTRTRATaTQHFLSARLRKRNLKN 177

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 492308484 156 QFlpHHQEKRRYRRVLIIDDVITTGSSVHALSQALKQLGCTSIHTACLAAT 206
Cdd:PRK11595 178 AF--RLELPVQGQHMAIVDDVVTTGSTVAEIAQLLLRNGAASVQVWCLCRT 226
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 78-207 5.29e-13

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: 63.18  E-value: 5.29e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492308484  78 QILLGEILKQLkfPKVQAIVPMPisnqrliERGFNqsllLANILSRHLKIPVWQPIQRLNEHSQKGLTRLERFENIEqqf 157
Cdd:cd06223    3 RLLAEEIREDL--LEPDVVVGIL-------RGGLP----LAAALARALGLPLAFIRKERKGPGRTPSEPYGLELPLG--- 66

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 492308484 158 lphhqEKRRYRRVLIIDDVITTGSSVHALSQALKQLGCTSIHTACLAATP 207
Cdd:cd06223   67 -----GDVKGKRVLLVDDVIATGGTLLAAIELLKEAGAKVVGVAVLLDKP 111
Hpt1 COG2236
Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism]; Hypoxanthine ...
 115-209 8.17e-09

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


Pssm-ID: 441837 [Multi-domain]  Cd Length: 153  Bit Score: 52.54  E-value: 8.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492308484 115 LLLANILSRHLKIPVWQPIqrlnehsqkgltRLERFENIEQQ-----FLPHHQEKRRYRRVLIIDDVITTGSSVHALSQA 189
Cdd:COG2236   43 LVPARILADALGVPDLASI------------RVSSYTGTAKRleepvVKGPLDEDLAGKRVLIVDDVADTGRTLEAVRDL 110

                         90       100
                 ....*....|....*....|
gi 492308484 190 LKQLGCTSIHTACLAATPKS 209
Cdd:COG2236  111 LKEAGPAEVRTAVLYYKPSS 130
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 107-209 1.95e-08

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: 51.21  E-value: 1.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492308484  107 IERGfnqSLLLANILSRHLKIPVwqpiqrlnehsqkGLTRLERFEN--IEQQFLPHHQEKRRYRRVLIIDDVITTGSSVH 184
Cdd:pfam00156  36 ILRG---GLPFAGILARRLDVPL-------------AFVRKVSYNPdtSEVMKTSSALPDLKGKTVLIVDDILDTGGTLL 99

                          90       100
                  ....*....|....*....|....*
gi 492308484  185 ALSQALKQLGCTSIHTACLAATPKS 209
Cdd:pfam00156 100 KVLELLKNVGPKEVKIAVLIDKPAG 124
PyrE COG0461
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ...
 168-203 1.74e-06

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


Pssm-ID: 440229  Cd Length: 201  Bit Score: 46.69  E-value: 1.74e-06
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 492308484 168 RRVLIIDDVITTGSSVHALSQALKQLGCTSIHTACL 203
Cdd:COG0461  113 ERVLVVEDVITTGGSVLEAVEALREAGAEVVGVAVI 148
PRK07322 PRK07322
adenine phosphoribosyltransferase; Provisional
 160-196 4.81e-06

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 180928  Cd Length: 178  Bit Score: 44.97  E-value: 4.81e-06
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 492308484 160 HHQEKRRYRRVLIIDDVITTGSSVHALSQALKQLGCT 196
Cdd:PRK07322 113 ADAEKLKGKRVAIVDDVVSTGGTLTALERLVERAGGQ 149
pyrE PRK00455
orotate phosphoribosyltransferase; Validated
 168-203 1.32e-05

orotate phosphoribosyltransferase; Validated


Pssm-ID: 234771  Cd Length: 202  Bit Score: 43.99  E-value: 1.32e-05
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 492308484 168 RRVLIIDDVITTGSSVHALSQALKQLGCTSIHTACL 203
Cdd:PRK00455 114 KRVLVVEDVITTGGSVLEAVEAIRAAGAEVVGVAVI 149
Apt COG0503
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ...
 168-207 4.65e-05

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: 42.37  E-value: 4.65e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 492308484 168 RRVLIIDDVITTGSSVHALSQALKQLGCTSIHTACLAATP 207
Cdd:COG0503  113 DRVLIVDDLLATGGTAKAAIKLVEEAGAEVVGIAFLIELG 152
PRK00934 PRK00934
ribose-phosphate pyrophosphokinase; Provisional
 65-202 5.11e-05

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 234868 [Multi-domain]  Cd Length: 285  Bit Score: 42.98  E-value: 5.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492308484  65 IIQQFKYEQ--KLHYQILLGEILKQLKFPKVQAIVPM--------------PISNQ---RLIErGFNQSLLLANI----L 121
Cdd:PRK00934  50 VIISTTYPQdeNLVELLLLIDALRDEGAKSITLVIPYlgyarqdkrfkpgePISARaiaKIIS-AYYDRIITINIhepsI 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492308484 122 SRHLKIPV--WQPIQRLNEHSQKGLTR----------LERFENI-EQQFLPH-HQEKRRY----------------RRVL 171
Cdd:PRK00934 129 LEFFPIPFinLDAAPLIAEYIGDKLDDplvlapdkgaLELAKEAaEILGCEYdYLEKTRIspteveiapknldvkgKDVL 208

                        170       180       190
                 ....*....|....*....|....*....|.
gi 492308484 172 IIDDVITTGSSVHALSQALKQLGCTSIHTAC 202
Cdd:PRK00934 209 IVDDIISTGGTMATAIKILKEQGAKKVYVAC 239
PRK02304 PRK02304
adenine phosphoribosyltransferase; Provisional
 169-203 5.49e-05

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 235028  Cd Length: 175  Bit Score: 41.99  E-value: 5.49e-05
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 492308484 169 RVLIIDDVITTGSSVHALSQALKQLGCTSIHTACL 203
Cdd:PRK02304 116 RVLIVDDLLATGGTLEAAIKLLERLGAEVVGAAFV 150
upp PRK00129
uracil phosphoribosyltransferase; Reviewed
 168-207 1.03e-04

uracil phosphoribosyltransferase; Reviewed


Pssm-ID: 234653  Cd Length: 209  Bit Score: 41.61  E-value: 1.03e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 492308484 168 RRVLIIDDVITTGSS-VHALsQALKQLGCTSIHTACLAATP 207
Cdd:PRK00129 125 RTVIVVDPMLATGGSaIAAI-DLLKKRGAKNIKVLCLVAAP 164
HptA COG0634
Hypoxanthine-guanine phosphoribosyltransferase [Nucleotide transport and metabolism]; ...
 168-203 6.49e-04

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: 38.85  E-value: 6.49e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 492308484 168 RRVLIIDDVITTGSSVHALSQALKQLGCTSIHTACL 203
Cdd:COG0634   92 RDVLIVEDIIDTGLTLSYLLELLKSRGPASVKIATL 127
PRK02277 PRK02277
orotate phosphoribosyltransferase-like protein; Provisional
 166-196 1.39e-03

orotate phosphoribosyltransferase-like protein; Provisional


Pssm-ID: 235023 [Multi-domain]  Cd Length: 200  Bit Score: 38.31  E-value: 1.39e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 492308484 166 RYRRVLIIDDVITTGSSVHALSQALKQLGCT 196
Cdd:PRK02277 139 EGKRCVIVDDVITSGTTMKETIEYLKEHGGK 169
COG1926 COG1926
Predicted phosphoribosyltransferase [General function prediction only];
168-207 6.19e-03

Predicted phosphoribosyltransferase [General function prediction only];


Pssm-ID: 441529  Cd Length: 209  Bit Score: 36.20  E-value: 6.19e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 492308484 168 RRVLIIDDVITTGSSVHALSQALKQLGCTSIhtacLAATP 207
Cdd:COG1926  122 RTVILVDDGIATGATMRAALRALRRQGPARI----VVAVP 157
PRK09162 PRK09162
hypoxanthine-guanine phosphoribosyltransferase; Provisional
 168-204 8.21e-03

hypoxanthine-guanine phosphoribosyltransferase; Provisional


Pssm-ID: 181675  Cd Length: 181  Bit Score: 35.99  E-value: 8.21e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 492308484 168 RRVLIIDDVITTGSSVHALSQALKQLGCTSIHTACLA 204
Cdd:PRK09162  98 RTVLVVDDILDEGHTLAAIRDRCLEMGAAEVYSAVLV 134
 
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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