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Conserved domains on  [gi|896573899|ref|WP_049468845|]
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MULTISPECIES: ComF family protein [Stenotrophomonas]

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 ...
14-231 1.09e-54

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


:

Pssm-ID: 440662 [Multi-domain]  Cd Length: 196  Bit Score: 173.47  E-value: 1.09e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896573899  14 RALLGILLPLRCLVCGDPGHDDLdlcraclaelpwagraclrcalplsdaalivCGSCREEAPpqaathasLLYLPPVDQ 93
Cdd:COG1040    6 RALLDLLFPPRCLLCGAAPGGGL-------------------------------CPDCRAKAA--------FRYEGPLRR 46
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896573899  94 LLLRYKFHQDLAAGRLLAQLMQRAPPPWSCPP---LVPVPLHRRRLRQRGYNQAAEL----CRLLPLPVW-QGLYRRRHT 165
Cdd:COG1040   47 LILALKYRGRLDLARLLARLLARALREALLPRpdlIVPVPLHRRRLRRRGFNQAELLaralARALGIPVLpDLLRRVRAT 126
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 896573899 166 APQSERTAEQRRENLFDAFDVHGPV---PTRLTVVDDVMTTGSTVTEIAETLRCVGAEEVRVWVCARVP 231
Cdd:COG1040  127 PSQAGLSRAERRRNLRGAFAVRPPArlaGKHVLLVDDVLTTGATLAEAARALKAAGAARVDVLVLARTP 195
 
Name Accession Description Interval E-value
ComFC COG1040
DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General ...
14-231 1.09e-54

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


Pssm-ID: 440662 [Multi-domain]  Cd Length: 196  Bit Score: 173.47  E-value: 1.09e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896573899  14 RALLGILLPLRCLVCGDPGHDDLdlcraclaelpwagraclrcalplsdaalivCGSCREEAPpqaathasLLYLPPVDQ 93
Cdd:COG1040    6 RALLDLLFPPRCLLCGAAPGGGL-------------------------------CPDCRAKAA--------FRYEGPLRR 46
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896573899  94 LLLRYKFHQDLAAGRLLAQLMQRAPPPWSCPP---LVPVPLHRRRLRQRGYNQAAEL----CRLLPLPVW-QGLYRRRHT 165
Cdd:COG1040   47 LILALKYRGRLDLARLLARLLARALREALLPRpdlIVPVPLHRRRLRRRGFNQAELLaralARALGIPVLpDLLRRVRAT 126
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 896573899 166 APQSERTAEQRRENLFDAFDVHGPV---PTRLTVVDDVMTTGSTVTEIAETLRCVGAEEVRVWVCARVP 231
Cdd:COG1040  127 PSQAGLSRAERRRNLRGAFAVRPPArlaGKHVLLVDDVLTTGATLAEAARALKAAGAARVDVLVLARTP 195
PRK11595 PRK11595
DNA utilization protein GntX; Provisional
21-229 5.89e-33

DNA utilization protein GntX; Provisional


Pssm-ID: 183221 [Multi-domain]  Cd Length: 227  Bit Score: 118.99  E-value: 5.89e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896573899  21 LPLRCLVCGDP-GHDDLDLCRACLAELPWAGRACLRCALPLSDAALiVCGSCREEAPPQAATHASLLYLPPVDQLLLRYK 99
Cdd:PRK11595   4 VPGLCWLCRMPlALSHWGICSVCSRALRTLKTCCPQCGLPATHPHL-PCGRCLQKPPPWQRLVFVSDYAPPLSGLIHQLK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896573899 100 FHQD------LAAGRLLAQLMQRAPPPWSCPP-LVPVPLHRRRLRQRGYNQAAELCRllPLPVWQG-------LYRRRHT 165
Cdd:PRK11595  83 FSRRselasvLARLLLLEWLQARRSTGLQKPDrIISVPLHQRRHWRRGFNQSDLLCR--PLARWLGcdydseaLTRTRAT 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896573899 166 APQSERTAEQRRENLFDAFDVHGPVPTR-LTVVDDVMTTGSTVTEIAETLRCVGAEEVRVWVCAR 229
Cdd:PRK11595 161 ATQHFLSARLRKRNLKNAFRLELPVQGQhMAIVDDVVTTGSTVAEIAQLLLRNGAASVQVWCLCR 225
comF TIGR00201
comF family protein; This protein is found in species that do (Bacillus subtilis, Haemophilus ...
87-229 3.98e-22

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: 89.50  E-value: 3.98e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896573899   87 YLPPVDQLLLRYKFHQDLAAGRLLAQLMQ---RAPPPWSCPPLVPVPLHRRRLRQRGYNQAAELCRLL--PLPVWQGLYR 161
Cdd:TIGR00201  41 YNEPLKELISRFKFRGQAEIIRALASLLSltvSKAYRDLPDVIVPVPLSKEREWRRGFNQADLLAQCLsrWLFNYHNIVI 120
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896573899  162 RRHTAPQSERTAEQRRENLFDAFDVHGPVPT--RLTVVDDVMTTGSTVTEIAETLRCVGAEEVRVWVCAR 229
Cdd:TIGR00201 121 RLNNETQSKLKATLRFLNLENAFDLKNNSFQgrNIVLVDDVVTTGATLHEIARLLLELGAASVQVWTLAR 190
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
106-231 1.10e-10

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: 57.41  E-value: 1.10e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896573899 106 AGRLLAQLMQRAPppWSCPPLVPVPLhrrrlrqRGYNQAAELCRLLPLPVWQGLyRRRHTAPQSERTAEQRRENLFDafD 185
Cdd:cd06223    1 AGRLLAEEIREDL--LEPDVVVGILR-------GGLPLAAALARALGLPLAFIR-KERKGPGRTPSEPYGLELPLGG--D 68
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 896573899 186 VHGpvpTRLTVVDDVMTTGSTVTEIAETLRCVGAEEVRVWVCARVP 231
Cdd:cd06223   69 VKG---KRVLLVDDVIATGGTLLAAIELLKEAGAKVVGVAVLLDKP 111
DZR_2 pfam18912
Double zinc ribbon domain; This domain family is found in bacteria, archaea and eukaryotes, ...
16-72 1.76e-10

Double zinc ribbon domain; This domain family is found in bacteria, archaea and eukaryotes, and is approximately 60 amino acids in length. The family is found in association with pfam00156. This entry corresponds to two zinc ribbon motifs. This domain is found at the N-terminus of the ComF operon protein 3.


Pssm-ID: 465906 [Multi-domain]  Cd Length: 56  Bit Score: 54.99  E-value: 1.76e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 896573899   16 LLGILLPLRCLVCGDPGHDDLDLCRACLAEL-PWAGRACLRCALPLSDAALivCGSCR 72
Cdd:pfam18912   1 LLDLLFPPRCPLCGAIVAEGGGLCAACWAELpFITEPRCPRCGKPLEEGEL--CGDCL 56
 
Name Accession Description Interval E-value
ComFC COG1040
DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General ...
14-231 1.09e-54

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


Pssm-ID: 440662 [Multi-domain]  Cd Length: 196  Bit Score: 173.47  E-value: 1.09e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896573899  14 RALLGILLPLRCLVCGDPGHDDLdlcraclaelpwagraclrcalplsdaalivCGSCREEAPpqaathasLLYLPPVDQ 93
Cdd:COG1040    6 RALLDLLFPPRCLLCGAAPGGGL-------------------------------CPDCRAKAA--------FRYEGPLRR 46
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896573899  94 LLLRYKFHQDLAAGRLLAQLMQRAPPPWSCPP---LVPVPLHRRRLRQRGYNQAAEL----CRLLPLPVW-QGLYRRRHT 165
Cdd:COG1040   47 LILALKYRGRLDLARLLARLLARALREALLPRpdlIVPVPLHRRRLRRRGFNQAELLaralARALGIPVLpDLLRRVRAT 126
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 896573899 166 APQSERTAEQRRENLFDAFDVHGPV---PTRLTVVDDVMTTGSTVTEIAETLRCVGAEEVRVWVCARVP 231
Cdd:COG1040  127 PSQAGLSRAERRRNLRGAFAVRPPArlaGKHVLLVDDVLTTGATLAEAARALKAAGAARVDVLVLARTP 195
PRK11595 PRK11595
DNA utilization protein GntX; Provisional
21-229 5.89e-33

DNA utilization protein GntX; Provisional


Pssm-ID: 183221 [Multi-domain]  Cd Length: 227  Bit Score: 118.99  E-value: 5.89e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896573899  21 LPLRCLVCGDP-GHDDLDLCRACLAELPWAGRACLRCALPLSDAALiVCGSCREEAPPQAATHASLLYLPPVDQLLLRYK 99
Cdd:PRK11595   4 VPGLCWLCRMPlALSHWGICSVCSRALRTLKTCCPQCGLPATHPHL-PCGRCLQKPPPWQRLVFVSDYAPPLSGLIHQLK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896573899 100 FHQD------LAAGRLLAQLMQRAPPPWSCPP-LVPVPLHRRRLRQRGYNQAAELCRllPLPVWQG-------LYRRRHT 165
Cdd:PRK11595  83 FSRRselasvLARLLLLEWLQARRSTGLQKPDrIISVPLHQRRHWRRGFNQSDLLCR--PLARWLGcdydseaLTRTRAT 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896573899 166 APQSERTAEQRRENLFDAFDVHGPVPTR-LTVVDDVMTTGSTVTEIAETLRCVGAEEVRVWVCAR 229
Cdd:PRK11595 161 ATQHFLSARLRKRNLKNAFRLELPVQGQhMAIVDDVVTTGSTVAEIAQLLLRNGAASVQVWCLCR 225
comF TIGR00201
comF family protein; This protein is found in species that do (Bacillus subtilis, Haemophilus ...
87-229 3.98e-22

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: 89.50  E-value: 3.98e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896573899   87 YLPPVDQLLLRYKFHQDLAAGRLLAQLMQ---RAPPPWSCPPLVPVPLHRRRLRQRGYNQAAELCRLL--PLPVWQGLYR 161
Cdd:TIGR00201  41 YNEPLKELISRFKFRGQAEIIRALASLLSltvSKAYRDLPDVIVPVPLSKEREWRRGFNQADLLAQCLsrWLFNYHNIVI 120
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896573899  162 RRHTAPQSERTAEQRRENLFDAFDVHGPVPT--RLTVVDDVMTTGSTVTEIAETLRCVGAEEVRVWVCAR 229
Cdd:TIGR00201 121 RLNNETQSKLKATLRFLNLENAFDLKNNSFQgrNIVLVDDVVTTGATLHEIARLLLELGAASVQVWTLAR 190
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
106-231 1.10e-10

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: 57.41  E-value: 1.10e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896573899 106 AGRLLAQLMQRAPppWSCPPLVPVPLhrrrlrqRGYNQAAELCRLLPLPVWQGLyRRRHTAPQSERTAEQRRENLFDafD 185
Cdd:cd06223    1 AGRLLAEEIREDL--LEPDVVVGILR-------GGLPLAAALARALGLPLAFIR-KERKGPGRTPSEPYGLELPLGG--D 68
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 896573899 186 VHGpvpTRLTVVDDVMTTGSTVTEIAETLRCVGAEEVRVWVCARVP 231
Cdd:cd06223   69 VKG---KRVLLVDDVIATGGTLLAAIELLKEAGAKVVGVAVLLDKP 111
DZR_2 pfam18912
Double zinc ribbon domain; This domain family is found in bacteria, archaea and eukaryotes, ...
16-72 1.76e-10

Double zinc ribbon domain; This domain family is found in bacteria, archaea and eukaryotes, and is approximately 60 amino acids in length. The family is found in association with pfam00156. This entry corresponds to two zinc ribbon motifs. This domain is found at the N-terminus of the ComF operon protein 3.


Pssm-ID: 465906 [Multi-domain]  Cd Length: 56  Bit Score: 54.99  E-value: 1.76e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 896573899   16 LLGILLPLRCLVCGDPGHDDLDLCRACLAEL-PWAGRACLRCALPLSDAALivCGSCR 72
Cdd:pfam18912   1 LLDLLFPPRCPLCGAIVAEGGGLCAACWAELpFITEPRCPRCGKPLEEGEL--CGDCL 56
PRK02277 PRK02277
orotate phosphoribosyltransferase-like protein; Provisional
196-226 1.57e-06

orotate phosphoribosyltransferase-like protein; Provisional


Pssm-ID: 235023 [Multi-domain]  Cd Length: 200  Bit Score: 47.17  E-value: 1.57e-06
                         10        20        30
                 ....*....|....*....|....*....|.
gi 896573899 196 VVDDVMTTGSTVTEIAETLRCVGAEEVRVWV 226
Cdd:PRK02277 145 IVDDVITSGTTMKETIEYLKEHGGKPVAVVV 175
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
196-223 1.58e-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: 37.73  E-value: 1.58e-03
                          10        20
                  ....*....|....*....|....*...
gi 896573899  196 VVDDVMTTGSTVTEIAETLRCVGAEEVR 223
Cdd:pfam00156  87 IVDDILDTGGTLLKVLELLKNVGPKEVK 114
 
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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