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Conserved domains on  [gi|1029908846|emb|SAZ77309|]
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II DNA/RNA helicase ComFC [Staphylococcus aureus]

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 ...
 61-224 3.71e-36

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


:

Pssm-ID: 440662 [Multi-domain]  Cd Length: 196  Bit Score: 126.09  E-value: 3.71e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029908846  61 CLDCKFLSAhfnlmeqlycqFQYDGLMKEMIHQYKFSKDYYLCELLAHLI-----EIPQTSYDYIVPIPSSPAHDLSRTF 135
Cdd:COG1040    29 CPDCRAKAA-----------FRYEGPLRRLILALKYRGRLDLARLLARLLaralrEALLPRPDLIVPVPLHRRRLRRRGF 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029908846 136 NPVEAVLKA----KGIRFDK--ILKMSNRPKQSHLTKKERLAD-ENPFIIDTELDLNGKEILLVDDIYTTGLTIHRAGCK 208
Cdd:COG1040    98 NQAELLARAlaraLGIPVLPdlLRRVRATPSQAGLSRAERRRNlRGAFAVRPPARLAGKHVLLVDDVLTTGATLAEAARA 177

                         170
                  ....*....|....*.
gi 1029908846 209 LYAKNIRKFKVFAFAR 224
Cdd:COG1040   178 LKAAGAARVDVLVLAR 193
 
Name Accession Description Interval E-value
ComFC COG1040
DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General ...
 61-224 3.71e-36

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


Pssm-ID: 440662 [Multi-domain]  Cd Length: 196  Bit Score: 126.09  E-value: 3.71e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029908846  61 CLDCKFLSAhfnlmeqlycqFQYDGLMKEMIHQYKFSKDYYLCELLAHLI-----EIPQTSYDYIVPIPSSPAHDLSRTF 135
Cdd:COG1040    29 CPDCRAKAA-----------FRYEGPLRRLILALKYRGRLDLARLLARLLaralrEALLPRPDLIVPVPLHRRRLRRRGF 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029908846 136 NPVEAVLKA----KGIRFDK--ILKMSNRPKQSHLTKKERLAD-ENPFIIDTELDLNGKEILLVDDIYTTGLTIHRAGCK 208
Cdd:COG1040    98 NQAELLARAlaraLGIPVLPdlLRRVRATPSQAGLSRAERRRNlRGAFAVRPPARLAGKHVLLVDDVLTTGATLAEAARA 177

                         170
                  ....*....|....*.
gi 1029908846 209 LYAKNIRKFKVFAFAR 224
Cdd:COG1040   178 LKAAGAARVDVLVLAR 193
comF TIGR00201
comF family protein; This protein is found in species that do (Bacillus subtilis, Haemophilus ...
 47-224 2.46e-16

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: 74.09  E-value: 2.46e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029908846  47 CSRCLKYLDQNEAYCLDCKFLSAHFN----LMEQLYCQFQYDGLMKEMIHQYKFSKDYYLCELLAHLI-----EIPQTSY 117
Cdd:TIGR00201   1 CSLCGRPYQSVHALCRQCGSWRTRIRdslcLRQNLVSVYTYNEPLKELISRFKFRGQAEIIRALASLLsltvsKAYRDLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029908846 118 DYIVPIPSSPAHDLSRTFNPVEAV---LKAKGIRFDKILKMSNRPKQSHLTKKERLAD-ENpfIIDTEL-DLNGKEILLV 192
Cdd:TIGR00201  81 DVIVPVPLSKEREWRRGFNQADLLaqcLSRWLFNYHNIVIRLNNETQSKLKATLRFLNlEN--AFDLKNnSFQGRNIVLV 158

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1029908846 193 DDIYTTGLTIHRAGCKLYAKNIRKFKVFAFAR 224
Cdd:TIGR00201 159 DDVVTTGATLHEIARLLLELGAASVQVWTLAR 190
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 102-205 6.50e-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: 55.09  E-value: 6.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029908846 102 LCELLAHLIEIPQTSYDYIVPIPSspahdlsRTFNPVEAVLKAKGIRFDKILKMSNRPKQSHLTKKERLADENPfiidte 181
Cdd:cd06223     1 AGRLLAEEIREDLLEPDVVVGILR-------GGLPLAAALARALGLPLAFIRKERKGPGRTPSEPYGLELPLGG------ 67

                          90       100
                  ....*....|....*....|....
gi 1029908846 182 lDLNGKEILLVDDIYTTGLTIHRA 205
Cdd:cd06223    68 -DVKGKRVLLVDDVIATGGTLLAA 90
PRK00934 PRK00934
ribose-phosphate pyrophosphokinase; Provisional
 162-205 9.25e-04

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 234868 [Multi-domain]  Cd Length: 285  Bit Score: 39.51  E-value: 9.25e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1029908846 162 SHLTKKeRLADENPFIIDTELDLNGKEILLVDDIYTTGLTIHRA 205
Cdd:PRK00934  181 DYLEKT-RISPTEVEIAPKNLDVKGKDVLIVDDIISTGGTMATA 223
 
Name Accession Description Interval E-value
ComFC COG1040
DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General ...
 61-224 3.71e-36

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


Pssm-ID: 440662 [Multi-domain]  Cd Length: 196  Bit Score: 126.09  E-value: 3.71e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029908846  61 CLDCKFLSAhfnlmeqlycqFQYDGLMKEMIHQYKFSKDYYLCELLAHLI-----EIPQTSYDYIVPIPSSPAHDLSRTF 135
Cdd:COG1040    29 CPDCRAKAA-----------FRYEGPLRRLILALKYRGRLDLARLLARLLaralrEALLPRPDLIVPVPLHRRRLRRRGF 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029908846 136 NPVEAVLKA----KGIRFDK--ILKMSNRPKQSHLTKKERLAD-ENPFIIDTELDLNGKEILLVDDIYTTGLTIHRAGCK 208
Cdd:COG1040    98 NQAELLARAlaraLGIPVLPdlLRRVRATPSQAGLSRAERRRNlRGAFAVRPPARLAGKHVLLVDDVLTTGATLAEAARA 177

                         170
                  ....*....|....*.
gi 1029908846 209 LYAKNIRKFKVFAFAR 224
Cdd:COG1040   178 LKAAGAARVDVLVLAR 193
comF TIGR00201
comF family protein; This protein is found in species that do (Bacillus subtilis, Haemophilus ...
 47-224 2.46e-16

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: 74.09  E-value: 2.46e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029908846  47 CSRCLKYLDQNEAYCLDCKFLSAHFN----LMEQLYCQFQYDGLMKEMIHQYKFSKDYYLCELLAHLI-----EIPQTSY 117
Cdd:TIGR00201   1 CSLCGRPYQSVHALCRQCGSWRTRIRdslcLRQNLVSVYTYNEPLKELISRFKFRGQAEIIRALASLLsltvsKAYRDLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029908846 118 DYIVPIPSSPAHDLSRTFNPVEAV---LKAKGIRFDKILKMSNRPKQSHLTKKERLAD-ENpfIIDTEL-DLNGKEILLV 192
Cdd:TIGR00201  81 DVIVPVPLSKEREWRRGFNQADLLaqcLSRWLFNYHNIVIRLNNETQSKLKATLRFLNlEN--AFDLKNnSFQGRNIVLV 158

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1029908846 193 DDIYTTGLTIHRAGCKLYAKNIRKFKVFAFAR 224
Cdd:TIGR00201 159 DDVVTTGATLHEIARLLLELGAASVQVWTLAR 190
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 102-205 6.50e-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: 55.09  E-value: 6.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029908846 102 LCELLAHLIEIPQTSYDYIVPIPSspahdlsRTFNPVEAVLKAKGIRFDKILKMSNRPKQSHLTKKERLADENPfiidte 181
Cdd:cd06223     1 AGRLLAEEIREDLLEPDVVVGILR-------GGLPLAAALARALGLPLAFIRKERKGPGRTPSEPYGLELPLGG------ 67

                          90       100
                  ....*....|....*....|....
gi 1029908846 182 lDLNGKEILLVDDIYTTGLTIHRA 205
Cdd:cd06223    68 -DVKGKRVLLVDDVIATGGTLLAA 90
PRK00934 PRK00934
ribose-phosphate pyrophosphokinase; Provisional
 162-205 9.25e-04

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 234868 [Multi-domain]  Cd Length: 285  Bit Score: 39.51  E-value: 9.25e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1029908846 162 SHLTKKeRLADENPFIIDTELDLNGKEILLVDDIYTTGLTIHRA 205
Cdd:PRK00934  181 DYLEKT-RISPTEVEIAPKNLDVKGKDVLIVDDIISTGGTMATA 223
HptA COG0634
Hypoxanthine-guanine phosphoribosyltransferase [Nucleotide transport and metabolism]; ...
 177-224 2.72e-03

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: 37.31  E-value: 2.72e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1029908846 177 IIDTELDLNGKEILLVDDIYTTGLTIHRAGCKLYAKNIRKFKVFAFAR 224
Cdd:COG0634    82 LKDLDEDIEGRDVLIVEDIIDTGLTLSYLLELLKSRGPASVKIATLLD 129
 
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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