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Conserved domains on  [gi|1178006571|ref|WP_082892491|]
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MULTISPECIES: ComF family protein [Mammaliicoccus]

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 ...
 11-174 1.27e-32

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


:

Pssm-ID: 440662 [Multi-domain]  Cd Length: 196  Bit Score: 114.92  E-value: 1.27e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178006571  11 CLDCmwLSQSyklinqlhtLYDYQTFIKTLMHQYKFSGDLALYEIF------QIPRKIIKNYDLIVPAPINDNKLRNRTF 84
Cdd:COG1040    29 CPDC--RAKA---------AFRYEGPLRRLILALKYRGRLDLARLLarllarALREALLPRPDLIVPVPLHRRRLRRRGF 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178006571  85 DHVAYVLD----KQNIPY-TQLFQ-TEERKKQACLSKKERsEQN--NPFKLINEINLENKKILLVDDIYTTGLTIHQLAE 156
Cdd:COG1040    98 NQAELLARalarALGIPVlPDLLRrVRATPSQAGLSRAER-RRNlrGAFAVRPPARLAGKHVLLVDDVLTTGATLAEAAR 176

                         170
                  ....*....|....*...
gi 1178006571 157 HLLVRKIRKLDALTFARG 174
Cdd:COG1040   177 ALKAAGAARVDVLVLART 194
 
Name Accession Description Interval E-value
ComFC COG1040
DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General ...
 11-174 1.27e-32

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


Pssm-ID: 440662 [Multi-domain]  Cd Length: 196  Bit Score: 114.92  E-value: 1.27e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178006571  11 CLDCmwLSQSyklinqlhtLYDYQTFIKTLMHQYKFSGDLALYEIF------QIPRKIIKNYDLIVPAPINDNKLRNRTF 84
Cdd:COG1040    29 CPDC--RAKA---------AFRYEGPLRRLILALKYRGRLDLARLLarllarALREALLPRPDLIVPVPLHRRRLRRRGF 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178006571  85 DHVAYVLD----KQNIPY-TQLFQ-TEERKKQACLSKKERsEQN--NPFKLINEINLENKKILLVDDIYTTGLTIHQLAE 156
Cdd:COG1040    98 NQAELLARalarALGIPVlPDLLRrVRATPSQAGLSRAER-RRNlrGAFAVRPPARLAGKHVLLVDDVLTTGATLAEAAR 176

                         170
                  ....*....|....*...
gi 1178006571 157 HLLVRKIRKLDALTFARG 174
Cdd:COG1040   177 ALKAAGAARVDVLVLART 194
comF TIGR00201
comF family protein; This protein is found in species that do (Bacillus subtilis, Haemophilus ...
 11-173 6.34e-14

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: 66.39  E-value: 6.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178006571  11 CLDC-MWLS---QSYKLINQLHTLYDYQTFIKTLMHQYKFSGD---------LALYEIFQIPRKIiknYDLIVPAPINDN 77
Cdd:TIGR00201  15 CRQCgSWRTrirDSLCLRQNLVSVYTYNEPLKELISRFKFRGQaeiiralasLLSLTVSKAYRDL---PDVIVPVPLSKE 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178006571  78 KLRNRTFDHVAYV---LDKQNIPYTQLFQTEERKKQACLSKKERSEQ-NNPFKLINEiNLENKKILLVDDIYTTGLTIHQ 153
Cdd:TIGR00201  92 REWRRGFNQADLLaqcLSRWLFNYHNIVIRLNNETQSKLKATLRFLNlENAFDLKNN-SFQGRNIVLVDDVVTTGATLHE 170

                         170       180
                  ....*....|....*....|
gi 1178006571 154 LAEHLLVRKIRKLDALTFAR 173
Cdd:TIGR00201 171 IARLLLELGAASVQVWTLAR 190
PRK11595 PRK11595
DNA utilization protein GntX; Provisional
 32-161 1.89e-06

DNA utilization protein GntX; Provisional


Pssm-ID: 183221 [Multi-domain]  Cd Length: 227  Bit Score: 46.19  E-value: 1.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178006571  32 DYQTFIKTLMHQYKFSG--DLA-------LYEIFQIPR--KIIKNyDLIVPAPINDNKLRNRTFDH-------VAYVLdk 93
Cdd:PRK11595   69 DYAPPLSGLIHQLKFSRrsELAsvlarllLLEWLQARRstGLQKP-DRIISVPLHQRRHWRRGFNQsdllcrpLARWL-- 145

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1178006571  94 qNIPYTQLFQTEERKK--QACLSKKERSEQ-NNPFKLinEINLENKKILLVDDIYTTGLTIHQLAeHLLVR 161
Cdd:PRK11595  146 -GCDYDSEALTRTRATatQHFLSARLRKRNlKNAFRL--ELPVQGQHMAIVDDVVTTGSTVAEIA-QLLLR 212
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 117-170 2.40e-06

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: 44.69  E-value: 2.40e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1178006571 117 ERSEQNNPFKLINEINLENKKILLVDDIYTTGLTIHQLAEHLLVRKIRKLDALT 170
Cdd:cd06223    53 RTPSEPYGLELPLGGDVKGKRVLLVDDVIATGGTLLAAIELLKEAGAKVVGVAV 106
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 129-158 1.22e-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: 37.34  E-value: 1.22e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1178006571 129 NEINLENKKILLVDDIYTTGLTIHQLAEHL 158
Cdd:pfam00156  76 ALPDLKGKTVLIVDDILDTGGTLLKVLELL 105
 
Name Accession Description Interval E-value
ComFC COG1040
DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General ...
 11-174 1.27e-32

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


Pssm-ID: 440662 [Multi-domain]  Cd Length: 196  Bit Score: 114.92  E-value: 1.27e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178006571  11 CLDCmwLSQSyklinqlhtLYDYQTFIKTLMHQYKFSGDLALYEIF------QIPRKIIKNYDLIVPAPINDNKLRNRTF 84
Cdd:COG1040    29 CPDC--RAKA---------AFRYEGPLRRLILALKYRGRLDLARLLarllarALREALLPRPDLIVPVPLHRRRLRRRGF 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178006571  85 DHVAYVLD----KQNIPY-TQLFQ-TEERKKQACLSKKERsEQN--NPFKLINEINLENKKILLVDDIYTTGLTIHQLAE 156
Cdd:COG1040    98 NQAELLARalarALGIPVlPDLLRrVRATPSQAGLSRAER-RRNlrGAFAVRPPARLAGKHVLLVDDVLTTGATLAEAAR 176

                         170
                  ....*....|....*...
gi 1178006571 157 HLLVRKIRKLDALTFARG 174
Cdd:COG1040   177 ALKAAGAARVDVLVLART 194
comF TIGR00201
comF family protein; This protein is found in species that do (Bacillus subtilis, Haemophilus ...
 11-173 6.34e-14

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: 66.39  E-value: 6.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178006571  11 CLDC-MWLS---QSYKLINQLHTLYDYQTFIKTLMHQYKFSGD---------LALYEIFQIPRKIiknYDLIVPAPINDN 77
Cdd:TIGR00201  15 CRQCgSWRTrirDSLCLRQNLVSVYTYNEPLKELISRFKFRGQaeiiralasLLSLTVSKAYRDL---PDVIVPVPLSKE 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178006571  78 KLRNRTFDHVAYV---LDKQNIPYTQLFQTEERKKQACLSKKERSEQ-NNPFKLINEiNLENKKILLVDDIYTTGLTIHQ 153
Cdd:TIGR00201  92 REWRRGFNQADLLaqcLSRWLFNYHNIVIRLNNETQSKLKATLRFLNlENAFDLKNN-SFQGRNIVLVDDVVTTGATLHE 170

                         170       180
                  ....*....|....*....|
gi 1178006571 154 LAEHLLVRKIRKLDALTFAR 173
Cdd:TIGR00201 171 IARLLLELGAASVQVWTLAR 190
PRK11595 PRK11595
DNA utilization protein GntX; Provisional
 32-161 1.89e-06

DNA utilization protein GntX; Provisional


Pssm-ID: 183221 [Multi-domain]  Cd Length: 227  Bit Score: 46.19  E-value: 1.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178006571  32 DYQTFIKTLMHQYKFSG--DLA-------LYEIFQIPR--KIIKNyDLIVPAPINDNKLRNRTFDH-------VAYVLdk 93
Cdd:PRK11595   69 DYAPPLSGLIHQLKFSRrsELAsvlarllLLEWLQARRstGLQKP-DRIISVPLHQRRHWRRGFNQsdllcrpLARWL-- 145

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1178006571  94 qNIPYTQLFQTEERKK--QACLSKKERSEQ-NNPFKLinEINLENKKILLVDDIYTTGLTIHQLAeHLLVR 161
Cdd:PRK11595  146 -GCDYDSEALTRTRATatQHFLSARLRKRNlKNAFRL--ELPVQGQHMAIVDDVVTTGSTVAEIA-QLLLR 212
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 117-170 2.40e-06

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: 44.69  E-value: 2.40e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1178006571 117 ERSEQNNPFKLINEINLENKKILLVDDIYTTGLTIHQLAEHLLVRKIRKLDALT 170
Cdd:cd06223    53 RTPSEPYGLELPLGGDVKGKRVLLVDDVIATGGTLLAAIELLKEAGAKVVGVAV 106
HptA COG0634
Hypoxanthine-guanine phosphoribosyltransferase [Nucleotide transport and metabolism]; ...
 130-162 7.40e-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: 41.16  E-value: 7.40e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1178006571 130 EINLENKKILLVDDIYTTGLTIHQLAEHLLVRK 162
Cdd:COG0634    86 DEDIEGRDVLIVEDIIDTGLTLSYLLELLKSRG 118
Hpt1 COG2236
Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism]; Hypoxanthine ...
 131-158 2.96e-04

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: 39.06  E-value: 2.96e-04
                          10        20
                  ....*....|....*....|....*...
gi 1178006571 131 INLENKKILLVDDIYTTGLTIHQLAEHL 158
Cdd:COG2236    84 EDLAGKRVLIVDDVADTGRTLEAVRDLL 111
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 129-158 1.22e-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: 37.34  E-value: 1.22e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1178006571 129 NEINLENKKILLVDDIYTTGLTIHQLAEHL 158
Cdd:pfam00156  76 ALPDLKGKTVLIVDDILDTGGTLLKVLELL 105
PLN02238 PLN02238
hypoxanthine phosphoribosyltransferase
 130-162 6.67e-03

hypoxanthine phosphoribosyltransferase


Pssm-ID: 215132  Cd Length: 189  Bit Score: 35.78  E-value: 6.67e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1178006571 130 EINLENKKILLVDDIYTTGLTIHQLAEHLLVRK 162
Cdd:PLN02238   92 KIDVKGKHVLLVEDIVDTGNTLSALVAHLEAKG 124
 
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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