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Conserved domains on  [gi|657893378|ref|WP_029596833|]
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ComF family protein [Flavobacterium sp. ACAM 123]

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 ...
 2-227 4.92e-63

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


:

Pssm-ID: 440662 [Multi-domain]  Cd Length: 196  Bit Score: 194.66  E-value: 4.92e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657893378   2 LKYLLNLFFPPVCAGCNsflMKNEKVICTVCRHhipltnhhitpeneafkkfygripleyASAFLYfhkKGIVQELIHKL 81
Cdd:COG1040    5 LRALLDLLFPPRCLLCG---AAPGGGLCPDCRA---------------------------KAAFRY---EGPLRRLILAL 51

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657893378  82 KYKGHEEIGSVIGKWYAEDLKEkTILKTADMIIPVPLHKKKFRERGYNQVTTFGVALSAEFGIPYNDSLLFRTVYSKTQS 161
Cdd:COG1040   52 KYRGRLDLARLLARLLARALRE-ALLPRPDLIVPVPLHRRRLRRRGFNQAELLARALARALGIPVLPDLLRRVRATPSQA 130

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 657893378 162 QKSLLDRSEKINLIFDVSFNEKDHNKHYILVDDVITTGATLEACSRALMKIPGAKVSIVCMAMAQS 227
Cdd:COG1040  131 GLSRAERRRNLRGAFAVRPPARLAGKHVLLVDDVLTTGATLAEAARALKAAGAARVDVLVLARTPR 196
 
Name Accession Description Interval E-value
ComFC COG1040
DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General ...
 2-227 4.92e-63

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


Pssm-ID: 440662 [Multi-domain]  Cd Length: 196  Bit Score: 194.66  E-value: 4.92e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657893378   2 LKYLLNLFFPPVCAGCNsflMKNEKVICTVCRHhipltnhhitpeneafkkfygripleyASAFLYfhkKGIVQELIHKL 81
Cdd:COG1040    5 LRALLDLLFPPRCLLCG---AAPGGGLCPDCRA---------------------------KAAFRY---EGPLRRLILAL 51

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657893378  82 KYKGHEEIGSVIGKWYAEDLKEkTILKTADMIIPVPLHKKKFRERGYNQVTTFGVALSAEFGIPYNDSLLFRTVYSKTQS 161
Cdd:COG1040   52 KYRGRLDLARLLARLLARALRE-ALLPRPDLIVPVPLHRRRLRRRGFNQAELLARALARALGIPVLPDLLRRVRATPSQA 130

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 657893378 162 QKSLLDRSEKINLIFDVSFNEKDHNKHYILVDDVITTGATLEACSRALMKIPGAKVSIVCMAMAQS 227
Cdd:COG1040  131 GLSRAERRRNLRGAFAVRPPARLAGKHVLLVDDVLTTGATLAEAARALKAAGAARVDVLVLARTPR 196
comF TIGR00201
comF family protein; This protein is found in species that do (Bacillus subtilis, Haemophilus ...
 68-223 4.82e-23

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: 91.81  E-value: 4.82e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657893378   68 FHKKGIVQELIHKLKYKGHEEIGSVIGKWYAEDLKeKTILKTADMIIPVPLHKKKFRERGYNQVTTFGVALSaEFGipYN 147
Cdd:TIGR00201  39 YTYNEPLKELISRFKFRGQAEIIRALASLLSLTVS-KAYRDLPDVIVPVPLSKEREWRRGFNQADLLAQCLS-RWL--FN 114

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 657893378  148 DSLLFRTVYSKTQSQKSLLDRSEKINLIFDVSFNEKDHnKHYILVDDVITTGATLEACSRALMKIPGAKVSIVCMA 223
Cdd:TIGR00201 115 YHNIVIRLNNETQSKLKATLRFLNLENAFDLKNNSFQG-RNIVLVDDVVTTGATLHEIARLLLELGAASVQVWTLA 189
PRK11595 PRK11595
DNA utilization protein GntX; Provisional
 77-222 3.32e-19

DNA utilization protein GntX; Provisional


Pssm-ID: 183221 [Multi-domain]  Cd Length: 227  Bit Score: 82.39  E-value: 3.32e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657893378  77 LIHKLKYKGHEEIGSVIGK-----WyaEDLKEKTILKTADMIIPVPLHKKKFRERGYNQVTTFGVALSAEFGIPYNDSLL 151
Cdd:PRK11595  77 LIHQLKFSRRSELASVLARlllleW--LQARRSTGLQKPDRIISVPLHQRRHWRRGFNQSDLLCRPLARWLGCDYDSEAL 154

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 657893378 152 FRTvySKTQSQKSLLDRSEKINL--IFDVSFNEKDhnKHYILVDDVITTGATLEACSRALMKIPGAKVSIVCM 222
Cdd:PRK11595 155 TRT--RATATQHFLSARLRKRNLknAFRLELPVQG--QHMAIVDDVVTTGSTVAEIAQLLLRNGAASVQVWCL 223
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 93-227 8.50e-12

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: 60.49  E-value: 8.50e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657893378  93 IGKWYAEDLKEKtiLKTADMIIPVPlhkkkfrERGYNqvttFGVALSAEFGIPYndslLFRTVYSKTQSQKSLLDRSEKI 172
Cdd:cd06223    1 AGRLLAEEIRED--LLEPDVVVGIL-------RGGLP----LAAALARALGLPL----AFIRKERKGPGRTPSEPYGLEL 63

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 657893378 173 NLIFDVSfnekdhNKHYILVDDVITTGATLEACSRALMKIPGAKVSIVCMAMAQS 227
Cdd:cd06223   64 PLGGDVK------GKRVLLVDDVIATGGTLLAAIELLKEAGAKVVGVAVLLDKPE 112
DZR_2 pfam18912
Double zinc ribbon domain; This domain family is found in bacteria, archaea and eukaryotes, ...
 5-33 5.23e-04

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: 36.88  E-value: 5.23e-04
                          10        20
                  ....*....|....*....|....*....
gi 657893378    5 LLNLFFPPVCAGCNSfLMKNEKVICTVCR 33
Cdd:pfam18912   1 LLDLLFPPRCPLCGA-IVAEGGGLCAACW 28
 
Name Accession Description Interval E-value
ComFC COG1040
DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General ...
 2-227 4.92e-63

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


Pssm-ID: 440662 [Multi-domain]  Cd Length: 196  Bit Score: 194.66  E-value: 4.92e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657893378   2 LKYLLNLFFPPVCAGCNsflMKNEKVICTVCRHhipltnhhitpeneafkkfygripleyASAFLYfhkKGIVQELIHKL 81
Cdd:COG1040    5 LRALLDLLFPPRCLLCG---AAPGGGLCPDCRA---------------------------KAAFRY---EGPLRRLILAL 51

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657893378  82 KYKGHEEIGSVIGKWYAEDLKEkTILKTADMIIPVPLHKKKFRERGYNQVTTFGVALSAEFGIPYNDSLLFRTVYSKTQS 161
Cdd:COG1040   52 KYRGRLDLARLLARLLARALRE-ALLPRPDLIVPVPLHRRRLRRRGFNQAELLARALARALGIPVLPDLLRRVRATPSQA 130

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 657893378 162 QKSLLDRSEKINLIFDVSFNEKDHNKHYILVDDVITTGATLEACSRALMKIPGAKVSIVCMAMAQS 227
Cdd:COG1040  131 GLSRAERRRNLRGAFAVRPPARLAGKHVLLVDDVLTTGATLAEAARALKAAGAARVDVLVLARTPR 196
comF TIGR00201
comF family protein; This protein is found in species that do (Bacillus subtilis, Haemophilus ...
 68-223 4.82e-23

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: 91.81  E-value: 4.82e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657893378   68 FHKKGIVQELIHKLKYKGHEEIGSVIGKWYAEDLKeKTILKTADMIIPVPLHKKKFRERGYNQVTTFGVALSaEFGipYN 147
Cdd:TIGR00201  39 YTYNEPLKELISRFKFRGQAEIIRALASLLSLTVS-KAYRDLPDVIVPVPLSKEREWRRGFNQADLLAQCLS-RWL--FN 114

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 657893378  148 DSLLFRTVYSKTQSQKSLLDRSEKINLIFDVSFNEKDHnKHYILVDDVITTGATLEACSRALMKIPGAKVSIVCMA 223
Cdd:TIGR00201 115 YHNIVIRLNNETQSKLKATLRFLNLENAFDLKNNSFQG-RNIVLVDDVVTTGATLHEIARLLLELGAASVQVWTLA 189
PRK11595 PRK11595
DNA utilization protein GntX; Provisional
 77-222 3.32e-19

DNA utilization protein GntX; Provisional


Pssm-ID: 183221 [Multi-domain]  Cd Length: 227  Bit Score: 82.39  E-value: 3.32e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657893378  77 LIHKLKYKGHEEIGSVIGK-----WyaEDLKEKTILKTADMIIPVPLHKKKFRERGYNQVTTFGVALSAEFGIPYNDSLL 151
Cdd:PRK11595  77 LIHQLKFSRRSELASVLARlllleW--LQARRSTGLQKPDRIISVPLHQRRHWRRGFNQSDLLCRPLARWLGCDYDSEAL 154

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 657893378 152 FRTvySKTQSQKSLLDRSEKINL--IFDVSFNEKDhnKHYILVDDVITTGATLEACSRALMKIPGAKVSIVCM 222
Cdd:PRK11595 155 TRT--RATATQHFLSARLRKRNLknAFRLELPVQG--QHMAIVDDVVTTGSTVAEIAQLLLRNGAASVQVWCL 223
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 93-227 8.50e-12

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: 60.49  E-value: 8.50e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657893378  93 IGKWYAEDLKEKtiLKTADMIIPVPlhkkkfrERGYNqvttFGVALSAEFGIPYndslLFRTVYSKTQSQKSLLDRSEKI 172
Cdd:cd06223    1 AGRLLAEEIRED--LLEPDVVVGIL-------RGGLP----LAAALARALGLPL----AFIRKERKGPGRTPSEPYGLEL 63

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 657893378 173 NLIFDVSfnekdhNKHYILVDDVITTGATLEACSRALMKIPGAKVSIVCMAMAQS 227
Cdd:cd06223   64 PLGGDVK------GKRVLLVDDVIATGGTLLAAIELLKEAGAKVVGVAVLLDKPE 112
PRK07322 PRK07322
adenine phosphoribosyltransferase; Provisional
 137-226 1.31e-05

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 180928  Cd Length: 178  Bit Score: 44.20  E-value: 1.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657893378 137 ALSAEFGIPY-----------NDSLLfRTVYSKTQSQKSLLdrsekinlIFDVSFNEKDHNKHYILVDDVITTGATLEAC 205
Cdd:PRK07322  69 ALSRRLGKPYvvarksrkpymQDPII-QEVVSITTGKPQLL--------VLDGADAEKLKGKRVAIVDDVVSTGGTLTAL 139

                         90       100
                 ....*....|....*....|.
gi 657893378 206 SRaLMKIPGAKVSIVCMAMAQ 226
Cdd:PRK07322 140 ER-LVERAGGQVVAKAAIFAE 159
DZR_2 pfam18912
Double zinc ribbon domain; This domain family is found in bacteria, archaea and eukaryotes, ...
 5-33 5.23e-04

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: 36.88  E-value: 5.23e-04
                          10        20
                  ....*....|....*....|....*....
gi 657893378    5 LLNLFFPPVCAGCNSfLMKNEKVICTVCR 33
Cdd:pfam18912   1 LLDLLFPPRCPLCGA-IVAEGGGLCAACW 28
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 120-221 5.96e-04

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: 38.89  E-value: 5.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657893378  120 KKKFRERGYNQVT---------TFGVALSAEFGIPYNDSLLFRtvYSKTQSQKSLLdrsekINLIFDVSfnekdhNKHYI 190
Cdd:pfam00156  20 AQINEDYGGKPDVvvgilrgglPFAGILARRLDVPLAFVRKVS--YNPDTSEVMKT-----SSALPDLK------GKTVL 86

                          90       100       110
                  ....*....|....*....|....*....|.
gi 657893378  191 LVDDVITTGATLEACSRALMKIPGAKVSIVC 221
Cdd:pfam00156  87 IVDDILDTGGTLLKVLELLKNVGPKEVKIAV 117
PRK06031 PRK06031
phosphoribosyltransferase; Provisional
 186-227 5.18e-03

phosphoribosyltransferase; Provisional


Pssm-ID: 235678  Cd Length: 233  Bit Score: 37.04  E-value: 5.18e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 657893378 186 NKHYILVDDVITTGATLEACSRALMKIpGAKVSIVCMAMAQS 227
Cdd:PRK06031 154 GRRVALIDDVISSGASIVAGLRLLAAC-GIEPAGIGAAMLQS 194
Apt COG0503
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ...
 121-227 7.07e-03

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: 36.21  E-value: 7.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657893378 121 KKFRERGYNQVTT-------FGVALSAEFGIPYndsLLFRT---VYSKTQSQKSLLDRSEKINLIFDVSFNEKdhNKHYI 190
Cdd:COG0503   42 ERFADKGIDKVVGieargfiLAAALAYALGVPF---VPARKpgkLPGETVSEEYDLEYGTGDTLELHKDALKP--GDRVL 116

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 657893378 191 LVDDVITTGATLEACSRaLMKIPGAKVSIVCMAMAQS 227
Cdd:COG0503  117 IVDDLLATGGTAKAAIK-LVEEAGAEVVGIAFLIELG 152
COG1926 COG1926
Predicted phosphoribosyltransferase [General function prediction only];
185-209 7.19e-03

Predicted phosphoribosyltransferase [General function prediction only];


Pssm-ID: 441529  Cd Length: 209  Bit Score: 36.20  E-value: 7.19e-03
                         10        20
                 ....*....|....*....|....*
gi 657893378 185 HNKHYILVDDVITTGATLEACSRAL 209
Cdd:COG1926  120 KGRTVILVDDGIATGATMRAALRAL 144
 
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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