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Conserved domains on  [gi|2158765764|dbj|GJC31037|]
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hypothetical protein KAM392_10160 [Acinetobacter sp. KAM392]

Protein Classification

ComEA family DNA-binding protein( domain architecture ID 11446237)

ComEA family DNA-binding protein contains a helix-hairpin-helix (HhH) motif, similar to Bacillus subtilis ComE operon protein 1, an integral membrane protein required for both DNA binding and transport

Gene Ontology:  GO:0003677
PubMed:  10908318|8692686
SCOP:  4001398

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ComEA COG1555
DNA uptake protein ComE or related DNA-binding protein [Replication, recombination and repair]; ...
 53-123 1.08e-30

DNA uptake protein ComE or related DNA-binding protein [Replication, recombination and repair];


:

Pssm-ID: 441164 [Multi-domain]  Cd Length: 72  Bit Score: 104.56  E-value: 1.08e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2158765764  53 ARPTQQSAHSNQVRLNSASLEQLQQLSGVGMKKAQAIVEYRKQNGKFQSIEELQQVKGIGPALFAKNKHKL 123
Cdd:COG1555     1 APASASAAAGGKVDINTATAEELQTLPGIGPKLAQRIVEYREKNGPFKSVEDLLEVKGIGPKTLEKLKPYL 71
 
Name Accession Description Interval E-value
ComEA COG1555
DNA uptake protein ComE or related DNA-binding protein [Replication, recombination and repair]; ...
 53-123 1.08e-30

DNA uptake protein ComE or related DNA-binding protein [Replication, recombination and repair];


Pssm-ID: 441164 [Multi-domain]  Cd Length: 72  Bit Score: 104.56  E-value: 1.08e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2158765764  53 ARPTQQSAHSNQVRLNSASLEQLQQLSGVGMKKAQAIVEYRKQNGKFQSIEELQQVKGIGPALFAKNKHKL 123
Cdd:COG1555     1 APASASAAAGGKVDINTATAEELQTLPGIGPKLAQRIVEYREKNGPFKSVEDLLEVKGIGPKTLEKLKPYL 71
HHH_3 pfam12836
Helix-hairpin-helix motif; The HhH domain is a short DNA-binding domain.
 62-123 2.12e-24

Helix-hairpin-helix motif; The HhH domain is a short DNA-binding domain.


Pssm-ID: 463723 [Multi-domain]  Cd Length: 62  Bit Score: 88.31  E-value: 2.12e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2158765764  62 SNQVRLNSASLEQLQQLSGVGMKKAQAIVEYRKQNGKFQSIEELQQVKGIGPALFAKNKHKL 123
Cdd:pfam12836   1 AVGVDINTASAELLSRVPGLGPKLAKNIVEYREENGPFRSREDLLKVKGLGPKTFEQLAGFL 62
comE TIGR01259
comEA protein; This model describes the ComEA protein in bacteria. The com E locus is ...
 48-125 4.18e-20

comEA protein; This model describes the ComEA protein in bacteria. The com E locus is obligatory for bacterial cell competence - the process of internalizing the exogenous added DNA. Lesions in the loci has been variously described for the appearance of competence-related pheonotypes and impairment of competence, suggesting their intimate functional role in bacterial transformation. [Cellular processes, DNA transformation]


Pssm-ID: 213597 [Multi-domain]  Cd Length: 120  Bit Score: 79.18  E-value: 4.18e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2158765764  48 EAHYLARPTQQSAHSNQ-VRLNSASLEQLQQLSGVGMKKAQAIVEYRKQNGKFQSIEELQQVKGIGPALFAKNKHKLAL 125
Cdd:TIGR01259  42 EEAVSQQGTQSSAGKLAaVNINAASLEELQALPGIGPAKAKAIIEYREENGAFKSVDDLTKVSGIGEKSLEKLKDYATV 120
NT_POLXc cd00141
Nucleotidyltransferase (NT) domain of family X DNA Polymerases; X family polymerases fill in ...
 70-114 9.70e-03

Nucleotidyltransferase (NT) domain of family X DNA Polymerases; X family polymerases fill in short gaps during DNA repair. They are relatively inaccurate enzymes and play roles in base excision repair, in non-homologous end joining (NHEJ) which acts mainly to repair damage due to ionizing radiation, and in V(D)J recombination. This family includes eukaryotic Pol beta, Pol lambda, Pol mu, and terminal deoxyribonucleotidyl transferase (TdT). Pol beta and Pol lambda are primarily DNA template-dependent polymerases. TdT is a DNA template-independent polymerase. Pol mu has both template dependent and template independent activities. This subgroup belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, coordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. These three carboxylate residues are fairly well conserved in this family.


Pssm-ID: 143386 [Multi-domain]  Cd Length: 307  Bit Score: 34.48  E-value: 9.70e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2158765764  70 ASLEQLQQLSGVGMKKAQAIVEYRK----------QNGKFQSIEELQQVKGIGPA 114
Cdd:cd00141    42 ESLEEAKKLPGIGKKIAEKIEEILEtgklrkleelREDVPPGLLLLLRVPGVGPK 96
 
Name Accession Description Interval E-value
ComEA COG1555
DNA uptake protein ComE or related DNA-binding protein [Replication, recombination and repair]; ...
 53-123 1.08e-30

DNA uptake protein ComE or related DNA-binding protein [Replication, recombination and repair];


Pssm-ID: 441164 [Multi-domain]  Cd Length: 72  Bit Score: 104.56  E-value: 1.08e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2158765764  53 ARPTQQSAHSNQVRLNSASLEQLQQLSGVGMKKAQAIVEYRKQNGKFQSIEELQQVKGIGPALFAKNKHKL 123
Cdd:COG1555     1 APASASAAAGGKVDINTATAEELQTLPGIGPKLAQRIVEYREKNGPFKSVEDLLEVKGIGPKTLEKLKPYL 71
HHH_3 pfam12836
Helix-hairpin-helix motif; The HhH domain is a short DNA-binding domain.
 62-123 2.12e-24

Helix-hairpin-helix motif; The HhH domain is a short DNA-binding domain.


Pssm-ID: 463723 [Multi-domain]  Cd Length: 62  Bit Score: 88.31  E-value: 2.12e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2158765764  62 SNQVRLNSASLEQLQQLSGVGMKKAQAIVEYRKQNGKFQSIEELQQVKGIGPALFAKNKHKL 123
Cdd:pfam12836   1 AVGVDINTASAELLSRVPGLGPKLAKNIVEYREENGPFRSREDLLKVKGLGPKTFEQLAGFL 62
comE TIGR01259
comEA protein; This model describes the ComEA protein in bacteria. The com E locus is ...
 48-125 4.18e-20

comEA protein; This model describes the ComEA protein in bacteria. The com E locus is obligatory for bacterial cell competence - the process of internalizing the exogenous added DNA. Lesions in the loci has been variously described for the appearance of competence-related pheonotypes and impairment of competence, suggesting their intimate functional role in bacterial transformation. [Cellular processes, DNA transformation]


Pssm-ID: 213597 [Multi-domain]  Cd Length: 120  Bit Score: 79.18  E-value: 4.18e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2158765764  48 EAHYLARPTQQSAHSNQ-VRLNSASLEQLQQLSGVGMKKAQAIVEYRKQNGKFQSIEELQQVKGIGPALFAKNKHKLAL 125
Cdd:TIGR01259  42 EEAVSQQGTQSSAGKLAaVNINAASLEELQALPGIGPAKAKAIIEYREENGAFKSVDDLTKVSGIGEKSLEKLKDYATV 120
TIGR00426 TIGR00426
competence protein ComEA helix-hairpin-helix repeat region; Members of the subfamily ...
 65-125 5.71e-17

competence protein ComEA helix-hairpin-helix repeat region; Members of the subfamily recognized by this model include competence protein ComEA and closely related proteins from a number of species that exhibit competence for transformation by exongenous DNA, including Streptococcus pneumoniae, Bacillus subtilis, Neisseria meningitidis, and Haemophilus influenzae. This model represents a region of two tandem copies of a helix-hairpin-helix domain (pfam00633), each about 30 residues in length. Limited sequence similarity can be found among some members of this family N-terminal to the region covered by this model. [Cellular processes, DNA transformation]


Pssm-ID: 129520 [Multi-domain]  Cd Length: 69  Bit Score: 69.57  E-value: 5.71e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2158765764  65 VRLNSASLEQLQQ-LSGVGMKKAQAIVEYRKQNGKFQSIEELQQVKGIGPALFAKNKHKLAL 125
Cdd:TIGR00426   8 VNINTATAEELQRaMNGVGLKKAEAIVSYREEYGPFKTVEDLKQVPGIGNSLVEKNLAVITL 69
Tex COG2183
Transcriptional accessory protein Tex/SPT6 [Transcription];
65-116 2.75e-12

Transcriptional accessory protein Tex/SPT6 [Transcription];


Pssm-ID: 441786 [Multi-domain]  Cd Length: 719  Bit Score: 61.96  E-value: 2.75e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2158765764  65 VRLNSASLEQLQQLSGVGMKKAQAIVEYRKQNGKFQSIEELQQVKGIGPALF 116
Cdd:COG2183   487 VDLNTASAPLLSYVSGLNPTLAKNIVAYRDENGAFKSRKELLKVPRLGPKAF 538
HHH pfam00633
Helix-hairpin-helix motif; The helix-hairpin-helix DNA-binding motif is found to be duplicated ...
 66-92 9.37e-06

Helix-hairpin-helix motif; The helix-hairpin-helix DNA-binding motif is found to be duplicated in the central domain of RuvA. The HhH domain of DisA, a bacterial checkpoint control protein, is a DNA-binding domain.


Pssm-ID: 425789 [Multi-domain]  Cd Length: 30  Bit Score: 39.71  E-value: 9.37e-06
                          10        20
                  ....*....|....*....|....*..
gi 2158765764  66 RLNSASLEQLQQLSGVGMKKAQAIVEY 92
Cdd:pfam00633   4 GLIPASVEELLALPGVGPKTAEAILSY 30
DnaE COG0587
DNA polymerase III, alpha subunit [Replication, recombination and repair];
75-105 1.99e-03

DNA polymerase III, alpha subunit [Replication, recombination and repair];


Pssm-ID: 440352 [Multi-domain]  Cd Length: 1050  Bit Score: 36.59  E-value: 1.99e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 2158765764   75 LQQLSGVGMKKAQAIVEYRKQNGKFQSIEEL 105
Cdd:COG0587    817 LGAIKGVGEAAAEAIVAAREENGPFTSLFDF 847
PulK COG3156
Type II secretory pathway, component PulK [Intracellular trafficking, secretion, and vesicular ...
 92-118 2.38e-03

Type II secretory pathway, component PulK [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 442390 [Multi-domain]  Cd Length: 307  Bit Score: 36.13  E-value: 2.38e-03
                          10        20
                  ....*....|....*....|....*..
gi 2158765764  92 YRKQNGKFQSIEELQQVKGIGPALFAK 118
Cdd:COG3156   173 YRPANGPFASVSELRLVKGMTPELYAR 199
HHH_2 pfam12826
Helix-hairpin-helix motif; The HhH domain of DisA, a bacterial checkpoint control protein, is ...
 66-92 2.40e-03

Helix-hairpin-helix motif; The HhH domain of DisA, a bacterial checkpoint control protein, is a DNA-binding domain.


Pssm-ID: 432812 [Multi-domain]  Cd Length: 64  Bit Score: 34.04  E-value: 2.40e-03
                          10        20
                  ....*....|....*....|....*..
gi 2158765764  66 RLNSASLEQLQQLSGVGMKKAQAIVEY 92
Cdd:pfam12826  28 ALAEASLEELLEVDDIGPEIAQSIVEF 54
Lig COG0272
NAD-dependent DNA ligase [Replication, recombination and repair];
66-107 9.16e-03

NAD-dependent DNA ligase [Replication, recombination and repair];


Pssm-ID: 440042 [Multi-domain]  Cd Length: 668  Bit Score: 34.62  E-value: 9.16e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2158765764  66 RLNSASLEQLQQLSGVGMKKAQAIVEYRKQNGKFQSIEELQQ 107
Cdd:COG0272   537 ALMAASEEELAAVDGIGPVVAESIVEFFAEPHNRELIERLRA 578
NT_POLXc cd00141
Nucleotidyltransferase (NT) domain of family X DNA Polymerases; X family polymerases fill in ...
 70-114 9.70e-03

Nucleotidyltransferase (NT) domain of family X DNA Polymerases; X family polymerases fill in short gaps during DNA repair. They are relatively inaccurate enzymes and play roles in base excision repair, in non-homologous end joining (NHEJ) which acts mainly to repair damage due to ionizing radiation, and in V(D)J recombination. This family includes eukaryotic Pol beta, Pol lambda, Pol mu, and terminal deoxyribonucleotidyl transferase (TdT). Pol beta and Pol lambda are primarily DNA template-dependent polymerases. TdT is a DNA template-independent polymerase. Pol mu has both template dependent and template independent activities. This subgroup belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, coordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. These three carboxylate residues are fairly well conserved in this family.


Pssm-ID: 143386 [Multi-domain]  Cd Length: 307  Bit Score: 34.48  E-value: 9.70e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2158765764  70 ASLEQLQQLSGVGMKKAQAIVEYRK----------QNGKFQSIEELQQVKGIGPA 114
Cdd:cd00141    42 ESLEEAKKLPGIGKKIAEKIEEILEtgklrkleelREDVPPGLLLLLRVPGVGPK 96
 
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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