NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1797185676|ref|WP_159124105|]
View 

MULTISPECIES: ComEA family DNA-binding protein [Acinetobacter]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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]; ...
 71-140 1.50e-29

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


:

Pssm-ID: 441164 [Multi-domain]  Cd Length: 72  Bit Score: 102.25  E-value: 1.50e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797185676  71 PALSASSAADKISLNQASIEQLQQLNGIGQKKAEAIIEYRQKNGKFKTIEDIQQVKGIGPALFAKNKDKL 140
Cdd:COG1555     2 PASASAAAGGKVDINTATAEELQTLPGIGPKLAQRIVEYREKNGPFKSVEDLLEVKGIGPKTLEKLKPYL 71
 
Name Accession Description Interval E-value
ComEA COG1555
DNA uptake protein ComE or related DNA-binding protein [Replication, recombination and repair]; ...
 71-140 1.50e-29

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


Pssm-ID: 441164 [Multi-domain]  Cd Length: 72  Bit Score: 102.25  E-value: 1.50e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797185676  71 PALSASSAADKISLNQASIEQLQQLNGIGQKKAEAIIEYRQKNGKFKTIEDIQQVKGIGPALFAKNKDKL 140
Cdd:COG1555     2 PASASAAAGGKVDINTATAEELQTLPGIGPKLAQRIVEYREKNGPFKSVEDLLEVKGIGPKTLEKLKPYL 71
HHH_3 pfam12836
Helix-hairpin-helix motif; The HhH domain is a short DNA-binding domain.
 81-140 1.78e-22

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


Pssm-ID: 463723 [Multi-domain]  Cd Length: 62  Bit Score: 83.69  E-value: 1.78e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797185676  81 KISLNQASIEQLQQLNGIGQKKAEAIIEYRQKNGKFKTIEDIQQVKGIGPALFAKNKDKL 140
Cdd:pfam12836   3 GVDINTASAELLSRVPGLGPKLAKNIVEYREENGPFRSREDLLKVKGLGPKTFEQLAGFL 62
comE TIGR01259
comEA protein; This model describes the ComEA protein in bacteria. The com E locus is ...
 74-142 1.62e-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: 80.72  E-value: 1.62e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1797185676  74 SASSAADKISLNQASIEQLQQLNGIGQKKAEAIIEYRQKNGKFKTIEDIQQVKGIGPALFAKNKDKLAL 142
Cdd:TIGR01259  52 SSAGKLAAVNINAASLEELQALPGIGPAKAKAIIEYREENGAFKSVDDLTKVSGIGEKSLEKLKDYATV 120
psbU PRK02515
photosystem II complex extrinsic protein PsbU;
80-139 1.88e-03

photosystem II complex extrinsic protein PsbU;


Pssm-ID: 235048 [Multi-domain]  Cd Length: 132  Bit Score: 36.19  E-value: 1.88e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1797185676  80 DKISLNQASIEQLQQLNGIGQKKAEAIIeyrqKNGKFKTIEDIQQVKGIG---PALFAKNKDK 139
Cdd:PRK02515   51 EKIDLNNSSVRAFRQFPGMYPTLAGKIV----KNAPYDSVEDVLNLPGLSerqKELLEANLDN 109
NT_POLXc cd00141
Nucleotidyltransferase (NT) domain of family X DNA Polymerases; X family polymerases fill in ...
 87-131 7.98e-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: 35.25  E-value: 7.98e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1797185676  87 ASIEQLQQLNGIGQKKAEAIIEYRQkNGKFKTIEDIQ-----------QVKGIGPA 131
Cdd:cd00141    42 ESLEEAKKLPGIGKKIAEKIEEILE-TGKLRKLEELRedvppglllllRVPGVGPK 96
 
Name Accession Description Interval E-value
ComEA COG1555
DNA uptake protein ComE or related DNA-binding protein [Replication, recombination and repair]; ...
 71-140 1.50e-29

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


Pssm-ID: 441164 [Multi-domain]  Cd Length: 72  Bit Score: 102.25  E-value: 1.50e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797185676  71 PALSASSAADKISLNQASIEQLQQLNGIGQKKAEAIIEYRQKNGKFKTIEDIQQVKGIGPALFAKNKDKL 140
Cdd:COG1555     2 PASASAAAGGKVDINTATAEELQTLPGIGPKLAQRIVEYREKNGPFKSVEDLLEVKGIGPKTLEKLKPYL 71
HHH_3 pfam12836
Helix-hairpin-helix motif; The HhH domain is a short DNA-binding domain.
 81-140 1.78e-22

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


Pssm-ID: 463723 [Multi-domain]  Cd Length: 62  Bit Score: 83.69  E-value: 1.78e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797185676  81 KISLNQASIEQLQQLNGIGQKKAEAIIEYRQKNGKFKTIEDIQQVKGIGPALFAKNKDKL 140
Cdd:pfam12836   3 GVDINTASAELLSRVPGLGPKLAKNIVEYREENGPFRSREDLLKVKGLGPKTFEQLAGFL 62
comE TIGR01259
comEA protein; This model describes the ComEA protein in bacteria. The com E locus is ...
 74-142 1.62e-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: 80.72  E-value: 1.62e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1797185676  74 SASSAADKISLNQASIEQLQQLNGIGQKKAEAIIEYRQKNGKFKTIEDIQQVKGIGPALFAKNKDKLAL 142
Cdd:TIGR01259  52 SSAGKLAAVNINAASLEELQALPGIGPAKAKAIIEYREENGAFKSVDDLTKVSGIGEKSLEKLKDYATV 120
TIGR00426 TIGR00426
competence protein ComEA helix-hairpin-helix repeat region; Members of the subfamily ...
 81-142 8.73e-19

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: 74.97  E-value: 8.73e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1797185676  81 KISLNQASIEQLQQ-LNGIGQKKAEAIIEYRQKNGKFKTIEDIQQVKGIGPALFAKNKDKLAL 142
Cdd:TIGR00426   7 RVNINTATAEELQRaMNGVGLKKAEAIVSYREEYGPFKTVEDLKQVPGIGNSLVEKNLAVITL 69
Tex COG2183
Transcriptional accessory protein Tex/SPT6 [Transcription];
84-133 7.37e-09

Transcriptional accessory protein Tex/SPT6 [Transcription];


Pssm-ID: 441786 [Multi-domain]  Cd Length: 719  Bit Score: 52.72  E-value: 7.37e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1797185676  84 LNQASIEQLQQLNGIGQKKAEAIIEYRQKNGKFKTIEDIQQVKGIGPALF 133
Cdd:COG2183   489 LNTASAPLLSYVSGLNPTLAKNIVAYRDENGAFKSRKELLKVPRLGPKAF 538
HHH pfam00633
Helix-hairpin-helix motif; The helix-hairpin-helix DNA-binding motif is found to be duplicated ...
 83-109 4.26e-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: 40.86  E-value: 4.26e-06
                          10        20
                  ....*....|....*....|....*..
gi 1797185676  83 SLNQASIEQLQQLNGIGQKKAEAIIEY 109
Cdd:pfam00633   4 GLIPASVEELLALPGVGPKTAEAILSY 30
COG1491 COG1491
Predicted nucleic acid-binding OB-fold protein [General function prediction only];
91-128 2.52e-04

Predicted nucleic acid-binding OB-fold protein [General function prediction only];


Pssm-ID: 441100  Cd Length: 189  Bit Score: 39.01  E-value: 2.52e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1797185676  91 QLQQLNGIGQKKAEAIIEYRqKNGKFKTIEDIQQ-VKGI 128
Cdd:COG1491   125 QLELLPGIGKKLMWAILEER-KKKPFESFEDLEErVKGL 162
DnaE COG0587
DNA polymerase III, alpha subunit [Replication, recombination and repair];
92-121 5.93e-04

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


Pssm-ID: 440352 [Multi-domain]  Cd Length: 1050  Bit Score: 38.51  E-value: 5.93e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1797185676   92 LQQLNGIGQKKAEAIIEYRQKNGKFKTIED 121
Cdd:COG0587    817 LGAIKGVGEAAAEAIVAAREENGPFTSLFD 846
psbU PRK02515
photosystem II complex extrinsic protein PsbU;
80-139 1.88e-03

photosystem II complex extrinsic protein PsbU;


Pssm-ID: 235048 [Multi-domain]  Cd Length: 132  Bit Score: 36.19  E-value: 1.88e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1797185676  80 DKISLNQASIEQLQQLNGIGQKKAEAIIeyrqKNGKFKTIEDIQQVKGIG---PALFAKNKDK 139
Cdd:PRK02515   51 EKIDLNNSSVRAFRQFPGMYPTLAGKIV----KNAPYDSVEDVLNLPGLSerqKELLEANLDN 109
Lig COG0272
NAD-dependent DNA ligase [Replication, recombination and repair];
86-109 2.11e-03

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


Pssm-ID: 440042 [Multi-domain]  Cd Length: 668  Bit Score: 36.93  E-value: 2.11e-03
                          10        20
                  ....*....|....*....|....
gi 1797185676  86 QASIEQLQQLNGIGQKKAEAIIEY 109
Cdd:COG0272   540 AASEEELAAVDGIGPVVAESIVEF 563
uvrC PRK00558
excinuclease ABC subunit UvrC;
80-109 2.67e-03

excinuclease ABC subunit UvrC;


Pssm-ID: 234792 [Multi-domain]  Cd Length: 598  Bit Score: 36.63  E-value: 2.67e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1797185676  80 DKISlnQASIEQLQQLNGIGQKKAEAIIEY 109
Cdd:PRK00558  567 KAIK--EASVEELAKVPGISKKLAEAIYEA 594
ligB PRK08097
NAD-dependent DNA ligase LigB;
68-111 3.22e-03

NAD-dependent DNA ligase LigB;


Pssm-ID: 236150 [Multi-domain]  Cd Length: 562  Bit Score: 36.43  E-value: 3.22e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1797185676  68 LAKPALSASSAADKISLNQASIEQLQQLNGIGQKKAEAIIEYRQ 111
Cdd:PRK08097  498 LPQAALNALDDRSWQQLLSRSEQQWQQLPGIGEGRARQLIAFLQ 541
HHH_6 pfam14579
Helix-hairpin-helix motif; The HHH domain is a short DNA-binding domain.
 92-121 4.67e-03

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


Pssm-ID: 434050 [Multi-domain]  Cd Length: 88  Bit Score: 34.37  E-value: 4.67e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1797185676  92 LQQLNGIGQKKAEAIIEYRqKNGKFKTIED 121
Cdd:pfam14579  27 LGAIKGLGEAAAERIVEER-ENGPFKSLED 55
NT_POLXc cd00141
Nucleotidyltransferase (NT) domain of family X DNA Polymerases; X family polymerases fill in ...
 87-131 7.98e-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: 35.25  E-value: 7.98e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1797185676  87 ASIEQLQQLNGIGQKKAEAIIEYRQkNGKFKTIEDIQ-----------QVKGIGPA 131
Cdd:cd00141    42 ESLEEAKKLPGIGKKIAEKIEEILE-TGKLRKLEELRedvppglllllRVPGVGPK 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH