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Conserved domains on  [gi|507073952|ref|WP_016144726|]
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MULTISPECIES: four-helix bundle copper-binding protein [Acinetobacter calcoaceticus/baumannii complex]

Protein Classification

four-helix bundle copper-binding protein( domain architecture ID 10168930)

four-helix bundle copper-binding protein similar to Methylosinus trichosporium copper storage protein 3 (Csp3) that is capable of binding large quantities of copper and preventing toxicity

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DUF326 cd08026
Cysteine-rich 4 helical bundle widely conserved in bacteria; This functionally uncharacterized ...
 19-113 2.80e-23

Cysteine-rich 4 helical bundle widely conserved in bacteria; This functionally uncharacterized protein forms a 4-helical bundle with a bromodomain-like topology. It is present in major bacterial lineages and contains highly conserved cysteines in a repeated pattern, whose sidechains appear buried. Some family members have been (mis)annotated as putative ferredoxins.


:

Pssm-ID: 153434  Cd Length: 102  Bit Score: 86.20  E-value: 2.80e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507073952  19 IQACIECMIACKTCAAACLQEEHVSMMRECIKHCMTCVETCQLCTSLELRNSELAEPAMQLCANACQLCAAECGKHDHEH 98
Cdd:cd08026    5 IDACLACARACEECADACLEEGGVHAMAECIRLDLDCADICRLAANLMSRGSPFAKALCALCAEICEACAEECEKHAHEH 84

                         90
                 ....*....|....*
gi 507073952  99 CQVCAKACLACAQAC 113
Cdd:cd08026   85 CQECAEACRRCAEAC 99
 
Name Accession Description Interval E-value
DUF326 cd08026
Cysteine-rich 4 helical bundle widely conserved in bacteria; This functionally uncharacterized ...
 19-113 2.80e-23

Cysteine-rich 4 helical bundle widely conserved in bacteria; This functionally uncharacterized protein forms a 4-helical bundle with a bromodomain-like topology. It is present in major bacterial lineages and contains highly conserved cysteines in a repeated pattern, whose sidechains appear buried. Some family members have been (mis)annotated as putative ferredoxins.


Pssm-ID: 153434  Cd Length: 102  Bit Score: 86.20  E-value: 2.80e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507073952  19 IQACIECMIACKTCAAACLQEEHVSMMRECIKHCMTCVETCQLCTSLELRNSELAEPAMQLCANACQLCAAECGKHDHEH 98
Cdd:cd08026    5 IDACLACARACEECADACLEEGGVHAMAECIRLDLDCADICRLAANLMSRGSPFAKALCALCAEICEACAEECEKHAHEH 84

                         90
                 ....*....|....*
gi 507073952  99 CQVCAKACLACAQAC 113
Cdd:cd08026   85 CQECAEACRRCAEAC 99
 
Name Accession Description Interval E-value
DUF326 cd08026
Cysteine-rich 4 helical bundle widely conserved in bacteria; This functionally uncharacterized ...
 19-113 2.80e-23

Cysteine-rich 4 helical bundle widely conserved in bacteria; This functionally uncharacterized protein forms a 4-helical bundle with a bromodomain-like topology. It is present in major bacterial lineages and contains highly conserved cysteines in a repeated pattern, whose sidechains appear buried. Some family members have been (mis)annotated as putative ferredoxins.


Pssm-ID: 153434  Cd Length: 102  Bit Score: 86.20  E-value: 2.80e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507073952  19 IQACIECMIACKTCAAACLQEEHVSMMRECIKHCMTCVETCQLCTSLELRNSELAEPAMQLCANACQLCAAECGKHDHEH 98
Cdd:cd08026    5 IDACLACARACEECADACLEEGGVHAMAECIRLDLDCADICRLAANLMSRGSPFAKALCALCAEICEACAEECEKHAHEH 84

                         90
                 ....*....|....*
gi 507073952  99 CQVCAKACLACAQAC 113
Cdd:cd08026   85 CQECAEACRRCAEAC 99
 
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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