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Conserved domains on  [gi|16078124|ref|NP_388941|]
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putative metal-chelating cysteine-rich protein of unknown function [Bacillus subtilis subsp. subtilis str. 168]

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 ...
 6-106 6.64e-29

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: 100.07  E-value: 6.64e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078124   6 EACIEACIDCMKACNHCFTKCLEESVQHHLSGCIRLDRECADICALAVKAMQTDSPFMKEICALCADICEACGTECGKHD 85
Cdd:cd08026   2 QECIDACLACARACEECADACLEEGGVHAMAECIRLDLDCADICRLAANLMSRGSPFAKALCALCAEICEACAEECEKHA 81

                        90       100
                ....*....|....*....|.
gi 16078124  86 HDHCQACAKACFTCAEQCRSM 106
Cdd:cd08026  82 HEHCQECAEACRRCAEACRKM 102
 
Name Accession Description Interval E-value
DUF326 cd08026
Cysteine-rich 4 helical bundle widely conserved in bacteria; This functionally uncharacterized ...
 6-106 6.64e-29

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: 100.07  E-value: 6.64e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078124   6 EACIEACIDCMKACNHCFTKCLEESVQHHLSGCIRLDRECADICALAVKAMQTDSPFMKEICALCADICEACGTECGKHD 85
Cdd:cd08026   2 QECIDACLACARACEECADACLEEGGVHAMAECIRLDLDCADICRLAANLMSRGSPFAKALCALCAEICEACAEECEKHA 81

                        90       100
                ....*....|....*....|.
gi 16078124  86 HDHCQACAKACFTCAEQCRSM 106
Cdd:cd08026  82 HEHCQECAEACRRCAEACRKM 102
 
Name Accession Description Interval E-value
DUF326 cd08026
Cysteine-rich 4 helical bundle widely conserved in bacteria; This functionally uncharacterized ...
 6-106 6.64e-29

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: 100.07  E-value: 6.64e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078124   6 EACIEACIDCMKACNHCFTKCLEESVQHHLSGCIRLDRECADICALAVKAMQTDSPFMKEICALCADICEACGTECGKHD 85
Cdd:cd08026   2 QECIDACLACARACEECADACLEEGGVHAMAECIRLDLDCADICRLAANLMSRGSPFAKALCALCAEICEACAEECEKHA 81

                        90       100
                ....*....|....*....|.
gi 16078124  86 HDHCQACAKACFTCAEQCRSM 106
Cdd:cd08026  82 HEHCQECAEACRRCAEACRKM 102
 
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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