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Conserved domains on  [gi|503147523|ref|WP_013382184|]
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MULTISPECIES: arsenic metallochaperone ArsD family protein [Eubacterium]

Protein Classification

arsenic metallochaperone ArsD family protein( domain architecture ID 10536562)

arsenic metallochaperone ArsD family protein such as the arsenical resistance operon trans-acting repressor ArsD

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ArsD pfam06953
Arsenical resistance operon protein ArsD; ArsD was initially reported to be a trans-acting ...
 3-127 1.45e-50

Arsenical resistance operon protein ArsD; ArsD was initially reported to be a trans-acting repressor of the arsRDABC operon, which confers resistance to arsenicals and antimonials in Escherichia coli. It has since been shown to be a metallochaperone that delivers As(III) to ArsA (the catalytic subunit of the ArsAB pump encoded by arsRDABC), increasing its affinity for As(III) allowing resistance to environmental concentrations of arsenic. ArsD has three conserved cysteines Cys(12), Cys(13), and Cys(18), which form a three sulfur-coordinated As(III) binding site that is essential for delivery of As(III) to, and activation of the ArsAB pump. This family also includes ArsD homologs which do not contain the conserved CCxxxxC required for function.


:

Pssm-ID: 462048  Cd Length: 120  Bit Score: 156.22  E-value: 1.45e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503147523    3 HHIEIFDPDIQCYAGECEPMGNKEYMRITTMVENLKIAGKDIIRYNPMQEPSLYKEMPEIRQLMDEKGIEALPAVMLDGK 82
Cdd:pfam06953   1 KKIEIFDPAMCCSTGVCGPSVDPELVRFAADVDWLKQQGIEVERYNLAQQPQAFAENKVVKEFLEREGAEALPLTLVDGE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 503147523   83 IVKSGEYPSNKELLDWSGLSQEELVKTIMQKkmSNCkCGNdlDCC 127
Cdd:pfam06953  81 IVKTGRYPTREELARWLGLPQEELEEPLKKK--GGC-CGG--GCC 120
 
Name Accession Description Interval E-value
ArsD pfam06953
Arsenical resistance operon protein ArsD; ArsD was initially reported to be a trans-acting ...
 3-127 1.45e-50

Arsenical resistance operon protein ArsD; ArsD was initially reported to be a trans-acting repressor of the arsRDABC operon, which confers resistance to arsenicals and antimonials in Escherichia coli. It has since been shown to be a metallochaperone that delivers As(III) to ArsA (the catalytic subunit of the ArsAB pump encoded by arsRDABC), increasing its affinity for As(III) allowing resistance to environmental concentrations of arsenic. ArsD has three conserved cysteines Cys(12), Cys(13), and Cys(18), which form a three sulfur-coordinated As(III) binding site that is essential for delivery of As(III) to, and activation of the ArsAB pump. This family also includes ArsD homologs which do not contain the conserved CCxxxxC required for function.


Pssm-ID: 462048  Cd Length: 120  Bit Score: 156.22  E-value: 1.45e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503147523    3 HHIEIFDPDIQCYAGECEPMGNKEYMRITTMVENLKIAGKDIIRYNPMQEPSLYKEMPEIRQLMDEKGIEALPAVMLDGK 82
Cdd:pfam06953   1 KKIEIFDPAMCCSTGVCGPSVDPELVRFAADVDWLKQQGIEVERYNLAQQPQAFAENKVVKEFLEREGAEALPLTLVDGE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 503147523   83 IVKSGEYPSNKELLDWSGLSQEELVKTIMQKkmSNCkCGNdlDCC 127
Cdd:pfam06953  81 IVKTGRYPTREELARWLGLPQEELEEPLKKK--GGC-CGG--GCC 120
 
Name Accession Description Interval E-value
ArsD pfam06953
Arsenical resistance operon protein ArsD; ArsD was initially reported to be a trans-acting ...
 3-127 1.45e-50

Arsenical resistance operon protein ArsD; ArsD was initially reported to be a trans-acting repressor of the arsRDABC operon, which confers resistance to arsenicals and antimonials in Escherichia coli. It has since been shown to be a metallochaperone that delivers As(III) to ArsA (the catalytic subunit of the ArsAB pump encoded by arsRDABC), increasing its affinity for As(III) allowing resistance to environmental concentrations of arsenic. ArsD has three conserved cysteines Cys(12), Cys(13), and Cys(18), which form a three sulfur-coordinated As(III) binding site that is essential for delivery of As(III) to, and activation of the ArsAB pump. This family also includes ArsD homologs which do not contain the conserved CCxxxxC required for function.


Pssm-ID: 462048  Cd Length: 120  Bit Score: 156.22  E-value: 1.45e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503147523    3 HHIEIFDPDIQCYAGECEPMGNKEYMRITTMVENLKIAGKDIIRYNPMQEPSLYKEMPEIRQLMDEKGIEALPAVMLDGK 82
Cdd:pfam06953   1 KKIEIFDPAMCCSTGVCGPSVDPELVRFAADVDWLKQQGIEVERYNLAQQPQAFAENKVVKEFLEREGAEALPLTLVDGE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 503147523   83 IVKSGEYPSNKELLDWSGLSQEELVKTIMQKkmSNCkCGNdlDCC 127
Cdd:pfam06953  81 IVKTGRYPTREELARWLGLPQEELEEPLKKK--GGC-CGG--GCC 120
Thioredoxin_3 pfam13192
Thioredoxin domain;
57-98 3.26e-03

Thioredoxin domain;


Pssm-ID: 433026 [Multi-domain]  Cd Length: 71  Bit Score: 34.11  E-value: 3.26e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 503147523   57 KEMPEIrqlmDEKGIEALPAVMLDGKIVKSGEYPSNKELLDW 98
Cdd:pfam13192  32 TDFPEI----AKYGVMSTPALVINGKVVSSGKVPSEEEIRKL 69
 
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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