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Conserved domains on  [gi|447168896|ref|WP_001246152|]
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MULTISPECIES: Cu(+)/Ag(+) efflux RND transporter periplasmic metallochaperone SilF [Enterobacterales]

Protein Classification

efflux RND transporter periplasmic adaptor subunit( domain architecture ID 10013354)

efflux RND (resistance-nodulation-division) transporter periplasmic adaptor subunit, similar to Escherichia coli cation efflux system protein CusB, which is part of a cation efflux system that mediates resistance to copper and silver; contains a copper binding periplasmic protein CusF domain

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK09838 PRK09838
periplasmic copper-binding protein; Provisional
 1-116 8.60e-62

periplasmic copper-binding protein; Provisional


:

Pssm-ID: 182104  Cd Length: 115  Bit Score: 184.30  E-value: 8.60e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447168896   1 MRNSLKAVLFGAFSVMFSAGLHAETHQHGDMNAASDASVQQVIKGTGIVKDIDMNSKKITISHEAIPAVGWPAMTMRFTF 80
Cdd:PRK09838   1 MKKALKVAMFSLFSVIGFNAQANEHHQHGDMHEAMSAAQPQVISGTGVVKGIDLESKKITIHHEPIPAVNWPEMTMRFTI 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 447168896  81 VNAdDAINALKTGNHVDFSFIQQGNISLLKSINVTQ 116
Cdd:PRK09838  81 TPQ-TKMSEIKTGDKVAFNFVQQGNLSLLQDIKVSQ 115
 
Name Accession Description Interval E-value
PRK09838 PRK09838
periplasmic copper-binding protein; Provisional
 1-116 8.60e-62

periplasmic copper-binding protein; Provisional


Pssm-ID: 182104  Cd Length: 115  Bit Score: 184.30  E-value: 8.60e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447168896   1 MRNSLKAVLFGAFSVMFSAGLHAETHQHGDMNAASDASVQQVIKGTGIVKDIDMNSKKITISHEAIPAVGWPAMTMRFTF 80
Cdd:PRK09838   1 MKKALKVAMFSLFSVIGFNAQANEHHQHGDMHEAMSAAQPQVISGTGVVKGIDLESKKITIHHEPIPAVNWPEMTMRFTI 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 447168896  81 VNAdDAINALKTGNHVDFSFIQQGNISLLKSINVTQ 116
Cdd:PRK09838  81 TPQ-TKMSEIKTGDKVAFNFVQQGNLSLLQDIKVSQ 115
CusF COG5569
Periplasmic Cu and Ag efflux protein CusF [Inorganic ion transport and metabolism];
29-105 5.92e-24

Periplasmic Cu and Ag efflux protein CusF [Inorganic ion transport and metabolism];


Pssm-ID: 444311  Cd Length: 101  Bit Score: 87.74  E-value: 5.92e-24
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447168896  29 GDMNAASDASVQQVIKGTGIVKDIDMNSKKITISHEAIPAVGWPAMTMRFTFVNADDaINALKTGNHVDFSFIQQGN 105
Cdd:COG5569   14 SDGAAAAAAAAAATAEAEGTVKAVDAAAGKVTIAHGPIPALGWPAMTMDFKVADPAL-LKGLKVGDKVRFEFERVGD 89
CusF_Ec pfam11604
Copper binding periplasmic protein CusF; CusF is a periplasmic protein involved in copper and ...
 47-105 1.47e-19

Copper binding periplasmic protein CusF; CusF is a periplasmic protein involved in copper and silver resistance in Escherichia coil. CusF forms a five-stranded beta-barrel OB fold. Cu(I) binds to H36, M47 and M49 which are conserved residues in the protein.


Pssm-ID: 463306  Cd Length: 68  Bit Score: 75.70  E-value: 1.47e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 447168896   47 GIVKDIDMNSKKITISHEAIPAVGWPAMTMRFTFVNADDaINALKTGNHVDFSFIQQGN 105
Cdd:pfam11604   1 GVVKKVDAAAGTVTLSHGPIPALGWPAMTMDFKVADPAL-LAGLKPGDKVRFEFEKDDG 58
 
Name Accession Description Interval E-value
PRK09838 PRK09838
periplasmic copper-binding protein; Provisional
 1-116 8.60e-62

periplasmic copper-binding protein; Provisional


Pssm-ID: 182104  Cd Length: 115  Bit Score: 184.30  E-value: 8.60e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447168896   1 MRNSLKAVLFGAFSVMFSAGLHAETHQHGDMNAASDASVQQVIKGTGIVKDIDMNSKKITISHEAIPAVGWPAMTMRFTF 80
Cdd:PRK09838   1 MKKALKVAMFSLFSVIGFNAQANEHHQHGDMHEAMSAAQPQVISGTGVVKGIDLESKKITIHHEPIPAVNWPEMTMRFTI 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 447168896  81 VNAdDAINALKTGNHVDFSFIQQGNISLLKSINVTQ 116
Cdd:PRK09838  81 TPQ-TKMSEIKTGDKVAFNFVQQGNLSLLQDIKVSQ 115
CusF COG5569
Periplasmic Cu and Ag efflux protein CusF [Inorganic ion transport and metabolism];
29-105 5.92e-24

Periplasmic Cu and Ag efflux protein CusF [Inorganic ion transport and metabolism];


Pssm-ID: 444311  Cd Length: 101  Bit Score: 87.74  E-value: 5.92e-24
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447168896  29 GDMNAASDASVQQVIKGTGIVKDIDMNSKKITISHEAIPAVGWPAMTMRFTFVNADDaINALKTGNHVDFSFIQQGN 105
Cdd:COG5569   14 SDGAAAAAAAAAATAEAEGTVKAVDAAAGKVTIAHGPIPALGWPAMTMDFKVADPAL-LKGLKVGDKVRFEFERVGD 89
CusF_Ec pfam11604
Copper binding periplasmic protein CusF; CusF is a periplasmic protein involved in copper and ...
 47-105 1.47e-19

Copper binding periplasmic protein CusF; CusF is a periplasmic protein involved in copper and silver resistance in Escherichia coil. CusF forms a five-stranded beta-barrel OB fold. Cu(I) binds to H36, M47 and M49 which are conserved residues in the protein.


Pssm-ID: 463306  Cd Length: 68  Bit Score: 75.70  E-value: 1.47e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 447168896   47 GIVKDIDMNSKKITISHEAIPAVGWPAMTMRFTFVNADDaINALKTGNHVDFSFIQQGN 105
Cdd:pfam11604   1 GVVKKVDAAAGTVTLSHGPIPALGWPAMTMDFKVADPAL-LAGLKPGDKVRFEFEKDDG 58
 
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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