NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1267291125|ref|WP_098141135|]
View 

MULTISPECIES: cation efflux system protein CusF [Klebsiella/Raoultella group]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PRK09838 PRK09838
periplasmic copper-binding protein; Provisional
 1-116 2.81e-60

periplasmic copper-binding protein; Provisional


:

Pssm-ID: 182104  Cd Length: 115  Bit Score: 180.45  E-value: 2.81e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267291125   1 MRNSLKAILFGAFSVMFSAGLHAETHQHGDMNTASDASVQQVIKGTGVVKEIDINSKKITISHEAIPAVGWPAMTMRFTF 80
Cdd:PRK09838    1 MKKALKVAMFSLFSVIGFNAQANEHHQHGDMHEAMSAAQPQVISGTGVVKGIDLESKKITIHHEPIPAVNWPEMTMRFTI 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1267291125  81 VNAdDAINALKTGNHVDFSFIQQGNISLLKSINVTQ 116
Cdd:PRK09838   81 TPQ-TKMSEIKTGDKVAFNFVQQGNLSLLQDIKVSQ 115
 
Name Accession Description Interval E-value
PRK09838 PRK09838
periplasmic copper-binding protein; Provisional
 1-116 2.81e-60

periplasmic copper-binding protein; Provisional


Pssm-ID: 182104  Cd Length: 115  Bit Score: 180.45  E-value: 2.81e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267291125   1 MRNSLKAILFGAFSVMFSAGLHAETHQHGDMNTASDASVQQVIKGTGVVKEIDINSKKITISHEAIPAVGWPAMTMRFTF 80
Cdd:PRK09838    1 MKKALKVAMFSLFSVIGFNAQANEHHQHGDMHEAMSAAQPQVISGTGVVKGIDLESKKITIHHEPIPAVNWPEMTMRFTI 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1267291125  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 1.06e-24

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


Pssm-ID: 444311  Cd Length: 101  Bit Score: 89.66  E-value: 1.06e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1267291125  29 GDMNTASDASVQQVIKGTGVVKEIDINSKKITISHEAIPAVGWPAMTMRFTFVNADDaINALKTGNHVDFSFIQQGN 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 4.93e-20

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: 76.86  E-value: 4.93e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1267291125  47 GVVKEIDINSKKITISHEAIPAVGWPAMTMRFTFVNADDaINALKTGNHVDFSFIQQGN 105
Cdd:pfam11604   1 GVVKKVDAAAGTVTLSHGPIPALGWPAMTMDFKVADPAL-LAGLKPGDKVRFEFEKDDG 58
 
Name Accession Description Interval E-value
PRK09838 PRK09838
periplasmic copper-binding protein; Provisional
 1-116 2.81e-60

periplasmic copper-binding protein; Provisional


Pssm-ID: 182104  Cd Length: 115  Bit Score: 180.45  E-value: 2.81e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267291125   1 MRNSLKAILFGAFSVMFSAGLHAETHQHGDMNTASDASVQQVIKGTGVVKEIDINSKKITISHEAIPAVGWPAMTMRFTF 80
Cdd:PRK09838    1 MKKALKVAMFSLFSVIGFNAQANEHHQHGDMHEAMSAAQPQVISGTGVVKGIDLESKKITIHHEPIPAVNWPEMTMRFTI 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1267291125  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 1.06e-24

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


Pssm-ID: 444311  Cd Length: 101  Bit Score: 89.66  E-value: 1.06e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1267291125  29 GDMNTASDASVQQVIKGTGVVKEIDINSKKITISHEAIPAVGWPAMTMRFTFVNADDaINALKTGNHVDFSFIQQGN 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 4.93e-20

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: 76.86  E-value: 4.93e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1267291125  47 GVVKEIDINSKKITISHEAIPAVGWPAMTMRFTFVNADDaINALKTGNHVDFSFIQQGN 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH