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Conserved domains on  [gi|798818441|ref|WP_045888224|]
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MULTISPECIES: cation efflux system protein CusF [Enterobacter]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CusF_Ec super family cl02363
Copper binding periplasmic protein CusF; CusF is a periplasmic protein involved in copper and ...
1-113 4.64e-56

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.


The actual alignment was detected with superfamily member PRK09838:

Pssm-ID: 470550  Cd Length: 115  Bit Score: 169.66  E-value: 4.64e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798818441   1 MRNSLKAVVFGAISIVFSAGLQAEVHQHEMMSAASEGTSEQLITGTGIVKDIDLTNKKVTISHEAIPEIGWPAMTMRFTF 80
Cdd:PRK09838   1 MKKALKVAMFSLFSVIGFNAQANEHHQHGDMHEAMSAAQPQVISGTGVVKGIDLESKKITIHHEPIPAVNWPEMTMRFTI 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 798818441  81 IQADeSINALKIGNHVNFSFVQQGNLSLLKSIK 113
Cdd:PRK09838  81 TPQT-KMSEIKTGDKVAFNFVQQGNLSLLQDIK 112
 
Name Accession Description Interval E-value
PRK09838 PRK09838
periplasmic copper-binding protein; Provisional
1-113 4.64e-56

periplasmic copper-binding protein; Provisional


Pssm-ID: 182104  Cd Length: 115  Bit Score: 169.66  E-value: 4.64e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798818441   1 MRNSLKAVVFGAISIVFSAGLQAEVHQHEMMSAASEGTSEQLITGTGIVKDIDLTNKKVTISHEAIPEIGWPAMTMRFTF 80
Cdd:PRK09838   1 MKKALKVAMFSLFSVIGFNAQANEHHQHGDMHEAMSAAQPQVISGTGVVKGIDLESKKITIHHEPIPAVNWPEMTMRFTI 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 798818441  81 IQADeSINALKIGNHVNFSFVQQGNLSLLKSIK 113
Cdd:PRK09838  81 TPQT-KMSEIKTGDKVAFNFVQQGNLSLLQDIK 112
CusF COG5569
Periplasmic Cu and Ag efflux protein CusF [Inorganic ion transport and metabolism];
16-108 5.60e-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: 5.60e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798818441  16 VFSAGLQAEVHQHEMMSAASEgtsEQLITGTGIVKDIDLTNKKVTISHEAIPEIGWPAMTMRFTfIQADESINALKIGNH 95
Cdd:COG5569    4 LLAAALALAASDGAAAAAAAA---AATAEAEGTVKAVDAAAGKVTIAHGPIPALGWPAMTMDFK-VADPALLKGLKVGDK 79
                         90
                 ....*....|...
gi 798818441  96 VNFSFVQQGNLSL 108
Cdd:COG5569   80 VRFEFERVGDGGY 92
CusF_Ec pfam11604
Copper binding periplasmic protein CusF; CusF is a periplasmic protein involved in copper and ...
47-105 5.64e-21

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: 79.17  E-value: 5.64e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 798818441   47 GIVKDIDLTNKKVTISHEAIPEIGWPAMTMRFTfIQADESINALKIGNHVNFSFVQQGN 105
Cdd:pfam11604   1 GVVKKVDAAAGTVTLSHGPIPALGWPAMTMDFK-VADPALLAGLKPGDKVRFEFEKDDG 58
 
Name Accession Description Interval E-value
PRK09838 PRK09838
periplasmic copper-binding protein; Provisional
1-113 4.64e-56

periplasmic copper-binding protein; Provisional


Pssm-ID: 182104  Cd Length: 115  Bit Score: 169.66  E-value: 4.64e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798818441   1 MRNSLKAVVFGAISIVFSAGLQAEVHQHEMMSAASEGTSEQLITGTGIVKDIDLTNKKVTISHEAIPEIGWPAMTMRFTF 80
Cdd:PRK09838   1 MKKALKVAMFSLFSVIGFNAQANEHHQHGDMHEAMSAAQPQVISGTGVVKGIDLESKKITIHHEPIPAVNWPEMTMRFTI 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 798818441  81 IQADeSINALKIGNHVNFSFVQQGNLSLLKSIK 113
Cdd:PRK09838  81 TPQT-KMSEIKTGDKVAFNFVQQGNLSLLQDIK 112
CusF COG5569
Periplasmic Cu and Ag efflux protein CusF [Inorganic ion transport and metabolism];
16-108 5.60e-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: 5.60e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798818441  16 VFSAGLQAEVHQHEMMSAASEgtsEQLITGTGIVKDIDLTNKKVTISHEAIPEIGWPAMTMRFTfIQADESINALKIGNH 95
Cdd:COG5569    4 LLAAALALAASDGAAAAAAAA---AATAEAEGTVKAVDAAAGKVTIAHGPIPALGWPAMTMDFK-VADPALLKGLKVGDK 79
                         90
                 ....*....|...
gi 798818441  96 VNFSFVQQGNLSL 108
Cdd:COG5569   80 VRFEFERVGDGGY 92
CusF_Ec pfam11604
Copper binding periplasmic protein CusF; CusF is a periplasmic protein involved in copper and ...
47-105 5.64e-21

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: 79.17  E-value: 5.64e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 798818441   47 GIVKDIDLTNKKVTISHEAIPEIGWPAMTMRFTfIQADESINALKIGNHVNFSFVQQGN 105
Cdd:pfam11604   1 GVVKKVDAAAGTVTLSHGPIPALGWPAMTMDFK-VADPALLAGLKPGDKVRFEFEKDDG 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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