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DVU2104 iron-sulfur cluster-binding/ATPase [ Desulfovibrio vulgaris str. Hildenborough ]

Gene ID: 2795480, updated on 14-Apr-2016

Summary

Gene symbol
DVU2104
Gene description
iron-sulfur cluster-binding/ATPase
Locus tag
DVU2104
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Desulfovibrio vulgaris str. Hildenborough (strain: Hildenborough, old-name: Desulfovibrio vulgaris subsp. vulgaris str. Hildenborough)
Lineage
Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; Desulfovibrionaceae; Desulfovibrio

Genomic context

Sequence:
NC_002937.3 (2198750..2199655, complement)

NC_002937.3Genomic Context describing neighboring genes Neighboring gene hypothetical protein Neighboring gene OMP85 family outer membrane protein Neighboring gene iron-sulfur cluster-binding/ATPase Neighboring gene hypothetical protein Neighboring gene sigma-54 dependent transcriptional regulator

Bibliography

Related articles in PubMed

GeneRIFs: Gene References Into FunctionsWhat's a GeneRIF?

General protein information

Names
iron-sulfur cluster-binding/ATPase
YP_011317.1
  • identified by match to protein family HMM PF00037; match to protein family HMM PF00991

NCBI Reference Sequences (RefSeq)

Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_002937.3 Reference assembly

    Range
    2198750..2199655 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. YP_011317.1 iron-sulfur cluster-binding/ATPase [Desulfovibrio vulgaris str. Hildenborough]

    See identical proteins and their annotated locations for YP_011317.1

    Status: REVIEWED

    UniProtKB/TrEMBL
    Q72A93
    Conserved Domains (2) summary
    COG1149
    Location:1279
    COG1149; MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function prediction only]
    cd03110
    Location:2261
    Fer4_NifH_child; This protein family's function is unkown. It contains nucleotide binding site. It uses NTP as energy source to transfer electron or ion.
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