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Database: UniProt
Entry: A0A541B177_9NOCA
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ID   A0A541B177_9NOCA        Unreviewed;        57 AA.
AC   A0A541B177;
DT   16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2019, sequence version 1.
DT   02-APR-2025, entry version 22.
DE   RecName: Full=Rubredoxin {ECO:0000256|RuleBase:RU003820};
GN   ORFNames=FK531_19540 {ECO:0000313|EMBL:TQF66059.1};
OS   Rhodococcus spelaei.
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=2546320 {ECO:0000313|EMBL:TQF66059.1, ECO:0000313|Proteomes:UP000316256};
RN   [1] {ECO:0000313|EMBL:TQF66059.1, ECO:0000313|Proteomes:UP000316256}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C9-5 {ECO:0000313|EMBL:TQF66059.1,
RC   ECO:0000313|Proteomes:UP000316256};
RA   Lee S.D.;
RT   "Rhodococcus spaelei sp. nov., isolated from a cave.";
RL   Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the hydrocarbon hydroxylating system, which
CC       transfers electrons from NADH to rubredoxin reductase and then through
CC       rubredoxin to alkane 1 monooxygenase. {ECO:0000256|ARBA:ARBA00002792}.
CC   -!- COFACTOR:
CC       Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC         Evidence={ECO:0000256|RuleBase:RU003820};
CC   -!- SIMILARITY: Belongs to the rubredoxin family.
CC       {ECO:0000256|RuleBase:RU003820}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:TQF66059.1}.
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DR   EMBL; VIGH01000009; TQF66059.1; -; Genomic_DNA.
DR   RefSeq; WP_142102330.1; NZ_VIGH01000009.1.
DR   AlphaFoldDB; A0A541B177; -.
DR   OrthoDB; 9800607at2; -.
DR   Proteomes; UP000316256; Unassembled WGS sequence.
DR   GO; GO:0009055; F:electron transfer activity; IEA:TreeGrafter.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0043448; P:alkane catabolic process; IEA:TreeGrafter.
DR   CDD; cd00730; rubredoxin; 1.
DR   FunFam; 2.20.28.10:FF:000001; Rubredoxin; 1.
DR   Gene3D; 2.20.28.10; -; 1.
DR   InterPro; IPR024934; Rubredoxin-like_dom.
DR   InterPro; IPR024935; Rubredoxin_dom.
DR   InterPro; IPR050526; Rubredoxin_ET.
DR   InterPro; IPR018527; Rubredoxin_Fe_BS.
DR   PANTHER; PTHR47627; RUBREDOXIN; 1.
DR   PANTHER; PTHR47627:SF1; RUBREDOXIN-1-RELATED; 1.
DR   Pfam; PF00301; Rubredoxin; 1.
DR   PRINTS; PR00163; RUBREDOXIN.
DR   SUPFAM; SSF57802; Rubredoxin-like; 1.
DR   PROSITE; PS00202; RUBREDOXIN; 1.
DR   PROSITE; PS50903; RUBREDOXIN_LIKE; 1.
PE   3: Inferred from homology;
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982,
KW   ECO:0000256|RuleBase:RU003820};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU003820};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU003820};
KW   Reference proteome {ECO:0000313|Proteomes:UP000316256};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          1..52
FT                   /note="Rubredoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50903"
SQ   SEQUENCE   57 AA;  6563 MW;  6FD14DA6382EC417 CRC64;
     MKLYRCVQCG FEYDEELGWP EDGIAPGTRW DEIPDDWSCP DCGAAKADFY MEEVARP
//
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