RUBY_METJA
ID RUBY_METJA Reviewed; 204 AA.
AC Q58144;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Putative rubrerythrin;
GN OrderedLocusNames=MJ0734;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
CC -!- FUNCTION: May provide oxidative stress protection via catalytic
CC reduction of intracellular hydrogen peroxide. {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034; Evidence={ECO:0000250};
CC Note=Binds 3 Fe(3+) ions per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. Possesses two rubredoxin-like centers and two non-
CC sulfur oxo-bridged di-iron centers per dimer (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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DR EMBL; L77117; AAB98729.1; -; Genomic_DNA.
DR PIR; F64391; F64391.
DR AlphaFoldDB; Q58144; -.
DR SMR; Q58144; -.
DR STRING; 243232.MJ_0734; -.
DR EnsemblBacteria; AAB98729; AAB98729; MJ_0734.
DR KEGG; mja:MJ_0734; -.
DR eggNOG; arCOG01097; Archaea.
DR HOGENOM; CLU_095256_0_0_2; -.
DR InParanoid; Q58144; -.
DR OMA; PQAYFEV; -.
DR PhylomeDB; Q58144; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd01041; Rubrerythrin; 1.
DR Gene3D; 1.20.1260.10; -; 1.
DR InterPro; IPR012347; Ferritin-like.
DR InterPro; IPR009040; Ferritin-like_diiron.
DR InterPro; IPR009078; Ferritin-like_SF.
DR InterPro; IPR024934; Rubredoxin-like_dom.
DR InterPro; IPR003251; Rubrerythrin.
DR Pfam; PF02915; Rubrerythrin; 1.
DR SUPFAM; SSF47240; SSF47240; 1.
DR PROSITE; PS50905; FERRITIN_LIKE; 1.
DR PROSITE; PS50903; RUBREDOXIN_LIKE; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Electron transport; Iron; Metal-binding; Reference proteome;
KW Transport.
FT CHAIN 1..204
FT /note="Putative rubrerythrin"
FT /id="PRO_0000135067"
FT DOMAIN 1..159
FT /note="Ferritin-like diiron"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT DOMAIN 166..204
FT /note="Rubredoxin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00241"
FT BINDING 24
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P24931"
FT BINDING 57
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P24931"
FT BINDING 57
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P24931"
FT BINDING 107
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P24931"
FT BINDING 110
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P24931"
FT BINDING 141
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P24931"
FT BINDING 141
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P24931"
FT BINDING 144
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P24931"
FT BINDING 171
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P24931"
FT BINDING 174
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P24931"
FT BINDING 187
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P24931"
FT BINDING 190
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P24931"
SQ SEQUENCE 204 AA; 23835 MW; 25B2ABFB53DB6769 CRC64;
MINNFFVINM KETLKNLTKA YIGESLARNR YTCYAKIAKQ EGYEQIAEIF LLTAENEREH
AKWLYYLITE LKKKYNIDDK AIKVDGVEVP IVLGNTAENL KASIEGEHFE HTEMYPKFAD
IAEKEGLKEI ADRLRAIGIA EKHHEERFKK LLKEVEEGTV FKKDKPVEWV CRKCGFVHLG
KEPPEKCPSC SHPRKYFEVK CEKY
