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Database: UniProt
Entry: A0LR60_ACIC1
LinkDB: A0LR60_ACIC1
Original site: A0LR60_ACIC1 
ID   A0LR60_ACIC1            Unreviewed;       381 AA.
AC   A0LR60;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   27-MAR-2024, entry version 97.
DE   SubName: Full=Rieske (2Fe-2S) domain protein {ECO:0000313|EMBL:ABK51920.1};
GN   OrderedLocusNames=Acel_0145 {ECO:0000313|EMBL:ABK51920.1};
OS   Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B).
OC   Bacteria; Actinomycetota; Actinomycetes; Acidothermales; Acidothermaceae;
OC   Acidothermus.
OX   NCBI_TaxID=351607 {ECO:0000313|EMBL:ABK51920.1, ECO:0000313|Proteomes:UP000008221};
RN   [1] {ECO:0000313|EMBL:ABK51920.1, ECO:0000313|Proteomes:UP000008221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43068 / DSM 8971 / 11B
RC   {ECO:0000313|Proteomes:UP000008221};
RX   PubMed=19270083; DOI=10.1101/gr.084848.108;
RA   Barabote R.D., Xie G., Leu D.H., Normand P., Necsulea A., Daubin V.,
RA   Medigue C., Adney W.S., Xu X.C., Lapidus A., Parales R.E., Detter C.,
RA   Pujic P., Bruce D., Lavire C., Challacombe J.F., Brettin T.S., Berry A.M.;
RT   "Complete genome of the cellulolytic thermophile Acidothermus
RT   cellulolyticus 11B provides insights into its ecophysiological and
RT   evolutionary adaptations.";
RL   Genome Res. 19:1033-1043(2009).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; CP000481; ABK51920.1; -; Genomic_DNA.
DR   RefSeq; WP_011718984.1; NC_008578.1.
DR   AlphaFoldDB; A0LR60; -.
DR   STRING; 351607.Acel_0145; -.
DR   KEGG; ace:Acel_0145; -.
DR   eggNOG; COG2146; Bacteria.
DR   eggNOG; COG2259; Bacteria.
DR   HOGENOM; CLU_818310_0_0_11; -.
DR   InParanoid; A0LR60; -.
DR   OrthoDB; 25106at2; -.
DR   Proteomes; UP000008221; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProt.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR   CDD; cd03467; Rieske; 1.
DR   Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 1.
DR   InterPro; IPR032808; DoxX.
DR   InterPro; IPR017941; Rieske_2Fe-2S.
DR   InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR   InterPro; IPR005805; Rieske_Fe-S_prot_C.
DR   PANTHER; PTHR39157; INTEGRAL MEMBRANE PROTEIN-RELATED; 1.
DR   PANTHER; PTHR39157:SF1; INTEGRAL MEMBRANE PROTEIN-RELATED; 1.
DR   Pfam; PF07681; DoxX; 1.
DR   Pfam; PF00355; Rieske; 1.
DR   PRINTS; PR00162; RIESKE.
DR   SUPFAM; SSF50022; ISP domain; 1.
DR   PROSITE; PS51296; RIESKE; 1.
PE   4: Predicted;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008221};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        28..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        89..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        115..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        145..167
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        196..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          284..379
FT                   /note="Rieske"
FT                   /evidence="ECO:0000259|PROSITE:PS51296"
FT   REGION          229..284
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   381 AA;  38382 MW;  416A3F64EC7841FC CRC64;
     MGSKPDARIE RRSLRVPLSV SDSRPERAAY ALLPLRAFLG FTFCYAGLQK LANPAFFNAR
     SPISIQAQFL GAVRRSPIHA LLQPLSSHAW AIGVLMALGE LAVGLGTLAG LFTRIAALGG
     AVISFSLFLT VSFHSNPWYT GSDIVFFFAW LPLLVAGGGP FSLDAWVDRA VQRRASSRAR
     ADVPPDEMRR RLVGSLAVLL GAFGMALAGL TAGIGRLLYT PATSGATSAL PGGGSPGLAR
     PSPSGGTAAG GTPSGGAASG NPSPAGGPSA GASSPGASSG GVRIGPASAV PIGGAASFQD
     PATGDPAIVV RPSAGVFHAF DAVCPHAGCT VGYDPSSAVL VCPCHGSRFN ATSGAVLNGP
     APTGLTPIKI REGSDGQLYV D
//
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