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Database: UniProt
Entry: A0A0D0EYE3_9FLAO
LinkDB: A0A0D0EYE3_9FLAO
Original site: A0A0D0EYE3_9FLAO 
ID   A0A0D0EYE3_9FLAO        Unreviewed;       221 AA.
AC   A0A0D0EYE3;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Cytochrome C oxidase assembly protein {ECO:0000313|EMBL:KIO50677.1};
GN   ORFNames=IW18_22260 {ECO:0000313|EMBL:KIO50677.1};
OS   Flavobacterium hibernum.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=37752 {ECO:0000313|EMBL:KIO50677.1, ECO:0000313|Proteomes:UP000032061};
RN   [1] {ECO:0000313|EMBL:KIO50677.1, ECO:0000313|Proteomes:UP000032061}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12611 {ECO:0000313|EMBL:KIO50677.1,
RC   ECO:0000313|Proteomes:UP000032061};
RA   Stropko S.J., Pipes S.E., Newman J.D.;
RT   "Genome of Flavobacterium hibernum DSM 12611.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the SCO1/2 family.
CC       {ECO:0000256|ARBA:ARBA00010996}.
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:KIO50677.1}.
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DR   EMBL; JPRK01000027; KIO50677.1; -; Genomic_DNA.
DR   RefSeq; WP_041520406.1; NZ_UGGR01000004.1.
DR   AlphaFoldDB; A0A0D0EYE3; -.
DR   STRING; 37752.IW18_22260; -.
DR   OrthoDB; 9811998at2; -.
DR   Proteomes; UP000032061; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd02968; SCO; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR003782; SCO1/SenC.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR12151; ELECTRON TRANSPORT PROTIN SCO1/SENC FAMILY MEMBER; 1.
DR   PANTHER; PTHR12151:SF25; SCO1 PROTEIN HOMOLOG; 1.
DR   Pfam; PF02630; SCO1-SenC; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
PE   3: Inferred from homology;
KW   Copper {ECO:0000256|PIRSR:PIRSR603782-1};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR603782-2};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR603782-1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   BINDING         94
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         98
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         183
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   DISULFID        94..98
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   221 AA;  25603 MW;  1CAE358407BCD6F8 CRC64;
     MKSLLYKYRK FFIVLIVFSA VTISLFYSAL KPQKTLPIYN PADVNPELVD STVQYKSKYH
     TIADFSFVNQ NGDTITQKNY EGKIYVADFF FTTCGSICPK MTTNLEEVQK AVLNNPKVML
     LSHTVFPEVD SIPVLKEYAV KHHVVDSKWN LVTGDKKEIY TMARKSYLAV KLGRPDQLYD
     MVHTENFVLV DQKRRVRGFY DGTNKEEIKR LLEDINFLSQ E
//
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