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Database: UniProt
Entry: A0A1R1BW79_9BACL
LinkDB: A0A1R1BW79_9BACL
Original site: A0A1R1BW79_9BACL 
ID   A0A1R1BW79_9BACL        Unreviewed;       191 AA.
AC   A0A1R1BW79;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Cytochrome c oxidase assembly protein {ECO:0000313|EMBL:OMF14122.1};
GN   ORFNames=BK127_19530 {ECO:0000313|EMBL:OMF14122.1};
OS   Paenibacillus sp. FSL H7-0331.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1920421 {ECO:0000313|EMBL:OMF14122.1, ECO:0000313|Proteomes:UP000187480};
RN   [1] {ECO:0000313|EMBL:OMF14122.1, ECO:0000313|Proteomes:UP000187480}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL H7-0331 {ECO:0000313|EMBL:OMF14122.1,
RC   ECO:0000313|Proteomes:UP000187480};
RA   Beno S.M.;
RT   "Paenibacillus species isolates.";
RL   Submitted (NOV-2016) 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:OMF14122.1}.
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DR   EMBL; MRTH01000012; OMF14122.1; -; Genomic_DNA.
DR   RefSeq; WP_076233167.1; NZ_MRTH01000012.1.
DR   AlphaFoldDB; A0A1R1BW79; -.
DR   STRING; 1920421.BK127_19530; -.
DR   OrthoDB; 9811998at2; -.
DR   Proteomes; UP000187480; Unassembled WGS sequence.
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   InterPro; IPR013766; Thioredoxin_domain.
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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Copper {ECO:0000256|ARBA:ARBA00023008, ECO:0000256|PIRSR:PIRSR603782-1};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR603782-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR603782-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000187480}.
FT   DOMAIN          26..191
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   BINDING         64
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         68
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         154
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   DISULFID        64..68
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   191 AA;  21361 MW;  5D75668D84539F6E CRC64;
     MKKVILVGWL GLILIFTAAC GNGKPNQLHY QVAPFNFINQ DEKPVALSDL KGKVWIADFV
     FTYCTTVCPT MTANMSKLQK QLKAAGVEAQ IVSFSVDPER DKPEALKKYL SKFDADFSNW
     HALTGYEFDE IQTFALKSFK SIVTRDASSN QVIHGTLFYL VDSSGTVVAK YDGSMDTPYD
     KIIKDIKALQ R
//
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