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Database: UniProt
Entry: A0A1E4UUA2_9PSED
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ID   A0A1E4UUA2_9PSED        Unreviewed;       210 AA.
AC   A0A1E4UUA2;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Cytochrome c oxidase assembly protein {ECO:0000313|EMBL:OEC33310.1};
GN   ORFNames=A7D25_19425 {ECO:0000313|EMBL:OEC33310.1};
OS   Pseudomonas sp. 21C1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1843690 {ECO:0000313|EMBL:OEC33310.1, ECO:0000313|Proteomes:UP000094259};
RN   [1] {ECO:0000313|EMBL:OEC33310.1, ECO:0000313|Proteomes:UP000094259}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=21C1 {ECO:0000313|EMBL:OEC33310.1,
RC   ECO:0000313|Proteomes:UP000094259};
RA   Souza V., Ponce-Soto G.Y.;
RT   "Genomic analysis from strains isolated from an enrichment experiment in
RT   Cuatro Cienegas.";
RL   Submitted (MAY-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:OEC33310.1}.
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DR   EMBL; LXJR01000032; OEC33310.1; -; Genomic_DNA.
DR   RefSeq; WP_069521040.1; NZ_LXJR01000032.1.
DR   AlphaFoldDB; A0A1E4UUA2; -.
DR   OrthoDB; 9790194at2; -.
DR   Proteomes; UP000094259; 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; 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:UP000094259}.
FT   DOMAIN          46..208
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   BINDING         84
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         88
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         173
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   DISULFID        84..88
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   210 AA;  23142 MW;  6A741E0D0694CDC4 CRC64;
     MSRTHLTVFI LVGLVALVLG LTVNKVLNSK GQGDPTQLLD AGIVLLPQSR TLPDLELLDQ
     DGQPVVTSQY RDKWTLMFFG YTFCPDICPA TLAQLRQLRT QLPEAARDNL RIVMVSVDPH
     RDTPEQLKKY LAYFDAGYLG LTGEETTLQK LANAVSIPYI PADTSKENYT VDHSGNLVIL
     GPDGTQRGFI RAPVNTEKLA AQLPGLLQRP
//
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