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Database: UniProt
Entry: A9DPI2_9FLAO
LinkDB: A9DPI2_9FLAO
Original site: A9DPI2_9FLAO 
ID   A9DPI2_9FLAO            Unreviewed;       233 AA.
AC   A9DPI2;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   SubName: Full=YpmQ {ECO:0000313|EMBL:EDP97441.1};
GN   ORFNames=KAOT1_19802 {ECO:0000313|EMBL:EDP97441.1};
OS   Kordia algicida OT-1.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Kordia.
OX   NCBI_TaxID=391587 {ECO:0000313|EMBL:EDP97441.1, ECO:0000313|Proteomes:UP000002945};
RN   [1] {ECO:0000313|EMBL:EDP97441.1, ECO:0000313|Proteomes:UP000002945}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OT-1 {ECO:0000313|EMBL:EDP97441.1,
RC   ECO:0000313|Proteomes:UP000002945};
RX   PubMed=21622754; DOI=10.1128/JB.05241-11;
RA   Lee H.S., Kang S.G., Kwon K.K., Lee J.H., Kim S.J.;
RT   "Genome sequence of the algicidal bacterium Kordia algicida OT-1.";
RL   J. Bacteriol. 193:4031-4032(2011).
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:EDP97441.1}.
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DR   EMBL; ABIB01000002; EDP97441.1; -; Genomic_DNA.
DR   RefSeq; WP_007096491.1; NZ_DS544873.1.
DR   AlphaFoldDB; A9DPI2; -.
DR   STRING; 391587.KAOT1_19802; -.
DR   eggNOG; COG1999; Bacteria.
DR   HOGENOM; CLU_050131_2_0_10; -.
DR   OrthoDB; 9811998at2; -.
DR   Proteomes; UP000002945; 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   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   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR603782-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002945};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          57..231
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   BINDING         95
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         99
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         184
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   DISULFID        95..99
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   233 AA;  26871 MW;  9149C620ED05C9DE CRC64;
     MNKNYSYIGI AFIILVFGII FIPRIVNTVK EESIVEKDRM NIEGKERNKK LLYLKINGKA
     RSVPDFLFTN QDGLQISNDD FKGKVTVMEF FFTTCPTICP VMNSNMRTLD EEFHERDDFA
     IASFTIDPET DTPKKLKEYA ERYGVKSLNW HFLTGDLEKI HELSNTGFNI FAGINPEVAG
     GFEHQGYFAL VDKNGFIRSR RDNHGNPKIY YQGTDVKEVA MLKEDIKNLL EEE
//
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