GenomeNet

Database: UniProt
Entry: A0A0P7BR19_9BACT
LinkDB: A0A0P7BR19_9BACT
Original site: A0A0P7BR19_9BACT 
ID   A0A0P7BR19_9BACT        Unreviewed;       229 AA.
AC   A0A0P7BR19;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Electron transporter SenC {ECO:0000313|EMBL:KPM46627.1};
GN   ORFNames=AFM12_19010 {ECO:0000313|EMBL:KPM46627.1};
OS   Jiulongibacter sediminis.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC   Jiulongibacter.
OX   NCBI_TaxID=1605367 {ECO:0000313|EMBL:KPM46627.1, ECO:0000313|Proteomes:UP000050454};
RN   [1] {ECO:0000313|EMBL:KPM46627.1, ECO:0000313|Proteomes:UP000050454}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JN14-9 {ECO:0000313|EMBL:KPM46627.1,
RC   ECO:0000313|Proteomes:UP000050454};
RA   Liu Y., Du J., Shao Z.;
RT   "The draft genome sequence of Leadbetterella sp. JN14-9.";
RL   Submitted (JUL-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:KPM46627.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LGTQ01000016; KPM46627.1; -; Genomic_DNA.
DR   RefSeq; WP_055151922.1; NZ_LGTQ01000016.1.
DR   AlphaFoldDB; A0A0P7BR19; -.
DR   STRING; 1605367.AFM12_19010; -.
DR   PATRIC; fig|1605367.3.peg.1244; -.
DR   OrthoDB; 9811998at2; -.
DR   Proteomes; UP000050454; 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:UP000050454}.
FT   DOMAIN          54..224
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   BINDING         91
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         95
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         187
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   DISULFID        91..95
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   229 AA;  26024 MW;  35DA7064CE5763C0 CRC64;
     MSKRLLKAGI LIAVLVLPAF VFIFLNVFGE NRFDLPYYFP ELNESGRPQV VSGDTVYHKV
     PDFTLINQNN QEIALKDLSD IKIANFFFTR CGTICPVMNS NIARVQNQFD HTGQVSFISI
     SIDPEHDSVM VLKDYAATFD ALESNWNFLT GKKDYIYGLA IKGFKLPVSD ASVYDPEITN
     IDDAFIHSEK ALLLDKDNYI RGIYDSTSKP DMERLNVEIK VLLDSYEKQ
//
DBGET integrated database retrieval system