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Database: UniProt
Entry: A0A239DI15_9BACT
LinkDB: A0A239DI15_9BACT
Original site: A0A239DI15_9BACT 
ID   A0A239DI15_9BACT        Unreviewed;       310 AA.
AC   A0A239DI15;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Protein SCO1/2 {ECO:0000313|EMBL:SNS32145.1};
GN   ORFNames=SAMN05421770_101488 {ECO:0000313|EMBL:SNS32145.1};
OS   Granulicella rosea.
OC   Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC   Granulicella.
OX   NCBI_TaxID=474952 {ECO:0000313|EMBL:SNS32145.1, ECO:0000313|Proteomes:UP000198356};
RN   [1] {ECO:0000313|EMBL:SNS32145.1, ECO:0000313|Proteomes:UP000198356}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18704 {ECO:0000313|EMBL:SNS32145.1,
RC   ECO:0000313|Proteomes:UP000198356};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the SCO1/2 family.
CC       {ECO:0000256|ARBA:ARBA00010996}.
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DR   EMBL; FZOU01000001; SNS32145.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A239DI15; -.
DR   OrthoDB; 9786756at2; -.
DR   Proteomes; UP000198356; 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:SF8; THIOREDOXIN DOMAIN-CONTAINING PROTEIN; 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   Reference proteome {ECO:0000313|Proteomes:UP000198356};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..310
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012647305"
FT   TRANSMEM        262..282
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   BINDING         97
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         101
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         195
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   DISULFID        97..101
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   310 AA;  33570 MW;  E2A87554B45AACED CRC64;
     MNLLQTIRRS RKIAVMACAI LLAGTLSAQV SSYGEKQAGE NTGDQLPQVL QKVAVNQHLN
     QSLPLNAEFV DETGKTVHLG DYFGKRPAVI SLVYYTCPLL CSEELDGLTG ALEMVKLTPG
     KDFDVIIISI DPADTPALAA KKKAFYLKRY GRPETADGWH FLTGKTPAID ATTSAVGFGY
     VKVPGPDGTM SQFAHASSIE IATTEGKLSQ YYLGVEYSPK DVLLGLIEGS GNKIGSPVAN
     ILTYCYHYDP QTNKHSLIVA RVVQFGGMVT MAGLGGFMFL MFRRDLKLGR DHNLTGDLTS
     PDLTKRTDKG
//
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