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}.
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; 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
//