ID A0A369CG49_9GAMM Unreviewed; 476 AA.
AC A0A369CG49;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Protein SCO1/2 {ECO:0000313|EMBL:RCX32218.1};
GN ORFNames=DFQ59_102578 {ECO:0000313|EMBL:RCX32218.1};
OS Thioalbus denitrificans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Thioalbus.
OX NCBI_TaxID=547122 {ECO:0000313|EMBL:RCX32218.1, ECO:0000313|Proteomes:UP000252707};
RN [1] {ECO:0000313|EMBL:RCX32218.1, ECO:0000313|Proteomes:UP000252707}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26407 {ECO:0000313|EMBL:RCX32218.1,
RC ECO:0000313|Proteomes:UP000252707};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (JUL-2018) 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:RCX32218.1}.
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DR EMBL; QPJY01000002; RCX32218.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A369CG49; -.
DR OrthoDB; 7346865at2; -.
DR Proteomes; UP000252707; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030001; P:metal ion transport; IEA:InterPro.
DR CDD; cd02968; SCO; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 3.40.50.1980; Nitrogenase molybdenum iron protein domain; 2.
DR InterPro; IPR003782; SCO1/SenC.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR006127; ZnuA-like.
DR PANTHER; PTHR12151:SF5; AT19154P; 1.
DR PANTHER; PTHR12151; ELECTRON TRANSPORT PROTIN SCO1/SENC FAMILY MEMBER; 1.
DR Pfam; PF02630; SCO1-SenC; 1.
DR Pfam; PF01297; ZnuA; 1.
DR SUPFAM; SSF53807; Helical backbone' metal receptor; 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 Metal-binding {ECO:0000256|PIRSR:PIRSR603782-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000252707};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..476
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016595298"
FT BINDING 350
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 354
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 441
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT DISULFID 350..354
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ SEQUENCE 476 AA; 52285 MW; 7C82FAF54A751D2C CRC64;
MRLLSVRLAL AGFLLLLTSG AWAAEVPKVV VSIKPIHSLV AGLMENVAEP TLLIDSGSPL
TYRPTAVQQA RIAEADLVFW VGPELEQGLA EALPGIQSRG RVLALLDNQN LKILSAPGNP
DLRDPFFWLD TRNALILLDE IAELLVEMDP GREHLYMQNR ERMRTVLSSL DWELEVSYRA
LKSGRVYLYD PTQQYFSQAY AMRSAGSLNA LPGGPADAAS LLKARATLGS GEATCLLYEA
AFPAENLGLL QTEGVQQVKL DSFGSDLEPG PMLYPDMMRG QFKAIAGCFG EETPAIGREK
GHTVLDDTVA AVPSAQLVGR YMLLDQNGAL VTNETFLGSY QLIYFGYTFC PDICPTSLQV
MAAGLSGLGK KAERIQPLFI TVDPERDTPP VMRQYVGYFH PRLVGLTGTP EMIERVAEQF
RVRYEKYLPE GAPPDRYSMD HTASLYLLDP DGVFITKFAH GITAQQLAAE LDQLIQ
//
