ID A0A099FAC9_9RHOB Unreviewed; 209 AA.
AC A0A099FAC9;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Electron transport protein SCO1/SenC {ECO:0000313|EMBL:KGJ07161.1};
GN ORFNames=IC63_09420 {ECO:0000313|EMBL:KGJ07161.1};
OS Paracoccus sphaerophysae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=690417 {ECO:0000313|EMBL:KGJ07161.1, ECO:0000313|Proteomes:UP000029917};
RN [1] {ECO:0000313|EMBL:KGJ07161.1, ECO:0000313|Proteomes:UP000029917}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HAMBI 3106 {ECO:0000313|EMBL:KGJ07161.1,
RC ECO:0000313|Proteomes:UP000029917};
RA McGinnis J.M., Wolfgang W.J.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KGJ07161.1, ECO:0000313|Proteomes:UP000029917}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HAMBI 3106 {ECO:0000313|EMBL:KGJ07161.1,
RC ECO:0000313|Proteomes:UP000029917};
RA Mingle L.A., Cole J.A., Lapierre P., Musser K.A.;
RT "Paracoccus sanguinis sp. nov., isolated from clinical specimens of New
RT York State patients.";
RL Submitted (OCT-2014) 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:KGJ07161.1}.
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DR EMBL; JRKS01000025; KGJ07161.1; -; Genomic_DNA.
DR RefSeq; WP_036700237.1; NZ_JRKS01000025.1.
DR AlphaFoldDB; A0A099FAC9; -.
DR STRING; 690417.IC63_09420; -.
DR OrthoDB; 9790194at2; -.
DR Proteomes; UP000029917; 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; IPR006311; TAT_signal.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR12151:SF5; AT19154P; 1.
DR PANTHER; PTHR12151; ELECTRON TRANSPORT PROTIN SCO1/SENC FAMILY MEMBER; 1.
DR Pfam; PF02630; SCO1-SenC; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51318; TAT; 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:UP000029917}.
FT DOMAIN 44..209
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT BINDING 82
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 86
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 170
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT DISULFID 82..86
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ SEQUENCE 209 AA; 22922 MW; E704E16E7E990D55 CRC64;
MSLSRRLLLG AGAVTALGAG ALGLGWWQVD GPGAAQPASP TRNLPRPLGE MDVTLTDHRG
RRVTISDWVG RPSLVFFGFT WCPDVCPTTL SDISLWLEEL GPDADRLNVA LISVDPERDT
PEVLADYLGY FDPRIVGVTG EPGEVARILG DFRAKAERIE DVNGDYTMNH TAGVFLFRAD
GSFGSIIDFH EDRRFAVPKI RRAMKKEQP
//
