ID U2APR3_9FLAO Unreviewed; 210 AA.
AC U2APR3;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=SCO1/SenC {ECO:0000313|EMBL:ERI62105.1};
GN ORFNames=HMPREF1551_02103 {ECO:0000313|EMBL:ERI62105.1};
OS Capnocytophaga sp. oral taxon 863 str. F0517.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Capnocytophaga.
OX NCBI_TaxID=1227266 {ECO:0000313|EMBL:ERI62105.1, ECO:0000313|Proteomes:UP000016494};
RN [1] {ECO:0000313|EMBL:ERI62105.1, ECO:0000313|Proteomes:UP000016494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0517 {ECO:0000313|EMBL:ERI62105.1,
RC ECO:0000313|Proteomes:UP000016494};
RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA Pepin K.H., Bhonagiri V., Zhang X., Warren W., Mitreva M., Mardis E.R.,
RA Wilson R.K.;
RL Submitted (JUN-2013) 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:ERI62105.1}.
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DR EMBL; AWSR01000151; ERI62105.1; -; Genomic_DNA.
DR RefSeq; WP_021628849.1; NZ_KE992168.1.
DR AlphaFoldDB; U2APR3; -.
DR STRING; 1227266.HMPREF1551_02103; -.
DR PATRIC; fig|1227266.3.peg.1870; -.
DR eggNOG; COG1999; Bacteria.
DR HOGENOM; CLU_050131_2_1_10; -.
DR OrthoDB; 9811998at2; -.
DR Proteomes; UP000016494; 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}.
FT DOMAIN 36..204
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT BINDING 74
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 78
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 161
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT DISULFID 74..78
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ SEQUENCE 210 AA; 23303 MW; 2517188F03A13382 CRC64;
MKKKLHSFLY SALALALLLG SAWGVHTLRK GKSHGLFIVG KAPAFCLTDQ HNQPFCNTDF
KGKIWVVDFF FTSCPTICPV MTANMVAVQD AFADNSIGIA SFSIDPETDT PEVLQAYAQK
KGVRSPHWHL LTGAEDQIYD IANKGFNSYA KAGDTPENFE HSGRFVLVDA QGNIVCRKEN
SKPIFFYDGM TPEGIAMLIE DIHRLKNNDQ
//
