ID A0A150AGD3_9BACT Unreviewed; 224 AA.
AC A0A150AGD3;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Thioredoxin domain-containing protein {ECO:0000259|PROSITE:PS51352};
GN ORFNames=AVL50_17720 {ECO:0000313|EMBL:KXX68995.1};
OS Flammeovirga sp. SJP92.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Flammeovirgaceae;
OC Flammeovirga.
OX NCBI_TaxID=1775430 {ECO:0000313|EMBL:KXX68995.1, ECO:0000313|Proteomes:UP000075267};
RN [1] {ECO:0000313|EMBL:KXX68995.1, ECO:0000313|Proteomes:UP000075267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SJP92 {ECO:0000313|EMBL:KXX68995.1,
RC ECO:0000313|Proteomes:UP000075267};
RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL Submitted (DEC-2015) 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:KXX68995.1}.
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DR EMBL; LQAQ01000090; KXX68995.1; -; Genomic_DNA.
DR RefSeq; WP_062618173.1; NZ_LQAQ01000090.1.
DR AlphaFoldDB; A0A150AGD3; -.
DR STRING; 1775430.AVL50_17720; -.
DR OrthoDB; 9811998at2; -.
DR Proteomes; UP000075267; 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 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 Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR603782-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000075267};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 9..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 57..222
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT BINDING 95
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 99
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 185
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT DISULFID 95..99
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ SEQUENCE 224 AA; 25735 MW; 0EB6FEEEE055AB85 CRC64;
MNKPNAKKWI FLFALIGTPL FIFFFLKNFG TNEYKLESPE ELQVYNLKSV NCTPNEINGV
HRIPSFDFLN QDSVRFTNRN LEGKVYVADF FFTSCPDICK AMTSGLLRVQ ERFKNEPNVE
ILSFSIDPNY DTPKVLKDYA SKYKIDTNKW NLLTGDKQTI MDLGQCGFYI TAKEEALGQS
TSLSHSDKLI MVDTEGRIRG FYSGTDQEDV KRLLTEISIL LTEK
//
