ID A0A1V2YFW3_9FIRM Unreviewed; 464 AA.
AC A0A1V2YFW3;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Thioredoxin domain-containing protein {ECO:0000259|PROSITE:PS51352};
GN ORFNames=BEN18_07185 {ECO:0000313|EMBL:OOB78450.1};
OS Epulopiscium sp. Nuni2H_MBin001.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Candidatus Epulonipiscium.
OX NCBI_TaxID=1884656 {ECO:0000313|EMBL:OOB78450.1, ECO:0000313|Proteomes:UP000189057};
RN [1] {ECO:0000313|Proteomes:UP000189057}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:OOB78450.1}.
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DR EMBL; MDJM01000047; OOB78450.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V2YFW3; -.
DR STRING; 1884656.BEN18_07185; -.
DR Proteomes; UP000189057; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0016209; F:antioxidant activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0017004; P:cytochrome complex assembly; IEA:InterPro.
DR CDD; cd02966; TlpA_like_family; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR003834; Cyt_c_assmbl_TM_dom.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR31272; CYTOCHROME C-TYPE BIOGENESIS PROTEIN HI_1454-RELATED; 1.
DR PANTHER; PTHR31272:SF4; CYTOCHROME C-TYPE BIOGENESIS PROTEIN HI_1454-RELATED; 1.
DR Pfam; PF00578; AhpC-TSA; 1.
DR Pfam; PF02683; DsbD; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000189057};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 56..80
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 141..170
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 176..200
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 221..238
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 288..438
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 464 AA; 52142 MW; 63F0E8DD1667637A CRC64;
MGINIELTGL AMFAQGILSF FTPFVIPIIP LYILYLSAGA LNAAGEEDEV GTCIEYNLFS
VFINTIFFVL GINCAFIILT INFSSIGKFL LTNQAEFRRL GGLCILMLGV FQVGTFDVRA
KTLNHEDKKL SVQALRLQMN PGVALIIGFI LSFAWTPYVG SILTSIIIMI SSTRSVFTGI
VLMVMYTLGF AFPFIVIGTL TTYIFNIIDR KKDVIIPSTK LAGAIMGLMG VFMMTGLTDQ
LENHKPQTNF AVVDEVENRM YEALNVLNDV VRQFKHTIAN ARAIPREQEV KAFAKDFCLL
DQYGFTHTLE QYKGKIVFLN FLATWCDQSV YMMKEVQDLY EAYGYNANDI VVLSIVAPQT
EQNPFSKDLE LADMKKFIKN KTVTYPVMFD LSGDITRSYM LEAYPATVMI DTDGDVFGYV
PDTLTLEMMV NVIDQTVAHS EVSDLIEYLP AWMEEDNTHY GRHS
//
