ID A0A0W1RUQ8_9GAMM Unreviewed; 457 AA.
AC A0A0W1RUQ8;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Thioredoxin domain-containing protein {ECO:0000259|PROSITE:PS51352};
GN ORFNames=AUR63_09740 {ECO:0000313|EMBL:KTG17415.1};
OS Guyparkeria sp. XI15.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Thioalkalibacteraceae; Guyparkeria.
OX NCBI_TaxID=1766620 {ECO:0000313|EMBL:KTG17415.1, ECO:0000313|Proteomes:UP000053033};
RN [1] {ECO:0000313|Proteomes:UP000053033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XI15 {ECO:0000313|Proteomes:UP000053033};
RA Zhang G., Stingl U., Rashid M.;
RT "Haloferax marisrubri sp. nov., isolated from the Discovery deep brine-
RT seawater interface in the Red Sea.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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:KTG17415.1}.
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DR EMBL; LOPX01000004; KTG17415.1; -; Genomic_DNA.
DR RefSeq; WP_058574606.1; NZ_LOPX01000004.1.
DR AlphaFoldDB; A0A0W1RUQ8; -.
DR STRING; 1766620.AUR63_09740; -.
DR Proteomes; UP000053033; Unassembled WGS sequence.
DR GO; GO:0016209; F:antioxidant activity; IEA:InterPro.
DR GO; GO:0015036; F:disulfide oxidoreductase activity; IEA:UniProt.
DR CDD; cd02966; TlpA_like_family; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR42852; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBE; 1.
DR PANTHER; PTHR42852:SF6; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBE; 1.
DR Pfam; PF00578; AhpC-TSA; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000053033};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..37
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 38..457
FT /note="Thioredoxin domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006927483"
FT DOMAIN 312..453
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 457 AA; 49660 MW; 4EC542C77727AFE4 CRC64;
MHAENEGKVG REGGSRRWWC GLLSAVGLLL ASAGATAADL SVPVGEGGDR LEVTVIEPEG
GTAADGPLLL WVANQYGDMA GPRSVAHALA RRGATVWMVD VLDSLFLTRS DTVVRERDGA
AVEALIRHAV EQAGGQREIA IIGSDRMAVP ILRGMRLWQG GVEDTSTLAG AVLLFPNLYR
GTPVAGTEPE FFGIVDATNL PVMIFQPERG VYMNRLGNLW QRLLQGGSAT FVRVVPKVKD
YYFIEMAEPH TDSLERVAEV LESPKAAPAV QALPGQILES IPLLAAAPHP ADALALDDSR
SEPLEKQTGL TRVTPQRAPD FELTDLAGRA QGLDEEFDGV QIVNFWATWC PACVEEIPSM
ERLAGRYPDR LKIYAIAFKQ SPEHLREFVR EHGFELSFPI PVDPDGEVAE RYGAFAFPTS
FLVAPDGRIH YAVNAGIIWD TPEVDAIVRE LLAIEPD
//
