ID L9Y7N2_9EURY Unreviewed; 159 AA.
AC L9Y7N2;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Alkyl hydroperoxide reductase/ thiol specific antioxidant/ Mal allergen {ECO:0000313|EMBL:ELY70034.1};
GN ORFNames=C489_03766 {ECO:0000313|EMBL:ELY70034.1};
OS Natrinema versiforme JCM 10478.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrinema.
OX NCBI_TaxID=1227496 {ECO:0000313|EMBL:ELY70034.1, ECO:0000313|Proteomes:UP000011632};
RN [1] {ECO:0000313|EMBL:ELY70034.1, ECO:0000313|Proteomes:UP000011632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10478 {ECO:0000313|EMBL:ELY70034.1,
RC ECO:0000313|Proteomes:UP000011632};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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:ELY70034.1}.
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DR EMBL; AOID01000013; ELY70034.1; -; Genomic_DNA.
DR RefSeq; WP_006429802.1; NZ_AOID01000013.1.
DR AlphaFoldDB; L9Y7N2; -.
DR STRING; 1227496.C489_03766; -.
DR PATRIC; fig|1227496.3.peg.755; -.
DR OrthoDB; 6924at2157; -.
DR Proteomes; UP000011632; Unassembled WGS sequence.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR43110; THIOL PEROXIDASE; 1.
DR PANTHER; PTHR43110:SF1; THIOL PEROXIDASE; 1.
DR Pfam; PF00578; AhpC-TSA; 1.
DR PIRSF; PIRSF000239; AHPC; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
KW Antioxidant {ECO:0000256|ARBA:ARBA00022862};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284}.
FT DOMAIN 2..159
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 48
FT /note="Cysteine sulfenic acid (-SOH) intermediate; for
FT peroxidase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000239-1"
SQ SEQUENCE 159 AA; 17343 MW; F01C5D7431583090 CRC64;
MVTTGDAAPD FTAPLANGDI EEFTLSERLE DEAPIVLAFF PGAFTGVCTT EMCTFQDRLA
AFNDLDATVY GVSRDSPFTL NEFREQNGLE FGLISDYNKE IIDDYGIPMD FADLGVHGVA
KRSVFVIDAD GEVAYSWVSD DPGVEPDYDE VEAAVDDLS
//
