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Database: UniProt
Entry: D0MJX3_RHOM4
LinkDB: D0MJX3_RHOM4
Original site: D0MJX3_RHOM4 
ID   D0MJX3_RHOM4            Unreviewed;       187 AA.
AC   D0MJX3;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   SubName: Full=Alkyl hydroperoxide reductase/ Thiol specific antioxidant/ Mal allergen {ECO:0000313|EMBL:ACY48781.1};
GN   OrderedLocusNames=Rmar_1898 {ECO:0000313|EMBL:ACY48781.1};
OS   Rhodothermus marinus (strain ATCC 43812 / DSM 4252 / R-10) (Rhodothermus
OS   obamensis).
OC   Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Rhodothermaceae;
OC   Rhodothermus.
OX   NCBI_TaxID=518766 {ECO:0000313|EMBL:ACY48781.1, ECO:0000313|Proteomes:UP000002221};
RN   [1] {ECO:0000313|EMBL:ACY48781.1, ECO:0000313|Proteomes:UP000002221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43812 / DSM 4252 / R-10
RC   {ECO:0000313|Proteomes:UP000002221};
RX   PubMed=21304669; DOI=10.4056/sigs.46736;
RA   Nolan M., Tindall B.J., Pomrenke H., Lapidus A., Copeland A.,
RA   Glavina Del Rio T., Lucas S., Chen F., Tice H., Cheng J.F., Saunders E.,
RA   Han C., Bruce D., Goodwin L., Chain P., Pitluck S., Ovchinikova G.,
RA   Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K., Land M.,
RA   Hauser L., Chang Y.J., Jeffries C.D., Brettin T., Goker M., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA   Detter J.C.;
RT   "Complete genome sequence of Rhodothermus marinus type strain (R-10).";
RL   Stand. Genomic Sci. 1:283-291(2009).
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DR   EMBL; CP001807; ACY48781.1; -; Genomic_DNA.
DR   AlphaFoldDB; D0MJX3; -.
DR   STRING; 518766.Rmar_1898; -.
DR   KEGG; rmr:Rmar_1898; -.
DR   eggNOG; COG0526; Bacteria.
DR   HOGENOM; CLU_042529_11_4_10; -.
DR   Proteomes; UP000002221; Chromosome.
DR   GO; GO:0016209; F:antioxidant activity; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd02966; TlpA_like_family; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
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; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000002221}.
FT   DOMAIN          44..183
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   187 AA;  20455 MW;  41F8B72B816D3322 CRC64;
     MRHWINWTAP VLLTGSLLLI GCRPKAPEQA TASEQVPLSG VDEIKPPRPA PDFEAPGLDG
     APFRLSAHRG SVILLNFWAT WCLPCRTEIP DLIALQRELG DRGLLVVGVS TDEEGAEVVA
     PFVKNFKINY PVVLDDGSVS EAYGGVWALP TTVVIDRAGR IRYEIIGIFP TKEMRPRLEA
     LLDESAS
//
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