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Database: UniProt
Entry: A0A3M8S6Y3_9PROT
LinkDB: A0A3M8S6Y3_9PROT
Original site: A0A3M8S6Y3_9PROT 
ID   A0A3M8S6Y3_9PROT        Unreviewed;       289 AA.
AC   A0A3M8S6Y3;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Thioredoxin {ECO:0000313|EMBL:RNF76719.1};
GN   Name=trxA {ECO:0000313|EMBL:RNF76719.1};
GN   ORFNames=EC580_00670 {ECO:0000313|EMBL:RNF76719.1};
OS   Acidithiobacillus sulfuriphilus.
OC   Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales;
OC   Acidithiobacillaceae; Acidithiobacillus.
OX   NCBI_TaxID=1867749 {ECO:0000313|EMBL:RNF76719.1, ECO:0000313|Proteomes:UP000271650};
RN   [1] {ECO:0000313|EMBL:RNF76719.1, ECO:0000313|Proteomes:UP000271650}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CJ-2 {ECO:0000313|EMBL:RNF76719.1,
RC   ECO:0000313|Proteomes:UP000271650};
RA   Falagan C., Moya-Beltran A., Quatrini R., Johnson D.B.;
RT   "Acidithiobacillus sulfuriphilus sp. nov.: an extremely acidophilic sulfur-
RT   oxidizing chemolithotroph isolated from a neutral pH environment.";
RL   Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the thioredoxin family.
CC       {ECO:0000256|ARBA:ARBA00008987}.
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:RNF76719.1}.
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DR   EMBL; RIZI01000062; RNF76719.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M8S6Y3; -.
DR   OrthoDB; 9790390at2; -.
DR   Proteomes; UP000271650; Unassembled WGS sequence.
DR   GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR   CDD; cd02947; TRX_family; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR   InterPro; IPR005746; Thioredoxin.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   NCBIfam; TIGR01068; thioredoxin; 1.
DR   PANTHER; PTHR45663; GEO12009P1; 1.
DR   PANTHER; PTHR45663:SF11; GEO12009P1; 1.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   Pfam; PF14559; TPR_19; 1.
DR   Pfam; PF14561; TPR_20; 1.
DR   PRINTS; PR00421; THIOREDOXIN.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW   Reference proteome {ECO:0000313|Proteomes:UP000271650};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          1..113
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   289 AA;  31883 MW;  3AC717457241CD47 CRC64;
     MATGKHVMDV HLGNFQESVI EISRQVPVVV DFWAPWCGPC RALGPVLEKL AEEYGGRFLL
     AKINSDENPE LSREYQVRGI PAVKAFRDGR VVDEFTGALP ESAVRQFIER LLPPPGDEWR
     REALLLLERG ETAQAEALLH KALEANPGND RARLELARMA VHGGRFADAE ALVTAMSPTF
     RMEPEVSGVM ALIGFAGAVK DAPDLPALAG IITASKGDER ALAMYQRAAR LVLQGDLEGA
     LEQLMDMVER HRSYQDDLAR KTVLQVFALL GNQGALVDRF RTRLSRALF
//
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