ID   TRX2_MAGO7              Reviewed;         171 AA.
AC   G4NFB7;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   25-MAY-2022, entry version 48.
DE   RecName: Full=Thioredoxin-2 {ECO:0000303|PubMed:27059015};
GN   Name=TRX2 {ECO:0000303|PubMed:27059015}; ORFNames=MGG_04236;
OS   Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS   fungus) (Pyricularia oryzae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX   NCBI_TaxID=242507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX   PubMed=15846337; DOI=10.1038/nature03449;
RA   Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA   Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA   Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA   Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA   Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA   Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT   "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL   Nature 434:980-986(2005).
RN   [2]
RP   FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, INDUCTION, AND
RP   INTERACTION WITH MST7.
RX   PubMed=27059015; DOI=10.1111/1462-2920.13315;
RA   Zhang S., Jiang C., Zhang Q., Qi L., Li C., Xu J.R.;
RT   "Thioredoxins are involved in the activation of the PMK1 MAP kinase pathway
RT   during appressorium penetration and invasive growth in Magnaporthe
RT   oryzae.";
RL   Environ. Microbiol. 18:3768-3784(2016).
CC   -!- FUNCTION: Thioredoxin involved in responses to oxidative and cell wall
CC       stresses (PubMed:27059015). Plays an important role in appressorium
CC       formation on hyphal tips (PubMed:27059015). TRX2 may affect invasive
CC       growth via the MST11-MST7-PMK1 pathway since it is required for the
CC       proper folding or dimerization of MAPKK MST7 (PubMed:27059015).
CC       {ECO:0000269|PubMed:27059015}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27059015}. Vacuole
CC       {ECO:0000269|PubMed:27059015}. Note=Localizes in the cytoplasm and
CC       vacuoles in conidia, appressoria, and invasive hyphae.
CC       {ECO:0000269|PubMed:27059015}.
CC   -!- INDUCTION: Expression is induced in the absence of TRX1.
CC       {ECO:0000269|PubMed:27059015}.
CC   -!- DISRUPTION PHENOTYPE: Leads to reduced growth rate and reduced
CC       conidiation and impairs appressorium formation (PubMed:27059015). Leads
CC       also to defects in response to light/ dark transitions
CC       (PubMed:27059015). {ECO:0000269|PubMed:27059015}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CM001236; EHA47211.1; -; Genomic_DNA.
DR   RefSeq; XP_003719578.1; XM_003719530.1.
DR   AlphaFoldDB; G4NFB7; -.
DR   SMR; G4NFB7; -.
DR   STRING; 318829.MGG_04236T0; -.
DR   EnsemblFungi; MGG_04236T0; MGG_04236T0; MGG_04236.
DR   GeneID; 2677571; -.
DR   KEGG; mgr:MGG_04236; -.
DR   VEuPathDB; FungiDB:MGG_04236; -.
DR   eggNOG; KOG0907; Eukaryota.
DR   HOGENOM; CLU_090389_14_5_1; -.
DR   InParanoid; G4NFB7; -.
DR   OMA; GDECAPE; -.
DR   OrthoDB; 1482186at2759; -.
DR   Proteomes; UP000009058; Chromosome 6.
DR   GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR   GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR   InterPro; IPR005746; Thioredoxin.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   TIGRFAMs; TIGR01068; thioredoxin; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Disulfide bond; Reference proteome; Vacuole.
FT   CHAIN           1..171
FT                   /note="Thioredoxin-2"
FT                   /id="PRO_0000453106"
FT   DOMAIN          41..169
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        95..98
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   171 AA;  18751 MW;  85524A85F3BB7F32 CRC64;
     MSCISRSRAL FQIRSLASSS HLPLPKLRPS PAIYKSANKT AFNASPSTSQ SATTTRGFRS
     TAAKMTVHNL TNAQDFKDAL KSHKFVLVDF FATWCGPCRA IAPKIAEWSD AFPNIHYVKV
     DVDEVPDVAQ EYNVRAMPTF LLFKDGEKVD EVVGANPPKL QALISANHPS S