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Database: UniProt
Entry: M5FT84_DACPD
LinkDB: M5FT84_DACPD
Original site: M5FT84_DACPD 
ID   M5FT84_DACPD            Unreviewed;       293 AA.
AC   M5FT84;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Thioredoxin-like protein {ECO:0000313|EMBL:EJT99223.1};
GN   ORFNames=DACRYDRAFT_23831 {ECO:0000313|EMBL:EJT99223.1};
OS   Dacryopinax primogenitus (strain DJM 731) (Brown rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC   Dacrymycetales; Dacrymycetaceae; Dacryopinax.
OX   NCBI_TaxID=1858805 {ECO:0000313|EMBL:EJT99223.1, ECO:0000313|Proteomes:UP000030653};
RN   [1] {ECO:0000313|EMBL:EJT99223.1, ECO:0000313|Proteomes:UP000030653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DJM-731 SS1 {ECO:0000313|EMBL:EJT99223.1,
RC   ECO:0000313|Proteomes:UP000030653};
RX   PubMed=22745431; DOI=10.1126/science.1221748;
RA   Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA   Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA   Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA   Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA   Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA   Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA   Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA   Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA   Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA   Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA   Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA   Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA   Hibbett D.S.;
RT   "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT   31 fungal genomes.";
RL   Science 336:1715-1719(2012).
CC   -!- SIMILARITY: Belongs to the GST superfamily.
CC       {ECO:0000256|ARBA:ARBA00007409}.
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DR   EMBL; JH795870; EJT99223.1; -; Genomic_DNA.
DR   AlphaFoldDB; M5FT84; -.
DR   STRING; 1858805.M5FT84; -.
DR   HOGENOM; CLU_011226_15_0_1; -.
DR   OMA; WIHFAES; -.
DR   OrthoDB; 1925613at2759; -.
DR   Proteomes; UP000030653; Unassembled WGS sequence.
DR   CDD; cd03046; GST_N_GTT1_like; 1.
DR   Gene3D; 1.20.1050.10; -; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR040079; Glutathione_S-Trfase.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR44051:SF9; GLUTATHIONE S-TRANSFERASE 1; 1.
DR   PANTHER; PTHR44051; GLUTATHIONE S-TRANSFERASE-RELATED; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SFLD; SFLDG00358; Main_(cytGST); 1.
DR   SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000030653}.
FT   DOMAIN          73..154
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   REGION          1..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        16..36
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   293 AA;  31931 MW;  8C52305776B86F72 CRC64;
     MATEQPATDV PADAPVAAPE PAPAAPAEPA PSEPAPNESH PDEGKVVAPE IEAAAVPDVT
     PAAAEVVPVA QEGSRLVLHH LNNSRSQRIL WLLEELGVPY EIKSYHRLPS MQAPPELKAI
     HPLGKSPVMQ DGDVKLAESG AIIEYLIKKY GKGRFDPGED GWVDNLYYTH YAEGSLQPII
     VMSLIFSILP PRAPFFIRPI ARLICNNVQH LLIEPQLKEN AEMIEAHLSK SSTGWFASAP
     NPTSADFLMI FTLETLVSRG PGVGPKIKEY VARVHEREAW KRGIERGGKY TVA
//
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