ID I4YJ01_WALMC Unreviewed; 230 AA.
AC I4YJ01;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Putative thioredoxin {ECO:0000313|EMBL:EIM23943.1};
GN ORFNames=WALSEDRAFT_30747 {ECO:0000313|EMBL:EIM23943.1};
OS Wallemia mellicola (strain ATCC MYA-4683 / CBS 633.66) (Wallemia sebi (CBS
OS 633.66)).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Wallemiomycotina;
OC Wallemiomycetes; Wallemiales; Wallemiaceae; Wallemia.
OX NCBI_TaxID=671144 {ECO:0000313|EMBL:EIM23943.1, ECO:0000313|Proteomes:UP000005242};
RN [1] {ECO:0000313|EMBL:EIM23943.1, ECO:0000313|Proteomes:UP000005242}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4683 / CBS 633.66 {ECO:0000313|Proteomes:UP000005242};
RX PubMed=22326418; DOI=10.1016/j.fgb.2012.01.007;
RA Padamsee M., Kumar T.K.A., Riley R., Binder M., Boyd A., Calvo A.M.,
RA Furukawa K., Hesse C., Hohmann S., James T.Y., LaButti K., Lapidus A.,
RA Lindquist E., Lucas S., Miller K., Shantappa S., Grigoriev I.V.,
RA Hibbett D.S., McLaughlin D.J., Spatafora J.W., Aime M.C.;
RT "The genome of the xerotolerant mold Wallemia sebi reveals adaptations to
RT osmotic stress and suggests cryptic sexual reproduction.";
RL Fungal Genet. Biol. 49:217-226(2012).
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DR EMBL; JH668223; EIM23943.1; -; Genomic_DNA.
DR RefSeq; XP_006955782.1; XM_006955720.1.
DR AlphaFoldDB; I4YJ01; -.
DR STRING; 671144.I4YJ01; -.
DR GeneID; 18471170; -.
DR KEGG; wse:WALSEDRAFT_30747; -.
DR eggNOG; KOG0911; Eukaryota.
DR HOGENOM; CLU_026126_12_0_1; -.
DR InParanoid; I4YJ01; -.
DR OMA; CEPCTAV; -.
DR OrthoDB; 1038at2759; -.
DR Proteomes; UP000005242; Unassembled WGS sequence.
DR GO; GO:0015036; F:disulfide oxidoreductase activity; IEA:UniProt.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd03028; GRX_PICOT_like; 1.
DR CDD; cd02984; TRX_PICOT; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 2.
DR InterPro; IPR002109; Glutaredoxin.
DR InterPro; IPR033658; GRX_PICOT-like.
DR InterPro; IPR004480; Monothiol_GRX-rel.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR NCBIfam; TIGR00365; Grx4 family monothiol glutaredoxin; 1.
DR PANTHER; PTHR10293; GLUTAREDOXIN FAMILY MEMBER; 1.
DR PANTHER; PTHR10293:SF73; GLUTAREDOXIN-3; 1.
DR Pfam; PF00462; Glutaredoxin; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 2.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000005242}.
FT DOMAIN 1..111
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 230 AA; 25818 MW; B7F344B8DF6C7229 CRC64;
MLKEVQSPEE FQDILSNNLN SLSVLNFWAP WAEPCQQMNQ VTKELAEKYT NVVFLQIEAE
SLPDISETFD IEAVPSFILL RGHTLLERIS GANAALLAQS VSKHALNSAQ KSAQSSTILP
PQAPAAVETE EELNSRCLNI MKQSDVVLFM KGDPDAPRCG FSKQTVALLR EQSIEFSHFD
ILQDESVRQH LKKLNDWPTF PQIIVKGELI GGLDILREMI EQGELQQLME
//
