ID K2SH52_MACPH Unreviewed; 298 AA.
AC K2SH52;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 22-FEB-2023, entry version 39.
DE RecName: Full=Thioredoxin domain-containing protein {ECO:0000259|PROSITE:PS51352};
GN ORFNames=MPH_00723 {ECO:0000313|EMBL:EKG21804.1};
OS Macrophomina phaseolina (strain MS6) (Charcoal rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Macrophomina.
OX NCBI_TaxID=1126212 {ECO:0000313|EMBL:EKG21804.1, ECO:0000313|Proteomes:UP000007129};
RN [1] {ECO:0000313|EMBL:EKG21804.1, ECO:0000313|Proteomes:UP000007129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS6 {ECO:0000313|EMBL:EKG21804.1,
RC ECO:0000313|Proteomes:UP000007129};
RX PubMed=22992219; DOI=10.1186/1471-2164-13-493;
RA Islam M.S., Haque M.S., Islam M.M., Emdad E.M., Halim A., Hossen Q.M.M.,
RA Hossain M.Z., Ahmed B., Rahim S., Rahman M.S., Alam M.M., Hou S., Wan X.,
RA Saito J.A., Alam M.;
RT "Tools to kill: Genome of one of the most destructive plant pathogenic
RT fungi Macrophomina phaseolina.";
RL BMC Genomics 13:493-493(2012).
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:EKG21804.1}.
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DR EMBL; AHHD01000035; EKG21804.1; -; Genomic_DNA.
DR AlphaFoldDB; K2SH52; -.
DR STRING; 1126212.K2SH52; -.
DR VEuPathDB; FungiDB:MPH_00723; -.
DR eggNOG; KOG0911; Eukaryota.
DR HOGENOM; CLU_026126_12_0_1; -.
DR InParanoid; K2SH52; -.
DR OrthoDB; 1038at2759; -.
DR Proteomes; UP000007129; 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 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:UP000007129}.
FT DOMAIN 1..118
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 113..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 298 AA; 31494 MW; F2CBB67C0B574158 CRC64;
MSAPTATVTE ITTEADFAQY TSSFPPNALL VVYFHAPWAA PCKQMTTVLE TLASTYTVES
PPTIGFVSIN AEELPEVSEA YDVTAVPYIV LQKGGQTVDT VSGSDASKVR AAVEKHAGKS
GNPGKLGLPP PQAVTKPAEP AGAAPNGSAQ NLSGYAPGTN DPATAPEYSS GEQETSKEEL
FARLDGLVKA APVMLFMKGT PSAPQCGFSR QTVSLLREKG IRYGFFNILA DDEVRQGLKE
YADWPTFPQL WVGGELVGGL DIVREEFENN EEFLKEYAVS TARNTGGPAS AGAQAQPA
//
