ID S3CZ48_GLAL2 Unreviewed; 275 AA.
AC S3CZ48;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Thioredoxin-like protein {ECO:0000313|EMBL:EPE30855.1};
GN ORFNames=GLAREA_03822 {ECO:0000313|EMBL:EPE30855.1};
OS Glarea lozoyensis (strain ATCC 20868 / MF5171).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Helotiaceae; Glarea.
OX NCBI_TaxID=1116229 {ECO:0000313|EMBL:EPE30855.1, ECO:0000313|Proteomes:UP000016922};
RN [1] {ECO:0000313|EMBL:EPE30855.1, ECO:0000313|Proteomes:UP000016922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 20868 / MF5171 {ECO:0000313|Proteomes:UP000016922};
RX PubMed=23688303; DOI=10.1186/1471-2164-14-339;
RA Chen L., Yue Q., Zhang X., Xiang M., Wang C., Li S., Che Y.,
RA Ortiz-Lopez F.J., Bills G.F., Liu X., An Z.;
RT "Genomics-driven discovery of the pneumocandin biosynthetic gene cluster in
RT the fungus Glarea lozoyensis.";
RL BMC Genomics 14:339-339(2013).
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DR EMBL; KE145363; EPE30855.1; -; Genomic_DNA.
DR RefSeq; XP_008082266.1; XM_008084075.1.
DR AlphaFoldDB; S3CZ48; -.
DR STRING; 1116229.S3CZ48; -.
DR GeneID; 19462877; -.
DR KEGG; glz:GLAREA_03822; -.
DR eggNOG; KOG0911; Eukaryota.
DR HOGENOM; CLU_026126_12_0_1; -.
DR OMA; NGPRCGF; -.
DR OrthoDB; 1038at2759; -.
DR Proteomes; UP000016922; 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.
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:UP000016922}.
FT DOMAIN 9..109
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|Pfam:PF00085"
FT DOMAIN 178..242
FT /note="Glutaredoxin"
FT /evidence="ECO:0000259|Pfam:PF00462"
FT REGION 110..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 275 AA; 29578 MW; CBA390F7D7D85AF3 CRC64;
MSTLLEIKSE EEWHKHTASL PSSTLQIISF HAPWAAPCTQ MRTVLETLAS SYPVTEPLST
SWVSMNAEEV MDVSDSFDVT AVPYLVLTRN NQVLETVSGS DATKVRAAIE KHAKSSGGSS
NGSTAAANNS GSVAKNLSSY TPTAADPATA PQYSSGEVKE DKEALHERLA TLVKAAPVML
FMKGTPSAPQ CGFSRQTVAL LRENSVKYGF FNILADDDVR QGLKEFSDWP TFPQLYVDGE
LVGGLDIVKE EMANDPDFFK AYSVPKSTPD SAAAS
//
