ID G0S083_CHATD Unreviewed; 262 AA.
AC G0S083;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Disulfide oxidoreductase-like protein {ECO:0000313|EMBL:EGS23244.1};
GN ORFNames=CTHT_0009100 {ECO:0000313|EMBL:EGS23244.1};
OS Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
OS (Thermochaetoides thermophila).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermochaetoides.
OX NCBI_TaxID=759272 {ECO:0000313|Proteomes:UP000008066};
RN [1] {ECO:0000313|EMBL:EGS23244.1, ECO:0000313|Proteomes:UP000008066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1495 / CBS 144.50 / IMI 039719
RC {ECO:0000313|Proteomes:UP000008066};
RX PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA Arumugam M., Bork P., Hurt E.;
RT "Insight into structure and assembly of the nuclear pore complex by
RT utilizing the genome of a eukaryotic thermophile.";
RL Cell 146:277-289(2011).
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DR EMBL; GL988037; EGS23244.1; -; Genomic_DNA.
DR RefSeq; XP_006691435.1; XM_006691372.1.
DR AlphaFoldDB; G0S083; -.
DR STRING; 759272.G0S083; -.
DR GeneID; 18254948; -.
DR KEGG; cthr:CTHT_0009100; -.
DR eggNOG; KOG1752; Eukaryota.
DR HOGENOM; CLU_026126_0_0_1; -.
DR OMA; FYHKTMD; -.
DR OrthoDB; 1333222at2759; -.
DR Proteomes; UP000008066; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProt.
DR CDD; cd03419; GRX_GRXh_1_2_like; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR002109; Glutaredoxin.
DR InterPro; IPR011899; Glutaredoxin_euk/vir.
DR InterPro; IPR014025; Glutaredoxin_subgr.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR NCBIfam; TIGR02180; GRX_euk; 1.
DR PANTHER; PTHR45694; GLUTAREDOXIN 2; 1.
DR PANTHER; PTHR45694:SF30; GLUTAREDOXIN 2; 1.
DR Pfam; PF00462; Glutaredoxin; 1.
DR PRINTS; PR00160; GLUTAREDOXIN.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000008066};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..262
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003408800"
FT DOMAIN 156..221
FT /note="Glutaredoxin"
FT /evidence="ECO:0000259|Pfam:PF00462"
FT REGION 51..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..109
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 262 AA; 29125 MW; C40621AFF6BE188F CRC64;
MLSSRRLRAY MYITLAAVVL LLFFTSHARH DRDTELASIR DFYTKTRNAM DRAHDTPSAQ
QPFTHDTDAD GDIDEDDLRL EKEMAERLRQ AEKIAKDNAN AKSPHKPDAP EDVIGVGSSA
KGQDPGTKEN KPAKLDGEDE RLVEMELDSI LKKSPIIIFS KSYCPYSKRA KGILLEKYVI
EPAPYVVELD LHPLGPKIQS RLAEMTGRKT VPNIMIYGQS IGGGDEIAAL DKEKSLADKI
TSLGKDRINV SERFVGSLPN AS
//
