ID A0A165B6Y9_EXIGL Unreviewed; 143 AA.
AC A0A165B6Y9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Putative GRX1-glutaredoxin {ECO:0000313|EMBL:KZV79963.1};
GN ORFNames=EXIGLDRAFT_668609 {ECO:0000313|EMBL:KZV99222.1},
GN EXIGLDRAFT_706064 {ECO:0000313|EMBL:KZV79963.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV79963.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZV79963.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZV79963.1,
RC ECO:0000313|Proteomes:UP000077266};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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DR EMBL; KV426537; KZV79963.1; -; Genomic_DNA.
DR EMBL; KV425911; KZV99222.1; -; Genomic_DNA.
DR STRING; 1314781.A0A165B6Y9; -.
DR OrthoDB; 203654at2759; -.
DR Proteomes; UP000077266; 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; IPR011767; GLR_AS.
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:SF18; GLUTAREDOXIN-1; 1.
DR Pfam; PF00462; Glutaredoxin; 1.
DR PRINTS; PR00160; GLUTAREDOXIN.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00195; GLUTAREDOXIN_1; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000077266};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 56..121
FT /note="Glutaredoxin"
FT /evidence="ECO:0000259|Pfam:PF00462"
SQ SEQUENCE 143 AA; 15897 MW; 7798EF6CD7565B4C CRC64;
MTRSITLVQC ARLVPLIRQR TLRSSSATFF TLGASSSKSE MSVRTEVEDI IAKNDIAVFA
KSWCPYCRKA RGILDSVNTE GKTVKIVDLD KMDEGSAYQE YLNKKTGQRT VPNIFIHQQH
IGGCDDLSAQ KDEGKLQALI DAK
//
