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Database: UniProt
Entry: A0A0G2EHK1_9PEZI
LinkDB: A0A0G2EHK1_9PEZI
Original site: A0A0G2EHK1_9PEZI 
ID   A0A0G2EHK1_9PEZI        Unreviewed;       311 AA.
AC   A0A0G2EHK1;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Putative glutaredoxin domain-containing protein {ECO:0000313|EMBL:KKY22322.1};
GN   ORFNames=UCDDS831_g03487 {ECO:0000313|EMBL:KKY22322.1};
OS   Diplodia seriata.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC   Diplodia.
OX   NCBI_TaxID=420778 {ECO:0000313|EMBL:KKY22322.1, ECO:0000313|Proteomes:UP000034182};
RN   [1] {ECO:0000313|EMBL:KKY22322.1, ECO:0000313|Proteomes:UP000034182}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS831 {ECO:0000313|EMBL:KKY22322.1};
RA   Morales-Cruz A., Amrine K.C., Cantu D.;
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KKY22322.1, ECO:0000313|Proteomes:UP000034182}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS831 {ECO:0000313|EMBL:KKY22322.1};
RA   Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT   "Distinctive expansion of gene families associated with plant cell wall
RT   degradation and secondary metabolism in the genomes of grapevine trunk
RT   pathogens.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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:KKY22322.1}.
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DR   EMBL; LAQI01000077; KKY22322.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G2EHK1; -.
DR   Proteomes; UP000034182; 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   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..311
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002543427"
FT   DOMAIN          192..257
FT                   /note="Glutaredoxin"
FT                   /evidence="ECO:0000259|Pfam:PF00462"
FT   REGION          66..123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        86..123
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   311 AA;  33375 MW;  5995105E98F15C76 CRC64;
     MKLFAIAVLL IVLTTLYLTS AARQTRESAF YTRTKSAISE RERTANAVAE PNLATDDDVS
     KRLKAAEDKA KKSANNKGNR IQEVVAAGDA EKEKDRVSGK TSQQNARVEK ETKAGEHDEV
     TGEKSVAGRV IMKDSSKAAD GVDGVAKVGN VGDSVKAAAS SKATSSSEAD DETQEEHEAE
     LEINAILKKS PIIIFSKSYC PFSAKAKKIL LEDYSIIPAP YVVELDQHPL GSAIQAQLKK
     STNRSTVPNV LINGRSIGGG DDIETLHLNG KIEETVRSMG GKRITEAKPA AEATAKKSGL
     KKRRVKRTLV A
//
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