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Database: UniProt
Entry: A0A0L1J9U7_ASPNO
LinkDB: A0A0L1J9U7_ASPNO
Original site: A0A0L1J9U7_ASPNO 
ID   A0A0L1J9U7_ASPNO        Unreviewed;       223 AA.
AC   A0A0L1J9U7;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Translation elongation factor eEF-1B gamma subunit {ECO:0000313|EMBL:KNG88487.1};
GN   ORFNames=ANOM_003236 {ECO:0000313|EMBL:KNG88487.1};
OS   Aspergillus nomiae NRRL 13137.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1509407 {ECO:0000313|EMBL:KNG88487.1, ECO:0000313|Proteomes:UP000037505};
RN   [1] {ECO:0000313|EMBL:KNG88487.1, ECO:0000313|Proteomes:UP000037505}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 13137 {ECO:0000313|EMBL:KNG88487.1,
RC   ECO:0000313|Proteomes:UP000037505};
RA   Moore M.G., Shannon B.M., Brian M.M.;
RT   "The Genome of the Aflatoxigenic Filamentous Fungus Aspergillus nomius.";
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the GST superfamily.
CC       {ECO:0000256|ARBA:ARBA00007409, ECO:0000256|RuleBase:RU003494}.
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:KNG88487.1}.
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DR   EMBL; JNOM01000051; KNG88487.1; -; Genomic_DNA.
DR   RefSeq; XP_015409410.1; XM_015548493.1.
DR   AlphaFoldDB; A0A0L1J9U7; -.
DR   STRING; 1509407.A0A0L1J9U7; -.
DR   GeneID; 26805040; -.
DR   OrthoDB; 159792at2759; -.
DR   Proteomes; UP000037505; Unassembled WGS sequence.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR   CDD; cd03181; GST_C_EF1Bgamma_like; 1.
DR   CDD; cd03044; GST_N_EF1Bgamma; 1.
DR   Gene3D; 1.20.1050.10; -; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR040079; Glutathione_S-Trfase.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR004046; GST_C.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR43986; ELONGATION FACTOR 1-GAMMA; 1.
DR   PANTHER; PTHR43986:SF1; ELONGATION FACTOR 1-GAMMA; 1.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SFLD; SFLDG00358; Main_(cytGST); 1.
DR   SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Elongation factor {ECO:0000313|EMBL:KNG88487.1};
KW   Protein biosynthesis {ECO:0000313|EMBL:KNG88487.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037505}.
FT   DOMAIN          3..85
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          91..222
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
FT   COILED          121..148
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   223 AA;  24473 MW;  B1CB9897AC55561A CRC64;
     MASFGKIYSY PNNPRVMKIQ AAGNLNSLNI TVDPNFQMGV TNRSPEFLAK FPMGKAPAFE
     GTDGTLLFES DAIAQYVAES GPAKDQLLGA SAVERAHIRQ WSCFGEGDGM GAVVPFALWH
     MKLAQYSAEE LEAQLAKVER VVGAVEAHLK AGDRKWLATE EKLSLADISV AAALNWAFGL
     LLDEELRAKY PAVVAWYERT IESEGVKQAF GEKKFIDKRP AFQ
//
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