ID A0A0W0FE35_9AGAR Unreviewed; 421 AA.
AC A0A0W0FE35;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Putative elongation factor 1-gamma {ECO:0000313|EMBL:KTB34636.1};
GN ORFNames=WG66_12800 {ECO:0000313|EMBL:KTB34636.1};
OS Moniliophthora roreri.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=221103 {ECO:0000313|EMBL:KTB34636.1, ECO:0000313|Proteomes:UP000054988};
RN [1] {ECO:0000313|EMBL:KTB34636.1, ECO:0000313|Proteomes:UP000054988}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2952 {ECO:0000313|EMBL:KTB34636.1,
RC ECO:0000313|Proteomes:UP000054988};
RA Aime M.C., Diaz-Valderrama J.R., Kijpornyongpan T., Phillips-Mora W.;
RT "Draft genome sequence of Moniliophthora roreri, the causal agent of frosty
RT pod rot of cacao.";
RL Submitted (DEC-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:KTB34636.1}.
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DR EMBL; LATX01002055; KTB34636.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W0FE35; -.
DR eggNOG; KOG0867; Eukaryota.
DR eggNOG; KOG1627; Eukaryota.
DR Proteomes; UP000054988; Unassembled WGS sequence.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
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 Gene3D; 3.30.70.1010; Translation elongation factor EF1B, gamma chain, conserved domain; 1.
DR InterPro; IPR001662; EF1B_G_C.
DR InterPro; IPR036433; EF1B_G_C_sf.
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; PF00647; EF1G; 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 SMART; SM01183; EF1G; 1.
DR SUPFAM; SSF89942; eEF1-gamma domain; 1.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS50040; EF1G_C; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 4: Predicted;
KW Elongation factor {ECO:0000256|ARBA:ARBA00022768, ECO:0000256|PROSITE-
KW ProRule:PRU00519};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|PROSITE-
KW ProRule:PRU00519}; Reference proteome {ECO:0000313|Proteomes:UP000054988}.
FT DOMAIN 2..85
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 90..216
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
FT DOMAIN 262..421
FT /note="EF-1-gamma C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50040"
FT REGION 217..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..248
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 421 AA; 46583 MW; 60FC9CCE4B6E5C4C CRC64;
MSLGTLYTTP QQATGKIIKA AAALGNFAFD APQGYVHFET NKTEAFLSKF PHGKIPAFES
KDGGFKLFEG YAIARYVASQ ASNANLLGQT PEDAALVDQW SHLADSELDP PTSLIGQLCR
GVIPYSKPVH TALLERIHRA LGTFNKHLTT NTFLVGERLT LADLVLAGLV QRGVATTIDA
EVRAKYPAVI RHLETITNQP KLKEIYGETN YTEKGIVFTP PQKEKKEAAP KPAAAPKAEK
KPKAKEDDDD DDEPAAPAEP KVKNPLDDLP KSSFNLEDWK RAYSNKDTRG ADGSIEWFYQ
NFDKDGFSLW RVDFKYNEEL TQTFMSSNQI VGFFNRLEAS RKYLFGSMGV LGKANDSIIT
GVLIARGSDI VPVVNVAPDY ESYEYKKLSL DDAADKEFLE GALAWDLKVG DKEWADGKNF
K
//
