ID A0A024UAW0_9STRA Unreviewed; 418 AA.
AC A0A024UAW0;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Elongation factor 1-gamma {ECO:0008006|Google:ProtNLM};
GN ORFNames=H310_04829 {ECO:0000313|EMBL:ETW03335.1};
OS Aphanomyces invadans.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Aphanomyces.
OX NCBI_TaxID=157072 {ECO:0000313|EMBL:ETW03335.1};
RN [1] {ECO:0000313|EMBL:ETW03335.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJM9701 {ECO:0000313|EMBL:ETW03335.1};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., van West P., Dieguez-Uribeondo J., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Chapman S.B.,
RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Aphanomyces invadans NJM9701.";
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KI913959; ETW03335.1; -; Genomic_DNA.
DR RefSeq; XP_008867564.1; XM_008869342.1.
DR AlphaFoldDB; A0A024UAW0; -.
DR STRING; 157072.A0A024UAW0; -.
DR EnsemblFungi; H310_04829-t26_1; H310_04829-t26_1-p1; H310_04829.
DR EnsemblProtists; ETW03335; ETW03335; H310_04829.
DR GeneID; 20081879; -.
DR VEuPathDB; FungiDB:H310_04829; -.
DR eggNOG; KOG0867; Eukaryota.
DR eggNOG; KOG1627; Eukaryota.
DR OrthoDB; 159792at2759; -.
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}.
FT DOMAIN 1..82
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 87..227
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
FT DOMAIN 257..418
FT /note="EF-1-gamma C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50040"
FT REGION 218..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 418 AA; 47240 MW; C874AA5FA0635DAB CRC64;
MSYKLFVPQG SSRAFKILIA AEYNGVNLEI PEHFQMGVDN KSAEFLKLNP LGKVPVLQTP
EGPIFESNAI ARYVARIRAD TGLLGKTFYE SGQVDQWVDF VANELEVPLN ALLYPIFGYR
KWEAELEKKA IEDTKKVLQI LENHLLLRTY FVGEQITLAD ISVFGALIYA FKFALDKDFR
KPYSNLLRWF TTVAAQPEFA AVVGDVFLAD TATLADGAPS KQAPKKAAAA PKAKKEEKPK
EADDDADFDD APKEKKVEHP LAVLNRTSPS KLKFDDWKVT YSNTKPLSKA MQWLWDNYDP
EGYSFWFCTY NYNQENTKLF MTCNAVSGFL QRSEAMRKFS FGVQSVLGAE GGLIEIVGCW
MFRGQSVEHM LEANPDAEYY TWTKVEVLDD AAKARIEEYF CSEETIDGKV IADGKVFK
//
