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Database: UniProt
Entry: A0A0N4U4E0_DRAME
LinkDB: A0A0N4U4E0_DRAME
Original site: A0A0N4U4E0_DRAME 
ID   A0A0N4U4E0_DRAME        Unreviewed;       375 AA.
AC   A0A0N4U4E0;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   13-SEP-2023, entry version 28.
DE   RecName: Full=Elongation factor 1-gamma {ECO:0008006|Google:ProtNLM};
GN   ORFNames=DME_LOCUS6004 {ECO:0000313|EMBL:VDN56031.1};
OS   Dracunculus medinensis (Guinea worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Dracunculoidea; Dracunculidae; Dracunculus.
OX   NCBI_TaxID=318479 {ECO:0000313|Proteomes:UP000038040, ECO:0000313|WBParaSite:DME_0000164401-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:DME_0000164401-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDN56031.1, ECO:0000313|Proteomes:UP000274756}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Probably plays a role in anchoring the complex to other
CC       cellular components. {ECO:0000256|ARBA:ARBA00003468}.
CC   -!- SUBUNIT: EF-1 is composed of four subunits: alpha, beta, delta, and
CC       gamma. {ECO:0000256|ARBA:ARBA00011237}.
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DR   EMBL; UYYG01001154; VDN56031.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N4U4E0; -.
DR   STRING; 318479.A0A0N4U4E0; -.
DR   WBParaSite; DME_0000164401-mRNA-1; DME_0000164401-mRNA-1; DME_0000164401.
DR   Proteomes; UP000038040; Unplaced.
DR   Proteomes; UP000274756; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR   CDD; cd03181; GST_C_EF1Bgamma_like; 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; IPR004046; GST_C.
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   SMART; SM01183; EF1G; 1.
DR   SUPFAM; SSF89942; eEF1-gamma domain; 1.
DR   SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR   PROSITE; PS50040; EF1G_C; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
PE   4: Predicted;
KW   Elongation factor {ECO:0000256|ARBA:ARBA00022768, ECO:0000256|PROSITE-
KW   ProRule:PRU00519}; Membrane {ECO:0000256|SAM:Phobius};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|PROSITE-
KW   ProRule:PRU00519}; Reference proteome {ECO:0000313|Proteomes:UP000274756};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        209..230
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          67..200
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
FT   DOMAIN          205..375
FT                   /note="EF-1-gamma C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50040"
SQ   SEQUENCE   375 AA;  43246 MW;  79A719862F1BF0B8 CRC64;
     MTCFCRNKLY GSKDSFRVKK VLIAAKIANI DLTLTEEKPP HNKFPIGTTP AYEDGDVLLF
     GAESIALHLL GNKLGQWLQW AEGSLLPNVL GYVLPSISVV QIAPKVVEAT RNELFAQLKC
     LDEFLLTRTF LSGERLSLAD ITVALDLLCA FEHVLDGESR ANLKNVTRWF NTIVNQPKIR
     DVVGQVHFAE HVEKFNMAKF KELSAKYRFV LLSFFHLLNF IFTFFSTFVM DAFKRVYSNE
     DTATKAIPYF WENFDAENYS IWFCEYKYPE ELTLTFMSCN LISGMFQRLE KLKKNAFASM
     CLFGSDNNST ISGVWVWRGH ELAFTLSPDW QVDYESYDWK KLDPADEKTK KLVNEYLLWE
     GEFGGRKFNQ GKIFK
//
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