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
//