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Database: UniProt
Entry: A0A182EL43_ONCOC
LinkDB: A0A182EL43_ONCOC
Original site: A0A182EL43_ONCOC 
ID   A0A182EL43_ONCOC        Unreviewed;       397 AA.
AC   A0A182EL43;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Elongation factor 1-alpha {ECO:0000256|RuleBase:RU000325};
GN   ORFNames=NOO_LOCUS8832 {ECO:0000313|EMBL:VDM91788.1};
OS   Onchocerca ochengi (Filarial nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Onchocerca.
OX   NCBI_TaxID=42157 {ECO:0000313|Proteomes:UP000077448, ECO:0000313|WBParaSite:nOo.2.0.1.t08832-RA};
RN   [1] {ECO:0000313|Proteomes:UP000077448, ECO:0000313|WBParaSite:nOo.2.0.1.t08832-RA}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22919073; DOI=10.1101/gr.138420.112;
RA   Darby A.C., Armstrong S.D., Bah G.S., Kaur G., Hughes M.A., Kay S.M.,
RA   Koldkaer P., Rainbow L., Radford A.D., Blaxter M.L., Tanya V.N.,
RA   Trees A.J., Cordaux R., Wastling J.M., Makepeace B.L.;
RT   "Analysis of gene expression from the Wolbachia genome of a filarial
RT   nematode supports both metabolic and defensive roles within the
RT   symbiosis.";
RL   Genome Res. 22:2467-2477(2012).
RN   [2] {ECO:0000313|WBParaSite:nOo.2.0.1.t08832-RA}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
RN   [3] {ECO:0000313|EMBL:VDM91788.1, ECO:0000313|Proteomes:UP000271087}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Laetsch R D., Stevens L., Kumar S., Blaxter L. M.;
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC       tRNA to the A-site of ribosomes during protein biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00003982, ECO:0000256|RuleBase:RU000325}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC       subfamily. {ECO:0000256|ARBA:ARBA00007249,
CC       ECO:0000256|RuleBase:RU000325}.
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DR   EMBL; UYRW01003914; VDM91788.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A182EL43; -.
DR   STRING; 42157.A0A182EL43; -.
DR   WBParaSite; nOo.2.0.1.t08832-RA; nOo.2.0.1.t08832-RA; nOo.2.0.1.g08832.
DR   Proteomes; UP000077448; Unassembled WGS sequence.
DR   Proteomes; UP000271087; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR   CDD; cd01883; EF1_alpha; 1.
DR   CDD; cd03693; EF1_alpha_II; 1.
DR   CDD; cd03705; EF1_alpha_III; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 2.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR031157; G_TR_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR   InterPro; IPR004539; Transl_elong_EF1A_euk/arc.
DR   InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR   NCBIfam; TIGR00483; EF-1_alpha; 1.
DR   PANTHER; PTHR23115:SF170; ELONGATION FACTOR 1-ALPHA 2; 1.
DR   PANTHER; PTHR23115; TRANSLATION FACTOR; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   Pfam; PF03143; GTP_EFTU_D3; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SUPFAM; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50447; Translation proteins; 1.
DR   PROSITE; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   Elongation factor {ECO:0000256|RuleBase:RU000325};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU000325};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU000325};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Protein biosynthesis {ECO:0000256|RuleBase:RU000325};
KW   Reference proteome {ECO:0000313|Proteomes:UP000271087}.
FT   DOMAIN          1..194
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   397 AA;  43309 MW;  0DE2AB71E9BCF1B7 CRC64;
     MGKGSFKYAW VLDKLKAERE RGITIDIALW KFETPKYYIT IIDAPGHRDF IKNMITGTSQ
     ADCAVLVVAC GTGEFEAGIS KNGQTREHAL LAQTLGVKQM IVACNKMDST DPPFSEARFG
     EVTTEVSNYI KKIGYNPKSI PFVPISGFNG DNMLEPSANM PWFKGWSVER KEGTMTGKTL
     LEALDSVVPP QRPTDKPLRL PLQDVYKIGG IGTVPVGRVE TGILKPGMIV TFAPQNLTTE
     VKSVEMHHEA LQEALPGDNV GFNVKNISIK DIRRGSVIIM NHPGQISAGY TPVLDCHTAH
     IACKFAELKE KVDRRSGKKV EDNPKSLKSG DAGIIDLIPT KPLCVETFTE YPPLGRFAVR
     DMRQTVAVGV IKNVDKSEGV GKVTKAAQKA GVGGKKK
//
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