ID A0A1J1GJV9_PLARL Unreviewed; 447 AA.
AC A0A1J1GJV9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Elongation factor 1-alpha {ECO:0000256|RuleBase:RU000325};
GN ORFNames=PRELSG_0018300 {ECO:0000313|EMBL:CRG84099.1};
OS Plasmodium relictum.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Haemamoeba).
OX NCBI_TaxID=85471 {ECO:0000313|EMBL:CRG84099.1, ECO:0000313|Proteomes:UP000220158};
RN [1] {ECO:0000313|EMBL:CRG84099.1, ECO:0000313|Proteomes:UP000220158}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SGS1 {ECO:0000313|EMBL:CRG84099.1,
RC ECO:0000313|Proteomes:UP000220158};
RG Pathogen Informatics;
RL Submitted (APR-2015) 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|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; CVMU01000027; CRG84099.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J1GJV9; -.
DR VEuPathDB; PlasmoDB:PRELSG_0018300; -.
DR OMA; RDMGQTV; -.
DR OrthoDB; 5477300at2759; -.
DR Proteomes; UP000220158; 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 HAMAP; MF_00118_A; EF_Tu_A; 1.
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 ECO:0000313|EMBL:CRG84099.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU000325};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000325};
KW Protein biosynthesis {ECO:0000256|RuleBase:RU000325,
KW ECO:0000313|EMBL:CRG84099.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000220158}.
FT DOMAIN 5..228
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 447 AA; 49400 MW; EF7B3D67D3B3A864 CRC64;
MGKEKTHINL VVIGHVDSGK STTTGHIIYK LGGIDRRTIE KFEKESAEMG KGSFKYAWVL
DKLKAERERG ITIDIALWKF ETPRYYFTVI DAPGHKDFIK NMITGTSQAD VALLIVPAEV
GGFEGAFSKE GQTKEHALLA FTLGVKQIVV GVNKMDTVKY SEERYEEIKK EVRDYLKKVG
YAADKVDFIP ISGFEGDNLI EKSDKTPWYK GRTLIEALDT MEPPKRPFDK PLRIPLQGVY
KIGGIGTVPV GRVETGILKA GMVLNFAPSA VVSECKSVEM HKEVLEEARP GDNIGFNVKN
VSVKEIKRGY VASDTKNEPA KGCAKFTAQV IILNHPGEIK NGYTPVLDCH TSHISCKFVN
IDSKIDKRSG KVVEENPKSI KSGDSALVTL EPKKPMVVET FTEYPPLGRF AIRDMRQTIA
VGIIKSVEKK EPGAVSSNKP AKTPAKK
//
