ID A0A1A9AMW2_9APIC Unreviewed; 395 AA.
AC A0A1A9AMW2;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Elongation factor 1-alpha {ECO:0000256|RuleBase:RU000325};
GN ORFNames=POVWA2_080340 {ECO:0000313|EMBL:SBT57543.1};
OS Plasmodium ovale wallikeri.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=864142 {ECO:0000313|EMBL:SBT57543.1, ECO:0000313|Proteomes:UP000078550};
RN [1] {ECO:0000313|Proteomes:UP000078550}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Naeem Raeece;
RL Submitted (MAY-2016) 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; FLRE01001894; SBT57543.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1A9AMW2; -.
DR Proteomes; UP000078550; 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 ECO:0000313|EMBL:SBT57543.1};
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:SBT57543.1}.
FT DOMAIN 1..180
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 395 AA; 43695 MW; D618FCF07E301406 CRC64;
MGKGSFKYAW VLDKLKAERE RGITIDIALW KFETPRYFFT VIDAPGHKDF IKNMITGTSQ
ADVALLVVPA EVGGFEGAFS KEGQTKEHAL LAFTLGVKQI VVGVNKMDTV KYSEDRYEEI
KKEVKDYLKK VGYQADKVDF IPISGFEGDN LIEKSDKTPW YKGRTLIEAL DTMEPPKRPY
DKPLRIPLQG VYKIGGIGTV PVGRVETGIL KAGMVLNFAP SAVVSECKSV EMHKEVLEEA
RPGDNIGFNV KNVSVKEIKR GYVASDTKNE PAKGCSKFTA QVIILNHPGE IKNGYTPVLD
CHTSHISCKF LNIDSKIDKR SGKVVEENPK AIKSGDSALV SLEPKKPMVV ETFTEYPPLG
RFAIRDMRQT IAVGIIKNVE KKEPGAVSAK TPAKK
//
