ID O96979_9CILI Unreviewed; 408 AA.
AC O96979;
DT 01-MAY-1999, integrated into UniProtKB/TrEMBL.
DT 01-MAY-1999, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=Elongation factor 1-alpha {ECO:0000256|RuleBase:RU000325};
DE Flags: Fragment;
GN Name=TEF1 {ECO:0000313|EMBL:AAD03258.1};
OS Paranophrys carnivora.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Scuticociliatia; Philasterida; Orchitophryidae;
OC Paranophrys.
OX NCBI_TaxID=85900 {ECO:0000313|EMBL:AAD03258.1};
RN [1] {ECO:0000313|EMBL:AAD03258.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=10028290;
RA Moreira D., Le Guyader H., Philippe H.;
RT "Unusually high evolutionary rate of the elongation factor 1 alpha genes
RT from the Ciliophora and its impact on the phylogeny of eukaryotes.";
RL Mol. Biol. Evol. 16:234-245(1999).
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; AF056103; AAD03258.1; -; Genomic_DNA.
DR AlphaFoldDB; O96979; -.
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:AAD03258.1};
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:AAD03258.1}.
FT DOMAIN 1..215
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAD03258.1"
FT NON_TER 408
FT /evidence="ECO:0000313|EMBL:AAD03258.1"
SQ SEQUENCE 408 AA; 45067 MW; 384973BB7F3F5FA1 CRC64;
VDSGKSTTTG HLIYKCGGID KRVIEKFEKE SAEMGKGSFK YAWVLDKLKA ERERGITIDI
SLWNFETAKR SYTIIDAPGH RDFIKNMITG TSQADAAILI IAAGQGEFEA GISKECQTRE
HALLAYTMGV KQMVVAVNKM DSKTVDWDEE RYEEIKKELS DYLAKIGLKP RQVPFIPISG
FNGDNMLERS TNAPWYKGPI LCAALDALDP PKRPIDKPLR LPLQDVYKIG GIGTVPVGRV
ETGLLKPGMS IQFAPMGIIT ECKSVEMHHE SLPEAEPGDN VGSNVKNISV KDLRRGFVAS
DSKSDPAKDT TNFLAQVIII NHPGQIQAGY TPVLDCHTAH IACKFEEIES KVDRRSGKVL
EEEPKFIKSG DAALVRLIPT KALCVEVFSE YPPLGRYAVR DMKQTVAV
//
