ID C1K9U4_9EUGL Unreviewed; 443 AA.
AC C1K9U4;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Elongation factor 1-alpha {ECO:0000256|RuleBase:RU000325};
DE Flags: Fragment;
OS Peranema trichophorum.
OC Eukaryota; Discoba; Euglenozoa; Euglenida; Spirocuta; Heteronematina;
OC Heteronematales; Peranemidae; Peranema.
OX NCBI_TaxID=56466 {ECO:0000313|EMBL:ACO50115.1};
RN [1] {ECO:0000313|EMBL:ACO50115.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCAP 1260/1 B {ECO:0000313|EMBL:ACO50115.1};
RX PubMed=19357788; DOI=10.1371/journal.pone.0005162;
RA Gile G.H., Faktorova D., Castlejohn C.A., Burger G., Lang B.F.,
RA Farmer M.A., Lukes J., Keeling P.J.;
RT "Distribution and phylogeny of EFL and EF-1alpha in Euglenozoa suggest
RT ancestral co-occurrence followed by differential loss.";
RL PLoS ONE 4:E5162-E5162(2009).
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; FJ807243; ACO50115.1; -; mRNA.
DR AlphaFoldDB; C1K9U4; -.
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 2: Evidence at transcript level;
KW Elongation factor {ECO:0000256|RuleBase:RU000325,
KW ECO:0000313|EMBL:ACO50115.1};
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:ACO50115.1}.
FT DOMAIN 2..227
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACO50115.1"
SQ SEQUENCE 443 AA; 48716 MW; 5A1BCAD22F23B80A CRC64;
DKVHVNLVVI GHVDAGKSTA TGHLIYKCGG IDKRTIEKFE KEAAEMGKAS FKYAWVLDKL
KAERERGITI DIALWKFETA KSVFTIIDAP GHRDFIKNMI TGTSQADAAV LVIDSTTGGF
EAGISKDGQT REHALLAYTL GVKQMIVAVN KMDDKTVKYN KDRYEEIKKE VSAYLKKVGY
NPEKVPFIPI SGWVGDNMIE ATENMPWYKG STLIDALDQL EPPKRPNDKP LRLPLQDVYK
IGGIGTVPVG RVETGILKPG DVVTFAPNNL TTEVKSIEMH HEALAEATPG DNVGFNVKNV
SVKDIRSGFV ASNSKNDPAK ETADFTAQVI VLNHPGQIQN GYAPVLDCHT SHIACKFYEI
KTKIDRRSGK ELEAEPKFIK SGDAAIVLMK PTKPMCVESF TDYPPLGRFA VRDMRQTVAV
GVIKAVNKKE TSGKVTKAAQ KKK
//
