ID Q2TTF1_9STRA Unreviewed; 415 AA.
AC Q2TTF1;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Elongation factor 1-alpha {ECO:0000256|RuleBase:RU000325};
DE Flags: Fragment;
OS Stramenopile sp. ex Nuclearia delicatula CCAP1552/1.
OC Eukaryota; Sar; Stramenopiles; environmental samples.
OX NCBI_TaxID=289359 {ECO:0000313|EMBL:AAU94657.1};
RN [1] {ECO:0000313|EMBL:AAU94657.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16151185; DOI=10.1093/molbev/msj011;
RA Steenkamp E.T., Wright J., Baldauf S.L.;
RT "The protistan origins of animals and fungi.";
RL Mol. Biol. Evol. 23:93-106(2006).
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; AY582830; AAU94657.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2TTF1; -.
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 Protein biosynthesis {ECO:0000256|RuleBase:RU000325}.
FT DOMAIN 1..219
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAU94657.1"
FT NON_TER 415
FT /evidence="ECO:0000313|EMBL:AAU94657.1"
SQ SEQUENCE 415 AA; 45850 MW; E0A8E088BB6B0E38 CRC64;
ELVIGHVDAG KSTTTGHLIY KCGGIDKRTI EKYEKEAAEM GKSSFKYAWV LDNLKAERER
GITIDIALWK FESPKYQFTV IDAPGHRDFI KNMITGTSQA DVAILVIDSA PGGFEGGWAA
EGQTKEHALL AFTLGVQQMI VALNKMDACQ YSEQRYNDIK EEVSAYLKKV GYKPAKIPFV
PISGWVGDNM IDRSSNMNWY KGPILLEALD LVNPPKRPTD KPLRLPLQDV YKIGGIGTVP
VGRVETGILK PNMQVTFGPI GLTTEVKSVE MHHESLPEAV PGDNVGFNCK NIAVKDIKRG
YVASNAAEDP CKGVETFQAQ VIIMSHPGQI QNGYTPVLDC HTCHIATKFK NIDEKMDRRT
GKSLEDNPKF VKAGDACMVT MEPTKPMVVE TFNDYPPLGR FAVRDMRQTV AVGIL
//
