ID A1C253_9EUKA Unreviewed; 402 AA.
AC A1C253;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Elongation factor 1-alpha {ECO:0000256|RuleBase:RU000325};
DE Flags: Fragment;
GN Name=ef1a {ECO:0000313|EMBL:ABL11259.1};
OS uncultured Oxymonadida sp.
OC Eukaryota; Metamonada; Preaxostyla; Oxymonadida; environmental samples.
OX NCBI_TaxID=413579 {ECO:0000313|EMBL:ABL11259.1};
RN [1] {ECO:0000313|EMBL:ABL11259.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=18211267; DOI=10.1111/j.1462-2920.2007.01430.x;
RA de Koning A.P., Noble G.P., Heiss A.A., Wong J., Keeling P.J.;
RT "Environmental PCR survey to determine the distribution of a non-canonical
RT genetic code in uncultivable oxymonads.";
RL Environ. Microbiol. 10:65-74(2008).
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; DQ925134; ABL11259.1; -; mRNA.
DR AlphaFoldDB; A1C253; -.
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 2: Evidence at transcript level;
KW Elongation factor {ECO:0000256|RuleBase:RU000325,
KW ECO:0000313|EMBL:ABL11259.1};
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:ABL11259.1}.
FT DOMAIN 1..213
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABL11259.1"
FT NON_TER 402
FT /evidence="ECO:0000313|EMBL:ABL11259.1"
SQ SEQUENCE 402 AA; 44343 MW; BD506389906DEF26 CRC64;
VGKSTTTGHL IYKCGGIDKR TIEKFEAESE AMGKGSFKYA WVLDKLKAER ERGITIDIAL
WKFESNKYYF TIIDAPGHRD FIKNMITGTS QADAAILVVA ANVGEFEAGI SKDGQTREHA
LLAYTLGVKQ MIVCVNKMDD RSCQWSETRY NEIKNELGSY LKKIGYNPDK IPVIPISGFN
GDNMLERSPN MPWYKGPILF EALDNLDIPK RPVDKPLRLP IQDVFKIGGI GTVPVGRVET
GILLPGSVIT IAPAMITTEV KTVEMHHGSL TQAVPGDNVG FNVKGVSVKE VKRGFVVGDS
KNDPPAEAES FNAQVIVMSH PGQISNGYTP VLDCHTSHIA CKFKEIQSKI DRRTNKVQEE
NPKSIKSGDS AIVQLVPSKP MVVEAFTEYP PLGRFAVRDM RS
//
