ID R1FU90_NANST Unreviewed; 443 AA.
AC R1FU90;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Elongation factor 1-alpha {ECO:0000256|HAMAP-Rule:MF_00118};
DE Short=EF-1-alpha {ECO:0000256|HAMAP-Rule:MF_00118};
DE AltName: Full=Elongation factor Tu {ECO:0000256|HAMAP-Rule:MF_00118};
DE Short=EF-Tu {ECO:0000256|HAMAP-Rule:MF_00118};
GN Name=tuf {ECO:0000256|HAMAP-Rule:MF_00118};
GN ORFNames=Nst1_013 {ECO:0000313|EMBL:EOD42675.1};
OS Nanobsidianus stetteri.
OC Archaea; Nanoarchaeota; Candidatus Nanoarchaeia; Nanoarchaeales;
OC Nanopusillaceae; Nanobsidianus.
OX NCBI_TaxID=1294122 {ECO:0000313|EMBL:EOD42675.1, ECO:0000313|Proteomes:UP000053279};
RN [1] {ECO:0000313|EMBL:EOD42675.1, ECO:0000313|Proteomes:UP000053279}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Podar M., Makarova K.S., Graham D.E., Wolf Y.I., Koonin E.V.,
RA Reysenbach A.-L.;
RT "Insights into archaeal evolution and symbiosis from the genomes of a
RT Nanoarchaeon and its crenarchaeal host from Yellowstone National Park.";
RL Submitted (FEB-2013) 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|HAMAP-Rule:MF_00118}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00118}.
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, ECO:0000256|HAMAP-
CC Rule:MF_00118}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00118}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EOD42675.1}.
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DR EMBL; APJZ01000001; EOD42675.1; -; Genomic_DNA.
DR AlphaFoldDB; R1FU90; -.
DR PATRIC; fig|1294122.7.peg.13; -.
DR Proteomes; UP000053279; 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:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
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; 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; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118,
KW ECO:0000313|EMBL:EOD42675.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_00118};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00118};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00118}; Reference proteome {ECO:0000313|Proteomes:UP000053279}.
FT DOMAIN 5..228
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 14..21
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
FT BINDING 91..95
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
SQ SEQUENCE 443 AA; 48626 MW; B52F1D992F4B38EC CRC64;
MAREKPHINL IVVGHVDNGK STLVGRLMVS LNLIDQKVLE ELKNIAKELG KETDYLAFLM
DKSIEERKRG LTIDVAAIKI PAKKYSLTIL DAPGHRDFIK NMISGTAQSD AAILVVSAAP
GEAETALGPE GQGREHLLLL RTLGIPQIII AISKMDAANY DQKRYEQIKN MILTLAKQIG
YTEKQIKAIV PIAAYSSDEN VTQKSQKMPW YNGPTIYEAF DLLDEPPRLV DKPLRIPIGD
VYNIKGVGLV PTGKVESGRL KPGDKVIFLP SKKPNGVVGE VKSIEMHHEK LDEALPGDNI
GFNVKGPESG DILRGDVCGK LGEPLPKLAE EFTARIYVLY HPSAVAVGYT PVIHIHTAAV
ACKIAEIQSK IDPRTGQEVE KNPQFLKTGD AAIVKFVPTK PLVVEKFEDF PNTSLGRFAI
RDMNKTIGIG QVLSVKEKQI QIK
//
