EF1A_HALMA
ID EF1A_HALMA Reviewed; 421 AA.
AC P16018; Q5UZT3;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Elongation factor 1-alpha {ECO:0000255|HAMAP-Rule:MF_00118};
DE Short=EF-1-alpha {ECO:0000255|HAMAP-Rule:MF_00118};
DE AltName: Full=Elongation factor Tu {ECO:0000255|HAMAP-Rule:MF_00118};
DE Short=EF-Tu {ECO:0000255|HAMAP-Rule:MF_00118};
GN Name=tuf {ECO:0000255|HAMAP-Rule:MF_00118}; Synonyms=eef1a;
GN OrderedLocusNames=rrnAC2406;
OS Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS B-1809) (Halobacterium marismortui).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=272569;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2155402; DOI=10.1093/nar/18.3.507;
RA Baldacci G., Guinet F., Tillit J., Zaccai G., de Recondo A.-M.;
RT "Functional implications related to the gene structure of the elongation
RT factor EF-Tu from Halobacterium marismortui.";
RL Nucleic Acids Res. 18:507-511(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=15520287; DOI=10.1101/gr.2700304;
RA Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA Hood L., Ng W.V.;
RT "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT Dead Sea.";
RL Genome Res. 14:2221-2234(2004).
RN [3]
RP PROTEIN SEQUENCE OF 2-24.
RX PubMed=3127212; DOI=10.1111/j.1432-1033.1988.tb13943.x;
RA Guinet F., Frank R., Leberman R.;
RT "Polypeptide elongation factor Tu from Halobacterium marismortui.";
RL Eur. J. Biochem. 172:687-694(1988).
CC -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC tRNA to the A-site of ribosomes during protein biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00118}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_00118}.
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DR EMBL; X16677; CAA34665.1; -; Genomic_DNA.
DR EMBL; AY596297; AAV47220.1; -; Genomic_DNA.
DR PIR; S15761; EFHST.
DR RefSeq; WP_007189404.1; NZ_CP039138.1.
DR AlphaFoldDB; P16018; -.
DR SMR; P16018; -.
DR STRING; 272569.rrnAC2406; -.
DR EnsemblBacteria; AAV47220; AAV47220; rrnAC2406.
DR GeneID; 40153308; -.
DR KEGG; hma:rrnAC2406; -.
DR PATRIC; fig|272569.17.peg.3021; -.
DR eggNOG; arCOG01561; Archaea.
DR HOGENOM; CLU_007265_3_5_2; -.
DR OMA; AIRDMGM; -.
DR Proteomes; UP000001169; Chromosome I.
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 Gene3D; 3.40.50.300; -; 1.
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; IPR005225; Small_GTP-bd_dom.
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 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; SSF50447; SSF50447; 1.
DR SUPFAM; SSF50465; SSF50465; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00483; EF-1_alpha; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Elongation factor; GTP-binding;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3127212"
FT CHAIN 2..421
FT /note="Elongation factor 1-alpha"
FT /id="PRO_0000090977"
FT DOMAIN 4..220
FT /note="tr-type G"
FT REGION 13..20
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 69..73
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 90..93
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 145..148
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 184..186
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 13..20
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT BINDING 90..94
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT BINDING 145..148
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
SQ SEQUENCE 421 AA; 45731 MW; CBA81BA0722000A5 CRC64;
MSDEQHQNLA IIGHVDHGKS TLVGRLLYET GSVPEHVIEQ HKEEAEEKGK GGFEFAYVMD
NLAEERERGV TIDIAHQEFS TDTYDFTIVD CPGHRDFVKN MITGASQADN AVLVVAADDG
VQPQTQEHVF LARTLGIGEL IVAVNKMDLV DYGESEYKQV VEEVKDLLTQ VRFDSENAKF
IPVSAFEGDN IAEESEHTGW YDGEILLEAL NELPAPEPPT DAPLRLPIQD VYTISGIGTV
PVGRVETGIL NTGDNVSFQP SDVSGEVKTV EMHHEEVPKA EPGDNVGFNV RGVGKDDIRR
GDVCGPADDP PSVAETFQAQ IVVMQHPSVI TEGYTPVFHA HTAQVACTVE SIDKKIDPSS
GEVAEENPDF IQNGDAAVVT VRPQKPLSIE PSSEIPELGS FAIRDMGQTI AAGKVLGVNE
R
