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EF1A_METHJ
ID   EF1A_METHJ              Reviewed;         425 AA.
AC   Q2FRI3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 88.
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}; OrderedLocusNames=Mhun_1592;
OS   Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 /
OS   JF-1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanospirillaceae; Methanospirillum.
OX   NCBI_TaxID=323259;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27890 / DSM 864 / NBRC 100397 / JF-1;
RX   PubMed=26744606; DOI=10.1186/s40793-015-0124-8;
RA   Gunsalus R.P., Cook L.E., Crable B., Rohlin L., McDonald E., Mouttaki H.,
RA   Sieber J.R., Poweleit N., Zhou H., Lapidus A.L., Daligault H.E., Land M.,
RA   Gilna P., Ivanova N., Kyrpides N., Culley D.E., McInerney M.J.;
RT   "Complete genome sequence of Methanospirillum hungatei type strain JF1.";
RL   Stand. Genomic Sci. 11:2-2(2016).
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; CP000254; ABD41323.1; -; Genomic_DNA.
DR   RefSeq; WP_011448588.1; NC_007796.1.
DR   AlphaFoldDB; Q2FRI3; -.
DR   SMR; Q2FRI3; -.
DR   STRING; 323259.Mhun_1592; -.
DR   EnsemblBacteria; ABD41323; ABD41323; Mhun_1592.
DR   GeneID; 3923589; -.
DR   KEGG; mhu:Mhun_1592; -.
DR   eggNOG; arCOG01561; Archaea.
DR   HOGENOM; CLU_007265_3_5_2; -.
DR   OMA; AIRDMGM; -.
DR   OrthoDB; 13117at2157; -.
DR   Proteomes; UP000001941; Chromosome.
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   3: Inferred from homology;
KW   Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome.
FT   CHAIN           1..425
FT                   /note="Elongation factor 1-alpha"
FT                   /id="PRO_1000015688"
FT   DOMAIN          5..221
FT                   /note="tr-type G"
FT   REGION          14..21
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          70..74
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          91..94
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          146..149
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          185..187
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         14..21
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT   BINDING         91..95
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT   BINDING         146..149
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
SQ   SEQUENCE   425 AA;  46531 MW;  E084669A9233F6DD CRC64;
     MATEKPHINL AVIGHIDHGK STTVGRLMYE AGAVPAHIIE QYKKEAESKG KGSFAFAWVM
     DNLKEERERG ITIDIAHKRF DTDKYYFTVV DCPGHRDFVK NMITGASQAD AAVIVVAAPD
     GVMEQTKEHV FLSKTLGIKQ LIVAVNKMDA ANYDEARFNQ VKSDVGALLK MVGTNPDTVK
     FIPISAFEGD NITKNSDKMP WYKGKTLFGL LDELEVPDKP TEKPLRVPIQ DAYSISGIGT
     VPVGRVETGI LKKGMNVTFM PANKSGEVKS IEMHHEEIPQ AVPGDNIGFN VRGIGKDDVR
     RGDVCGASDN PPAVAEEFTA QIVVLQHPSA ITVGYTPVFH CHTAQTACTF TELVKKLDPR
     TGQTLEENPT FLKAGDAAII KCHPTKPLCL ENAKEFPQLG RFAIRDMGQT IAAGMCINVV
     KKQMR
 
 
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