EFGM1_ARATH
ID EFGM1_ARATH Reviewed; 754 AA.
AC Q9C641; Q0WU55;
DT 27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Elongation factor G-1, mitochondrial;
DE Short=EF-Gmt {ECO:0000255|HAMAP-Rule:MF_03061};
DE Short=mEF-G 1-1 {ECO:0000255|HAMAP-Rule:MF_03061};
DE AltName: Full=Elongation factor G1-1 {ECO:0000255|HAMAP-Rule:MF_03061};
DE Flags: Precursor;
GN Name=MEFG1; OrderedLocusNames=At1g45332; ORFNames=F2G19.2;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-683.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=14671022; DOI=10.1105/tpc.016055;
RA Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J.,
RA Millar A.H.;
RT "Experimental analysis of the Arabidopsis mitochondrial proteome highlights
RT signaling and regulatory components, provides assessment of targeting
RT prediction programs, and indicates plant-specific mitochondrial proteins.";
RL Plant Cell 16:241-256(2004).
RN [5]
RP GENE FAMILY, AND TISSUE SPECIFICITY.
RX PubMed=17629920; DOI=10.1186/1471-2229-7-37;
RA Ruppel N.J., Hangarter R.P.;
RT "Mutations in a plastid-localized elongation factor G alter early stages of
RT plastid development in Arabidopsis thaliana.";
RL BMC Plant Biol. 7:37-37(2007).
CC -!- FUNCTION: Mitochondrial GTPase that catalyzes the GTP-dependent
CC ribosomal translocation step during translation elongation. During this
CC step, the ribosome changes from the pre-translocational (PRE) to the
CC post-translocational (POST) state as the newly formed A-site-bound
CC peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E
CC sites, respectively. Catalyzes the coordinated movement of the two tRNA
CC molecules, the mRNA and conformational changes in the ribosome.
CC {ECO:0000255|HAMAP-Rule:MF_03061}.
CC -!- PATHWAY: Protein biosynthesis; polypeptide chain elongation.
CC {ECO:0000255|HAMAP-Rule:MF_03061}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03061,
CC ECO:0000269|PubMed:14671022}.
CC -!- TISSUE SPECIFICITY: Expressed in cotyledons and adult leaves at the
CC same levels. {ECO:0000269|PubMed:17629920}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-G/EF-2
CC subfamily. {ECO:0000305}.
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DR EMBL; AC083835; AAG50635.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32115.1; -; Genomic_DNA.
DR EMBL; AK227329; BAE99343.1; -; mRNA.
DR PIR; D96510; D96510.
DR RefSeq; NP_175135.1; NM_103595.4.
DR AlphaFoldDB; Q9C641; -.
DR SMR; Q9C641; -.
DR BioGRID; 26322; 2.
DR STRING; 3702.AT1G45332.1; -.
DR iPTMnet; Q9C641; -.
DR PaxDb; Q9C641; -.
DR PRIDE; Q9C641; -.
DR ProteomicsDB; 247081; -.
DR EnsemblPlants; AT1G45332.1; AT1G45332.1; AT1G45332.
DR GeneID; 841097; -.
DR Gramene; AT1G45332.1; AT1G45332.1; AT1G45332.
DR KEGG; ath:AT1G45332; -.
DR Araport; AT1G45332; -.
DR TAIR; locus:2825721; AT1G45332.
DR eggNOG; KOG0465; Eukaryota.
DR HOGENOM; CLU_002794_4_0_1; -.
DR InParanoid; Q9C641; -.
DR OMA; FRVHRDE; -.
DR OrthoDB; 637899at2759; -.
DR PhylomeDB; Q9C641; -.
DR UniPathway; UPA00345; -.
DR PRO; PR:Q9C641; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C641; baseline and differential.
DR Genevisible; Q9C641; AT.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; HDA:TAIR.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
DR GO; GO:0070125; P:mitochondrial translational elongation; IBA:GO_Central.
DR CDD; cd16262; EFG_III; 1.
DR CDD; cd01434; EFG_mtEFG1_IV; 1.
DR CDD; cd04097; mtEFG1_C; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00054_B; EF_G_EF_2_B; 1.
DR InterPro; IPR045044; EFG1-like.
DR InterPro; IPR041095; EFG_II.
DR InterPro; IPR009022; EFG_III.
DR InterPro; IPR035647; EFG_III/V.
DR InterPro; IPR035649; EFG_V.
DR InterPro; IPR000640; EFG_V-like.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR004540; Transl_elong_EFG/EF2.
DR InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
DR PANTHER; PTHR43636; PTHR43636; 1.
DR Pfam; PF00679; EFG_C; 1.
DR Pfam; PF14492; EFG_III; 1.
DR Pfam; PF03764; EFG_IV; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SMART; SM00838; EFG_C; 1.
DR SMART; SM00889; EFG_IV; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF54980; SSF54980; 2.
DR TIGRFAMs; TIGR00484; EF-G; 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 Elongation factor; GTP-binding; Mitochondrion; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome; Transit peptide.
FT TRANSIT 1..17
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT CHAIN 18..754
FT /note="Elongation factor G-1, mitochondrial"
FT /id="PRO_0000007446"
FT DOMAIN 63..340
FT /note="tr-type G"
FT BINDING 72..79
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT BINDING 139..143
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT BINDING 193..196
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT CONFLICT 139
FT /note="D -> G (in Ref. 3; BAE99343)"
FT /evidence="ECO:0000305"
FT CONFLICT 627
FT /note="A -> T (in Ref. 3; BAE99343)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 754 AA; 83179 MW; 39B4E8AF9E66F377 CRC64;
MARFPTSPAP NRLLRLFSSN KRSSSPTAAL LTGDFQLIRH FSAGTAARVA KDEKEPWWKE
SMDKLRNIGI SAHIDSGKTT LTERVLFYTG RIHEIHEVRG RDGVGAKMDS MDLEREKGIT
IQSAATYCTW KDYKVNIIDT PGHVDFTIEV ERALRVLDGA ILVLCSVGGV QSQSITVDRQ
MRRYEVPRVA FINKLDRMGA DPWKVLNQAR AKLRHHSAAV QVPIGLEENF QGLIDLIHVK
AYFFHGSSGE NVVAGDIPAD MEGLVAEKRR ELIETVSEVD DVLAEKFLND EPVSASELEE
AIRRATIAQT FVPVFMGSAF KNKGVQPLLD GVVSFLPSPN EVNNYALDQN NNEERVTLTG
SPDGPLVALA FKLEEGRFGQ LTYLRVYEGV IKKGDFIINV NTGKRIKVPR LVRMHSNDME
DIQEAHAGQI VAVFGIECAS GDTFTDGSVK YTMTSMNVPE PVMSLAVQPV SKDSGGQFSK
ALNRFQKEDP TFRVGLDPES GQTIISGMGE LHLDIYVERM RREYKVDATV GKPRVNFRET
ITQRAEFDYL HKKQSGGAGQ YGRVTGYVEP LPPGSKEKFE FENMIVGQAI PSGFIPAIEK
GFKEAANSGS LIGHPVENLR IVLTDGASHA VDSSELAFKM AAIYAFRLCY TAARPVILEP
VMLVELKVPT EFQGTVAGDI NKRKGIIVGN DQEGDDSVIT ANVPLNNMFG YSTSLRSMTQ
GKGEFTMEYK EHSAVSNEVQ AQLVNAYSAS KATE
