EFGM_CHAGB
ID EFGM_CHAGB Reviewed; 798 AA.
AC Q2HEK0;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Elongation factor G, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03061};
DE Short=EF-Gmt {ECO:0000255|HAMAP-Rule:MF_03061};
DE AltName: Full=Elongation factor G 1, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03061};
DE Short=mEF-G 1 {ECO:0000255|HAMAP-Rule:MF_03061};
DE AltName: Full=Elongation factor G1 {ECO:0000255|HAMAP-Rule:MF_03061};
DE Flags: Precursor;
GN Name=MEF1 {ECO:0000255|HAMAP-Rule:MF_03061}; ORFNames=CHGG_01354;
OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS NRRL 1970) (Soil fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=306901;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL Genome Announc. 3:E0002115-E0002115(2015).
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 -!- 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; CH408029; EAQ93119.1; -; Genomic_DNA.
DR RefSeq; XP_001220575.1; XM_001220574.1.
DR AlphaFoldDB; Q2HEK0; -.
DR SMR; Q2HEK0; -.
DR STRING; 38033.XP_001220575.1; -.
DR EnsemblFungi; EAQ93119; EAQ93119; CHGG_01354.
DR GeneID; 4386316; -.
DR eggNOG; KOG0465; Eukaryota.
DR HOGENOM; CLU_002794_4_1_1; -.
DR InParanoid; Q2HEK0; -.
DR OMA; AATTCHW; -.
DR OrthoDB; 637899at2759; -.
DR UniPathway; UPA00345; -.
DR Proteomes; UP000001056; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; 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 GO; GO:0070125; P:mitochondrial translational elongation; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW Elongation factor; GTP-binding; Mitochondrion; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome; Transit peptide.
FT TRANSIT 1..24
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT CHAIN 25..798
FT /note="Elongation factor G, mitochondrial"
FT /id="PRO_0000385567"
FT DOMAIN 97..383
FT /note="tr-type G"
FT BINDING 106..113
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT BINDING 181..185
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT BINDING 235..238
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
SQ SEQUENCE 798 AA; 88113 MW; 7F93B8C3E7E01396 CRC64;
MRVIRAAAAL NSSCAASSRQ GARYASLACR TALTSSPLAP CYSARLSGLR YFTKTHAPRA
ASAAEAALKQ AKELAAANMT PEAAAARMTP EEAKRLSMVR NIGIAAHIDS GKTTVSERIL
FYTGRTKAIH EVRGRDGVGA KMDSMELERE RGITIQSAAT FADWKKVENG VEETYHFNLI
DTPGHIDFTI EVERAMRVLD GAVMVLCAVS GVQSQTITVD RQMKRYNVPR ISFVNKMDRM
GSNPFKAVEM INSKLKIPAA AVQIPIGSEK EFEGVVDLIH MRAIRNDGLR GINVRVSNTI
PENLKELAEQ KRQELIEKLA DVDDEIAEMF LEEKTPTPEQ IKAAIRRATI GLKFTPVLMG
SALADKSVQP MLDAVCDYLP NPGNVDNMAL DRSKKEEPVK LLPYDSLPFV GLAFKLEENP
YGQLTYIRVY QGTLKKGQYL FNARNDKKVR IPRIVRMHSN EMEDVNEIGA GEICAVFGVE
CASGDTFTDG RLPYGMSSMF VPDSVMSLSI KPKRSSDADA FSKAMNRFMR EDPTFRLHVD
EESEETIISG MGELHLDIYV ERLRREYKVD CETGKPRVAY RETISKRAEY DFLLKRQSGG
PGDYARVVGW IEPNVENAEG NKFETKVVGG NIPDKYLAAC GKGFEEACIK GPLLGHKVIG
AHMVVTDGAT HVTDSSDYAF NLATQMAFRK AFPDAGGAVL EPLMKTTITA PAEFQGNILM
LMNKRGSIVD TEVGADEFTM IAECSLNAMF GFSTHLRAAT QGKGEFSMEF SHYAPAPPHL
QKELVAQYEK ELEAKRSK
