EFGM_ASPTN
ID EFGM_ASPTN Reviewed; 802 AA.
AC Q0CLP3;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 101.
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; ORFNames=ATEG_05391;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CH476600; EAU34460.1; -; Genomic_DNA.
DR RefSeq; XP_001214569.1; XM_001214569.1.
DR AlphaFoldDB; Q0CLP3; -.
DR SMR; Q0CLP3; -.
DR STRING; 341663.Q0CLP3; -.
DR EnsemblFungi; EAU34460; EAU34460; ATEG_05391.
DR GeneID; 4320643; -.
DR VEuPathDB; FungiDB:ATEG_05391; -.
DR eggNOG; KOG0465; Eukaryota.
DR HOGENOM; CLU_002794_4_1_1; -.
DR OMA; AATTCHW; -.
DR OrthoDB; 637899at2759; -.
DR UniPathway; UPA00345; -.
DR Proteomes; UP000007963; 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 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; 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..802
FT /note="Elongation factor G, mitochondrial"
FT /id="PRO_0000385562"
FT DOMAIN 100..387
FT /note="tr-type G"
FT BINDING 109..116
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT BINDING 185..189
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT BINDING 239..242
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
SQ SEQUENCE 802 AA; 89070 MW; 30CEE88800BE4E9F CRC64;
MRYPSLARLP RRALSGLARA PVRLQSQNFL SQRCASTAAL RSASAVAPAC QSALHRQFQQ
RRYASATASA VLEAAASSPD NLTQEAIIDN LDPVEAERLS RVRNIGIAAH IDSGKTTCTE
RVLFYTGRIK AIHEVRGGDK VGAKMDSMDL EREKGITIQS AATFCDWVKK DKEGKEHKYH
INLIDTPGHI DFTIEVERAL RVLDGAVMIL CAVSGVQSQT MTVDRQMRRY NVPRISFINK
MDRMGANPFK AIDQINTKLK IPAAAVQVPI GAEDEFEGVV DLLRMKAIYN VGPSGEELRE
TDEIPEKVKA VAEERRNMLI ETLADVDDEI AELFLSETEP TEQQLRDAIR RATIGLKFTP
VFMGSALANK SVQPMLDGVI DYLPNPSEVQ NLALDKKRDE ASVKLVPYNS LPLVGLAFKL
EESNFGQLTY IRVYQGTLRK GANVFNARND KKVKIPRIVR MHSNEMEEVS EIGAGEICAV
FGVDCASGDT FTDGQLGYTM SSMFVPEPVI SLSIKPKNNK DAAKFSKAMA RFQREDPTFR
VTFDAESEQT LISGMGELHL DIYIERMRRE YNVDCETGPP QVAYRETIGN HVEFDHLLKK
QSGGPGDYAR VVGYMEPTEK LEENVFEEQI VGGSISEKFL FACEKGFHLA CEKGPLIGHK
VLGTKMLIND GATHMTDSSE MSFKNATQQA FRKAFMESNP SVLEPMMKTV VTAPAEFQGD
VIALLNKRNA TINDSDVGVD EVTVYADCSL NGMFGFSSHL RAATQGKGEY TMEFSHYEKA
TPQLQKELIA KYQKAQADRH KK
