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Database: UniProt
Entry: A0A1Q3EJ37_LENED
LinkDB: A0A1Q3EJ37_LENED
Original site: A0A1Q3EJ37_LENED 
ID   A0A1Q3EJ37_LENED        Unreviewed;       771 AA.
AC   A0A1Q3EJ37;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   08-NOV-2023, entry version 27.
DE   RecName: Full=Elongation factor G, mitochondrial {ECO:0000256|HAMAP-Rule:MF_03061};
DE            Short=EF-Gmt {ECO:0000256|HAMAP-Rule:MF_03061};
DE   AltName: Full=Elongation factor G 1, mitochondrial {ECO:0000256|HAMAP-Rule:MF_03061};
DE            Short=mEF-G 1 {ECO:0000256|HAMAP-Rule:MF_03061};
DE   AltName: Full=Elongation factor G1 {ECO:0000256|HAMAP-Rule:MF_03061};
GN   Name=MEF1 {ECO:0000256|HAMAP-Rule:MF_03061};
GN   ORFNames=LENED_009187 {ECO:0000313|EMBL:GAW07212.1};
OS   Lentinula edodes (Shiitake mushroom) (Lentinus edodes).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Marasmiineae; Omphalotaceae; Lentinula.
OX   NCBI_TaxID=5353 {ECO:0000313|EMBL:GAW07212.1, ECO:0000313|Proteomes:UP000188533};
RN   [1] {ECO:0000313|EMBL:GAW07212.1, ECO:0000313|Proteomes:UP000188533}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 111202 {ECO:0000313|EMBL:GAW07212.1,
RC   ECO:0000313|Proteomes:UP000188533};
RG   Lentinula edodes genome sequencing consortium;
RA   Sakamoto Y., Nakade K., Sato S., Yoshida Y., Miyazaki K., Natsume S.,
RA   Konno N.;
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:GAW07212.1, ECO:0000313|Proteomes:UP000188533}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 111202 {ECO:0000313|EMBL:GAW07212.1,
RC   ECO:0000313|Proteomes:UP000188533};
RA   Sakamoto Y., Nakade K., Sato S., Yoshida Y., Miyazaki K., Natsume S.,
RA   Konno N.;
RT   "A genome survey and senescence transcriptome analysis in Lentinula
RT   edodes.";
RL   Submitted (FEB-2017) 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:0000256|HAMAP-Rule:MF_03061}.
CC   -!- PATHWAY: Protein biosynthesis; polypeptide chain elongation.
CC       {ECO:0000256|HAMAP-Rule:MF_03061}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03061}.
CC   -!- SIMILARITY: Belongs to the GTP-binding elongation factor family. EF-
CC       G/EF-2 subfamily. {ECO:0000256|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:0000256|ARBA:ARBA00005870}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAW07212.1}.
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DR   EMBL; BDGU01000407; GAW07212.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q3EJ37; -.
DR   STRING; 5353.A0A1Q3EJ37; -.
DR   UniPathway; UPA00345; -.
DR   Proteomes; UP000188533; 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; cd01886; EF-G; 1.
DR   CDD; cd16262; EFG_III; 1.
DR   CDD; cd01434; EFG_mtEFG1_IV; 1.
DR   CDD; cd04091; mtEFG1_II_like; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.30.70.240; -; 1.
DR   Gene3D; 3.30.70.870; Elongation Factor G (Translational Gtpase), domain 3; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 1.
DR   HAMAP; MF_00054_B; EF_G_EF_2_B; 1.
DR   InterPro; IPR041095; EFG_II.
DR   InterPro; IPR009022; EFG_III.
DR   InterPro; IPR035647; EFG_III/V.
DR   InterPro; IPR047872; EFG_IV.
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_Su5_D2-typ_SF.
DR   InterPro; IPR014721; Ribsml_uS5_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   NCBIfam; TIGR00484; EF-G; 1.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR43636; ELONGATION FACTOR G, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43636:SF2; ELONGATION FACTOR G, MITOCHONDRIAL; 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; SSF54980; EF-G C-terminal domain-like; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR   SUPFAM; SSF50447; Translation proteins; 1.
DR   PROSITE; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   Elongation factor {ECO:0000256|ARBA:ARBA00022768, ECO:0000256|HAMAP-
KW   Rule:MF_03061};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW   Rule:MF_03061}; Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03061};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_03061};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_03061}; Reference proteome {ECO:0000313|Proteomes:UP000188533}.
FT   DOMAIN          63..351
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          38..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         72..79
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03061"
FT   BINDING         149..153
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03061"
FT   BINDING         203..206
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03061"
SQ   SEQUENCE   771 AA;  85586 MW;  BE23B65D9A7C7D84 CRC64;
     MLRNTLSHSF AFFSSSITRS ARCDRRWASA AAVLKKAPVT AEEKTTPPTP QYTLSEHDRS
     RLRLQRNIGV SAHIDSGKTT LTERILYYTG RIREIHEVRG RDNVGAKMDS MDLEREKGIT
     IQSAATFCDW EATNAITNEK EKYAINIIDT PGHVDFTIEV ERALRVLDGA ILVLCAVAGV
     QSQTTTVDRQ MRRYNVPRIS FINKMDRPGA NPWRIVNQIR TKLRIPAAAV HVPIGVEDEF
     RGVVDLVHWR SIYNQGVKGN EVVISEEIPA ELIDLATAKR RELIEQLADV DEEIGDLVLM
     DELPTNAQID AAIRRATTGL KFSPVFLGSA IKNTGVQPLL DGVCAYLPNP SEAEALAHDT
     EKPSSAPMVP LTPAADAPLV GLAFKLEEGR FGQLTYMRVY QGTLKKANTI YNARTGKKVK
     VPRLVRMHSN EMEDVSSIGP GEICAMFGVE CSSGDTFTDG ETSFSMTSMY VPEPVISLAI
     KSKGIETPNF SRALNRFQKE DPTFRVHVDH ESKETIISGM GELHLEIYVE RMRREYNVDC
     ITGKPRVAFR ETITSRADFN YTHKKQTGGA GQYAKVIGYI EPIQPDEETG KDTEFVNDIL
     GGAIPEGYFP GVEKGFFEAL EKGTLSGNVI SGCRLVLIDG GYHIVDSSEL AFRIATIGAF
     REAYKLANPV ILEPIMTVEV IAPVEFQSAV IGGLNTRRGT IIDSEVRDDE FTCIAEVALN
     DMFGYSNQLR GSTQGKGEFS MEYKTHMPVL PHFQKELEEA YKKTMPQAKT K
//
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