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
//