ID A0A2T7DZ75_9POAL Unreviewed; 758 AA.
AC A0A2T7DZ75;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 08-NOV-2023, entry version 18.
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 ORFNames=GQ55_4G208200 {ECO:0000313|EMBL:PUZ60882.1};
OS Panicum hallii var. hallii.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Panicinae; Panicum;
OC Panicum sect. Panicum.
OX NCBI_TaxID=1504633 {ECO:0000313|EMBL:PUZ60882.1, ECO:0000313|Proteomes:UP000244336};
RN [1] {ECO:0000313|EMBL:PUZ60882.1, ECO:0000313|Proteomes:UP000244336}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. HAL2 {ECO:0000313|Proteomes:UP000244336};
RA Lovell J., Jenkins J., Lowry D., Mamidi S., Sreedasyam A., Weng X.,
RA Barry K., Bonette J., Campitelli B., Daum C., Gordon S., Gould B.,
RA Lipzen A., MacQueen A., Palacio-Mejia J., Plott C., Shakirov E., Shu S.,
RA Yoshinaga Y., Zane M., Rokhsar D., Grimwood J., Schmutz J., Juenger T.;
RT "WGS assembly of Panicum hallii var. hallii HAL2.";
RL Submitted (APR-2018) 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}.
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DR EMBL; CM009752; PUZ60882.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T7DZ75; -.
DR STRING; 1504633.A0A2T7DZ75; -.
DR EnsemblPlants; PUZ60882; PUZ60882; GQ55_4G208200.
DR Gramene; PUZ60882; PUZ60882; GQ55_4G208200.
DR UniPathway; UPA00345; -.
DR Proteomes; UP000244336; Chromosome 4.
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:UP000244336}.
FT DOMAIN 67..345
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 76..83
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03061"
FT BINDING 143..147
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03061"
FT BINDING 197..200
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03061"
SQ SEQUENCE 758 AA; 83866 MW; 98D6058BFF1333D1 CRC64;
MAMARRSASH LLSSFRPFSL LLQPPLADAP SPVAAAAVAS ARRALSSASA LRARDEKDAA
RWRESMDRMR NIGISAHIDS GKTTLTERVL YYTGRIHEIH EVRGRDGVGA KMDSMDLERE
KGITIQSAAT YCTWKGYQVN IIDTPGHVDF TIEVERALRV LDGAILVLCS VGGVQSQSIT
VDRQMRRYEI PRVAFINKLD RMGADPWKVL NQARSKLRHH NAAVQVPIGL EEEFEGLVDL
VEMKAYKFGG SSGQNVTAYD VPSNMADLVT EKRRELIEVV SEVDDQLAEA FLNDEPITAN
QLKAAIRRAT VARKFIPVYM GSAFKNKGVQ PLLDGVLDYL PCPLEVDNYA LDQNKSEEKV
LLAGTPAEPL VALAFKLEEG RFGQLTYLRI YDGVIRKGDF IYNVNTGKKI KVPRLVRMHS
NEMEDIQEAH AGQIVAVFGV DCASGDTFTD GTVKYTMTSM NVPEPVMSLA VSPISKDSGG
QFSKALNRFQ KEDPTFRVGL DPESGQTIIS GMGELHLDIY VERIKREYKV DAKVGKPRVN
FRETITQRAE FDYLHKKQSG GQGQYGRVCG YIEPLPSGSD GKFEFDNMII GQAIPSNFIP
AIEKGFREAC NSGSLIGHPV ENIRIVLTDG ASHQVDSSEL AFKLAAIYAF RQCYTAAKPV
ILEPVMKVEL KFPTEFQGTV TGDMNKRKGI IVGNEQEGDD TIVVCHVPLN NMFGYATAIR
SVTQGKGEFT MEYLEHNIVS QDVQMQLVNS YKAAKGTE
//
