ID A0A098VV02_9MICR Unreviewed; 765 AA.
AC A0A098VV02;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 08-NOV-2023, entry version 41.
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=DI09_126p70 {ECO:0000313|EMBL:KGG52908.1};
OS Mitosporidium daphniae.
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Mitosporidium.
OX NCBI_TaxID=1485682 {ECO:0000313|EMBL:KGG52908.1, ECO:0000313|Proteomes:UP000029725};
RN [1] {ECO:0000313|EMBL:KGG52908.1, ECO:0000313|Proteomes:UP000029725}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UGP3 {ECO:0000313|EMBL:KGG52908.1,
RC ECO:0000313|Proteomes:UP000029725};
RC TISSUE=Spores {ECO:0000313|EMBL:KGG52908.1};
RA Haag K.L., James T.Y., Larsson R., Schaer T.M., Refardt D., Pombert J.-F.,
RA Ebert D.;
RT "A new species of microsporidia sheds light on the evolution of extreme
RT parasitism.";
RL Submitted (APR-2014) 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:KGG52908.1}.
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DR EMBL; JMKJ01000029; KGG52908.1; -; Genomic_DNA.
DR RefSeq; XP_013239344.1; XM_013383890.1.
DR AlphaFoldDB; A0A098VV02; -.
DR GeneID; 25258210; -.
DR VEuPathDB; MicrosporidiaDB:DI09_126p70; -.
DR HOGENOM; CLU_002794_4_0_1; -.
DR OrthoDB; 148165at2759; -.
DR UniPathway; UPA00345; -.
DR Proteomes; UP000029725; 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; 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; 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; 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; 2.
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:UP000029725};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..765
FT /note="Elongation factor G, mitochondrial"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001950474"
FT DOMAIN 34..314
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 43..50
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03061"
FT BINDING 110..114
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03061"
FT BINDING 164..167
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03061"
SQ SEQUENCE 765 AA; 84902 MW; 838565114A26ECE7 CRC64;
MLSLACKILL FKCCCRFCTF QFAGYICGEC MLCPLCLNIG ISAHIDSGKT TLTERILFYT
GRINEIHEVR GKDGVGAKMD SMDLEREKGI TIQSAATYCK WKHFNINIID TPGHVDFTIE
VERALRVLDA AILVVCGASG IQSQTITVDR QMKRYNVPRI AFINKLDRMG AKPIEIISQL
KTKLKLNAAA VQLPIGLEED HQGVVDLITM TGHYFSGKNG SDVTSCPADK LPEPLRFQAS
AYRMKLIEAI ANVDNEVADY YLLEEDPPQH ILKEAIKRAT IERKFVPVFM GSAYKNIGVQ
LLLDGVGDYL PDPSQVKNFA FDDKGNSLCL KCNSSEQTVA YAFKLDDGRF GQLTYMRVYQ
GSISRGALLI NTRTAKRLKV PRLVRMHASE MEDVDSVGSG EICAIFGVDC ATGDTFISPT
GPGDSSTLSM ISMSPMHVPD PVISLAIRPK LKDNSGFSRA LAKFQKEDPT FRMHIDPETQ
EVIISGMGEL HLEIYIERMK REYGCEVVTG KPRVAFRETI RERISFDYLH KKQTGGSGQF
GRVIGYIEPI TTDWNEICSN SQSTDKTNTA EALDASMTAA SMNTLLPNEF SNQVVGGTIP
PQFIPACEKG FYESCQEGLL IAHPITNLRM VMQEGASHIV DSNEHAFRAA TKAAFREAFF
AASPLILEPV MRVTVRIPAE FQGSVVTGIS KRKGIIVDSD AQEEGTNIIA DVPLNQMFGF
SSELRSMTQG KGEFSMEYKN HMPILPSSQE DIVSEYEKNR CKRRE
//
