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Database: UniProt
Entry: T0M945_COLGC
LinkDB: T0M945_COLGC
Original site: T0M945_COLGC 
ID   T0M945_COLGC            Unreviewed;       785 AA.
AC   T0M945;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 46.
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=CGLO_02362 {ECO:0000313|EMBL:EQB57500.1};
OS   Colletotrichum gloeosporioides (strain Cg-14) (Anthracnose fungus)
OS   (Glomerella cingulata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum gloeosporioides species complex.
OX   NCBI_TaxID=1237896 {ECO:0000313|EMBL:EQB57500.1, ECO:0000313|Proteomes:UP000015530};
RN   [1] {ECO:0000313|Proteomes:UP000015530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Cg-14 {ECO:0000313|Proteomes:UP000015530};
RX   PubMed=23902260; DOI=10.1094/MPMI-03-13-0080-R;
RA   Alkan N., Meng X., Friedlander G., Reuveni E., Sukno S., Sherman A.,
RA   Thon M., Fluhr R., Prusky D.;
RT   "Global aspects of pacC regulation of pathogenicity genes in Colletotrichum
RT   gloeosporioides as revealed by transcriptome analysis.";
RL   Mol. Plant Microbe Interact. 26:1345-1358(2013).
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:EQB57500.1}.
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DR   EMBL; AMYD01000482; EQB57500.1; -; Genomic_DNA.
DR   AlphaFoldDB; T0M945; -.
DR   STRING; 1237896.T0M945; -.
DR   eggNOG; KOG0465; Eukaryota.
DR   HOGENOM; CLU_002794_4_0_1; -.
DR   OMA; AATTCHW; -.
DR   OrthoDB; 148165at2759; -.
DR   UniPathway; UPA00345; -.
DR   Proteomes; UP000015530; 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; 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; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Elongation factor {ECO:0000256|HAMAP-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}; Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_03061};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015530}.
FT   DOMAIN          97..370
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   COILED          292..319
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         106..113
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03061"
FT   BINDING         169..173
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03061"
FT   BINDING         223..226
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03061"
SQ   SEQUENCE   785 AA;  87272 MW;  F8F6B6ACEA98901D CRC64;
     MRAPRAVRVP NGGLFTGAKP SSRPFSIAVN VKAAAPAAAT TQATPASWKL ARRAFSTTPR
     VRSAAEEALK LAQENAAALT PEVVAAKMSP EEAQRLSRVR NIGIAAHIDS GKTTCTERVL
     FYSGKIKAIH EVRGKDSVGA KMDSMDLERE KGITIQKRKD ETYHINIIDT PGHIDFTIEV
     ERALRVLDGA VMILCAVSGV QSQTITVDRQ MKRYNVPRIS FVNKMDRMGA NPWKAVEQIN
     KKLKIPAAAI QVPIGAENEF QGVIDIIEKK AYYFEGPRGT QVKVADLPNG YADIVEEKRQ
     ELIEKLADVD DEIAEIFLEE QTPTIPQIKA AIRRATIALK FSPVMMGSAL ADKGIQTVLD
     AVCDYLPNPS EVENKALDRK RDETEVKLVP YNSLPFVGLA FKLEENNYGQ LTYIRVYQGK
     LRKGSYLFNS RTDKKVRIPR IVRMHSNEME DVNEIGAGEI CAVFGVDCAS GDTFTDGNLP
     YTMSSMFVPD AVMSLSIKPK RTSDADNFSK AMNRFQREDP TFRLHVDEES EETIISGMGE
     LHLEIYVERL RREYKVDCET GKPRVSYRET ISRRTDYDFL FKRQSGGPGD YARVAGWIEP
     FEDPEKNFFE TQVVGGTIPD KFLSACGKGF EEVTERGPLL GHRVIGTKMI VNDGSTHVTD
     SSDHAFSLAT QMAFRKAFDE AGGQVLEPLM KTTITAPNEF QGNIIMLMNK RNATIHDTEV
     GTEDFTLIAD CSLNAMFGFS SQLRAATQGK GEFSMEFSHY AAAPPHLQKE LIANYQKELA
     AKRTK
//
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