ID T1JTG7_TETUR Unreviewed; 713 AA.
AC T1JTG7;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 49.
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};
OS Tetranychus urticae (Two-spotted spider mite).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Trombidiformes; Prostigmata; Eleutherengona; Raphignathae;
OC Tetranychoidea; Tetranychidae; Tetranychus.
OX NCBI_TaxID=32264 {ECO:0000313|EnsemblMetazoa:tetur01g14070.1, ECO:0000313|Proteomes:UP000015104};
RN [1] {ECO:0000313|Proteomes:UP000015104}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=London {ECO:0000313|Proteomes:UP000015104};
RA Rombauts S.;
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:tetur01g14070.1}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) to UniProtKB.
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; CAEY01000480; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; T1JTG7; -.
DR STRING; 32264.T1JTG7; -.
DR EnsemblMetazoa; tetur01g14070.1; tetur01g14070.1; tetur01g14070.
DR eggNOG; KOG0465; Eukaryota.
DR HOGENOM; CLU_002794_4_1_1; -.
DR OMA; AATTCHW; -.
DR UniPathway; UPA00345; -.
DR Proteomes; UP000015104; 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; 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; 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; IPR007110; Ig-like_dom.
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; 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.
DR PROSITE; PS50835; IG_LIKE; 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:UP000015104}.
FT DOMAIN 42..319
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT DOMAIN 393..493
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT BINDING 51..58
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03061"
FT BINDING 118..122
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03061"
FT BINDING 172..175
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03061"
SQ SEQUENCE 713 AA; 79916 MW; 335B92F515B69F8C CRC64;
MNKVLATMII TRFRKLVNPA SYRFCRAFLS DIRHHQEVRN VEDIRNIGIS AHIDSGKTTL
TERLLFYSGR IDEMHEVKGK DKVGAVMDSM ELERERGITI QSAATYVLWK SKNINIIDTP
GHVDFTVEVE RALRVLDGAI LVLCGVGGVQ AQTFTVTRQM ARYSVPCIAF INKLDRKGAD
PHRVLNQMKE KLHFTAALTQ IPIGIEDNLK GIIDLIDEKA IYFDGPHGEK VRHDEIPKDM
RAEAVDRRQE LVECISNVDD VLGEMFLEDK TPNNQDIKAA IRRNCISRKF IPVLVGSALK
NKGVQPLMDS VISYLPNPAE VENFAFKESD DGSEPSKVIL SPARDKSSPF VGLAFKMEQT
RFGQLTYIRT YQGSVSKGDI IWNARTGRKI KIPRLARMHS NNMEDISEAY AGDICAFFGS
QIIYGINSCT RSCYLDVCKD PTFHYTWDSD SKEMIVSGMG ELHLEIYGQR MANEYDCPVE
LGKPKVAFRE TLTAPCKFDY FHKKQSGGAG QYGRVVGILE PIPSPRNTEL IFSPEIVGNN
IPKQFLPSIE RGFRMMCEKG HLSGNKIRGI KFRLKDGQSH SVDSNDIAFA CAAVGAIKQV
QKLGRWHIIE PIMKLEVTVP YEFSGPAIAA ICKRSGVIVN TEEASGYMAV SAEAPLNDMF
GFTTELRTLS QGKGEFTMEF SKYAPVRGDV QQQLTSGYKD DNPDSHLERN IIL
//