ID A0A328VGB5_9CHLR Unreviewed; 685 AA.
AC A0A328VGB5;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Translation elongation factor G {ECO:0000313|EMBL:RAQ95102.1};
GN ORFNames=A4R35_06110 {ECO:0000313|EMBL:RAQ95102.1};
OS Thermogemmatispora tikiterensis.
OC Bacteria; Chloroflexota; Ktedonobacteria; Thermogemmatisporales;
OC Thermogemmatisporaceae; Thermogemmatispora.
OX NCBI_TaxID=1825093 {ECO:0000313|EMBL:RAQ95102.1, ECO:0000313|Proteomes:UP000248706};
RN [1] {ECO:0000313|EMBL:RAQ95102.1, ECO:0000313|Proteomes:UP000248706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T81 {ECO:0000313|EMBL:RAQ95102.1,
RC ECO:0000313|Proteomes:UP000248706};
RA Tomazini A., Lal S., Stott M., Henrissat B., Polikarpov I., Sparling R.,
RA Levin D.B.;
RT "Analysis of Carbohydrate Active Enzymes in Thermogemmatispora T81 Reveals
RT Carbohydrate Degradation Ability.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
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:RAQ95102.1}.
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DR EMBL; MCIF01000002; RAQ95102.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A328VGB5; -.
DR OrthoDB; 9804431at2; -.
DR Proteomes; UP000248706; Unassembled WGS sequence.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR CDD; cd04170; EF-G_bact; 1.
DR CDD; cd16262; EFG_III; 1.
DR CDD; cd01434; EFG_mtEFG1_IV; 1.
DR CDD; cd03713; EFG_mtEFG_C; 1.
DR CDD; cd04088; EFG_mtEFG_II; 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 InterPro; IPR041095; EFG_II.
DR InterPro; IPR009022; EFG_III.
DR InterPro; IPR035647; EFG_III/V.
DR InterPro; IPR047872; EFG_IV.
DR InterPro; IPR035649; EFG_V.
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; PTHR43261:SF1; RIBOSOME-RELEASING FACTOR 2, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43261; TRANSLATION ELONGATION FACTOR G-RELATED; 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 Elongation factor {ECO:0000313|EMBL:RAQ95102.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000313|EMBL:RAQ95102.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000248706}.
FT DOMAIN 7..279
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 685 AA; 75129 MW; CDFCECFB5D1C0EF3 CRC64;
MKVYTAEQIR NVALISHVGA GKTSLVDAAL YDSGAVTRQG KVDERTSAVD YDPEELKRGM
SLHAKPVPVE WRGQKLNLID TPGYPDFVGE VKAALRVADA ALIVTTAEKG VEVGTELTWQ
YADERRLPRM ILVNKLDREN TSFEQTLEAL RARFGLKVVP LQIPIGSQSN FKGVIDLVSR
RGFTFEGGNK VQEVPVPPDL QDQVSAFREQ LIESAVENDE ALMDKFLEGE ELSEEELRTL
VRQGTVSGEL VPVVCASALK NIGVQTALDA LLDYLPSAAE ALSDEVRALG ETPALFVFKT
AAAQVGTISL FRVYSGTLKA DSHVFNVQTH AEERIGQLII PRGKAQESAS EIAAGDIGGV
AKLTNTHTGD TLVGSKEVTT ALEPIQFPEP CFTVAVFPKS KADLDKMSNA LTRLVEEDHT
LRVTRDPETG ETRISGMGET HIQVAVDMIK RRFGIDLEVR DIHIAYRETI RRKARANGRH
KRQTGGHGQF GDVWLEIEPL PIGGPDTFIF EDRIVGGVVP SQFVPGVEKG VRESLKRGFI
SGNPMVYVKV ALVDGKYHPV DSSAQSFEIA ASICMQEAVP QANPTILEPV MNVTVIVPEQ
TMGDVMSDIN TKRGRVLGME SLGNGMQKIV AQVPQAEMLH YATDLRSLTQ GRGTFTMEFY
QYEEVPPQIQ QELIARYKKE KGEPA
//
