ID A0A3T1B905_9ACTN Unreviewed; 616 AA.
AC A0A3T1B905;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Translation elongation factor G {ECO:0000313|EMBL:BBH71619.1};
GN Name=fusA_3 {ECO:0000313|EMBL:BBH71619.1};
GN ORFNames=ACTI_83040 {ECO:0000313|EMBL:BBH71619.1};
OS Actinoplanes sp. OR16.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=946334 {ECO:0000313|EMBL:BBH71619.1, ECO:0000313|Proteomes:UP000282692};
RN [1] {ECO:0000313|EMBL:BBH71619.1, ECO:0000313|Proteomes:UP000282692}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OR16 {ECO:0000313|EMBL:BBH71619.1,
RC ECO:0000313|Proteomes:UP000282692};
RA Kasai D.;
RT "Complete genome sequence of natural rubber degrading Actinoplanes sp.
RT strain OR16 isolated form botanical garden in Japan.";
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the GTP-dependent ribosomal translocation step
CC during translation elongation. During this step, the ribosome changes
CC from the pre-translocational (PRE) to the post-translocational (POST)
CC state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound
CC deacylated tRNA move to the P and E sites, respectively. Catalyzes the
CC coordinated movement of the two tRNA molecules, the mRNA and
CC conformational changes in the ribosome.
CC {ECO:0000256|ARBA:ARBA00024731}.
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DR EMBL; AP019371; BBH71619.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3T1B905; -.
DR OrthoDB; 9801472at2; -.
DR Proteomes; UP000282692; Chromosome.
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; cd01886; EF-G; 1.
DR CDD; cd16262; EFG_III; 1.
DR CDD; cd03713; EFG_mtEFG_C; 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; IPR035649; EFG_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; IPR005517; Transl_elong_EFG/EF2_IV.
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 PRINTS; PR01037; TCRTETOQM.
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 4: Predicted;
KW Elongation factor {ECO:0000313|EMBL:BBH71619.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT DOMAIN 1..248
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 616 AA; 65461 MW; 84092831BA280A16 CRC64;
MRVRNLGILA HVDAGKTTLT ERILFATGAV HKTGEVHHGT TVTDFDPQER DRGITIFAAA
VSCDWKDHRL NLIDTPGHVD FSDEVERSLR VLDGAVAVFD AVAGVEPQSE AVWRKADRYE
VPRIAFVNKM DRPGADLGAA VESIRKRLDA IPLVLQVPMD DLSGVIDLVH NPPASVAAAR
RQLEEAVAEL HEAALDDIAD MSDVTLANAI RDLTLSRQAV PVLCGAAYRD IGVEELLDAV
VDYLPAPGGD PSGDLVALVF KRAGRMDYLR IYDGTMRKGD VVWDAGAGRN ERIARILRVQ
ADEHTDVDRA AAGDIVAVAG LKAVKAGSTL STRDHPVLLE APQAAEPLVS VAVEARTRQG
AQRLPQALAT LTHEDPSLLV RTDAETGQIL LSGLGELHLE VAVEKLRQTT GLEVTTGRPQ
VTFRERVATG VSGVTYRHVK QDGGAGQFAV VVLDVTPLDG DGFAFTSTVT GGRVPAEYIR
AVEAGCREAL AAGPLGGHPV VGLAVTLTDG QTHPKDSSET AFRAAGRFGL RQALHAATLR
LLEPVAEVTV TAPSDTLGAV LGDLAARRGQ VTDSALSTVT AIVPLSELFG YASRLRSRTH
GRGTFTSRPA GYRPAA
//
