ID A0A2P6V248_9CHLO Unreviewed; 734 AA.
AC A0A2P6V248;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 08-NOV-2023, entry version 18.
DE RecName: Full=Elongation factor G, chloroplastic {ECO:0000256|HAMAP-Rule:MF_03063};
DE Short=cEF-G {ECO:0000256|HAMAP-Rule:MF_03063};
GN ORFNames=C2E20_8243 {ECO:0000313|EMBL:PSC68167.1};
OS Micractinium conductrix.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Chlorella clade; Micractinium.
OX NCBI_TaxID=554055 {ECO:0000313|EMBL:PSC68167.1, ECO:0000313|Proteomes:UP000239649};
RN [1] {ECO:0000313|EMBL:PSC68167.1, ECO:0000313|Proteomes:UP000239649}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAG 241.80 {ECO:0000313|EMBL:PSC68167.1,
RC ECO:0000313|Proteomes:UP000239649};
RX PubMed=29178410; DOI=10.1111/tpj.13789;
RA Arriola M.B., Velmurugan N., Zhang Y., Plunkett M.H., Hondzo H.,
RA Barney B.M.;
RT "Genome sequences of Chlorella sorokiniana UTEX 1602 and Micractinium
RT conductrix SAG 241.80: implications to maltose excretion by a green alga.";
RL Plant J. 93:566-586(2018).
CC -!- FUNCTION: Chloroplast-localized elongation factor EF-G involved in
CC protein synthesis in plastids. Catalyzes the GTP-dependent ribosomal
CC translocation step during translation elongation. During this step, the
CC ribosome changes from the pre-translocational (PRE) to the post-
CC translocational (POST) state as the newly formed A-site-bound peptidyl-
CC tRNA and P-site-bound deacylated tRNA move to the P and E sites,
CC 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_03063}.
CC -!- PATHWAY: Protein biosynthesis; polypeptide chain elongation.
CC {ECO:0000256|HAMAP-Rule:MF_03063}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000256|HAMAP-
CC Rule:MF_03063}.
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, ECO:0000256|HAMAP-
CC Rule:MF_03063}.
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:PSC68167.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LHPF02000041; PSC68167.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P6V248; -.
DR STRING; 554055.A0A2P6V248; -.
DR UniPathway; UPA00345; -.
DR Proteomes; UP000239649; Unassembled WGS sequence.
DR GO; GO:0009507; C:chloroplast; 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 CDD; cd01886; EF-G; 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 HAMAP; MF_00054_B; EF_G_EF_2_B; 1.
DR HAMAP; MF_03063; EF_G_plantC; 1.
DR InterPro; IPR030848; EF_G_plantC.
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; 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; 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; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Chloroplast {ECO:0000256|HAMAP-Rule:MF_03063};
KW Elongation factor {ECO:0000256|ARBA:ARBA00022768, ECO:0000256|HAMAP-
KW Rule:MF_03063};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_03063};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_03063}; Plastid {ECO:0000256|HAMAP-Rule:MF_03063};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_03063}; Reference proteome {ECO:0000313|Proteomes:UP000239649}.
FT DOMAIN 44..319
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 53..60
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03063"
FT BINDING 117..121
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03063"
FT BINDING 171..174
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03063"
SQ SEQUENCE 734 AA; 80632 MW; 3590BDECF31D39D6 CRC64;
MAKGANVGGA GALTALKRPT GRVAGRRAGA HVVAMAGKRE VPLSMYRNIG IMAHIDAGKT
TTSERILFYT GKSYKIGEVH EGTATMDWME QEQERGITIT SAATTCSWND HRINIIDTPG
HVDFTLEVER ALRVLDGAVA VFDSVAGVEP QSETVWRQAD KYGVPRICFV NKMDRMGANF
YRTRDMVVSN LGANPMPIQL PIGQEDSFVG MVDLVKMKAL VWNGEELGAT FEELEIPEDM
KELAAEYREK MIEQVAELDD DVMMAYLDGE LPDEATIKRL IRKGTLDGKF VPMCCGTAFK
NKGVQPLLDA VVDYLPAPTD LPDIRGSDVD DAEKEVTRKS TDEEAFSGLA FKIMTDPFVG
SLTFVRVYSG VVEAGSYALN AAKGKKERIG RLMQMHANSR EDVKEARAGD IIAIAGLKDV
VTGDTLCDEK SPVLLERMEF PDPVIKVAIE PKTKGDLDKM TNGLIKLAQE DPSFHFSREE
ETNQTVIEGM GELHLEIIVD RLRREWKVEC DVGAPQVNYR EGISRNAEIR YVHKKQSGGS
GQFADVAIRF EPGEAGTGFV FRSEIKGGVV PKEYIPGVTK GLEEMMSSGS LAGFPVVDVT
TTLYDGSYHD VDSSVLAFQI AARAAFREGM KKAGVQLLEP IMKVEVVTPE DHMGDVIGDL
NSRRGIVQEF TDKPGGMKLV KASVPLSEMF NYVSTLRGMS KGRAQYTMQL EKYEVVPSHI
QEKIVTNAKA KAEA
//
