ID A0A2P5BIW9_PARAD Unreviewed; 685 AA.
AC A0A2P5BIW9;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Translation factor GUF1 homolog, chloroplastic {ECO:0000256|HAMAP-Rule:MF_03138};
DE EC=3.6.5.n1 {ECO:0000256|HAMAP-Rule:MF_03138};
DE AltName: Full=Elongation factor 4 homolog {ECO:0000256|HAMAP-Rule:MF_03138};
DE Short=EF-4 {ECO:0000256|HAMAP-Rule:MF_03138};
DE AltName: Full=GTPase GUF1 homolog {ECO:0000256|HAMAP-Rule:MF_03138};
DE AltName: Full=Ribosomal back-translocase {ECO:0000256|HAMAP-Rule:MF_03138};
GN ORFNames=PanWU01x14_234400 {ECO:0000313|EMBL:PON48737.1};
OS Parasponia andersonii (Sponia andersonii).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Cannabaceae; Parasponia.
OX NCBI_TaxID=3476 {ECO:0000313|EMBL:PON48737.1, ECO:0000313|Proteomes:UP000237105};
RN [1] {ECO:0000313|Proteomes:UP000237105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. WU1-14 {ECO:0000313|Proteomes:UP000237105};
RA Van Velzen R., Holmer R., Bu F., Rutten L., Van Zeijl A., Liu W.,
RA Santuari L., Cao Q., Sharma T., Shen D., Roswanjaya Y., Wardhani T.,
RA Kalhor M.S., Jansen J., Van den Hoogen J., Gungor B., Hartog M.,
RA Hontelez J., Verver J., Yang W.-C., Schijlen E., Repin R., Schilthuizen M.,
RA Schranz E., Heidstra R., Miyata K., Fedorova E., Kohlen W., Bisseling T.,
RA Smit S., Geurts R.;
RT "Parallel loss of symbiosis genes in relatives of nitrogen-fixing non-
RT legume Parasponia.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Promotes chloroplast protein synthesis. May act as a fidelity
CC factor of the translation reaction, by catalyzing a one-codon backward
CC translocation of tRNAs on improperly translocated ribosomes.
CC {ECO:0000256|HAMAP-Rule:MF_03138}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.n1;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03138};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000256|HAMAP-
CC Rule:MF_03138}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. LepA subfamily.
CC {ECO:0000256|ARBA:ARBA00005454, ECO:0000256|HAMAP-Rule:MF_03138}.
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:PON48737.1}.
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DR EMBL; JXTB01000271; PON48737.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P5BIW9; -.
DR STRING; 3476.A0A2P5BIW9; -.
DR OrthoDB; 5473535at2759; -.
DR Proteomes; UP000237105; 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-KW.
DR GO; GO:0045727; P:positive regulation of translation; IEA:UniProtKB-UniRule.
DR CDD; cd03699; EF4_II; 1.
DR CDD; cd16260; EF4_III; 1.
DR CDD; cd01890; LepA; 1.
DR CDD; cd03709; lepA_C; 1.
DR Gene3D; 3.30.70.240; -; 1.
DR Gene3D; 3.30.70.2570; Elongation factor 4, C-terminal domain; 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_03138; GUFP; 1.
DR HAMAP; MF_00071; LepA; 1.
DR InterPro; IPR006297; EF-4.
DR InterPro; IPR035647; EFG_III/V.
DR InterPro; IPR000640; EFG_V-like.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR027518; GUFP.
DR InterPro; IPR038363; LepA_C_sf.
DR InterPro; IPR013842; LepA_CTD.
DR InterPro; IPR035654; LepA_IV.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR NCBIfam; TIGR01393; lepA; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43512:SF4; TRANSLATION FACTOR GUF1 HOMOLOG, CHLOROPLASTIC; 1.
DR PANTHER; PTHR43512; TRANSLATION FACTOR GUF1-RELATED; 1.
DR Pfam; PF00679; EFG_C; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF06421; LepA_C; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SMART; SM00838; EFG_C; 1.
DR SUPFAM; SSF54980; EF-G C-terminal domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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_03138};
KW Elongation factor {ECO:0000313|EMBL:PON48737.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_03138};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_03138};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_03138}; Plastid {ECO:0000256|HAMAP-Rule:MF_03138};
KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_03138};
KW Reference proteome {ECO:0000313|Proteomes:UP000237105}.
FT DOMAIN 88..269
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 97..104
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03138"
FT BINDING 162..166
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03138"
FT BINDING 216..219
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03138"
SQ SEQUENCE 685 AA; 76774 MW; 0547B4A77FBD9C39 CRC64;
MAKELSSQAL LLLSTTTTTT IRTRTFISTG CFSQLPPFGL HSSKLYSQSQ SSRHWPRPLS
TQCSPSVSAD VELATKVGQD RLLKVPISHI RNFCIIAHID HGKSTLADKL LQITGTVQKR
EMKEQFLDNM DLERERGITI KLQAARMRYM FKNEAYCLNL IDTPGHVDFS YEVSRSLAAC
EGALLVVDAS QGVEAQTLAN VYLALENNLE IIPVLNKIDL PGAEPERVIR EIEEIVGLDC
SNAIQCSAKE GIGITEILNA IVERIPQPHD TANRPLRALI FDSYYDPYRG VIVYFRAIDG
TIKKGDRIYF MASNKDYFAD EIGVLSPNQL QVEELYAGEV GYLSASIRSV ADARVGDTIT
HYFRRAENSL PGYEEATPMV FCGLFPVDAD QFPELRDALE KLQLNDAALK FEPETSSAMG
FGFRCGFLGL LHMEIVQERL EREYNLSLIT TAPSVVYRVN GVDGDIMECS NPSLLPEPGK
RRSIEEPFVK IEMLTPKDYI GSLMELAQDR RGEFKEMKYI TENRASIIYE LPLAEMVGDF
FDQLKSRSKG YASMEYTFVG YKESDLIKLD IQINGDHVEP LATIVHKDKA YAVGRALTQK
LKELIPRQMF KVPIQACIGT KVIASEALSA IRKDVLAKCY GGDITRKKKL LRKQAEGKKR
MKAIGKVDVP QEAFMAVLKL EKEVL
//
