GUFP_PHYPA
ID GUFP_PHYPA Reviewed; 735 AA.
AC A9RFQ5;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Translation factor GUF1 homolog, chloroplastic {ECO:0000255|HAMAP-Rule:MF_03138};
DE EC=3.6.5.-;
DE AltName: Full=Elongation factor 4 homolog {ECO:0000255|HAMAP-Rule:MF_03138};
DE Short=EF-4 {ECO:0000255|HAMAP-Rule:MF_03138};
DE AltName: Full=GTPase GUF1 homolog {ECO:0000255|HAMAP-Rule:MF_03138};
DE AltName: Full=Ribosomal back-translocase {ECO:0000255|HAMAP-Rule:MF_03138};
DE Flags: Precursor;
GN ORFNames=PHYPADRAFT_158777;
OS Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium.
OX NCBI_TaxID=3218;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004;
RX PubMed=18079367; DOI=10.1126/science.1150646;
RA Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H.,
RA Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T.,
RA Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A.,
RA Suzuki Y., Hashimoto S.-I., Yamaguchi K., Sugano S., Kohara Y.,
RA Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E.,
RA Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M.,
RA Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J.,
RA Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B.,
RA Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A.,
RA Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y.,
RA Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M.,
RA Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S.,
RA Boore J.L.;
RT "The Physcomitrella genome reveals evolutionary insights into the conquest
RT of land by plants.";
RL Science 319:64-69(2008).
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:0000255|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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03138};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255|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:0000255|HAMAP-Rule:MF_03138}.
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; DS544895; EDQ82334.1; -; Genomic_DNA.
DR RefSeq; XP_001752830.1; XM_001752778.1.
DR AlphaFoldDB; A9RFQ5; -.
DR SMR; A9RFQ5; -.
DR STRING; 3218.PP1S6_407V6.1; -.
DR EnsemblPlants; Pp3c26_13410V3.2; PAC:32917303.CDS.1; Pp3c26_13410.
DR Gramene; Pp3c26_13410V3.2; PAC:32917303.CDS.1; Pp3c26_13410.
DR eggNOG; KOG0462; Eukaryota.
DR HOGENOM; CLU_009995_3_3_1; -.
DR InParanoid; A9RFQ5; -.
DR OMA; HIDFNHE; -.
DR OrthoDB; 165663at2759; -.
DR Proteomes; UP000006727; Chromosome 26.
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:0045727; P:positive regulation of translation; IEA:UniProtKB-UniRule.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR CDD; cd03709; lepA_C; 1.
DR Gene3D; 3.30.70.2570; -; 1.
DR Gene3D; 3.40.50.300; -; 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 PANTHER; PTHR43512; PTHR43512; 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; SSF50447; SSF50447; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54980; SSF54980; 2.
DR TIGRFAMs; TIGR01393; lepA; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Chloroplast; GTP-binding; Hydrolase; Nucleotide-binding; Plastid;
KW Protein biosynthesis; Reference proteome; Transit peptide.
FT TRANSIT 1..47
FT /note="Chloroplast"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03138"
FT CHAIN 48..735
FT /note="Translation factor GUF1 homolog, chloroplastic"
FT /id="PRO_0000402918"
FT DOMAIN 137..319
FT /note="tr-type G"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 106..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 146..153
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03138"
FT BINDING 212..216
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03138"
FT BINDING 266..269
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03138"
SQ SEQUENCE 735 AA; 81712 MW; A96A8A16FA9D54EC CRC64;
MAVPTIPSPA CISQSANGSI ISTRRSTETN PRQHPSTSYR CAGRVVRRQG RSAISRSGSR
YLHDLEAGRS LLKRVTLRRD WDSRLDEKDQ YPRLGARAAA TFEAKPENAE KDYSKNGKAA
NKGVDNGKDR LAKVPISNIR NFSIIAHIDH GKSTLADKLL QTTGTVLARE MKEQFLDNMD
LERERGITIK LQAARMRYVD ETGEAYCLNL IDTPGHVDFS YEVSRSLAAC EGALLVVDAS
QGVEAQTLAN VYLALESNLE IIPVLNKIDL PGADPERVRR EIEEIIGLDC SEAILCSAKE
GVGIPEILNA VVKKIPPPKD TAAEPLRALI FDSYYDSYRG VVVYFRVMDG RVKKGDYVQF
MNSKTEYQVD EVGVLSPIQM PVNELYAGEV GYLSASIKSV ADARVGDTIT TVSRKAAQAL
PGYQLATPMV FCGLFPIDAD QFVELREALE KLQLNDAALQ FEPETSSAMG FGFRCGFLGL
LHMEIVQERL EREYGLDLIT TAPSVVYRVH CTDGTITECS NPSALPDAGK RKSIEEPYVR
IELLTPKDYI GPLMELAQER RGEFKEMKFI TENRASLVYM LPLGEMVGDF FDQLKSRSKG
YASMEYSVKG YRESKLVKLD IRINDEAVDP LAVIVHQDKA YSVGRALTQQ LKKLIPRQLF
KIPIQACIGS KVIASENIAA MRKDVLAKCY GGDISRKKKL LKKQAEGKKR MKSLGRVDVP
QDAFMAILRL EKEVV
