GUFP_MICPC
ID GUFP_MICPC Reviewed; 702 AA.
AC C1N1Y2;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 73.
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};
GN ORFNames=MICPUCDRAFT_51778;
OS Micromonas pusilla (strain CCMP1545) (Picoplanktonic green alga).
OC Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC Mamiellaceae; Micromonas.
OX NCBI_TaxID=564608;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1545;
RX PubMed=19359590; DOI=10.1126/science.1167222;
RA Worden A.Z., Lee J.H., Mock T., Rouze P., Simmons M.P., Aerts A.L.,
RA Allen A.E., Cuvelier M.L., Derelle E., Everett M.V., Foulon E.,
RA Grimwood J., Gundlach H., Henrissat B., Napoli C., McDonald S.M.,
RA Parker M.S., Rombauts S., Salamov A., Von Dassow P., Badger J.H.,
RA Coutinho P.M., Demir E., Dubchak I., Gentemann C., Eikrem W., Gready J.E.,
RA John U., Lanier W., Lindquist E.A., Lucas S., Mayer K.F., Moreau H.,
RA Not F., Otillar R., Panaud O., Pangilinan J., Paulsen I., Piegu B.,
RA Poliakov A., Robbens S., Schmutz J., Toulza E., Wyss T., Zelensky A.,
RA Zhou K., Armbrust E.V., Bhattacharya D., Goodenough U.W., Van de Peer Y.,
RA Grigoriev I.V.;
RT "Green evolution and dynamic adaptations revealed by genomes of the marine
RT picoeukaryotes Micromonas.";
RL Science 324:268-272(2009).
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 -!- MISCELLANEOUS: This protein may be expected to contain an N-terminal
CC transit peptide but none has been predicted. {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}.
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DR EMBL; GG663745; EEH53909.1; -; Genomic_DNA.
DR RefSeq; XP_003062197.1; XM_003062151.1.
DR AlphaFoldDB; C1N1Y2; -.
DR SMR; C1N1Y2; -.
DR STRING; 564608.C1N1Y2; -.
DR GeneID; 9687434; -.
DR KEGG; mpp:MICPUCDRAFT_51778; -.
DR eggNOG; KOG0462; Eukaryota.
DR OMA; HIDFNHE; -.
DR OrthoDB; 165663at2759; -.
DR Proteomes; UP000001876; 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: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; 2.
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 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.
FT CHAIN 1..702
FT /note="Translation factor GUF1 homolog, chloroplastic"
FT /id="PRO_0000402914"
FT DOMAIN 87..283
FT /note="tr-type G"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 96..103
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03138"
FT BINDING 162..166
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03138"
FT BINDING 216..219
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03138"
SQ SEQUENCE 702 AA; 77159 MW; 197A2C03B414F524 CRC64;
MASAAPASRG AARASTAARD APFAAAARGP GRFRRDGNGR NRLVAVRAPR RWTTRAAATS
GDANVVIKPK KERAKVDPNA VLQVPPSQIR NFSIIAHIDH GKSTLADTLL SKTKTVAARD
MEAQLLDSMD IERERGITIK LNSARMNYVA NDGETYVLNL IDTPGHVDFS YEVSRSLAAC
EGALLVVDAS QGVEAQTVAN VYLALENDLE IITVLNKIDL PGAEPERVKV RSIHWFPYDR
VGVREIEDVL GLDTEDAVVA SAKANIGMED ILENIVKMIP PPPDTGDEPL RALIFDSYFD
PYRGVVVIFR VVDGNLGVGD AVKFMNTGKS YTIDEIGIMR PQKVPVNRLS AGEVGYMIAN
IKSVADARVG DTITTTKDSS TEPLPGYSEA TPMVYCGLFP TDSDQYEDLR VALGKLQIND
AALRYEPEQS SAMGFGFRCG FLGLLHMEIV QERLEREYDL GLITTAPSVV YKVYTSDGAC
VDIANPADLP DASVRDRIEE PFVKLEMFAP SDYVGSLMEL AQQRRGEFID MTYLSESRTC
LKYDIPLGEV VTDFFDELKS RSKGYASMEY SFNEYRKSDL VRLDVLINYE PADPLACICH
RDKSYVMGRG LVDKLKELIP RQMFRIPIQA SIGTKVIAST SISAMRKDVL AKCYGGDISR
KKKLLKKQAA GKKRMKQFGK VEVPQEAFMA VLKVDQNAGS GG
