GenomeNet

Database: UniProt
Entry: Q9SI75
LinkDB: Q9SI75
Original site: Q9SI75 
ID   EFGC_ARATH              Reviewed;         783 AA.
AC   Q9SI75; Q94BR7;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   24-JAN-2024, entry version 159.
DE   RecName: Full=Elongation factor G, chloroplastic {ECO:0000255|HAMAP-Rule:MF_03063};
DE            Short=cEF-G {ECO:0000255|HAMAP-Rule:MF_03063};
DE   AltName: Full=Elongation factor EF-G/SCO1;
DE   AltName: Full=Protein SNOWY COTYLEDON 1, chloroplastic;
DE            Short=AtSCO1;
DE   Flags: Precursor;
GN   Name=CPEFG; Synonyms=SCO1; OrderedLocusNames=At1g62750; ORFNames=F23N19.11;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MUTAGENESIS OF GLY-132, AND
RP   SUBCELLULAR LOCATION.
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=16525888; DOI=10.1007/s11103-005-4921-0;
RA   Albrecht V., Ingenfeld A., Apel K.;
RT   "Characterization of the snowy cotyledon 1 mutant of Arabidopsis thaliana:
RT   the impact of chloroplast elongation factor G on chloroplast development
RT   and plant vitality.";
RL   Plant Mol. Biol. 60:507-518(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF GLY-132, SUBCELLULAR
RP   LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=17629920; DOI=10.1186/1471-2229-7-37;
RA   Ruppel N.J., Hangarter R.P.;
RT   "Mutations in a plastid-localized elongation factor G alter early stages of
RT   plastid development in Arabidopsis thaliana.";
RL   BMC Plant Biol. 7:37-37(2007).
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       Required for the eoplasts redifferentiation into chloroplasts after
CC       germination. {ECO:0000255|HAMAP-Rule:MF_03063,
CC       ECO:0000269|PubMed:16525888, ECO:0000269|PubMed:17629920}.
CC   -!- PATHWAY: Protein biosynthesis; polypeptide chain elongation.
CC       {ECO:0000255|HAMAP-Rule:MF_03063}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255|HAMAP-
CC       Rule:MF_03063, ECO:0000269|PubMed:16525888,
CC       ECO:0000269|PubMed:17629920}.
CC   -!- TISSUE SPECIFICITY: Expressed in cotyledons and at lower levels in
CC       adult leaves. {ECO:0000269|PubMed:17629920}.
CC   -!- DISRUPTION PHENOTYPE: Embryo lethality. {ECO:0000269|PubMed:17629920}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EF-G/EF-2
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_03063}.
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DR   EMBL; BK005771; DAA05753.1; -; mRNA.
DR   EMBL; AC007190; AAF19548.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE34000.1; -; Genomic_DNA.
DR   EMBL; AY142646; AAN13104.1; -; mRNA.
DR   EMBL; AY039936; AAK64040.1; -; mRNA.
DR   PIR; E96652; E96652.
DR   RefSeq; NP_564801.1; NM_104952.2.
DR   AlphaFoldDB; Q9SI75; -.
DR   SMR; Q9SI75; -.
DR   BioGRID; 27794; 1.
DR   STRING; 3702.Q9SI75; -.
DR   MetOSite; Q9SI75; -.
DR   PaxDb; 3702-AT1G62750-1; -.
DR   ProteomicsDB; 221963; -.
DR   EnsemblPlants; AT1G62750.1; AT1G62750.1; AT1G62750.
DR   GeneID; 842573; -.
DR   Gramene; AT1G62750.1; AT1G62750.1; AT1G62750.
DR   KEGG; ath:AT1G62750; -.
DR   Araport; AT1G62750; -.
DR   TAIR; AT1G62750; SCO1.
DR   eggNOG; KOG0465; Eukaryota.
DR   HOGENOM; CLU_002794_4_1_1; -.
DR   InParanoid; Q9SI75; -.
DR   OMA; MDDMVGG; -.
DR   OrthoDB; 148165at2759; -.
DR   PhylomeDB; Q9SI75; -.
DR   UniPathway; UPA00345; -.
DR   PRO; PR:Q9SI75; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9SI75; baseline and differential.
DR   Genevisible; Q9SI75; AT.
DR   GO; GO:0048046; C:apoplast; HDA:TAIR.
DR   GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR   GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR   GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR   GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR   GO; GO:0005634; C:nucleus; HDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; HDA:TAIR.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009658; P:chloroplast organization; IMP:TAIR.
DR   GO; GO:0009791; P:post-embryonic development; IMP:TAIR.
DR   GO; GO:0009845; P:seed germination; IMP:TAIR.
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   1: Evidence at protein level;
KW   Chloroplast; Elongation factor; GTP-binding; Nucleotide-binding; Plastid;
KW   Protein biosynthesis; Reference proteome; Transit peptide.
FT   TRANSIT         1..80
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03063"
FT   CHAIN           81..783
FT                   /note="Elongation factor G, chloroplastic"
FT                   /id="PRO_0000423632"
FT   DOMAIN          94..369
FT                   /note="tr-type G"
FT   BINDING         103..110
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03063"
FT   BINDING         167..171
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03063"
FT   BINDING         221..224
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03063"
FT   MUTAGEN         132
FT                   /note="G->R: In sco1-1; chlorotic cotyledons and green true
FT                   leaves, and delayed development and germination."
FT                   /evidence="ECO:0000269|PubMed:16525888,
FT                   ECO:0000269|PubMed:17629920"
FT   CONFLICT        186
FT                   /note="D -> G (in Ref. 4; AAK64040)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   783 AA;  86058 MW;  3117557E49DC0746 CRC64;
     MAADALRISS SSSGSLVCNL NGSQRRPVLL PLSHRATFLG LPPRASSSSI SSSIPQFLGT
     SRIGLGSSKL SQKKKQFSVF AAAEAEAKRA VPLKDYRNIG IMAHIDAGKT TTTERILYYT
     GRNYKIGEVH EGTATMDWME QEQERGITIT SAATTTFWDK HRINIIDTPG HVDFTLEVER
     ALRVLDGAIC LFDSVAGVEP QSETVWRQAD KYGVPRICFV NKMDRLGANF FRTRDMIVTN
     LGAKPLVLQI PIGAEDVFKG VVDLVRMKAI VWSGEELGAK FSYEDIPEDL EDLAQEYRAA
     MMELIVDLDD EVMENYLEGV EPDEATVKRL VRKGTITGKF VPILCGSAFK NKGVQPLLDA
     VVDYLPSPVE VPPMNGTDPE NPEITIIRKP DDDEPFAGLA FKIMSDPFVG SLTFVRVYSG
     KISAGSYVLN ANKGKKERIG RLLEMHANSR EDVKVALTGD IIALAGLKDT ITGETLSDPE
     NPVVLERMDF PDPVIKVAIE PKTKADIDKM ATGLIKLAQE DPSFHFSRDE EMNQTVIEGM
     GELHLEIIVD RLKREFKVEA NVGAPQVNYR ESISKIAEVK YTHKKQSGGQ GQFADITVRF
     EPLEAGSGYE FKSEIKGGAV PREYIPGVMK GLEECMSTGV LAGFPVVDVR ACLVDGSYHD
     VDSSVLAFQL AARGAFREGM RKAGPRMLEP IMRVEVVTPE EHLGDVIGDL NSRRGQINSF
     GDKPGGLKVV DSLVPLAEMF QYVSTLRGMT KGRASYTMQL AKFDVVPQHI QNQLSSKDQE
     VAA
//
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