LSG11_ARATH
ID LSG11_ARATH Reviewed; 537 AA.
AC Q9SHS8;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=GTPase LSG1-1 {ECO:0000303|PubMed:25319368};
DE Short=AtLSG1-1 {ECO:0000303|PubMed:25319368};
DE AltName: Full=DAR GTPase 6 {ECO:0000303|PubMed:16849600};
DE AltName: Full=Protein YEAST LSG1 ORTHOLOG 1 {ECO:0000303|PubMed:25319368};
GN Name=LSG1-1 {ECO:0000303|PubMed:25319368};
GN Synonyms=DGP6 {ECO:0000303|PubMed:16849600};
GN OrderedLocusNames=At2g27200 {ECO:0000312|Araport:AT2G27200};
GN ORFNames=T22O13.3 {ECO:0000312|EMBL:AAD26884.1};
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 {ECO:0000312|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Cheuk R., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP DOMAIN, AND GENE FAMILY.
RX PubMed=9573393; DOI=10.1016/s0378-1119(98)00088-2;
RA Fu G., Melville S., Brewster S., Warner J., Barker D.C.;
RT "Analysis of the genomic organisation of a small chromosome of Leishmania
RT braziliensis M2903 reveals two genes encoding GTP-binding proteins, one of
RT which belongs to a new G-protein family and is an antigen.";
RL Gene 210:325-333(1998).
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16849600; DOI=10.1534/genetics.106.060657;
RA Hill T.A., Broadhvest J., Kuzoff R.K., Gasser C.S.;
RT "Arabidopsis SHORT INTEGUMENTS 2 is a mitochondrial DAR GTPase.";
RL Genetics 174:707-718(2006).
RN [6]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=25319368; DOI=10.1111/tpj.12703;
RA Weis B.L., Missbach S., Marzi J., Bohnsack M.T., Schleiff E.;
RT "The 60S associated ribosome biogenesis factor LSG1-2 is required for 40S
RT maturation in Arabidopsis thaliana.";
RL Plant J. 80:1043-1056(2014).
CC -!- FUNCTION: GTPase that might be redundant with LSG1-2 for ribosome
CC biogenesis (Probable). Binds to 23S rRNA (PubMed:25319368).
CC {ECO:0000269|PubMed:25319368}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Note=kcat is 0.19 min(-1). {ECO:0000269|PubMed:25319368};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25319368}.
CC -!- TISSUE SPECIFICITY: Ubiquitous, with the highest expression in stem and
CC hypsophyll on day 66. {ECO:0000269|PubMed:25319368}.
CC -!- DOMAIN: In contrast to other GTP-binding proteins, this family is
CC characterized by a circular permutation of the GTPase motifs described
CC by a G4-G1-G3 pattern. {ECO:0000305}.
CC -!- DOMAIN: The DARXP motif is also sometime designated as G6 region.
CC {ECO:0000305|PubMed:9573393}.
CC -!- DISRUPTION PHENOTYPE: No effect on the rRNA processing
CC (PubMed:25319368). Lsg1-1 and lsg1-2 double mutants are lethal, when
CC homozygous (PubMed:25319368). {ECO:0000269|PubMed:25319368}.
CC -!- MISCELLANEOUS: Although LSG1-1 does not show a nuclear localization, is
CC not associated with ribosomes and the lsg1-1 mutant does not show any
CC rRNA processing alterations, it might be redundant with LSG1-2 since it
CC can partially complement a yeast lsg1 depletion strain, it binds to
CC rRNA and a lsg1-1 and lsg1-2 double mutant is lethal.
CC {ECO:0000305|PubMed:25319368}.
CC -!- SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family.
CC {ECO:0000255|PROSITE-ProRule:PRU01058}.
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DR EMBL; AC007290; AAD26884.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07952.1; -; Genomic_DNA.
DR EMBL; BT022030; AAY25442.1; -; mRNA.
DR PIR; A84670; A84670.
DR RefSeq; NP_180288.1; NM_128278.3.
DR AlphaFoldDB; Q9SHS8; -.
DR SMR; Q9SHS8; -.
DR STRING; 3702.AT2G27200.1; -.
DR PaxDb; Q9SHS8; -.
DR PRIDE; Q9SHS8; -.
DR ProteomicsDB; 238575; -.
DR EnsemblPlants; AT2G27200.1; AT2G27200.1; AT2G27200.
DR GeneID; 817262; -.
DR Gramene; AT2G27200.1; AT2G27200.1; AT2G27200.
DR KEGG; ath:AT2G27200; -.
DR Araport; AT2G27200; -.
DR TAIR; locus:2059615; AT2G27200.
DR eggNOG; KOG1424; Eukaryota.
DR HOGENOM; CLU_011072_10_0_1; -.
DR InParanoid; Q9SHS8; -.
DR OMA; KEQWRAP; -.
DR OrthoDB; 839833at2759; -.
DR PhylomeDB; Q9SHS8; -.
DR PRO; PR:Q9SHS8; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SHS8; baseline and differential.
DR Genevisible; Q9SHS8; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR Gene3D; 1.10.1580.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR030378; G_CP_dom.
DR InterPro; IPR043358; GNL1-like.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR023179; GTP-bd_ortho_bundle_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR45709; PTHR45709; 1.
DR Pfam; PF01926; MMR_HSR1; 1.
DR PRINTS; PR00326; GTP1OBG.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51721; G_CP; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; GTP-binding; Hydrolase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..537
FT /note="GTPase LSG1-1"
FT /id="PRO_0000432559"
FT DOMAIN 158..362
FT /note="CP-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT REGION 206..209
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT REGION 234..236
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT REGION 311..318
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT REGION 337..341
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT REGION 355..358
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT REGION 484..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 176..180
FT /note="DARXP motif"
FT COMPBIAS 484..502
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 206..209
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O31743"
FT BINDING 314..319
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O31743"
FT BINDING 358
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O31743"
SQ SEQUENCE 537 AA; 60758 MW; 0B92805D5A1F9545 CRC64;
MGKNEKTSLG RALVKHHNHM IQETKEKGKS YKDQHKKVLE SVTEVSDIDA IIEQAEEAER
LFAIHHDSAT PVPINMDTGS SSSGITAKEW KEQRMREEAL HASSLQVPRR PHWTPKMNVE
KLDANEKQAF LTWRRKLASL EENEKLVLTP FEKNLDIWRQ LWRVLERSDL IVMVVDARDP
LFYRCPDLEA YAQEIDEHKK TMLLVNKADL LPSYVREKWA EYFSRNNILF VFWSAKAATA
TLEGKPLKEQ WRAPDTTQKT DNPAVKVYGR DDLLDRLKLE ALEIVKMRKS RGVSATSTES
HCEQVVVGFV GYPNVGKSST INALVGQKRT GVTSTPGKTK HFQTLIISED LMLCDCPGLV
FPSFSSSRYE MVASGVLPID RMTEHLEAIK VVAELVPRHA IEDVYNISLP KPKSYEPQSR
PPLASELLRT YCLSRGYVAS SGLPDETRAA RQILKDYIEG KLPHFAMPPE ITRDDENETA
DDTLGAETRE GSQTEKKGEE APSLGLDQVL DDLSSFDLAN GLVSSKTKQH KKSHRKQ
