NUG1_YEAST
ID NUG1_YEAST Reviewed; 520 AA.
AC P40010; D3DLQ2;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Nuclear GTP-binding protein NUG1;
DE AltName: Full=Nuclear GTPase 1;
GN Name=NUG1; OrderedLocusNames=YER006W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11583615; DOI=10.1016/s1097-2765(01)00342-2;
RA Bassler J., Grandi P., Gadal O., Lessmann T., Petfalski E., Tollervey D.,
RA Lechner J., Hurt E.;
RT "Identification of a 60S preribosomal particle that is closely linked to
RT nuclear export.";
RL Mol. Cell 8:517-529(2001).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-337, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: GTPase required for 60S ribosomal subunit export to the
CC cytoplasm. {ECO:0000269|PubMed:11583615}.
CC -!- INTERACTION:
CC P40010; P43586: LOC1; NbExp=4; IntAct=EBI-22449, EBI-22906;
CC P40010; P37838: NOP4; NbExp=3; IntAct=EBI-22449, EBI-12122;
CC P40010; P36160: RPF2; NbExp=6; IntAct=EBI-22449, EBI-15881;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11583615}.
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.
CC -!- MISCELLANEOUS: Present with 7130 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family.
CC {ECO:0000255|PROSITE-ProRule:PRU01058}.
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DR EMBL; U18778; AAB64539.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07656.1; -; Genomic_DNA.
DR PIR; S50464; S50464.
DR RefSeq; NP_010921.1; NM_001178897.1.
DR PDB; 3JCT; EM; 3.08 A; s=1-520.
DR PDB; 6ELZ; EM; 3.30 A; s=1-520.
DR PDB; 6EM1; EM; 3.60 A; s=1-520.
DR PDB; 6EM5; EM; 4.30 A; s=1-520.
DR PDB; 6FT6; EM; 3.90 A; s=1-520.
DR PDB; 6M62; EM; 3.20 A; s=1-520.
DR PDB; 6YLG; EM; 3.00 A; s=1-520.
DR PDB; 6YLH; EM; 3.10 A; s=1-520.
DR PDB; 6YLX; EM; 3.90 A; s=1-520.
DR PDB; 6YLY; EM; 3.80 A; s=1-520.
DR PDB; 7OH3; EM; 3.40 A; s=1-520.
DR PDB; 7OHQ; EM; 3.10 A; s=1-520.
DR PDB; 7OHR; EM; 4.72 A; s=1-520.
DR PDBsum; 3JCT; -.
DR PDBsum; 6ELZ; -.
DR PDBsum; 6EM1; -.
DR PDBsum; 6EM5; -.
DR PDBsum; 6FT6; -.
DR PDBsum; 6M62; -.
DR PDBsum; 6YLG; -.
DR PDBsum; 6YLH; -.
DR PDBsum; 6YLX; -.
DR PDBsum; 6YLY; -.
DR PDBsum; 7OH3; -.
DR PDBsum; 7OHQ; -.
DR PDBsum; 7OHR; -.
DR AlphaFoldDB; P40010; -.
DR SMR; P40010; -.
DR BioGRID; 36736; 259.
DR DIP; DIP-6291N; -.
DR IntAct; P40010; 76.
DR MINT; P40010; -.
DR STRING; 4932.YER006W; -.
DR iPTMnet; P40010; -.
DR MaxQB; P40010; -.
DR PaxDb; P40010; -.
DR PRIDE; P40010; -.
DR EnsemblFungi; YER006W_mRNA; YER006W; YER006W.
DR GeneID; 856723; -.
DR KEGG; sce:YER006W; -.
DR SGD; S000000808; NUG1.
DR VEuPathDB; FungiDB:YER006W; -.
DR eggNOG; KOG2484; Eukaryota.
DR GeneTree; ENSGT00940000166920; -.
DR HOGENOM; CLU_011106_5_5_1; -.
DR InParanoid; P40010; -.
DR OMA; FKLDGLW; -.
DR BioCyc; YEAST:G3O-30193-MON; -.
DR Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:P40010; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P40010; protein.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IGI:SGD.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IDA:SGD.
DR GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR GO; GO:0003723; F:RNA binding; IDA:SGD.
DR GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0000055; P:ribosomal large subunit export from nucleus; IMP:SGD.
DR Gene3D; 1.10.1580.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR030378; G_CP_dom.
DR InterPro; IPR014813; Gnl3_N_dom.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR023179; GTP-bd_ortho_bundle_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF08701; GN3L_Grn1; 1.
DR Pfam; PF01926; MMR_HSR1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51721; G_CP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; GTP-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Ribosome biogenesis; Transport.
FT CHAIN 1..520
FT /note="Nuclear GTP-binding protein NUG1"
FT /id="PRO_0000122452"
FT DOMAIN 165..343
FT /note="CP-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..34
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 213..216
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 287..294
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 336..339
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT MOD_RES 337
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 520 AA; 57709 MW; F75E4860D114756A CRC64;
MRVRKRQSRR TSTKLKEGIK KKASAHRKKE KKMAKKDVTW RSRSKKDPGI PSNFPYKAKI
LEEIEAKKMK DLEERELAKQ QRLEARKAAK EQGVDAMDED MIEDDENGLA ALVESAQQAA
AEYEGTPSND ADVRDDELDV IDYNIDFYGE DVEGESELEK SRKAYDKIFK SVIDASDVIL
YVLDARDPES TRSRKVEEAV LQSQGKRLIL ILNKVDLIPP HVLEQWLNYL KSSFPTIPLR
ASSGAVNGTS FNRKLSQTTT ASALLESLKT YSNNSNLKRS IVVGVIGYPN VGKSSVINAL
LARRGGQSKA CPVGNEAGVT TSLREIKIDN KLKILDSPGI CFPSENKKRS KVEHEAELAL
LNALPAKHIV DPYPAVLMLV KRLAKSDEMT ESFKKLYEIP PIPANDADTF TKHFLIHVAR
KRGRLGKGGI PNLASAGLSV LNDWRDGKIL GWVLPNTSAA ASQQDKQNLS TINTGTKQAP
IAANESTIVS EWSKEFDLDG LFSSLDKAID ASKDQDTMME
