BMS1_YEAST
ID BMS1_YEAST Reviewed; 1183 AA.
AC Q08965; D6W3F3;
DT 13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Ribosome biogenesis protein BMS1;
GN Name=BMS1; OrderedLocusNames=YPL217C;
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=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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 INTERACTION WITH RCL1.
RX PubMed=11565748; DOI=10.1017/s1355838201012079;
RA Wegierski T., Billy E., Nasr F., Filipowicz W.;
RT "Bms1p, a G-domain-containing protein, associates with Rcl1p and is
RT required for 18S rRNA biogenesis in yeast.";
RL RNA 7:1254-1267(2001).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11565749; DOI=10.1017/s1355838201013073;
RA Gelperin D., Horton L., Beckman J., Hensold J., Lemmon S.K.;
RT "Bms1p, a novel GTP-binding protein, and the related Tsr1p are required for
RT distinct steps of 40S ribosome biogenesis in yeast.";
RL RNA 7:1268-1283(2001).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-578, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-478, AND IDENTIFICATION BY
RP 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438; SER-478; SER-492;
RP THR-504; THR-516; SER-518; SER-523; SER-574 AND SER-578, AND IDENTIFICATION
RP BY 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: May act as a molecular switch during maturation of the 40S
CC ribosomal subunit in the nucleolus. The depletion of BMS1 interferes
CC with processing of the 35S pre-rRNA at sites A0, A1, and A2, and the
CC formation of 40S subunits. {ECO:0000269|PubMed:11565748,
CC ECO:0000269|PubMed:11565749}.
CC -!- SUBUNIT: Associates with RCL1.
CC -!- INTERACTION:
CC Q08965; Q08096: RCL1; NbExp=7; IntAct=EBI-3683, EBI-14892;
CC Q08965; Q02354: UTP6; NbExp=4; IntAct=EBI-3683, EBI-22119;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11565749}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:11565749}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Bms1-like GTPase family. BMS1 subfamily. {ECO:0000305}.
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DR EMBL; Z73573; CAA97932.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11219.1; -; Genomic_DNA.
DR PIR; S65236; S65236.
DR RefSeq; NP_015107.1; NM_001184031.1.
DR PDB; 4CLQ; X-ray; 2.02 A; B=547-636.
DR PDB; 5JPQ; EM; 7.30 A; a=1-1183.
DR PDB; 5TZS; EM; 5.10 A; i=547-636.
DR PDB; 5WLC; EM; 3.80 A; SI=1-1183.
DR PDB; 5WYJ; EM; 8.70 A; B1=1-1183.
DR PDB; 5WYK; EM; 4.50 A; B1=1-1183.
DR PDB; 6KE6; EM; 3.40 A; RJ=1-1183.
DR PDB; 6LQP; EM; 3.20 A; RJ=1-1183.
DR PDB; 6LQQ; EM; 4.10 A; RJ=1-1183.
DR PDB; 6LQR; EM; 8.60 A; RJ=1-1183.
DR PDB; 6LQS; EM; 3.80 A; RJ=1-1183.
DR PDB; 6LQT; EM; 4.90 A; RJ=1-1183.
DR PDB; 6LQU; EM; 3.70 A; RJ=1-1183.
DR PDB; 6LQV; EM; 4.80 A; RJ=1-1183.
DR PDB; 6ZQA; EM; 4.40 A; CL=1-1183.
DR PDB; 6ZQB; EM; 3.90 A; CL=1-1183.
DR PDB; 6ZQC; EM; 3.80 A; CL=1-1183.
DR PDB; 6ZQD; EM; 3.80 A; CL=1-1183.
DR PDB; 6ZQE; EM; 7.10 A; CL=1-1183.
DR PDB; 6ZQF; EM; 4.90 A; CL=1-1183.
DR PDB; 6ZQG; EM; 3.50 A; CL=1-1183.
DR PDB; 7AJT; EM; 4.60 A; CL=1-1183.
DR PDB; 7AJU; EM; 3.80 A; CL=1-1183.
DR PDB; 7D4I; EM; 4.00 A; RJ=1-1183.
DR PDB; 7D5S; EM; 4.60 A; RJ=1-1183.
DR PDB; 7D5T; EM; 6.00 A; RJ=1-1183.
DR PDB; 7D63; EM; 12.30 A; RJ=1-1183.
DR PDBsum; 4CLQ; -.
DR PDBsum; 5JPQ; -.
DR PDBsum; 5TZS; -.
DR PDBsum; 5WLC; -.
DR PDBsum; 5WYJ; -.
DR PDBsum; 5WYK; -.
DR PDBsum; 6KE6; -.
DR PDBsum; 6LQP; -.
DR PDBsum; 6LQQ; -.
DR PDBsum; 6LQR; -.
DR PDBsum; 6LQS; -.
DR PDBsum; 6LQT; -.
DR PDBsum; 6LQU; -.
DR PDBsum; 6LQV; -.
DR PDBsum; 6ZQA; -.
DR PDBsum; 6ZQB; -.
DR PDBsum; 6ZQC; -.
DR PDBsum; 6ZQD; -.
DR PDBsum; 6ZQE; -.
DR PDBsum; 6ZQF; -.
DR PDBsum; 6ZQG; -.
DR PDBsum; 7AJT; -.
DR PDBsum; 7AJU; -.
DR PDBsum; 7D4I; -.
DR PDBsum; 7D5S; -.
DR PDBsum; 7D5T; -.
DR PDBsum; 7D63; -.
DR AlphaFoldDB; Q08965; -.
DR SMR; Q08965; -.
DR BioGRID; 35968; 475.
DR ComplexPortal; CPX-1606; RCL1-BMS1 40S ribosomal subunit maturation complex.
DR DIP; DIP-6562N; -.
DR IntAct; Q08965; 86.
DR MINT; Q08965; -.
DR STRING; 4932.YPL217C; -.
DR iPTMnet; Q08965; -.
DR MaxQB; Q08965; -.
DR PaxDb; Q08965; -.
DR PRIDE; Q08965; -.
DR EnsemblFungi; YPL217C_mRNA; YPL217C; YPL217C.
DR GeneID; 855884; -.
DR KEGG; sce:YPL217C; -.
DR SGD; S000006138; BMS1.
DR VEuPathDB; FungiDB:YPL217C; -.
DR eggNOG; KOG1951; Eukaryota.
DR GeneTree; ENSGT00940000153195; -.
DR HOGENOM; CLU_002486_0_0_1; -.
DR InParanoid; Q08965; -.
DR OMA; QMEQQEF; -.
DR BioCyc; YEAST:G3O-34106-MON; -.
DR Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:Q08965; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q08965; protein.
DR GO; GO:0030686; C:90S preribosome; IDA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0032040; C:small-subunit processome; IPI:ComplexPortal.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IDA:SGD.
DR GO; GO:0003924; F:GTPase activity; IDA:SGD.
DR GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR GO; GO:0034511; F:U3 snoRNA binding; IDA:SGD.
DR GO; GO:0000480; P:endonucleolytic cleavage in 5'-ETS of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0000479; P:endonucleolytic cleavage of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR GO; GO:0000472; P:endonucleolytic cleavage to generate mature 5'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0030490; P:maturation of SSU-rRNA; IC:ComplexPortal.
DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR GO; GO:2000232; P:regulation of rRNA processing; IDA:ComplexPortal.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IC:ComplexPortal.
DR CDD; cd01882; BMS1; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR012948; AARP2CN.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR039761; Bms1/Tsr1.
DR InterPro; IPR037875; Bms1_N.
DR InterPro; IPR007034; BMS1_TSR1_C.
DR InterPro; IPR030387; G_Bms1/Tsr1_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR12858; PTHR12858; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF08142; AARP2CN; 1.
DR Pfam; PF04950; RIBIOP_C; 1.
DR SMART; SM00785; AARP2CN; 1.
DR SMART; SM01362; DUF663; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51714; G_BMS1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; GTP-binding; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Ribosome biogenesis.
FT CHAIN 1..1183
FT /note="Ribosome biogenesis protein BMS1"
FT /id="PRO_0000195006"
FT DOMAIN 68..233
FT /note="Bms1-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01051"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 76..83
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01051"
FT REGION 104..108
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01051"
FT REGION 119..122
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01051"
FT REGION 172..175
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01051"
FT REGION 207..216
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01051"
FT REGION 427..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 639..709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1123..1183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..25
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..487
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 656..696
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1123..1163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 76..83
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 438
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 478
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 492
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 504
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 516
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 518
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 523
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 574
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 578
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT HELIX 549..553
FT /evidence="ECO:0007829|PDB:4CLQ"
FT HELIX 560..567
FT /evidence="ECO:0007829|PDB:4CLQ"
FT HELIX 618..624
FT /evidence="ECO:0007829|PDB:4CLQ"
FT HELIX 629..634
FT /evidence="ECO:0007829|PDB:4CLQ"
SQ SEQUENCE 1183 AA; 135571 MW; 9A337F1EE0B0F21D CRC64;
MEQSNKQHRK AKEKNTAKKK LHTQGHNAKA FAVAAPGKMA RTMQRSSDVN ERKLHVPMVD
RTPEDDPPPF IVAVVGPPGT GKTTLIRSLV RRMTKSTLND IQGPITVVSG KHRRLTFLEC
PADDLNAMID IAKIADLVLL LIDGNFGFEM ETMEFLNIAQ HHGMPRVLGV ATHLDLFKSQ
STLRASKKRL KHRFWTEVYQ GAKLFYLSGV INGRYPDREI LNLSRFISVM KFRPLKWRNE
HPYMLADRFT DLTHPELIET QGLQIDRKVA IYGYLHGTPL PSAPGTRVHI AGVGDFSVAQ
IEKLPDPCPT PFYQQKLDDF EREKMKEEAK ANGEITTAST TRRRKRLDDK DKLIYAPMSD
VGGVLMDKDA VYIDIGKKNE EPSFVPGQER GEGEKLMTGL QSVEQSIAEK FDGVGLQLFS
NGTELHEVAD HEGMDVESGE ESIEDDEGKS KGRTSLRKPR IYGKPVQEED ADIDNLPSDE
EPYTNDDDVQ DSEPRMVEID FNNTGEQGAE KLALETDSEF EESEDEFSWE RTAANKLKKT
ESKKRTWNIG KLIYMDNISP EECIRRWRGE DDDSKDESDI EEDVDDDFFR KKDGTVTKEG
NKDHAVDLEK FVPYFDTFEK LAKKWKSVDA IKERFLGAGI LGNDNKTKSD SNEGGEELYG
DFEDLEDGNP SEQAEDNSDK ESEDEDENED TNGDDDNSFT NFDAEEKKDL TMEQEREMNA
AKKEKLRAQF EIEEGENFKE DDENNEYDTW YELQKAKISK QLEINNIEYQ EMTPEQRQRI
EGFKAGSYVR IVFEKVPMEF VKNFNPKFPI VMGGLLPTEI KFGIVKARLR RHRWHKKILK
TNDPLVLSLG WRRFQTLPIY TTTDSRTRTR MLKYTPEHTY CNAAFYGPLC SPNTPFCGVQ
IVANSDTGNG FRIAATGIVE EIDVNIEIVK KLKLVGFPYK IFKNTAFIKD MFSSAMEVAR
FEGAQIKTVS GIRGEIKRAL SKPEGHYRAA FEDKILMSDI VILRSWYPVR VKKFYNPVTS
LLLKEKTEWK GLRLTGQIRA AMNLETPSNP DSAYHKIERV ERHFNGLKVP KAVQKELPFK
SQIHQMKPQK KKTYMAKRAV VLGGDEKKAR SFIQKVLTIS KAKDSKRKEQ KASQRKERLK
KLAKMEEEKS QRDKEKKKEY FAQNGKRTTM GGDDESRPRK MRR
