ID BMS1_SCHPO Reviewed; 1121 AA.
AC O94653; Q9HGM0;
DT 13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 13-DEC-2002, sequence version 2.
DT 27-MAR-2024, entry version 133.
DE RecName: Full=Ribosome biogenesis protein bms1;
GN Name=bms1; ORFNames=SPBC31E1.06, SPBC800.01;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438; SER-442; SER-464;
RP SER-474; SER-476 AND SER-546, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: May act as a molecular switch during maturation of the 40S
CC ribosomal subunit in the nucleolus. {ECO:0000250|UniProtKB:Q08965}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:16823372}.
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; CU329671; CAB39140.1; -; Genomic_DNA.
DR RefSeq; NP_595102.2; NM_001021009.2.
DR AlphaFoldDB; O94653; -.
DR SMR; O94653; -.
DR BioGRID; 276918; 3.
DR STRING; 284812.O94653; -.
DR iPTMnet; O94653; -.
DR MaxQB; O94653; -.
DR PaxDb; 4896-SPBC31E1-06-1; -.
DR EnsemblFungi; SPBC31E1.06.1; SPBC31E1.06.1:pep; SPBC31E1.06.
DR GeneID; 2540390; -.
DR KEGG; spo:SPBC31E1.06; -.
DR PomBase; SPBC31E1.06; bms1.
DR VEuPathDB; FungiDB:SPBC31E1.06; -.
DR eggNOG; KOG1951; Eukaryota.
DR HOGENOM; CLU_002486_0_0_1; -.
DR InParanoid; O94653; -.
DR OMA; KLHVPMV; -.
DR PhylomeDB; O94653; -.
DR Reactome; R-SPO-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:O94653; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0030686; C:90S preribosome; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; ISS:PomBase.
DR GO; GO:0072686; C:mitotic spindle; HDA:PomBase.
DR GO; GO:0005730; C:nucleolus; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0034511; F:U3 snoRNA binding; IBA:GO_Central.
DR GO; GO:0000479; P:endonucleolytic cleavage of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
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:0042255; P:ribosome assembly; ISS:PomBase.
DR CDD; cd01882; BMS1; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR012948; AARP2CN.
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; RIBOSOME BIOGENESIS PROTEIN; 1.
DR PANTHER; PTHR12858:SF2; RIBOSOME BIOGENESIS PROTEIN BMS1 HOMOLOG; 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; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51714; G_BMS1; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Cytoskeleton; GTP-binding; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Ribosome biogenesis.
FT CHAIN 1..1121
FT /note="Ribosome biogenesis protein bms1"
FT /id="PRO_0000195005"
FT DOMAIN 72..237
FT /note="Bms1-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01051"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 81..88
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01051"
FT REGION 109..113
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01051"
FT REGION 124..127
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01051"
FT REGION 176..179
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01051"
FT REGION 211..220
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01051"
FT REGION 603..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1060..1085
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1099..1121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..632
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1106..1121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 81..88
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 438
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 442
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 464
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 474
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 476
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 546
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 1121 AA; 127645 MW; 5C462D8AB16A96F8 CRC64;
MDEKKGHYAK HSGPKAEKKK LKKVSDGSAS NNPKAFAVAS AGRMARQAMR TADISQKKLH
VPMVDRTPDE APPPVIVAVM GPPGTGKSTL IKSLVRRYSK YTISQITGPI TVVAGKKRRI
TFLECPNDLS SMIDVAKIAD LVLLLIDANF GFEMETMEFL NILAPHGMPR IMGVLTHLDL
FKKTSTLREA KKRLKHRFWT ELYQGAKLFY LSGVLNGRYP DREILNLSRF ISVMKFRPLR
WRNQHPYLLA DRMEDLTLPV DIEQNPKVGR KITLYGYLHG TNLPKHDASV HIPGVGDFVT
SDVSSLEDPC PPPDADKVRR RRLSEKQKLI YGPMADIGGI LFDKDRVYIE VPTSNFSKDE
NSEAGFGERM VMQLQEAQQP LGVDGNSGLQ LFSNSDAIDT VDRESSEIDN VGRKTRRQPT
GLINQELIKE DEGAFDDSDV NSADENEDVD FTGKIGAINN EDESDNEEVA FADSDSDLGG
QFDDEDSNLR WKEGLASKAA LAYSQSGKRR RNIQKIFYDE SLSPKDAYAE YKGESAKSSE
SDLVVSDDEE DFFKVSKVAN ESISSNHEKL MESESDRLSK KWENPQLLAQ LKSRFITGSL
LDSIEGQEEV SQDDEEGDFE DLEDEENSSD NEMEESSGSS VTAENEESAD EVDFQTEREE
NARKKEELRL RFEEEDRGDP EKKDVDWYTE EKEKIARQLV INREAFEDMD PESRAEIEGY
RAGTYVRIVI NDVPFEFVEH FDSRYPVVVG GLLPNEQRYG LVQVRIKRHR WHKKILKTND
PLIFSMGWRR FQSIPVYSIS DSRTRNRMLK YTPEHMHCFG TFYGPFVAPN SGFCAVQSVA
NSFAKAGSFR IAATGSVLNI DQSTDIVKKL KLTGVPYKIF KNTAFIKKMF SSPLEVAKFE
GANIRTVSGI RGQVKKAVDQ EHGHFRATFE DKILMSDIVF LRAWYPVQVR KFCTMVTNLL
ETDKTEWNGM RLTGEVRHEL GLKTPLRPNS QYQEIVRPSR HFNPLKVPAS LQAQLPFNSR
QKALRPRSKP TYMQKRTVLL NAEERKVRDL LQKVMTLHTD KEAKRKAKKA AEHERYHKRM
QKEEQAYIEK KREEKAEWFA QHGKRLRQDG NSSGSGKRSK N
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