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BMS1_SCHPO
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   03-AUG-2022, entry version 127.
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; 4896.SPBC31E1.06.1; -.
DR   iPTMnet; O94653; -.
DR   MaxQB; O94653; -.
DR   PaxDb; O94653; -.
DR   PRIDE; O94653; -.
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; QMEQQEF; -.
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; ISS:PomBase.
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; -; 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; PTHR12858; 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   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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