SPB1_SCHPO
ID SPB1_SCHPO Reviewed; 802 AA.
AC O42832;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1999, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=AdoMet-dependent rRNA methyltransferase spb1 {ECO:0000255|HAMAP-Rule:MF_03163};
DE EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_03163};
DE AltName: Full=2'-O-ribose RNA methyltransferase {ECO:0000255|HAMAP-Rule:MF_03163};
DE AltName: Full=S-adenosyl-L-methionine-dependent methyltransferase {ECO:0000255|HAMAP-Rule:MF_03163};
GN Name=spb1; Synonyms=pmt2; ORFNames=SPAC1687.11;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 23-802.
RX PubMed=10620770;
RX DOI=10.1002/(sici)1097-0061(20000115)16:1<1::aid-yea501>3.0.co;2-k;
RA Hilti N., Graeub R., Joerg M., Arnold P., Schweingruber A.-M.,
RA Schweingruber M.E.;
RT "Gene sam1 encoding adenosylmethionine synthetase: effects of its
RT expression in the fission yeast Schizosaccharomyces pombe.";
RL Yeast 16:1-10(2000).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362, AND IDENTIFICATION BY
RP 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: Required for proper assembly of pre-ribosomal particles
CC during the biogenesis of the 60S ribosomal subunit. {ECO:0000255|HAMAP-
CC Rule:MF_03163}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleotide in rRNA + S-adenosyl-L-methionine = a 2'-O-
CC methylribonucleotide in rRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:48628, Rhea:RHEA-COMP:12164, Rhea:RHEA-COMP:12165,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:90675, ChEBI:CHEBI:90676; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03163};
CC -!- SUBUNIT: Component of the nucleolar and nucleoplasmic pre-60S ribosomal
CC particle. {ECO:0000255|HAMAP-Rule:MF_03163}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000255|HAMAP-
CC Rule:MF_03163}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RNA methyltransferase RlmE family. SPB1 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03163}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA11034.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CU329670; CAA22605.1; -; Genomic_DNA.
DR EMBL; AJ223010; CAA11034.1; ALT_SEQ; Genomic_DNA.
DR PIR; T37754; T37754.
DR PIR; T52474; T52474.
DR RefSeq; NP_593129.1; NM_001018525.2.
DR AlphaFoldDB; O42832; -.
DR SMR; O42832; -.
DR BioGRID; 278588; 6.
DR STRING; 4896.SPAC1687.11.1; -.
DR iPTMnet; O42832; -.
DR MaxQB; O42832; -.
DR PaxDb; O42832; -.
DR PRIDE; O42832; -.
DR EnsemblFungi; SPAC1687.11.1; SPAC1687.11.1:pep; SPAC1687.11.
DR GeneID; 2542112; -.
DR KEGG; spo:SPAC1687.11; -.
DR PomBase; SPAC1687.11; spb1.
DR VEuPathDB; FungiDB:SPAC1687.11; -.
DR eggNOG; KOG1098; Eukaryota.
DR HOGENOM; CLU_009422_8_1_1; -.
DR InParanoid; O42832; -.
DR OMA; LMWVFQQ; -.
DR PhylomeDB; O42832; -.
DR PRO; PR:O42832; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005730; C:nucleolus; ISO:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IBA:GO_Central.
DR GO; GO:0008173; F:RNA methyltransferase activity; IBA:GO_Central.
DR GO; GO:0016435; F:rRNA (guanine) methyltransferase activity; IBA:GO_Central.
DR GO; GO:0070039; F:rRNA (guanosine-2'-O-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008650; F:rRNA (uridine-2'-O-)-methyltransferase activity; ISO:PomBase.
DR GO; GO:0000453; P:enzyme-directed rRNA 2'-O-methylation; IEA:UniProtKB-UniRule.
DR GO; GO:0000466; P:maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); ISO:PomBase.
DR GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); ISO:PomBase.
DR GO; GO:0001510; P:RNA methylation; IBA:GO_Central.
DR GO; GO:0031167; P:rRNA methylation; IBA:GO_Central.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_01547; RNA_methyltr_E; 1.
DR HAMAP; MF_03163; RNA_methyltr_E_SPB1; 1.
DR InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom.
DR InterPro; IPR015507; rRNA-MeTfrase_E.
DR InterPro; IPR012920; rRNA_MeTfrase_SPB1-like_C.
DR InterPro; IPR024576; rRNA_MeTfrase_Spb1_DUF3381.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR028589; SPB1-like.
DR Pfam; PF11861; DUF3381; 1.
DR Pfam; PF01728; FtsJ; 1.
DR Pfam; PF07780; Spb1_C; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Methyltransferase; Nucleus; Phosphoprotein;
KW Reference proteome; Ribosome biogenesis; rRNA processing;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..802
FT /note="AdoMet-dependent rRNA methyltransferase spb1"
FT /id="PRO_0000155601"
FT REGION 423..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 487..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 569..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 718..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 347..389
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03163"
FT COMPBIAS 436..451
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..746
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 776..790
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 158
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03163"
FT BINDING 57
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03163"
FT BINDING 59
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03163"
FT BINDING 77
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03163"
FT BINDING 93
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03163"
FT BINDING 118
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03163"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 802 AA; 90906 MW; 12385E08E100A1E5 CRC64;
MGKSQKKTAK GRLDKWYKLA KEQGYRSRAA FKLVQLNQKY SFLEKAKVII DLCAAPGGWL
QVASKTCKPG SLIVGVDLAP IKPIPNCHTF VEDITSDKCR SQLRGYLKTW KADVVLHDGA
PNVGSAWLQD AYGQAQLVLM SMKLACEFLV AGGTFVTKVF RSRDYNNLLW VFKQLFNKVE
ATKPPSSRNV SAEIFVVCRG YKAPKKLDPR FTDPRTVFEE VQEPVTNVDA KVFHPEKRKR
SREGYADDDY TLHKTVLASE FVTANDPIQI LGTSAEIVFP KDDEECQRLY NLDVTTEEIL
LCCSDLQVLG KKEFRDILRW RLKIRDEMGI GKKVEDEQKT VVEEIPEMDE EERLDQELQD
LSEAERVKLK RERRKANQRK QREIVRMQMG MLAPMDIGLE HEAMGEDSLF GLATAEKHGL
KELENGTLPV TESVDEEVST DNEVEYDSDD ERDRLEADLD SMYSDYTKRK AESDVKYRVK
KARGDLDDEE WNGIDNGTES DDSQIAETNF ATPDKDRLTT SLLDKGSTKD GLSRKARMFF
DQDIFDGIED ADADVEIMSM NRAAIKKREA ELASQNNDDG SKGDQSEDSN DHIEVVPVAS
AHDEDDDWNS DSDNDENNVE IVTAEAMTLA QDIASRRKSK ADLIDEGYNR WSFQSKEGLP
DWFLDEETTV NKPNKPITKE AVLALREKMK ALNARPIKKV LEAQGRKKMR TIKRLQRVAK
KAEGISESGD MTESEKAKEI SRLVSRATKS KPKAKPTLVV AKGPNKGLKS RPKGVKGKYK
MVDSRMKKDL RAQKRLAKKG RR
