NEP1_SCHPO
ID NEP1_SCHPO Reviewed; 359 AA.
AC Q10107;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Ribosomal RNA small subunit methyltransferase mra1 {ECO:0000305};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q06287};
DE AltName: Full=18S rRNA (pseudouridine-N1)-methyltransferase {ECO:0000250|UniProtKB:Q06287};
DE AltName: Full=Multicopy suppressor of ras1-deficiency protein {ECO:0000303|PubMed:9133664};
GN Name=mra1 {ECO:0000303|PubMed:9133664};
GN ORFNames=SPAC18G6.07c {ECO:0000312|PomBase:SPAC18G6.07c};
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 [GENOMIC DNA], AND FUNCTION.
RC STRAIN=JY450;
RX PubMed=9133664; DOI=10.1046/j.1365-2443.1996.27029.x;
RA Hakuno F., Hughes D.A., Yamamoto M.;
RT "The Schizosaccharomyces pombe mra1 gene, which is required for cell growth
RT and mating, can suppress the mating inefficiency caused by a deficit in the
RT Ras1 activity.";
RL Genes Cells 1:303-315(1996).
RN [2]
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; THR-33 AND SER-100, AND
RP 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: S-adenosyl-L-methionine-dependent pseudouridine N(1)-
CC methyltransferase that methylates the pseudouridine corresponding to
CC position 1189 (Psi1189) in S.cerevisiae 18S rRNA. Involved the
CC biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3-
CC carboxypropyl) pseudouridine (m1acp3-Psi) conserved in eukaryotic 18S
CC rRNA. Has also an essential role in 40S ribosomal subunit biogenesis
CC independent on its methyltransferase activity, facilitating the
CC incorporation of ribosomal protein S19 during the formation of pre-
CC ribosomes (By similarity). Essential for cell growth. It also has a key
CC role in promoting the mating function (PubMed:9133664).
CC {ECO:0000250|UniProtKB:Q06287, ECO:0000269|PubMed:9133664}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a pseudouridine in 16S/18S rRNA + S-adenosyl-L-methionine = an
CC N(1)-methylpseudouridine in 16S/18S rRNA + H(+) + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:46696, Rhea:RHEA-COMP:11633, Rhea:RHEA-
CC COMP:11634, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:74890;
CC Evidence={ECO:0000250|UniProtKB:Q06287};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q06287}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q06287}.
CC -!- SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase
CC superfamily. RNA methyltransferase NEP1 family. {ECO:0000305}.
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DR EMBL; D78582; BAA24497.1; -; Genomic_DNA.
DR EMBL; CU329670; CAA92394.1; -; Genomic_DNA.
DR PIR; T37921; T37921.
DR RefSeq; NP_593671.1; NM_001019103.2.
DR AlphaFoldDB; Q10107; -.
DR SMR; Q10107; -.
DR BioGRID; 278615; 8.
DR STRING; 4896.SPAC18G6.07c.1; -.
DR iPTMnet; Q10107; -.
DR MaxQB; Q10107; -.
DR PaxDb; Q10107; -.
DR PRIDE; Q10107; -.
DR EnsemblFungi; SPAC18G6.07c.1; SPAC18G6.07c.1:pep; SPAC18G6.07c.
DR GeneID; 2542139; -.
DR KEGG; spo:SPAC18G6.07c; -.
DR PomBase; SPAC18G6.07c; mra1.
DR VEuPathDB; FungiDB:SPAC18G6.07c; -.
DR eggNOG; KOG3073; Eukaryota.
DR HOGENOM; CLU_055846_0_0_1; -.
DR InParanoid; Q10107; -.
DR OMA; PNCRKAT; -.
DR PhylomeDB; Q10107; -.
DR Reactome; R-SPO-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:Q10107; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0032040; C:small-subunit processome; ISO:PomBase.
DR GO; GO:0070037; F:rRNA (pseudouridine) methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0019843; F:rRNA binding; IBA:GO_Central.
DR GO; GO:0019236; P:response to pheromone; IEA:UniProtKB-KW.
DR GO; GO:0070475; P:rRNA base methylation; ISO:PomBase.
DR CDD; cd18088; Nep1-like; 1.
DR Gene3D; 3.40.1280.10; -; 1.
DR InterPro; IPR029028; Alpha/beta_knot_MTases.
DR InterPro; IPR005304; Rbsml_bgen_MeTrfase_EMG1/NEP1.
DR InterPro; IPR029026; tRNA_m1G_MTases_N.
DR PANTHER; PTHR12636; PTHR12636; 1.
DR Pfam; PF03587; EMG1; 1.
DR SUPFAM; SSF75217; SSF75217; 1.
PE 1: Evidence at protein level;
KW Methyltransferase; Nucleus; Pheromone response; Phosphoprotein;
KW Reference proteome; Ribosome biogenesis; RNA-binding; rRNA processing;
KW rRNA-binding; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..359
FT /note="Ribosomal RNA small subunit methyltransferase mra1"
FT /id="PRO_0000158613"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 98..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 287
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q06287"
FT BINDING 314
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q06287"
FT BINDING 319..321
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q06287"
FT BINDING 334..339
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q06287"
FT SITE 195
FT /note="Interaction with substrate rRNA"
FT /evidence="ECO:0000250|UniProtKB:Q06287"
FT SITE 197
FT /note="Stabilizes Arg-195"
FT /evidence="ECO:0000250|UniProtKB:Q06287"
FT SITE 236
FT /note="Interaction with substrate rRNA"
FT /evidence="ECO:0000250|UniProtKB:Q06287"
FT SITE 239
FT /note="Interaction with substrate rRNA"
FT /evidence="ECO:0000250|UniProtKB:Q06287"
FT SITE 243
FT /note="Interaction with substrate rRNA"
FT /evidence="ECO:0000250|UniProtKB:Q06287"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 33
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 359 AA; 39775 MW; D7753DD546E2E3EC CRC64;
MPTYSKRKSR GSLEVSEKTN QPKFIKRSQS SETITSGETA SELMQDEKEQ SNGAVGSIED
EELQRLRENQ ASVEALSKKP ESIDRELGVE ALEIDNVVKS DEEKEDPNGA SSKTVKARPL
PAGSVHRVTT HMAPIPARSI GSHDTTTQRL IVVLDQACLE IYKVGKAKDA KYQLLNCDDH
QGILKKLNRN IAQARPDITH QCLLTLLDSP LNKAGRLQVY IHTAKKVLIE VNPSVRIPRT
FKRFSGLMVQ LLHKLSIRSV NGNEKLLKVI KNPVTDYLPP NCRKATLSFD APTVPPRKYL
ETLQPNQSVC IAIGAMAHGP DDFSDGWVDE KISISDYPLS ASIACSKFLH SMEDFLGIV
