ID   FBRL_ENCCU              Reviewed;         291 AA.
AC   Q8SR42;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=rRNA 2'-O-methyltransferase fibrillarin;
DE            EC=2.1.1.-;
DE   AltName: Full=Histone-glutamine methyltransferase;
GN   Name=NOP1; OrderedLocusNames=ECU10_0820;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
CC   -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that has
CC       the ability to methylate both RNAs and proteins. Involved in pre-rRNA
CC       processing. Utilizes the methyl donor S-adenosyl-L-methionine to
CC       catalyze the site-specific 2'-hydroxyl methylation of ribose moieties
CC       in pre-ribosomal RNA. Site specificity is provided by a guide RNA that
CC       base pairs with the substrate. Methylation occurs at a characteristic
CC       distance from the sequence involved in base pairing with the guide RNA.
CC       Also acts as a protein methyltransferase by mediating methylation of
CC       'Gln-105' of histone H2A (H2AQ105me), a modification that impairs
CC       binding of the FACT complex and is specifically present at 35S
CC       ribosomal DNA locus (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-glutaminyl-[histone H2A] + S-adenosyl-L-methionine = H(+) +
CC         N(5)-methyl-L-glutaminyl-[histone H2A] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:50904, Rhea:RHEA-COMP:12837, Rhea:RHEA-COMP:12839,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30011, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61891;
CC   -!- SUBUNIT: Component of box C/D small nucleolar ribonucleoprotein
CC       (snoRNP) particles. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Note=Fibrillar
CC       region of the nucleolus. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. Fibrillarin
CC       family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AL590449; CAD25801.1; -; Genomic_DNA.
DR   RefSeq; NP_586197.1; NM_001042030.1.
DR   AlphaFoldDB; Q8SR42; -.
DR   SMR; Q8SR42; -.
DR   STRING; 284813.Q8SR42; -.
DR   GeneID; 859846; -.
DR   KEGG; ecu:ECU10_0820; -.
DR   VEuPathDB; MicrosporidiaDB:ECU10_0820; -.
DR   HOGENOM; CLU_059055_1_0_1; -.
DR   InParanoid; Q8SR42; -.
DR   OMA; INMATHR; -.
DR   OrthoDB; 1411035at2759; -.
DR   Proteomes; UP000000819; Chromosome X.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   HAMAP; MF_00351; RNA_methyltransf_FlpA; 1.
DR   InterPro; IPR000692; Fibrillarin.
DR   InterPro; IPR020813; Fibrillarin_CS.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF01269; Fibrillarin; 1.
DR   PIRSF; PIRSF006540; Nop17p; 1.
DR   PRINTS; PR00052; FIBRILLARIN.
DR   SMART; SM01206; Fibrillarin; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS00566; FIBRILLARIN; 1.
PE   3: Inferred from homology;
KW   Methylation; Methyltransferase; Nucleus; Reference proteome;
KW   Ribonucleoprotein; RNA-binding; rRNA processing; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..291
FT                   /note="rRNA 2'-O-methyltransferase fibrillarin"
FT                   /id="PRO_0000148524"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..33
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         134..135
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         153..154
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         178..179
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         198..201
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         28
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         62
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   291 AA;  32356 MW;  899BD4F05C20E071 CRC64;
     MKKTNKRPDG RKFQKGGKPF RSDKGEGRGR MNNKKKGSVN AGLDRKVLVE PHPRFPGVYI
     SRGKEDLLLT RNLVPGVSVY GEKRVAVDLE GMKVEYRVWN AYRSKLAAGI VCGAENIHME
     PGSKVLYLGA SSGTTVSHVS DIVGKDGVVY AVEFSERSGR DLINMSMKRP NIVPIIEDAR
     YPSRYRMLVP IVDCIFSDVS QPDQTRIVAL NAQYFLKEGG GVDVSIKANC VNSAVPAETV
     FADEVNILRK NSIRPKEQVT LEPFEKDHAM IIGRFKLSAS EEKRQSSQKK D