ID   FBRL_TETTH              Reviewed;         294 AA.
AC   Q27200;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2001, sequence version 2.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=rRNA 2'-O-methyltransferase fibrillarin;
DE            EC=2.1.1.-;
DE   AltName: Full=Histone-glutamine methyltransferase;
GN   Name=FIB;
OS   Tetrahymena thermophila.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC   Tetrahymena.
OX   NCBI_TaxID=5911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9201715; DOI=10.1091/mbc.8.6.1051;
RA   David E., McNeil J.B., Basile V., Pearlman R.E.;
RT   "An unusual fibrillarin gene and protein: structure and functional
RT   implications.";
RL   Mol. Biol. Cell 8:1051-1061(1997).
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. It is associated with the U3, U8 and U13 small
CC       nuclear RNAs. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Note=Fibrillar region of the
CC       nucleolus.
CC   -!- PTM: By homology to other fibrillarins, some or all of the N-terminal
CC       domain arginines are modified to asymmetric dimethylarginine (DMA).
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. Fibrillarin
CC       family. {ECO:0000305}.
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DR   EMBL; X77962; CAA54924.2; -; mRNA.
DR   AlphaFoldDB; Q27200; -.
DR   SMR; Q27200; -.
DR   OMA; INMATHR; -.
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   2: Evidence at transcript level;
KW   Methylation; Methyltransferase; Nucleus; Ribonucleoprotein; RNA-binding;
KW   rRNA processing; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..294
FT                   /note="rRNA 2'-O-methyltransferase fibrillarin"
FT                   /id="PRO_0000148517"
FT   REGION          1..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         151..152
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         170..171
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         195..196
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         215..218
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         27
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         47
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         61
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   294 AA;  31288 MW;  3D08CE04A9AC6972 CRC64;
     MGKDFKSGGG NAGGKPFNKG PGGPGGRPFN KGPGGPGGPG GKFGGGRPGG PGGKFGAKGP
     RGPKTIIVKH RLEGVFICKG QQEALVTKNF FPGESVYNEK RMSVEENGEK IEYRVWNPYR
     SKIAAAVVGG ISDIHIKPGS KVLYLGGASG TTVSHVADIV GPTGVVYAVE FSHRSGRDLV
     NMAKKRTNVV PIIGDARKPQ EYRFLVGMVD VVFADVAQPD QARIMGMNCQ YFLKNGGHFL
     ISIKACCIDS TNEPAVVFAA EVQKLKEEGL KPEQQLTLEP YERDHAMVLG SYRA