FBRL_XENLA
ID FBRL_XENLA Reviewed; 323 AA.
AC P22232;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=rRNA 2'-O-methyltransferase fibrillarin;
DE EC=2.1.1.- {ECO:0000250|UniProtKB:P22087};
DE AltName: Full=Histone-glutamine methyltransferase;
DE AltName: Full=U6 snRNA 2'-O-methyltransferase fibrillarin {ECO:0000305};
GN Name=fbl;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2136767; DOI=10.1128/mcb.10.1.430-434.1990;
RA Lapeyre B., Mariottini P., Mathieu C., Ferrer P., Amaldi F., Amalric F.,
RA Caizergues-Ferrer M.;
RT "Molecular cloning of Xenopus fibrillarin, a conserved U3 small nuclear
RT ribonucleoprotein recognized by antisera from humans with autoimmune
RT disease.";
RL Mol. Cell. Biol. 10:430-434(1990).
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 by catalyzing the site-specific 2'-hydroxyl methylation of
CC ribose moieties in pre-ribosomal RNA. Probably catalyzes 2'-O-
CC methylation of U6 snRNAs in box C/D RNP complexes. U6 snRNA 2'-O-
CC methylation is required for mRNA splicing fidelity. Also acts as a
CC protein methyltransferase by mediating methylation of 'Gln-105' of
CC histone H2A (H2AQ104me), a modification that impairs binding of the
CC FACT complex and is specifically present at 35S ribosomal DNA locus.
CC {ECO:0000250|UniProtKB:P15646, ECO:0000250|UniProtKB:P22087}.
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 Evidence={ECO:0000250|UniProtKB:P22087};
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;
CC Evidence={ECO:0000250|UniProtKB:P15646};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48629;
CC Evidence={ECO:0000250|UniProtKB:P15646};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleotide in U6 snRNA + S-adenosyl-L-methionine = a 2'-
CC O-methylribonucleotide in U6 snRNA + H(+) + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:63088, Rhea:RHEA-COMP:16262, Rhea:RHEA-
CC COMP:16263, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:90675, ChEBI:CHEBI:90676;
CC Evidence={ECO:0000250|UniProtKB:P22087};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63089;
CC Evidence={ECO:0000250|UniProtKB:P22087};
CC -!- SUBUNIT: Component of box C/D small nucleolar ribonucleoprotein
CC (snoRNP) particles. {ECO:0000250|UniProtKB:P22087}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:P22087}. Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:P35550}. Note=Fibrillar region of the nucleolus.
CC {ECO:0000250|UniProtKB:P22087}.
CC -!- PTM: By homology to other fibrillarins, some or all of the N-terminal
CC domain arginines are modified to asymmetric dimethylarginine (DMA).
CC {ECO:0000250|UniProtKB:P22509}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. Fibrillarin
CC family. {ECO:0000305}.
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DR EMBL; M28874; AAA49710.1; -; mRNA.
DR PIR; I51417; I51417.
DR AlphaFoldDB; P22232; -.
DR SMR; P22232; -.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:1990259; F:histone-glutamine methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:1990258; P:histone glutamine methylation; ISS:UniProtKB.
DR GO; GO:0031167; P:rRNA methylation; ISS:UniProtKB.
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 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; Reference proteome;
KW Ribonucleoprotein; RNA-binding; rRNA processing; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..323
FT /note="rRNA 2'-O-methyltransferase fibrillarin"
FT /id="PRO_0000148510"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 276..308
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 174..175
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9Y9U3"
FT BINDING 193..194
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P22087"
FT BINDING 218..219
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P22087"
FT BINDING 238..241
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P22087"
FT MOD_RES 8
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P22509"
FT MOD_RES 17
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P22509"
FT MOD_RES 23
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P22509"
FT MOD_RES 29
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P22509"
SQ SEQUENCE 323 AA; 34332 MW; 1A27CEDDE78BECE6 CRC64;
MRPGFSPRGG RGGFGDRGGF GGRGGFGDRG GFRGGSRGGF GGRGRGGDRG GRGGFRGGFS
SPGRGGPRGG GRGGFGGGRG GFGAGRKVIV EPHRHEGIFI CRGKEDALVT KNLVPGESVY
GEKRISVEDG EVKTEYRAWN PFRSKIAAAI LGGVDQIHIK PGVKVLYLGA ASGTTVSHVS
DVVGPEGLVY AVEFSHRSGR DLINVAKKRT NIIPVIEDAR HPHKYRILVG MVDVVFADVA
QPDQTRIVAL NAHNFLKNGG HFVISIKANC IDSTAAPEAV FAAEVKKMQQ ENMKPQEQLT
LEPYERDHAV VVGIYRPPPK QKK
