FBRL_LEIMA
ID FBRL_LEIMA Reviewed; 297 AA.
AC P35549;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=rRNA 2'-O-methyltransferase fibrillarin;
DE EC=2.1.1.-;
DE AltName: Full=Histone-glutamine methyltransferase;
OS Leishmania major.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5664;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=V121;
RX PubMed=7935615; DOI=10.1016/0166-6851(94)00047-6;
RA Cappai R., Osborn A.H., Handman E.;
RT "Cloning and sequence of a Leishmania major homologue to the fibrillarin
RT gene.";
RL Mol. Biochem. Parasitol. 64:353-355(1994).
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; L26252; AAA67420.1; -; Genomic_DNA.
DR AlphaFoldDB; P35549; -.
DR SMR; P35549; -.
DR STRING; 5664.LmjF.36.3070; -.
DR VEuPathDB; TriTrypDB:LmjF.36.3070; -.
DR VEuPathDB; TriTrypDB:LMJLV39_360040100; -.
DR VEuPathDB; TriTrypDB:LMJSD75_360040000; -.
DR eggNOG; KOG1596; Eukaryota.
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; Ribonucleoprotein; RNA-binding;
KW rRNA processing; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..297
FT /note="rRNA 2'-O-methyltransferase fibrillarin"
FT /id="PRO_0000148515"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 149..150
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 168..169
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 192..193
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 212..215
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250"
FT MOD_RES 7
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250"
FT MOD_RES 12
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250"
FT MOD_RES 16
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250"
FT MOD_RES 19
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250"
FT MOD_RES 24
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250"
FT MOD_RES 28
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250"
FT MOD_RES 32
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250"
FT MOD_RES 36
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250"
FT MOD_RES 40
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250"
FT MOD_RES 44
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250"
FT MOD_RES 48
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250"
FT MOD_RES 52
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 297 AA; 31329 MW; 069EE98F9E27ABD2 CRC64;
MRGGFGRGGG GRGGSRGGRG GFGRGGGRGG GRGGGRGGGR GGGRGGGRGG GRGGAGAKVI
VEPHMLHPGV FISKAKTDSL CTLNMVPGIS VYGEKRIELG ATQGGDDKKE YRLWNPYRSK
LASAIYAGVS SIHMGPGSKV LYLGGATGTT VSHVSDLVGP EGMVYAVEFS HRVGRDLVEM
SKRRPIVPIV EDARYPMKYR MLVPMVDCIF MDVAQPDQAR ILALNAQAFL QNGGHYVISI
KANCIDSTLE APVVIASELN KLKKDKLKPL EQVSLEPFER DHAVVVGVYR PVKKSKQ
