FBRL_DROER
ID FBRL_DROER Reviewed; 345 AA.
AC Q8I1F4; B3NP08;
DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=rRNA 2'-O-methyltransferase fibrillarin;
DE EC=2.1.1.-;
DE AltName: Full=Histone-glutamine methyltransferase;
GN Name=Fib {ECO:0000312|EMBL:AAO01021.1}; ORFNames=GG20072;
OS Drosophila erecta (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7220;
RN [1] {ECO:0000312|EMBL:AAO01021.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12537575; DOI=10.1186/gb-2002-3-12-research0086;
RA Bergman C.M., Pfeiffer B.D., Rincon-Limas D.E., Hoskins R.A., Gnirke A.,
RA Mungall C.J., Wang A.M., Kronmiller B., Pacleb J.M., Park S., Stapleton M.,
RA Wan K.H., George R.A., de Jong P.J., Botas J., Rubin G.M., Celniker S.E.;
RT "Assessing the impact of comparative genomic sequence data on the
RT functional annotation of the Drosophila genome.";
RL Genome Biol. 3:RESEARCH0086.1-RESEARCH0086.20(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14021-0224.01;
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
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 {ECO:0000250}. Note=Fibrillar
CC region of the nucleolus. {ECO:0000250}.
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; AY190941; AAO01021.1; -; Genomic_DNA.
DR EMBL; CH954179; EDV56741.1; -; Genomic_DNA.
DR RefSeq; XP_001976341.1; XM_001976305.2.
DR AlphaFoldDB; Q8I1F4; -.
DR SMR; Q8I1F4; -.
DR STRING; 7220.FBpp0138618; -.
DR EnsemblMetazoa; FBtr0140126; FBpp0138618; FBgn0064623.
DR GeneID; 6547316; -.
DR KEGG; der:6547316; -.
DR eggNOG; KOG1596; Eukaryota.
DR HOGENOM; CLU_059055_1_0_1; -.
DR OMA; INMATHR; -.
DR OrthoDB; 1411035at2759; -.
DR PhylomeDB; Q8I1F4; -.
DR Proteomes; UP000008711; Unassembled WGS sequence.
DR GO; GO:0015030; C:Cajal body; IEA:EnsemblMetazoa.
DR GO; GO:0001651; C:dense fibrillar component; ISS:UniProtKB.
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 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..345
FT /note="rRNA 2'-O-methyltransferase fibrillarin"
FT /id="PRO_0000148512"
FT REGION 1..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 198..199
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 217..218
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 242..243
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 262..265
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT MOD_RES 9
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 25
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P22509"
FT MOD_RES 41
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P22509"
FT MOD_RES 43
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P22509"
FT MOD_RES 49
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P22509"
FT MOD_RES 52
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P22509"
FT MOD_RES 59
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P22509"
FT MOD_RES 64
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P22509"
FT MOD_RES 72
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P22509"
FT MOD_RES 78
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P22509"
FT MOD_RES 84
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P22509"
FT MOD_RES 89
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P22509"
FT MOD_RES 94
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P22509"
FT MOD_RES 99
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P22509"
SQ SEQUENCE 345 AA; 34709 MW; F05DAB01491AE66F CRC64;
MGKPGFSPRG GGGGGGGGGG GFRGRGGGGG GGGGGGFGGG RGRGGGGDRG GRGGFGGGRG
GGGRGGGGGG GRGGFGGRGG GGGRGGGGRG GGGRGGGGRG GGAGGFKGGK TVTIEPHRHE
GVFIARGKED ALVTRNFVPG SEVYGEKRIS VENNGEKIEY RVWNPFRSKL AAAVLGGVEQ
IHMPPGSKVL YLGAASGTTV SHVSDVVGPE GLVYAVEFSH RSGRDLINVA KKRTNIIPII
EDARHPHKYR MLVGMVDTIF ADVAQPDQGR IVALNAQHFL KNGGHFVISI KASCIDSTAQ
PEAVFASEVK KMQADKLKPQ EQLTLEPYER DHAVVVGVYR PPPKQ
