FBRL_GIAIN
ID FBRL_GIAIN Reviewed; 327 AA.
AC Q24957;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=rRNA 2'-O-methyltransferase fibrillarin;
DE EC=2.1.1.-;
DE AltName: Full=Histone-glutamine methyltransferase;
OS Giardia intestinalis (Giardia lamblia).
OC Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia.
OX NCBI_TaxID=5741;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 30957 / WB;
RX PubMed=9495039; DOI=10.1111/j.1550-7408.1998.tb05077.x;
RA Narcisi E.M., Glover C.V. III, Fechheimer M.;
RT "Fibrillarin, a conserved pre-ribosomal RNA processing protein of
RT Giardia.";
RL J. Eukaryot. Microbiol. 45:105-111(1998).
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 -!- SIMILARITY: Belongs to the methyltransferase superfamily. Fibrillarin
CC family. {ECO:0000305}.
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DR EMBL; L28115; AAA21687.1; -; Genomic_DNA.
DR PIR; T47231; T47231.
DR RefSeq; XP_001708536.1; XM_001708484.1.
DR AlphaFoldDB; Q24957; -.
DR SMR; Q24957; -.
DR PRIDE; Q24957; -.
DR GeneID; 5701450; -.
DR KEGG; gla:GL50803_0097219; -.
DR VEuPathDB; GiardiaDB:DHA2_97219; -.
DR VEuPathDB; GiardiaDB:GL50581_3741; -.
DR VEuPathDB; GiardiaDB:GL50803_0097219; -.
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 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..327
FT /note="rRNA 2'-O-methyltransferase fibrillarin"
FT /id="PRO_0000148514"
FT REGION 1..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..74
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 181..182
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 200..201
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 225..226
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 245..248
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT MOD_RES 10
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250"
FT MOD_RES 19
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250"
FT MOD_RES 44
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250"
FT MOD_RES 49
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250"
FT MOD_RES 55
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250"
FT MOD_RES 65
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250"
FT MOD_RES 69
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250"
FT MOD_RES 78
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 327 AA; 35243 MW; B6FF104CA60C8B7A CRC64;
MGTDYRNSGR GGRDGPGGRG PGNDRRDSGR SFGDRRPERP DFKRGDGGRG FGDRRGSGPP
GGPDRGDRRG PRDGPGGRGG PGGPGGGFKG GAKTMVKPHP KYDGIFISHG RGDVLVTKSL
APGVAVYGEK RISVEGTESK IEYREWNPFR SKLGAAVRLN VLDMPIKPGA KVLYLGAASG
TTVSHVSDIV GPTGAVYAVE FSQRSGRDLL EVAKARTNVY PIIADARHPY KYRMIVPEVD
CIFSDVAQPD QARIVAENAR YYLKANGGML ISIKASSVDS TLKPEAVFAR EIETLREHDF
KCKEQLDIGE FHRNHAIVVG RFRVKAA
