FBRL_CAEEL
ID FBRL_CAEEL Reviewed; 352 AA.
AC Q22053;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=rRNA 2'-O-methyltransferase fibrillarin;
DE EC=2.1.1.- {ECO:0000250|UniProtKB:P15646};
DE AltName: Full=Histone-glutamine methyltransferase;
GN Name=fib-1 {ECO:0000312|WormBase:T01C3.7};
GN ORFNames=T01C3.7 {ECO:0000312|WormBase:T01C3.7};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=22768349; DOI=10.1371/journal.pone.0040290;
RA Korcekova D., Gombitova A., Raska I., Cmarko D., Lanctot C.;
RT "Nucleologenesis in the Caenorhabditis elegans embryo.";
RL PLoS ONE 7:E40290-E40290(2012).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26492166; DOI=10.1371/journal.pgen.1005580;
RA Yi Y.H., Ma T.H., Lee L.W., Chiou P.T., Chen P.H., Lee C.M., Chu Y.D.,
RA Yu H., Hsiung K.C., Tsai Y.T., Lee C.C., Chang Y.S., Chan S.P., Tan B.C.,
RA Lo S.J.;
RT "A Genetic Cascade of let-7-ncl-1-fib-1 Modulates Nucleolar Size and rRNA
RT Pool in Caenorhabditis elegans.";
RL PLoS Genet. 11:E1005580-E1005580(2015).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that has
CC the ability to methylate both RNAs and proteins (By similarity).
CC Involved in pre-rRNA processing. Utilizes the methyl donor S-adenosyl-
CC L-methionine to catalyze the site-specific 2'-hydroxyl methylation of
CC ribose moieties in pre-ribosomal RNA (By similarity). Site specificity
CC is provided by a guide RNA that base pairs with the substrate.
CC Methylation occurs at a characteristic distance from the sequence
CC involved in base pairing with the guide RNA (By similarity). Also acts
CC as a protein methyltransferase by mediating methylation of 'Gln-105' of
CC histone H2A (H2AQ105me), a modification that impairs binding of the
CC FACT complex and is specifically present at 35S ribosomal DNA locus (By
CC similarity). Plays a role in modulation of nucleolus size most likely
CC through regulating the ribosomal RNA (rRNA) pool (PubMed:26492166).
CC {ECO:0000250|UniProtKB:P15646, ECO:0000269|PubMed:26492166}.
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:P15646};
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:0000269|PubMed:22768349}.
CC Nucleus, nucleoplasm {ECO:0000269|PubMed:22768349}. Note=Fibrillar
CC region of the nucleolus. Predominantly localizes to the nucleolus, but
CC also localizes to small punctate structures throughout the nucleoplasm.
CC Co-localizes with dao-5 in nucleoli. {ECO:0000269|PubMed:22768349}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout embryonic development and in
CC adults. During embryogenesis, expressed from the 2-cell stage and
CC persists throughout development in nucleoli containing cells.
CC {ECO:0000269|PubMed:22768349}.
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}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in reduced 26S
CC ribosomal RNA (rRNA) expression. RNAi-mediated knockdown in a ncl-1
CC (e1942) mutant background suppresses the enlarged nucleoli phenotype in
CC the single ncl-1 mutant. RNAi-mediated knockdown in a ncl-1 (e1942)
CC mutant background suppresses the increased 26S rRNA expression in the
CC single ncl-1 mutant. {ECO:0000269|PubMed:26492166}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. Fibrillarin
CC family. {ECO:0000305}.
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DR EMBL; BX284605; CAB01657.1; -; Genomic_DNA.
DR PIR; T24279; T24279.
DR RefSeq; NP_506691.1; NM_074290.4.
DR AlphaFoldDB; Q22053; -.
DR SMR; Q22053; -.
DR BioGRID; 44995; 53.
DR DIP; DIP-26332N; -.
DR STRING; 6239.T01C3.7.1; -.
DR iPTMnet; Q22053; -.
DR EPD; Q22053; -.
DR PaxDb; Q22053; -.
DR PeptideAtlas; Q22053; -.
DR EnsemblMetazoa; T01C3.7.1; T01C3.7.1; WBGene00001423.
DR EnsemblMetazoa; T01C3.7.2; T01C3.7.2; WBGene00001423.
DR GeneID; 179999; -.
DR KEGG; cel:CELE_T01C3.7; -.
DR UCSC; T01C3.7.1; c. elegans.
DR CTD; 179999; -.
DR WormBase; T01C3.7; CE12920; WBGene00001423; fib-1.
DR eggNOG; KOG1596; Eukaryota.
DR GeneTree; ENSGT00550000074792; -.
DR HOGENOM; CLU_059055_1_0_1; -.
DR InParanoid; Q22053; -.
DR OMA; INMATHR; -.
DR OrthoDB; 1411035at2759; -.
DR PhylomeDB; Q22053; -.
DR Reactome; R-CEL-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:Q22053; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00001423; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0031428; C:box C/D RNP complex; IBA:GO_Central.
DR GO; GO:0015030; C:Cajal body; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IDA:WormBase.
DR GO; GO:0005654; C:nucleoplasm; IDA:WormBase.
DR GO; GO:0032040; C:small-subunit processome; IBA:GO_Central.
DR GO; GO:1990259; F:histone-glutamine methyltransferase activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0008649; F:rRNA methyltransferase activity; IBA:GO_Central.
DR GO; GO:0000494; P:box C/D RNA 3'-end processing; IBA:GO_Central.
DR GO; GO:1990258; P:histone glutamine methylation; IBA:GO_Central.
DR GO; GO:0017126; P:nucleologenesis; IMP:UniProtKB.
DR GO; GO:0045727; P:positive regulation of translation; IMP:WormBase.
DR GO; GO:0031167; P:rRNA methylation; IBA:GO_Central.
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..352
FT /note="rRNA 2'-O-methyltransferase fibrillarin"
FT /id="PRO_0000148511"
FT REGION 1..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 203..204
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 222..223
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 247..248
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 267..270
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT MOD_RES 8
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 23
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250"
FT MOD_RES 27
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250"
FT MOD_RES 35
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250"
FT MOD_RES 43
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250"
FT MOD_RES 51
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250"
FT MOD_RES 55
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250"
FT MOD_RES 58
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250"
FT MOD_RES 63
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250"
FT MOD_RES 67
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250"
FT MOD_RES 70
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250"
FT MOD_RES 75
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250"
FT MOD_RES 81
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250"
FT MOD_RES 85
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250"
FT MOD_RES 91
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250"
FT MOD_RES 95
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250"
FT MOD_RES 98
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250"
FT MOD_RES 102
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250"
FT MOD_RES 105
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250"
FT MOD_RES 112
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 352 AA; 36383 MW; 52FDE6555DBCB717 CRC64;
MGRPEFNRGG GGGGFRGGRG GDRGGSRGGF GGGGRGGYGG GDRGSFGGGD RGGFRGGRGG
GDRGGFRGGR GGGDRGGFGG RGSPRGGFGG RGSPRGGRGS PRGGRGGAGG MRGGKTVVVE
PHRLGGVFIV KGKEDALATK NMVVGESVYG EKRVSVDDGA GSIEYRVWNP FRSKLAASIM
GGLENTHIKP GTKLLYLGAA SGTTVSHCSD VVGPEGIVYA VEFSHRSGRD LLGVAKKRPN
VVPIVEDARH PHKYRMLVGM VDVIFSDVAQ PDQARIVALN AQNFLRNGGH AVISIKANCI
DSTAEPEAVF AGEVNKLKEE KFKPLEQVTL EPYERDHAVV VAVYRPVKGK KV
