FBRL3_ARATH
ID FBRL3_ARATH Reviewed; 292 AA.
AC Q9FHB3;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Putative rRNA 2'-O-methyltransferase fibrillarin 3;
DE EC=2.1.1.-;
DE AltName: Full=Fibrillarin-like protein 3;
DE AltName: Full=Histone-glutamine methyltransferase;
GN Name=FIB3; OrderedLocusNames=At5g52490; ORFNames=K24M7.24;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=10829025; DOI=10.1074/jbc.m002996200;
RA Barneche F., Steinmetz F., Echeverria M.;
RT "Fibrillarin genes encode both a conserved nucleolar protein and a novel
RT small nucleolar RNA involved in ribosomal RNA methylation in Arabidopsis
RT thaliana.";
RL J. Biol. Chem. 275:27212-27220(2000).
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Note=Fibrillar
CC region of the nucleolus. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Not detectable by RT-PCR.
CC {ECO:0000269|PubMed:10829025}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. Fibrillarin
CC family. {ECO:0000305}.
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DR EMBL; AB019226; BAB10546.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96221.1; -; Genomic_DNA.
DR RefSeq; NP_568773.1; NM_124628.1.
DR AlphaFoldDB; Q9FHB3; -.
DR SMR; Q9FHB3; -.
DR BioGRID; 20570; 78.
DR STRING; 3702.AT5G52490.1; -.
DR PaxDb; Q9FHB3; -.
DR PRIDE; Q9FHB3; -.
DR EnsemblPlants; AT5G52490.1; AT5G52490.1; AT5G52490.
DR GeneID; 835325; -.
DR Gramene; AT5G52490.1; AT5G52490.1; AT5G52490.
DR KEGG; ath:AT5G52490; -.
DR Araport; AT5G52490; -.
DR TAIR; locus:2156682; AT5G52490.
DR eggNOG; KOG1596; Eukaryota.
DR HOGENOM; CLU_059055_1_0_1; -.
DR OMA; CEEKHAC; -.
DR OrthoDB; 1411035at2759; -.
DR PhylomeDB; Q9FHB3; -.
DR PRO; PR:Q9FHB3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FHB3; baseline and differential.
DR Genevisible; Q9FHB3; AT.
DR GO; GO:0031428; C:box C/D RNP complex; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
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:0031167; P:rRNA methylation; IBA:GO_Central.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR000692; Fibrillarin.
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.
PE 2: Evidence at transcript level;
KW Methyltransferase; Nucleus; Reference proteome; Ribonucleoprotein;
KW RNA-binding; rRNA processing; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..292
FT /note="Putative rRNA 2'-O-methyltransferase fibrillarin 3"
FT /id="PRO_0000148520"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 146..147
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 165..166
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 190..191
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 210..213
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
SQ SEQUENCE 292 AA; 31706 MW; 41454BB12D1C8144 CRC64;
MKPPQRGRGG GVRGGRGLAR GGEGSAVRGS GRGGESGRGR GPGRVKSESD GGIKGGSKVL
VTPHRHAGVF VAKSKADALV TKNLVPGEII YNEKRIFVQN EDRSTVEYRV WNPHRSKLAD
AITTGVDNIW IKPGVKVLYL GASSGYTVSH VSDIVGPEGC VYAVEHSDIC GKVLMNMAEK
RTNVIPIIED ARHPAKYRML VGMVDIIFSD VNHPEQANIL SLNASYFLKS GGHFMISIKA
NSIDSTIAAE TVYQMEVEKL QMEELRPTEI LHLDSCEEKH ACVFGGYRLP RK
