FBRL1_ARATH
ID FBRL1_ARATH Reviewed; 308 AA.
AC Q9FEF8; B3H6E7; Q0WLG3; Q9FUZ8; Q9SP30;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=rRNA 2'-O-methyltransferase fibrillarin 1;
DE Short=AtFbr1 {ECO:0000303|PubMed:10806224};
DE Short=AtFib1 {ECO:0000303|PubMed:10829025};
DE EC=2.1.1.- {ECO:0000305|PubMed:10829025};
DE AltName: Full=Fibrillarin-like protein 1;
DE AltName: Full=Histone-glutamine methyltransferase;
DE AltName: Full=SKP1-interacting partner 7 {ECO:0000303|PubMed:11387208};
GN Name=FIB1 {ECO:0000303|PubMed:10829025};
GN Synonyms=FBR1 {ECO:0000303|PubMed:10806224},
GN MED36_2 {ECO:0000303|PubMed:22021418}, MED36B,
GN SKIP7 {ECO:0000303|PubMed:11387208};
GN OrderedLocusNames=At5g52470 {ECO:0000312|Araport:AT5G52470};
GN ORFNames=K24M7.22 {ECO:0000312|EMBL:BAB10544.1};
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 [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP SUBCELLULAR LOCATION, AND 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).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION, SUBCELLULAR
RP LOCATION, AND DOMAIN.
RX PubMed=10806224; DOI=10.1104/pp.123.1.51;
RA Pih K.T., Yi M.J., Liang Y.S., Shin B.J., Cho M.J., Hwang I., Son D.;
RT "Molecular cloning and targeting of a fibrillarin homolog from
RT Arabidopsis.";
RL Plant Physiol. 123:51-58(2000).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 205-308, AND INTERACTION WITH SKP1A.
RX PubMed=11387208; DOI=10.1093/emboj/20.11.2742;
RA Farras R., Ferrando A., Jasik J., Kleinow T., Oekresz L., Tiburcio A.,
RA Salchert K., del Pozo C., Schell J., Koncz C.;
RT "SKP1-SnRK protein kinase interactions mediate proteasomal binding of a
RT plant SCF ubiquitin ligase.";
RL EMBO J. 20:2742-2756(2001).
RN [8]
RP NOMENCLATURE.
RX PubMed=22021418; DOI=10.1104/pp.111.188300;
RA Mathur S., Vyas S., Kapoor S., Tyagi A.K.;
RT "The Mediator complex in plants: structure, phylogeny, and expression
RT profiling of representative genes in a dicot (Arabidopsis) and a monocot
RT (rice) during reproduction and abiotic stress.";
RL Plant Physiol. 157:1609-1627(2011).
RN [9]
RP FUNCTION.
RX PubMed=29163603; DOI=10.3389/fpls.2017.01878;
RA Rodriguez-Corona U., Pereira-Santana A., Sobol M., Rodriguez-Zapata L.C.,
RA Hozak P., Castano E.;
RT "Novel ribonuclease activity differs between fibrillarins from Arabidopsis
RT thaliana.";
RL Front. Plant Sci. 8:1878-1878(2017).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that has
CC the ability to methylate both RNAs and proteins (Probable). Involved in
CC pre-rRNA processing. Utilizes the methyl donor S-adenosyl-L-methionine
CC to catalyze the site-specific 2'-hydroxyl methylation of ribose
CC moieties in pre-ribosomal RNA (Probable). Site specificity is provided
CC by a guide RNA that base pairs with the substrate (Probable).
CC Methylation occurs at a characteristic distance from the sequence
CC involved in base pairing with the guide RNA (Probable). Also acts as a
CC 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). Binds monophosphate phosphoinositides in vitro
CC (PubMed:29163603). {ECO:0000250|UniProtKB:P15646,
CC ECO:0000269|PubMed:29163603, ECO:0000305|PubMed:10829025}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleotide in rRNA + S-adenosyl-L-methionine = a 2'-O-
CC methylribonucleotide in rRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:48628, Rhea:RHEA-COMP:12164, Rhea:RHEA-COMP:12165,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:90675, ChEBI:CHEBI:90676;
CC Evidence={ECO:0000305|PubMed:10829025};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48629;
CC Evidence={ECO:0000305|PubMed:10829025};
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 (By similarity). Interacts with SKP1A
CC (PubMed:11387208). {ECO:0000250|UniProtKB:P15646,
CC ECO:0000269|PubMed:11387208}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:10806224,
CC ECO:0000269|PubMed:10829025}. Note=Localizes to the fibrillar region of
CC the nucleolus. {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9FEF8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FEF8-2; Sequence=VSP_043984, VSP_043985;
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves and flowers
CC (PubMed:10829025, PubMed:10806224). Expressed in stems
CC (PubMed:10829025). {ECO:0000269|PubMed:10806224,
CC ECO:0000269|PubMed:10829025}.
CC -!- INDUCTION: Repressed by abscisic acid (ABA).
CC {ECO:0000269|PubMed:10806224}.
CC -!- DOMAIN: The N-terminal DMA/Gly-rich region (also called GAR domain) is
CC rich in Gly and Arg and functions in nucleolar targeting.
CC {ECO:0000269|PubMed:10806224}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. Fibrillarin
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG21982.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF233443; AAG10103.1; -; mRNA.
DR EMBL; AF265547; AAG10152.1; -; Genomic_DNA.
DR EMBL; AF187871; AAF00542.1; -; mRNA.
DR EMBL; AB019226; BAB10544.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96217.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96218.1; -; Genomic_DNA.
DR EMBL; AY139769; AAM98088.1; -; mRNA.
DR EMBL; BT004541; AAO42787.1; -; mRNA.
DR EMBL; AK230239; BAF02044.1; -; mRNA.
DR EMBL; AF263383; AAG21982.1; ALT_INIT; mRNA.
DR RefSeq; NP_001119418.1; NM_001125946.1. [Q9FEF8-2]
DR RefSeq; NP_568772.3; NM_124626.5. [Q9FEF8-1]
DR AlphaFoldDB; Q9FEF8; -.
DR SMR; Q9FEF8; -.
DR BioGRID; 20568; 86.
DR IntAct; Q9FEF8; 5.
DR STRING; 3702.AT5G52470.1; -.
DR SwissPalm; Q9FEF8; -.
DR PaxDb; Q9FEF8; -.
DR PRIDE; Q9FEF8; -.
DR ProteomicsDB; 238824; -. [Q9FEF8-1]
DR EnsemblPlants; AT5G52470.1; AT5G52470.1; AT5G52470. [Q9FEF8-1]
DR EnsemblPlants; AT5G52470.2; AT5G52470.2; AT5G52470. [Q9FEF8-2]
DR GeneID; 835323; -.
DR Gramene; AT5G52470.1; AT5G52470.1; AT5G52470. [Q9FEF8-1]
DR Gramene; AT5G52470.2; AT5G52470.2; AT5G52470. [Q9FEF8-2]
DR KEGG; ath:AT5G52470; -.
DR Araport; AT5G52470; -.
DR TAIR; locus:2156747; AT5G52470.
DR eggNOG; KOG1596; Eukaryota.
DR HOGENOM; CLU_059055_1_0_1; -.
DR InParanoid; Q9FEF8; -.
DR OMA; GVDQIYM; -.
DR OrthoDB; 1411035at2759; -.
DR PhylomeDB; Q9FEF8; -.
DR PRO; PR:Q9FEF8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FEF8; baseline and differential.
DR Genevisible; Q9FEF8; AT.
DR GO; GO:0031428; C:box C/D RNP complex; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
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:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0008649; F:rRNA methyltransferase activity; IBA:GO_Central.
DR GO; GO:0030515; F:snoRNA binding; ISS:TAIR.
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 HAMAP; MF_00351; RNA_methyltransf_FlpA; 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 1: Evidence at protein level;
KW Alternative splicing; Methyltransferase; Nucleus; Reference proteome;
KW Ribonucleoprotein; RNA-binding; rRNA processing; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..308
FT /note="rRNA 2'-O-methyltransferase fibrillarin 1"
FT /id="PRO_0000148518"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 156..157
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9Y9U3"
FT BINDING 175..176
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P22087"
FT BINDING 200..201
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P22087"
FT BINDING 220..223
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P22087"
FT VAR_SEQ 227..273
FT /note="ARILALNASFFLKTGGHFVISIKANCIDSTVAAEAVFQSEVKKLQQE -> N
FT LGPECLIFPQNWWTLCYLNQGQLYRLYSCSRSSLPERGEEAATRAV (in isoform
FT 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_043984"
FT VAR_SEQ 274..308
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_043985"
FT CONFLICT 137
FT /note="D -> DLD (in Ref. 2; AAF00542)"
FT /evidence="ECO:0000305"
FT CONFLICT 305
FT /note="T -> A (in Ref. 2; AAF00542)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 308 AA; 32830 MW; 15DECE7938C93BB8 CRC64;
MRPPVTGGRG GGGFRGGRDG GGRGFGGGRS FGGGRSGDRG RSGPRGRGRG APRGRGGPPR
GGMKGGSKVI VEPHRHAGVF IAKGKEDALV TKNLVPGEAV YNEKRISVQN EDGTKVEYRV
WNPFRSKLAA AILGGVDNIW IKPGAKVLYL GAASGTTVSH VSDLVGPEGC VYAVEFSHRS
GRDLVNMAKK RTNVIPIIED ARHPAKYRML VGMVDVIFSD VAQPDQARIL ALNASFFLKT
GGHFVISIKA NCIDSTVAAE AVFQSEVKKL QQEQFKPAEQ VTLEPFERDH ACVVGGYRMP
KKQKTPAS
