FBRL_DROME
ID FBRL_DROME Reviewed; 344 AA.
AC Q9W1V3; Q24348; Q8IGK5;
DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 146.
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:AAF46950.1}; ORFNames=CG9888;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1] {ECO:0000312|EMBL:AAF46950.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAF46950.1}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3] {ECO:0000312|EMBL:AAN71493.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4] {ECO:0000305, ECO:0000312|EMBL:CAA28903.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 5-140.
RX PubMed=2884623; DOI=10.1093/nar/15.10.4035;
RA Flavell A.J., Dyson J., Ish-Horowicz D.;
RT "A novel GC-rich dispersed repeat sequence in Drosophila melanogaster.";
RL Nucleic Acids Res. 15:4035-4048(1987).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA28903.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA28903.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AE013599; AAF46950.1; -; Genomic_DNA.
DR EMBL; BT001738; AAN71493.1; -; mRNA.
DR EMBL; X05285; CAA28903.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; NP_523817.1; NM_079093.4.
DR AlphaFoldDB; Q9W1V3; -.
DR SMR; Q9W1V3; -.
DR BioGRID; 63268; 18.
DR IntAct; Q9W1V3; 9.
DR MINT; Q9W1V3; -.
DR STRING; 7227.FBpp0071892; -.
DR PaxDb; Q9W1V3; -.
DR PRIDE; Q9W1V3; -.
DR DNASU; 37662; -.
DR EnsemblMetazoa; FBtr0071982; FBpp0071892; FBgn0003062.
DR GeneID; 37662; -.
DR KEGG; dme:Dmel_CG9888; -.
DR UCSC; CG9888-RA; d. melanogaster.
DR CTD; 37662; -.
DR FlyBase; FBgn0003062; Fib.
DR VEuPathDB; VectorBase:FBgn0003062; -.
DR eggNOG; KOG1596; Eukaryota.
DR GeneTree; ENSGT00550000074792; -.
DR HOGENOM; CLU_059055_1_0_1; -.
DR InParanoid; Q9W1V3; -.
DR OMA; INMATHR; -.
DR OrthoDB; 1411035at2759; -.
DR PhylomeDB; Q9W1V3; -.
DR Reactome; R-DME-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR SignaLink; Q9W1V3; -.
DR BioGRID-ORCS; 37662; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 37662; -.
DR PRO; PR:Q9W1V3; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0003062; Expressed in ovary and 22 other tissues.
DR ExpressionAtlas; Q9W1V3; baseline and differential.
DR Genevisible; Q9W1V3; DM.
DR GO; GO:0031428; C:box C/D RNP complex; IBA:GO_Central.
DR GO; GO:0015030; C:Cajal body; IDA:FlyBase.
DR GO; GO:0001651; C:dense fibrillar component; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:FlyBase.
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 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..344
FT /note="rRNA 2'-O-methyltransferase fibrillarin"
FT /id="PRO_0000148513"
FT REGION 1..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 197..198
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 216..217
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 241..242
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 261..264
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 40
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P22509"
FT MOD_RES 42
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P22509"
FT MOD_RES 48
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P22509"
FT MOD_RES 51
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P22509"
FT MOD_RES 58
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P22509"
FT MOD_RES 63
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P22509"
FT MOD_RES 71
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P22509"
FT MOD_RES 77
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P22509"
FT MOD_RES 83
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P22509"
FT MOD_RES 88
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P22509"
FT MOD_RES 93
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P22509"
FT MOD_RES 98
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P22509"
FT CONFLICT 55..67
FT /note="Missing (in Ref. 3; AAN71493)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="R -> G (in Ref. 3; AAN71493)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 344 AA; 34637 MW; 58B536FAACAE01D6 CRC64;
MGKPGFSPRG GGGGGGGGGG GFRGRGGGGG GGGGGFGGGR GRGGGGDRGG RGGFGGGRGG
GGRGGGGGGG RGAFGGRGGG GGRGGGGRGG GGRGGGGRGG GAGGFKGGKT VTIEPHRHEG
VFIARGKEDA LVTRNFVPGS EVYGEKRISV ETNGEKIEYR VWNPFRSKLA AAVLGGVEQI
HMPPGSKVLY LGAASGTTVS HVSDVVGPEG LVYAVEFSHR SGRDLINVAK KRTNIIPIIE
DARHPHKYRM LVGMVDTIFA DVAQPDQGRI VALNAQHFLK NGGHFVISIK ASCIDSTAQP
EAVFAAEVKK MQADKLKPQE QLTLEPYERD HAVVVGVYRP PPKQ
