FBRL_CANGA
ID FBRL_CANGA Reviewed; 323 AA.
AC Q6FN88;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=rRNA 2'-O-methyltransferase fibrillarin;
DE EC=2.1.1.-;
DE AltName: Full=Histone-glutamine methyltransferase;
GN Name=NOP1; OrderedLocusNames=CAGL0K01859g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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 that contain SNU13, NOP1, SIK1/NOP56 and NOP58, plus
CC a guide RNA. {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}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. Fibrillarin
CC family. {ECO:0000305}.
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DR EMBL; CR380957; CAG61267.1; -; Genomic_DNA.
DR RefSeq; XP_448306.1; XM_448306.1.
DR AlphaFoldDB; Q6FN88; -.
DR SMR; Q6FN88; -.
DR STRING; 5478.XP_448306.1; -.
DR EnsemblFungi; CAG61267; CAG61267; CAGL0K01859g.
DR GeneID; 2890032; -.
DR KEGG; cgr:CAGL0K01859g; -.
DR CGD; CAL0134523; CAGL0K01859g.
DR VEuPathDB; FungiDB:CAGL0K01859g; -.
DR eggNOG; KOG1596; Eukaryota.
DR HOGENOM; CLU_059055_1_0_1; -.
DR InParanoid; Q6FN88; -.
DR OMA; INMATHR; -.
DR Proteomes; UP000002428; Chromosome K.
DR GO; GO:0031428; C:box C/D RNP complex; IEA:EnsemblFungi.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0032040; C:small-subunit processome; IEA:EnsemblFungi.
DR GO; GO:1990259; F:histone-glutamine methyltransferase activity; IEA:EnsemblFungi.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008649; F:rRNA methyltransferase activity; IEA:EnsemblFungi.
DR GO; GO:0000494; P:box C/D RNA 3'-end processing; IEA:EnsemblFungi.
DR GO; GO:1990258; P:histone glutamine methylation; IEA:EnsemblFungi.
DR GO; GO:0006356; P:regulation of transcription by RNA polymerase I; IEA:EnsemblFungi.
DR GO; GO:0000452; P:snoRNA guided rRNA 2'-O-methylation; IEA:EnsemblFungi.
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 PIRSF; PIRSF006540; Nop17p; 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; Reference proteome;
KW Ribonucleoprotein; RNA-binding; rRNA processing; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..323
FT /note="rRNA 2'-O-methyltransferase fibrillarin"
FT /id="PRO_0000148522"
FT REGION 1..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 175..176
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 194..195
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 219..220
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 239..242
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 12
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250"
FT MOD_RES 15
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250"
FT MOD_RES 19
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250"
FT MOD_RES 25
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250"
FT MOD_RES 29
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250"
FT MOD_RES 35
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250"
FT MOD_RES 39
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250"
FT MOD_RES 43
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250"
FT MOD_RES 49
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250"
FT MOD_RES 53
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250"
FT MOD_RES 57
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250"
FT MOD_RES 61
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 73
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 323 AA; 34129 MW; 8D60BD39C3A6A9D4 CRC64;
MSFRPGSRGG ARGGRGGSRG GFGGRGGSRG GFGGRGGSRG GSRGGFGGRG GSRGGPRGGS
RGGPRGGARG GARGGAKGGA KVVIEPHKHD GVYIARGKED LLVTKNMAPG ESVYGEKRVS
VEEPSKEDGV PPTKVEYRVW NPFRSKLAAG IMGGLDELFI APGKKVLYLG AASGTSVSHV
SDVVGPEGVV YAVEFSHRPG RELISMAKKR PNVIPIIEDA RHPQKYRMLV GMVDAVFADV
AQPDQARIIA LNSHMFLKDQ GGVVISIKAN CIDSTVDAET VFAREVQKLR EEKIKPLEQL
TLEPYERDHC IVIGRYMRSG LKK
