FBRL_ASHGO
ID FBRL_ASHGO Reviewed; 326 AA.
AC Q756P0;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=rRNA 2'-O-methyltransferase fibrillarin;
DE EC=2.1.1.-;
DE AltName: Full=Histone-glutamine methyltransferase;
GN Name=NOP1; OrderedLocusNames=AER214C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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; AE016818; AAS52895.1; -; Genomic_DNA.
DR RefSeq; NP_985071.1; NM_210425.1.
DR AlphaFoldDB; Q756P0; -.
DR SMR; Q756P0; -.
DR STRING; 33169.AAS52895; -.
DR EnsemblFungi; AAS52895; AAS52895; AGOS_AER214C.
DR GeneID; 4621281; -.
DR KEGG; ago:AGOS_AER214C; -.
DR eggNOG; KOG1596; Eukaryota.
DR HOGENOM; CLU_059055_1_0_1; -.
DR OMA; INMATHR; -.
DR Proteomes; UP000000591; Chromosome V.
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 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..326
FT /note="rRNA 2'-O-methyltransferase fibrillarin"
FT /id="PRO_0000148521"
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 180..181
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 199..200
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 224..225
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 244..247
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 11
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 23
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250"
FT MOD_RES 26
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250"
FT MOD_RES 32
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250"
FT MOD_RES 36
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250"
FT MOD_RES 39
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250"
FT MOD_RES 45
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250"
FT MOD_RES 49
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250"
FT MOD_RES 55
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250"
FT MOD_RES 59
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 71
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250"
FT MOD_RES 74
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250"
FT MOD_RES 78
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 326 AA; 34213 MW; 57B6385C6257ED00 CRC64;
MAFQPGSRGG RGGARGGARG GARGGRGGFG GRGGSRGGRG GFDSRGGARG GFGGRGGSRG
GPRGGPRGGA RGGRGGARGG AKGGAKVVIE PHKHAGVFIA RGKEDLLVTK NVAPGESVYG
EKRISVEEPA SEEGVPPTKV EYRVWNPFRS KLAAGIMGGL DELFIAPGKK VLYLGAASGT
SVSHVADVVG PEGLVYAVEF SHRPGRELIS MAKKRPNVIP IIEDARHPQK YRMLIGMVDA
VFADVAQPDQ ARIIALNSHM FLKDQGGVVI SIKANCIDST VDAETVFARE VQKLREEKIK
PLEQLTLEPY ERDHCIVIGR YMRSGL
