FBRL_PHYPO
ID FBRL_PHYPO Reviewed; 27 AA.
AC P22508;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 02-JUN-2021, entry version 55.
DE RecName: Full=rRNA/tRNA 2'-O-methyltransferase fibrillarin;
DE EC=2.1.1.-;
DE AltName: Full=34 kDa nucleolar protein B-36;
DE AltName: Full=Histone-glutamine methyltransferase;
DE Flags: Fragment;
OS Physarum polycephalum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Myxogastria;
OC Myxogastromycetidae; Physariida; Physaraceae; Physarum.
OX NCBI_TaxID=5791;
RN [1]
RP PROTEIN SEQUENCE, AND METHYLATION AT ARG-5; ARG-11; ARG-16 AND ARG-19.
RX PubMed=3140806; DOI=10.1016/s0006-291x(88)81279-8;
RA Christensen M.E., Fuxa K.P.;
RT "The nucleolar protein, B-36, contains a glycine and dimethylarginine-rich
RT sequence conserved in several other nuclear RNA-binding proteins.";
RL Biochem. Biophys. Res. Commun. 155:1278-1283(1988).
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Note=Fibrillar region of the
CC nucleolus.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. Fibrillarin
CC family. {ECO:0000305}.
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DR PIR; A31508; A31508.
DR iPTMnet; P22508; -.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Methylation; Methyltransferase; Nucleus;
KW Ribonucleoprotein; RNA-binding; rRNA processing; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..>27
FT /note="rRNA/tRNA 2'-O-methyltransferase fibrillarin"
FT /id="PRO_0000148516"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 5
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:3140806"
FT MOD_RES 11
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:3140806"
FT MOD_RES 16
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:3140806"
FT MOD_RES 19
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:3140806"
FT NON_TER 27
SQ SEQUENCE 27 AA; 2464 MW; F76AD7F8FAF442DA CRC64;
XFEGRGGFGG RGGGDRGGRG XGGFGGG
