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rRNA 2'-O-methyltransferase fibrillarin (EC 2.1.1.-) (Histone-glutamine methyltransferase)

 FBRL_DICDI              Reviewed;         334 AA.
Q55CW0;
29-APR-2008, integrated into UniProtKB/Swiss-Prot.
24-MAY-2005, sequence version 1.
07-JUN-2017, entry version 76.
RecName: Full=rRNA 2'-O-methyltransferase fibrillarin;
EC=2.1.1.-;
AltName: Full=Histone-glutamine methyltransferase;
Name=fbl; ORFNames=DDB_G0269878;
Dictyostelium discoideum (Slime mold).
Eukaryota; Amoebozoa; Mycetozoa; Dictyosteliida; Dictyostelium.
NCBI_TaxID=44689;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AX4;
PubMed=15875012; DOI=10.1038/nature03481;
Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A.,
Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q.,
Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F.,
Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P.,
Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P.,
Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N.,
Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M.,
Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I.,
Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R.,
Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
Knights A., Loulseged H., Mungall K.L., Oliver K., Price C.,
Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D.,
Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S.,
Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T.,
Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A.,
Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M.,
Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G.,
Kuspa A.;
"The genome of the social amoeba Dictyostelium discoideum.";
Nature 435:43-57(2005).
-!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that
has the ability to methylate both RNAs and proteins. Involved in
pre-rRNA processing. Utilizes the methyl donor S-adenosyl-L-
methionine to catalyze the site-specific 2'-hydroxyl methylation
of ribose moieties in pre-ribosomal RNA. Site specificity is
provided by a guide RNA that base pairs with the substrate.
Methylation occurs at a characteristic distance from the sequence
involved in base pairing with the guide RNA. Also acts as a
protein methyltransferase by mediating methylation of 'Gln-105' of
histone H2A (H2AQ105me), a modification that impairs binding of
the FACT complex and is specifically present at 35S ribosomal DNA
locus (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-glutamine-
[histone] = S-adenosyl-L-homocysteine + N(5)-methyl-L-glutamine-
[histone].
-!- SUBUNIT: Component of box C/D small nucleolar ribonucleoprotein
(snoRNP) particles. It is associated with the U3, U8 and U13 small
nuclear RNAs. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
Note=Fibrillar region of the nucleolus. {ECO:0000250}.
-!- PTM: By homology to other fibrillarins, some or all of the N-
terminal domain arginines are modified to asymmetric
dimethylarginine (DMA). {ECO:0000250}.
-!- SIMILARITY: Belongs to the methyltransferase superfamily.
Fibrillarin family. {ECO:0000305}.
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EMBL; AAFI02000005; EAL72289.1; -; Genomic_DNA.
RefSeq; XP_646371.1; XM_641279.1.
ProteinModelPortal; Q55CW0; -.
SMR; Q55CW0; -.
STRING; 44689.DDB0267046; -.
PaxDb; Q55CW0; -.
EnsemblProtists; EAL72289; EAL72289; DDB_G0269878.
GeneID; 8617326; -.
KEGG; ddi:DDB_G0269878; -.
dictyBase; DDB_G0269878; fbl.
eggNOG; KOG1596; Eukaryota.
eggNOG; COG1889; LUCA.
InParanoid; Q55CW0; -.
KO; K14563; -.
OMA; QPNQAEI; -.
PhylomeDB; Q55CW0; -.
Reactome; R-DDI-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
PRO; PR:Q55CW0; -.
Proteomes; UP000002195; Chromosome 1.
Proteomes; UP000002195; Unassembled WGS sequence.
GO; GO:0031428; C:box C/D snoRNP complex; IBA:GO_Central.
GO; GO:0015030; C:Cajal body; IBA:GO_Central.
GO; GO:0005730; C:nucleolus; ISS:dictyBase.
GO; GO:0032040; C:small-subunit processome; IBA:GO_Central.
GO; GO:1990259; F:histone-glutamine methyltransferase activity; IBA:GO_Central.
GO; GO:0003723; F:RNA binding; IBA:GO_Central.
GO; GO:0008649; F:rRNA methyltransferase activity; IBA:GO_Central.
GO; GO:0000494; P:box C/D snoRNA 3'-end processing; IBA:GO_Central.
GO; GO:1990258; P:histone glutamine methylation; IBA:GO_Central.
GO; GO:0031167; P:rRNA methylation; IBA:GO_Central.
GO; GO:0016074; P:snoRNA metabolic process; ISS:dictyBase.
GO; GO:0008033; P:tRNA processing; IEA:InterPro.
HAMAP; MF_00351; RNA_methyltransf_FlpA; 1.
InterPro; IPR000692; Fibrillarin.
InterPro; IPR029063; SAM-dependent_MTases.
Pfam; PF01269; Fibrillarin; 1.
PIRSF; PIRSF006540; Nop17p; 1.
PRINTS; PR00052; FIBRILLARIN.
SMART; SM01206; Fibrillarin; 1.
SUPFAM; SSF53335; SSF53335; 1.
3: Inferred from homology;
Complete proteome; Methylation; Methyltransferase; Nucleus;
Reference proteome; Ribonucleoprotein; RNA-binding; rRNA processing;
S-adenosyl-L-methionine; Transferase.
CHAIN 1 334 rRNA 2'-O-methyltransferase fibrillarin.
/FTId=PRO_0000331764.
REGION 184 185 S-adenosyl-L-methionine binding.
{ECO:0000250}.
REGION 203 204 S-adenosyl-L-methionine binding.
{ECO:0000250}.
REGION 228 229 S-adenosyl-L-methionine binding.
{ECO:0000250}.
REGION 248 251 S-adenosyl-L-methionine binding.
{ECO:0000250}.
COMPBIAS 4 94 DMA/Gly-rich.
SEQUENCE 334 AA; 34853 MW; 1D87773FC681EF01 CRC64;
MEGRGGSRGG AMARGGGRGG FGGGRGGFGG GDRGGRGGGR GGFGGGDRGG RGGFGGGRGG
RGGFGGGDRG GRGGARGGRG GARGGKPAAG GKPGAKVIVE KHPRHEGVFI VRGKEESLAT
LNSVPGESVY GEKRVSVGEG EDKKEYRIWN PFRSKIAAGL HRGVDEIHIK PGSKVLYIGA
ASGTTISHVS DIVGPTGVVY GIELSHRPGR DLIGMAKKRT NVIPIIEDAR HPQKYRMLIG
MVDVVFADVA QPNQAQIVAQ NSAYFLKNEG HFIISIKASC IDSTAPTEVV VQNEITKLKK
EKLRPQHLLK TLDPYERNHS LVIGVYRKFG SSEK


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