GENTAUR Molecular Products.

 FBRL_DICDI              Reviewed;         334 AA.
 Q55CW0;
 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
 24-MAY-2005, sequence version 1.
 25-APR-2018, entry version 79.
 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; Dictyostelids; Dictyosteliales;
 Dictyosteliaceae; 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.
 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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