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InterPro: IPR000692 Fibrillarin

Protein matches Help

UniProtKB

Matches:

313 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR000692 Fibrillarin

Type

Family

Signatures Help

Database	ID	Name	Proteins
HAMAP	MF_00351	Fibrillarin	241
Pfam	PF01269	Fibrillarin	313
PIRSF	PIRSF006540	Nop17p	260
PRINTS	PR00052	FIBRILLARIN	306
PANTHER	PTHR10335	Fibrillarin	308
Signatures in BioMart

InterPro Relationships Help

Contains

IPR020813 Fibrillarin, conserved site

GO Term annotation Help

Process

GO:0006364 rRNA processing
GO:0008033 tRNA processing

Function

GO:0003723 RNA binding
GO:0008168 methyltransferase activity

InterPro annotation

Entry Details in BioMart

Abstract

Fibrillarin is a component of a nucleolar small nuclear ribonucleoprotein (SnRNP), functioning in vivo in ribosomal RNA processing [1, 2]. It is associated with U3, U8 and U13 small nuclear RNAs in mammals [1] and is similar to the yeast NOP1 protein [3]. Fibrillarin has a well conserved sequence of around 320 amino acids, and contains 3 domains, an N-terminal Gly/Arg-rich region; a central domain resembling other RNA-binding proteins and containing an RNP-2-like consensus sequence; and a C-terminal alpha-helical domain. An evolutionarily related pre-rRNA processing protein, which lacks the Gly/Arg-rich domain, has been found in various archaebacteria.

Structural links Help

PDB - click here

SCOP: c.66.1.3

CATH: 3.30.200.20 , 3.40.50.150

Database links Help

PDBe-motif: PS00566

Enzyme: EC:2.1.1

PROSITE doc: PDOC00489

PANDIT: PF01269

Blocks: IPB000692

Pfam Clan: CL0102.19

AC	CL0102.19
ID	Methyltransfer
DE	Methyltransferase superfamily
PF00145	IPR001525	DNA methylase, C-5 cytosine-specific
PF00398	IPR001737	Ribosomal RNA adenine methylase transferase
PF00891	IPR001077	O-methyltransferase, family 2
PF01135	IPR000682	Protein-L-isoaspartate(D-aspartate) O-methyltransferase
PF01170	IPR000241	Putative RNA methylase
PF01189	IPR001678	Bacterial Fmu (Sun)/eukaryotic nucleolar NOL1/Nop2p
PF01209	IPR004033	UbiE/COQ5 methyltransferase
PF01234	IPR000940	Methyltransferase, NNMT/PNMT/TEMT
PF01269	IPR000692	Fibrillarin
PF01358	IPR000176	Poly A polymerase regulatory subunit
PF01555	IPR002941	DNA methylase N-4/N-6
PF01564	IPR001045	Spermine synthase
PF01596	IPR002935	O-methyltransferase, family 3
PF01728	IPR002877	Ribosomal RNA methyltransferase RrmJ/FtsJ
PF01739	IPR000780	MCP methyltransferase, CheR-type
PF01795	IPR002903	S-adenosyl-L-methionine-dependent methyltransferase, MraW
PF01861	IPR002723	Protein of unknown function DUF43
PF02005	IPR002905	N2,N2-dimethylguanosine tRNA methyltransferase
PF02086	IPR012327	D12 class N6 adenine-specific DNA methyltransferase
PF02353	IPR003333	Cyclopropane-fatty-acyl-phospholipid synthase
PF02384	IPR003356	DNA methylase, adenine-specific
PF02390	IPR003358	tRNA (guanine-N-7) methyltransferase
PF02475	IPR003402	Protein of unknown function Met10
PF02527	IPR003682	rRNA small subunit methyltransferase G
PF03141	IPR004159	Protein of unknown function DUF248, methyltransferase putative
PF03269	IPR004951	Protein of unknown function DUF268, Caenorhabditis species
PF03291	IPR004971	mRNA capping enzyme, large subunit
PF03602	IPR016065	Protein of unknown function methylase putative
PF03848	IPR015985	Tellurite resistance methyltransferase, TehB, core
PF04378	IPR007473	Protein of unknown function DUF519
PF04445	IPR007536	Protein of unknown function DUF548
PF04672	IPR006764	Protein of unknown function DUF574
PF04816	IPR006901	Protein of unknown function DUF633
PF05063	IPR007757	MT-A70
PF05148	IPR007823	Methyltransferase-related
PF05175	IPR007848	Methyltransferase small
PF05219	IPR007884	DREV methyltransferase
PF05401	IPR008715	NodS
PF05430	IPR008471	Protein of unknown function DUF752
PF05724	IPR008854	Thiopurine S-methyltransferase
PF05891	IPR008576	Protein of unknown function DUF858, methyltransferase-like
PF05958	IPR010280	(Uracil-5)-methyltransferase
PF05971	IPR010286	S-adenosyl-L-methionine dependent methyltransferase, predicted
PF06080	IPR010342	Protein of unknown function DUF938
PF06325	IPR010456	Ribosomal L11 methyltransferase
PF06460	IPR009461	Coronavirus NSP13
PF06859	IPR010675	Bicoid-interacting 3
PF06962	IPR010719	Putative rRNA methylase
PF07021	IPR010743	Methionine biosynthesis MetW
PF07109	IPR010940	Magnesium-protoporphyrin IX methyltransferase, C-terminal
PF07279	IPR009902	Protein of unknown function DUF1442
PF07669	IPR011639	Restriction endonuclease, Eco57I
PF07757	IPR011671	AdoMet-dependent methyltransferase, predicted
PF07942	IPR012901	N2227-like
PF08003	IPR010017	tRNA (mo5U34)-methyltransferase
PF08123	IPR013110	Histone methylation DOT1
PF08241	IPR013216	Methyltransferase type 11
PF08242	IPR013217	Methyltransferase type 12
PF08704	IPR014816	tRNA methyltransferase complex GCD14 subunit
PF09243	IPR015324	Ribosomal protein Rsm22, bacterial-type
PF09445	IPR019012	RNA cap guanine-N2 methyltransferase
PF10294	IPR019410	Methyltransferase-16, putative
PF10672	IPR019614	S-adenosylmethionine-dependent methyltransferase

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR000692

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P15646 rRNA 2'-O-methyltransferase fibrillarin

P22087 rRNA 2'-O-methyltransferase fibrillarin

P35550 rRNA 2'-O-methyltransferase fibrillarin

Q22053 rRNA 2'-O-methyltransferase fibrillarin

Q9W1V3 rRNA 2'-O-methyltransferase fibrillarin

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR020813	Fibrillarin, conserved site
IPR000692	Fibrillarin
	SWISS-MODEL
	PDB Chain
	ModBase
	CATH Domain

Publications Open in usermanual
1.	Jansen RP, Hurt EC, Kern H, Lehtonen H, Carmo-Fonseca M, Lapeyre B, Tollervey D. Evolutionary conservation of the human nucleolar protein fibrillarin and its functional expression in yeast. J. Cell Biol. 113 715-29 1991 [PubMed: 2026646] http://dx.doi.org/10.1083/jcb.113.4.715
2.	Girard JP, Feliu J, Caizergues-Ferrer M, Lapeyre B. Study of multiple fibrillarin mRNAs reveals that 3' end formation in Schizosaccharomyces pombe is sensitive to cold shock. Nucleic Acids Res. 21 1881-7 1993 [PubMed: 8493104] http://dx.doi.org/10.1093/nar/21.8.1881
3.	Schimmang T, Tollervey D, Kern H, Frank R, Hurt EC. A yeast nucleolar protein related to mammalian fibrillarin is associated with small nucleolar RNA and is essential for viability. EMBO J. 8 4015-24 1989 [PubMed: 2686980] http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=2686980&action=stream&blobtype=pdf

Additional Reading Open in usermanual
	Wang H, Boisvert D, Kim KK, Kim R, Kim SH. Crystal structure of a fibrillarin homologue from Methanococcus jannaschii, a hyperthermophile, at 1.6 A resolution. EMBO J. 19 2000 317-23 [PubMed: 10654930] http://dx.doi.org/10.1093/emboj/19.3.317
	Aittaleb M, Rashid R, Chen Q, Palmer JR, Daniels CJ, Li H. Structure and function of archaeal box C/D sRNP core proteins. Nat. Struct. Biol. 10 2003 256-63 [PubMed: 12598892] http://dx.doi.org/10.1038/nsb905
	Oruganti S, Zhang Y, Li H, Robinson H, Terns MP, Terns RM, Yang W, Li H. Alternative conformations of the archaeal Nop56/58-fibrillarin complex imply flexibility in box C/D RNPs. J. Mol. Biol. 371 2007 1141-50 [PubMed: 17617422] http://dx.doi.org/10.1016/j.jmb.2007.06.029
	Deng L, Starostina NG, Liu ZJ, Rose JP, Terns RM, Terns MP, Wang BC. Structure determination of fibrillarin from the hyperthermophilic archaeon Pyrococcus furiosus. Biochem. Biophys. Res. Commun. 315 2004 726-32 [PubMed: 14975761] http://dx.doi.org/10.1016/j.bbrc.2004.01.114

InterPro 23.1