Reviewed, UniProtKB/Swiss-Prot Q94AH9 (FBRL2_ARATH)

Names and origin

Protein names

Recommended name:
    rRNA 2'-O-methyltransferase fibrillarin 2
    EC=2.1.1.-
Alternative name(s):
    Fibrillarin-like protein 2

Gene names

Name:	FIB2
Synonyms:	FLP
Ordered Locus Names:	At4g25630
ORF Names:	L73G19.10

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	320 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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. Ref.1
Subunit structure	Component of box C/D small nucleolar ribonucleoprotein (snoRNP) particles By similarity.
Subcellular location	Nucleus › nucleolus By similarity. Note: Fibrillar region of the nucleolus By similarity.
Tissue specificity	Ubiquitously expressed, with higher levels in roots and flowers, and lower levels in siliques. Expression levels decrease during aging. Ref.1 Ref.5
Induction	Repressed by abscisic acid (ABA). Ref.5
Domain	The DMA/Gly-rich region (also called GAR domain) is rich in Gly and Arg and appear to function in nucleolar targeting By similarity.
Sequence similarities	Belongs to the fibrillarin family.

Ontologies

Keywords
Biological process	rRNA processing
Cellular component	Nucleus
Ligand	RNA-binding
Molecular function	Methyltransferase Ribonucleoprotein Transferase
PTM	Methylation
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	RNA methylation Ref.1 Inferred from genetic interaction. Source: TAIR rRNA processing Ref.1 Inferred from genetic interaction. Source: TAIR
Cellular component	nucleolus Ref.1 Inferred from direct assay. Source: TAIR ribonucleoprotein complex Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW methyltransferase activity Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PRMT1.1	Q9SU94	1	EBI-1382666,EBI-1382731
PRMT1.2	O82210	1	EBI-1382666,EBI-1382526

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 320	320	rRNA 2'-O-methyltransferase fibrillarin 2		PRO_0000148519
Regions
	Region	167 – 168	2	S-adenosyl-L-methionine binding By similarity
	Region	186 – 187	2	S-adenosyl-L-methionine binding By similarity
	Region	211 – 212	2	S-adenosyl-L-methionine binding By similarity
	Compositional bias	1 – 75	75	DMA/Gly-rich
Sites
	Binding site	138	1	S-adenosyl-L-methionine By similarity
	Binding site	231	1	S-adenosyl-L-methionine By similarity
Amino acid modifications
	Modified residue	2	1	Asymmetric dimethylarginine By similarity
	Modified residue	16	1	Asymmetric dimethylarginine By similarity
	Modified residue	25	1	Asymmetric dimethylarginine By similarity
	Modified residue	34	1	Asymmetric dimethylarginine By similarity
	Modified residue	39	1	Asymmetric dimethylarginine By similarity
	Modified residue	43	1	Asymmetric dimethylarginine By similarity
	Modified residue	48	1	Asymmetric dimethylarginine By similarity
	Modified residue	51	1	Asymmetric dimethylarginine By similarity
	Modified residue	53	1	Asymmetric dimethylarginine By similarity
	Modified residue	55	1	Asymmetric dimethylarginine By similarity
	Modified residue	59	1	Asymmetric dimethylarginine By similarity
	Modified residue	63	1	Asymmetric dimethylarginine By similarity
	Modified residue	66	1	Asymmetric dimethylarginine By similarity
	Modified residue	71	1	Asymmetric dimethylarginine By similarity
Experimental info
	Sequence conflict	181	1	C → S in AAK76701. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q94AH9-1 [UniParc]. Last modified June 7, 2005. Version 2. Checksum: 0E3DF1733F52CFDC	FASTA	320	33,653
	10 20 30 40 50 60 MRPPLTGSGG GFSGGRGRGG YSGGRGDGGF SGGRGGGGRG GGRGFSDRGG RGRGRGPPRG 70 80 90 100 110 120 GARGGRGPAG RGGMKGGSKV IVEPHRHAGV FIAKGKEDAL VTKNLVPGEA VYNEKRISVQ 130 140 150 160 170 180 NEDGTKTEYR VWNPFRSKLA AAILGGVDNI WIKPGAKVLY LGAASGTTVS HVSDLVGPEG 190 200 210 220 230 240 CVYAVEFSHR SGRDLVNMAK KRTNVIPIIE DARHPAKYRM LVGMVDVIFS DVAQPDQARI 250 260 270 280 290 300 LALNASYFLK SGGHFVISIK ANCIDSTVPA EAVFQTEVKK LQQEQFKPAE QVTLEPFERD 310 320 HACVVGGYRM PKKPKAATAA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Fibrillarin genes encode both a conserved nucleolar protein and a novel small nucleolar RNA involved in ribosomal RNA methylation in Arabidopsis thaliana." Barneche F., Steinmetz F., Echeverria M. J. Biol. Chem. 275:27212-27220(2000) [PubMed: 10829025] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, TISSUE SPECIFICITY. Strain: cv. Columbia.
[2]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R. Nature 402:769-777(1999) [PubMed: 10617198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"Molecular cloning and targeting of a fibrillarin homolog from Arabidopsis." Pih K.T., Yi M.J., Liang Y.S., Shin B.J., Cho M.J., Hwang I., Son D. Plant Physiol. 123:51-58(2000) [PubMed: 10806224] [Abstract] Cited for: DEVELOPMENTAL STAGE, INDUCTION, TISSUE SPECIFICITY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF233444 mRNA. Translation: AAG10104.1. AF267171 Genomic DNA. Translation: AAG10153.1. AL050400 Genomic DNA. Translation: CAB43694.1. AL161563 Genomic DNA. Translation: CAB81373.1. AY046027 mRNA. Translation: AAK76701.1. AY142647 mRNA. Translation: AAN13105.1. AY084608 mRNA. Translation: AAM61172.1.
IPI	IPI00546563.
PIR	T09555.
RefSeq	NP_567724.1.
UniGene	At.25589
3D structure databases
HSSP	HSSP built from PDB template 1G8A based on UniProtKB O57811.
SMR	Q94AH9. Positions 81-309.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q94AH9. 3 interactions.
Proteomic databases
PRIDE	Q94AH9.
Genome annotation databases
GeneID	828668.
GenomeReviews	Gene locus AT4G25630 in contig CT486007_GR.
KEGG	ath:AT4G25630.
NMPDR	fig|3702.1.peg.20475.
Organism-specific databases
GeneFarm	4930. 473.
TAIR	At4g25630.
Phylogenomic databases
OMA	Q94AH9. YERDHAC.
Gene expression databases
GermOnline	AT4G25630. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR000692. Fibrillarin. [Graphical view]
PANTHER	PTHR10335. Fibrillarin. 1 hit.
Pfam	PF01269. Fibrillarin. 1 hit. [Graphical view]
PIRSF	PIRSF006540. Nop17p. 1 hit.
PRINTS	PR00052. FIBRILLARIN.
ProtoNet	Search...

Entry information

Entry name

FBRL2_ARATH

Accession

Primary (citable) accession number: Q94AH9
Secondary accession number(s): Q9SZZ1

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	June 7, 2005
Last modified:	June 16, 2009
This is version 46 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)