Q94AH9 (FBRL2_ARATH) Reviewed, UniProtKB/Swiss-Prot

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)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	320 AA.
Sequence status	Complete.
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. Interacts with groundnut rosette virus long-distance movement protein; this interaction is required for virus long-distance movement protein transiting through host Cajal body and nucleolus, relocalization of fibrillarin to the cytoplasm, and in presence of viral RNA, leads to the formation of stable RNPs. Ref.7
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.6
Induction	Repressed by abscisic acid (ABA). Ref.6
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 methyltransferase superfamily. 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 Reference proteome
Gene Ontology (GO)
Biological process	RNA methylation Inferred from genetic interaction Ref.1. Source: TAIR rRNA processing Inferred from genetic interaction Ref.1. Source: TAIR tRNA processing Inferred from electronic annotation. Source: InterPro
Cellular component	nucleolus Inferred from direct assay Ref.1. Source: TAIR ribonucleoprotein complex Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	RNA binding Inferred from direct assay. Source: TAIR methyltransferase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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.4

Sequences

	Sequence		Length	Mass (Da)
	Q94AH9 [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]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[4]	"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.
[5]	"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].
[6]	"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.
[7]	"Interaction of a plant virus-encoded protein with the major nucleolar protein fibrillarin is required for systemic virus infection." Kim S.H., Macfarlane S., Kalinina N.O., Rakitina D.V., Ryabov E.V., Gillespie T., Haupt S., Brown J.W., Taliansky M. Proc. Natl. Acad. Sci. U.S.A. 104:11115-11120(2007) [PubMed: 17576925] [Abstract] Cited for: INTERACTION WITH GROUNDNUT ROSETTE VIRUS LONG-DISTANCE MOVEMENT PROTEIN.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF233444 mRNA. Translation: AAG10104.1. AF267171 Genomic DNA. Translation: AAG10153.1. AL050400 Genomic DNA. Translation: CAB43694.1. AL161563 Genomic DNA. Translation: CAB81373.1. CP002687 Genomic DNA. Translation: AEE85085.1. AY046027 mRNA. Translation: AAK76701.1. AY142647 mRNA. Translation: AAN13105.1. AY084608 mRNA. Translation: AAM61172.1.
IPI	IPI00546563.
PIR	T09555.
RefSeq	NP_567724.1. NM_118695.3.
UniGene	At.25589.
3D structure databases
ProteinModelPortal	Q94AH9.
SMR	Q94AH9. Positions 81-309.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q94AH9. 3 interactions.
STRING	Q94AH9.
Proteomic databases
PRIDE	Q94AH9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT4G25630.1; AT4G25630.1; AT4G25630.
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
eggNOG	KOG1596.
GeneTree	EPGT00050000003248.
HOGENOM	HBG297404.
InParanoid	Q94AH9.
OMA	CAERENI.
PhylomeDB	Q94AH9.
ProtClustDB	CLSN2689606.
Gene expression databases
Genevestigator	Q94AH9.
GermOnline	AT4G25630. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR000692. Fibrillarin. [Graphical view]
KO	K14563.
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:	December 14, 2011
This is version 66 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program