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UniProtKB/Swiss-Prot entry Q94AH9


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name FBRL2_ARATH
Primary accession number Q94AH9
Secondary accession number Q9SZZ1
Integrated into Swiss-Prot on June 7, 2005
Sequence was last modified on June 7, 2005 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 41)
Name and origin of the protein
Protein name rRNA 2'-O-methyltransferase fibrillarin 2
Synonyms EC 2.1.1.-
Fibrillarin-like protein 2
Gene name
Name: FIB2
Synonyms: FLP
OrderedLocusNames: At4g25630
ORFNames: L73G19.10
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, AND TISSUE SPECIFICITY.
STRAIN=cv. Columbia;
DOI=10.1074/jbc.M002996200; PubMed=10829025 [NCBI, ExPASy, EBI, Israel, Japan]
Barneche F., Steinmetz F., Echeverria M.;
"Fibrillarin genes encode both a conserved nucleolar protein and a novel small nucleolar RNA involved in ribosomal RNA methylation in Arabidopsis thaliana.";
J. Biol. Chem. 275:27212-27220(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/47134; PubMed=10617198 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
Nature 402:769-777(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Empirical analysis of transcriptional activity in the Arabidopsis genome.";
Science 302:842-846(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[5]
DEVELOPMENTAL STAGE, INDUCTION, AND TISSUE SPECIFICITY.
DOI=10.1104/pp.123.1.51; PubMed=10806224 [NCBI, ExPASy, EBI, Israel, Japan]
Pih K.T., Yi M.J., Liang Y.S., Shin B.J., Cho M.J., Hwang I., Son D.;
"Molecular cloning and targeting of a fibrillarin homolog from Arabidopsis.";
Plant Physiol. 123:51-58(2000).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF233444; AAG10104.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF267171; AAG10153.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL050400; CAB43694.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL161563; CAB81373.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY046027; AAK76701.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY142647; AAN13105.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY084608; AAM61172.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T09555; T09555.
RefSeq NP_567724.1; -.
UniGene At.25589
3D structure databases
HSSP O57811; 1G8A. [HSSP ENTRY / PDB]
SMR Q94AH9; 81-309.
ModBase Q94AH9.
Protein-protein interaction databases
IntAct Q94AH9; -.
Organism-specific databases
GeneFarm 4930; 473.
TAIR At4g25630; -.
Gene expression databases
GermOnline AT4G25630; Arabidopsis thaliana.
Ontologies
GO
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
QuickGo view.
Family and domain databases
InterPro IPR000692; Fibrillarin.
Graphical view of domain structure.
PANTHER PTHR10335; Fibrillarin; 1.
Pfam PF01269; Fibrillarin; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF006540; Nop17p; 1.
PRINTS PR00052; FIBRILLARIN.
BLOCKS Q94AH9.
ProtoNet Q94AH9.
Genome annotation databases
GeneID 828668; -.
GenomeReviews CT486007_GR; AT4G25630.
KEGG ath:AT4G25630; -.
NMPDR fig|3702.1.peg.20475; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Methylation; Methyltransferase; Nucleus; Ribonucleoprotein; RNA-binding; rRNA processing; Transferase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   320  320     rRNA 2'-O-methyltransferase fibrillarin 2. PRO_0000148519
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). 
COMPBIAS   1    75  75     DMA/Gly-rich. 
BINDING   138   138        S-adenosyl-L-methionine (By similarity). 
BINDING   231   231        S-adenosyl-L-methionine (By similarity). 
MOD_RES   2     2        Asymmetric dimethylarginine (By similarity). 
MOD_RES   16    16        Asymmetric dimethylarginine (By similarity). 
MOD_RES   25    25        Asymmetric dimethylarginine (By similarity). 
MOD_RES   34    34        Asymmetric dimethylarginine (By similarity). 
MOD_RES   39    39        Asymmetric dimethylarginine (By similarity). 
MOD_RES   43    43        Asymmetric dimethylarginine (By similarity). 
MOD_RES   48    48        Asymmetric dimethylarginine (By similarity). 
MOD_RES   51    51        Asymmetric dimethylarginine (By similarity). 
MOD_RES   53    53        Asymmetric dimethylarginine (By similarity). 
MOD_RES   55    55        Asymmetric dimethylarginine (By similarity). 
MOD_RES   59    59        Asymmetric dimethylarginine (By similarity). 
MOD_RES   63    63        Asymmetric dimethylarginine (By similarity). 
MOD_RES   66    66        Asymmetric dimethylarginine (By similarity). 
MOD_RES   71    71        Asymmetric dimethylarginine (By similarity). 
CONFLICT   181   181        C -> S (in Ref. 3; AAK76701). 
Sequence information
Length: 320 AA [This is the length of the unprocessed precursor] Molecular weight: 33653 Da [This is the MW of the unprocessed precursor] CRC64: 0E3DF1733F52CFDC [This is a checksum on the sequence]
        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 

Q94AH9 in FASTA format

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