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UniProtKB/Swiss-Prot entry O23237


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

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Entry information
Entry name PER49_ARATH
Primary accession number O23237
Secondary accession numbers None
Integrated into Swiss-Prot on December 6, 2002
Sequence was last modified on May 1, 1999 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 73)
Name and origin of the protein
Protein name Peroxidase 49 [Precursor]
Synonyms Atperox P49
EC 1.11.1.7
ATP31
Gene name
Name: PER49
Synonyms: DIDI 6G-3B, P49
OrderedLocusNames: At4g36430
ORFNames: C7A10.930, AP22.54
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 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
TISSUE=Root;
PubMed=11277426 [NCBI, ExPASy, EBI, Israel, Japan]
Vercauteren I., van der Schueren E., Van Montagu M., Gheysen G.;
"Arabidopsis thaliana genes expressed in the early compatible interaction with root-knot nematodes.";
Mol. Plant Microbe Interact. 14:288-299(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
TISSUE=Root;
PubMed=12473102 [NCBI, ExPASy, EBI, Israel, Japan]
Welinder K.G., Justesen A.F., Kjaersgaard I.V.H., Jensen R.B., Rasmussen S.K., Jespersen H.M., Duroux L.;
"Structural diversity and transcription of class III peroxidases from Arabidopsis thaliana.";
Eur. J. Biochem. 269:6063-6081(2002).
[3]
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).
[4]
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).
[5]
GENE FAMILY ORGANIZATION, AND NOMENCLATURE.
STRAIN=cv. Columbia;
DOI=10.1016/S0378-1119(02)00465-1; PubMed=12034502 [NCBI, ExPASy, EBI, Israel, Japan]
Tognolli M., Penel C., Greppin H., Simon P.;
"Analysis and expression of the class III peroxidase large gene family in Arabidopsis thaliana.";
Gene 288:129-138(2002).
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
AJ286345; CAB71009.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF452384; AAL40848.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z99708; CAB16848.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL161589; CAB80309.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY074296; AAL66993.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY117238; AAM51313.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A85430; A85430.
RefSeq NP_195361.1; -.
UniGene At.4607
3D structure databases
HSSP Q39034; 1QGJ. [HSSP ENTRY / PDB]
ModBase O23237.
Protein family/group databases
PeroxiBase 215; AtPrx49.
Organism-specific databases
GeneFarm 1881; 61.
TAIR At4g36430; -.
Gene expression databases
ArrayExpress O23237; -.
GermOnline AT4G36430; Arabidopsis thaliana.
Family and domain databases
InterPro IPR002016; Haem_peroxidase_pln/fun/bac.
IPR000823; Peroxidase_pln.
Graphical view of domain structure.
Pfam PF00141; peroxidase; 1.
Pfam graphical view of domain structure.
PRINTS PR00458; PEROXIDASE.
PR00461; PLPEROXIDASE.
PROSITE PS00435; PEROXIDASE_1; 1.
PS00436; PEROXIDASE_2; 1.
PS50873; PEROXIDASE_4; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS O23237.
Genome annotation databases
GeneID 829795; -.
GenomeReviews CT486007_GR; AT4G36430.
KEGG ath:AT4G36430; -.
NMPDR fig|3702.1.peg.21738; -.
Other
ProtoNet O23237.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Calcium; Complete proteome; Glycoprotein; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase; Secreted; Signal.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
SIGNAL   1    22  22     Potential. 
CHAIN   23   331  309     Peroxidase 49. PRO_0000023714
ACT_SITE   70    70        Proton acceptor (By similarity). 
METAL   71    71        Calcium 1 (By similarity). 
METAL   74    74        Calcium 1; via carbonyl oxygen (By similarity). 
METAL   76    76        Calcium 1; via carbonyl oxygen (By similarity). 
METAL   78    78        Calcium 1 (By similarity). 
METAL   80    80        Calcium 1 (By similarity). 
METAL   197   197        Iron (heme axial ligand) (By similarity). 
METAL   198   198        Calcium 2 (By similarity). 
METAL   249   249        Calcium 2 (By similarity). 
METAL   252   252        Calcium 2 (By similarity). 
METAL   257   257        Calcium 2 (By similarity). 
BINDING   167   167        Substrate; via carbonyl oxygen (By similarity). 
SITE   66    66  1     Transition state stabilizer (By similarity). 
CARBOHYD   170   170        N-linked (GlcNAc...) (Potential). 
CARBOHYD   213   213        N-linked (GlcNAc...) (Potential). 
DISULFID   39   119        By similarity. 
DISULFID   72    77        By similarity. 
DISULFID   125   326        By similarity. 
DISULFID   204   236        By similarity. 
Sequence information
Length: 331 AA [This is the length of the unprocessed precursor] Molecular weight: 36164 Da [This is the MW of the unprocessed precursor] CRC64: E9C0130D77406624 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MARLTSFLLL LSLICFVPLC LCDKSYGGKL FPGYYAHSCP QVNEIVRSVV AKAVARETRM 

        70         80         90        100        110        120 
AASLLRLHFH DCFVQGCDGS LLLDSSGRVA TEKNSNPNSK SARGFDVVDQ IKAELEKQCP 

       130        140        150        160        170        180 
GTVSCADVLT LAARDSSVLT GGPSWVVPLG RRDSRSASLS QSNNNIPAPN NTFQTILSKF 

       190        200        210        220        230        240 
NRQGLDITDL VALSGSHTIG FSRCTSFRQR LYNQSGNGSP DMTLEQSFAA NLRQRCPKSG 

       250        260        270        280        290        300 
GDQILSVLDI ISAASFDNSY FKNLIENKGL LNSDQVLFSS NEKSRELVKK YAEDQGEFFE 

       310        320        330 
QFAESMIKMG NISPLTGSSG EIRKNCRKIN S 

O23237 in FASTA format

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