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UniProtKB/Swiss-Prot entry Q9SZE7


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

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Entry information
Entry name PER51_ARATH
Primary accession number Q9SZE7
Secondary accession number Q8VYK8
Integrated into Swiss-Prot on December 6, 2002
Sequence was last modified on May 1, 2000 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 67)
Name and origin of the protein
Protein name Peroxidase 51 [Precursor]
Synonyms Atperox P51
EC 1.11.1.7
ATP37
Gene name
Name: PER51
Synonyms: P51
OrderedLocusNames: At4g37530
ORFNames: F19F18.20, F6G17.2
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;
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).
[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]
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
AF469928; AAL79842.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL035605; CAB38292.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL161591; CAB80418.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL035601; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
AY070459; AAL49862.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY150515; AAN13031.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T04710; T04710.
RefSeq NP_195469.1; -.
UniGene At.68229
3D structure databases
HSSP Q42578; 1PA2. [HSSP ENTRY / PDB]
ModBase Q9SZE7.
Protein family/group databases
PeroxiBase 217; AtPrx51.
Organism-specific databases
GeneFarm 1883; 61.
TAIR At4g37530; -.
Gene expression databases
ArrayExpress Q9SZE7; -.
GermOnline AT4G37530; 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; FALSE_NEG.
PS50873; PEROXIDASE_4; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q9SZE7.
Genome annotation databases
GeneID 829908; -.
GenomeReviews CT486007_GR; AT4G37530.
NMPDR fig|3702.1.peg.21864; -.
Other
ProtoNet Q9SZE7.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Calcium; Complete proteome; Glycoprotein; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase; Pyrrolidone carboxylic acid; Secreted; Signal.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
SIGNAL   1    25  25     Potential. 
CHAIN   26   329  304     Peroxidase 51. PRO_0000023716
ACT_SITE   67    67        Proton acceptor (By similarity). 
METAL   68    68        Calcium 1 (By similarity). 
METAL   71    71        Calcium 1; via carbonyl oxygen (By similarity). 
METAL   73    73        Calcium 1; via carbonyl oxygen (By similarity). 
METAL   75    75        Calcium 1 (By similarity). 
METAL   77    77        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   63    63  1     Transition state stabilizer (By similarity). 
MOD_RES   26    26        Pyrrolidone carboxylic acid (By similarity). 
CARBOHYD   215   215        N-linked (GlcNAc...) (Potential). 
DISULFID   36   119        By similarity. 
DISULFID   69    74        By similarity. 
DISULFID   125   325        By similarity. 
DISULFID   204   236        By similarity. 
CONFLICT   31    31        F -> L (in Ref. 3; AAL49862). 
Sequence information
Length: 329 AA [This is the length of the unprocessed precursor] Molecular weight: 35989 Da [This is the MW of the unprocessed precursor] CRC64: DF4D71BB1503F145 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MVVMNKTNLL LLILSLFLAI NLSSAQLRGD FYAGTCPNVE QIVRNAVQKK IQQTFTTIPA 

        70         80         90        100        110        120 
TLRLYFHDCF VNGCDASVMI ASTNTNKAEK DHEDNLSLAG DGFDTVIKAK EAVDAVPNCR 

       130        140        150        160        170        180 
NKVSCADILT MATRDVVNLA GGPQYAVELG RRDGLSSSAS SVTGKLPKPT FDLNQLNALF 

       190        200        210        220        230        240 
AENGLSPNDM IALSGAHTLG FAHCTKVFNR LYNFNKTNNV DPTINKDYVT ELKASCPQNI 

       250        260        270        280        290        300 
DPRVAINMDP NTPRQFDNVY YKNLQQGKGL FTSDQVLFTD SRSKPTVDLW ANNGQLFNQA 

       310        320 
FISSMIKLGR VGVKTGSNGN IRRDCGAFN 

Q9SZE7 in FASTA format

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