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UniProtKB/Swiss-Prot entry Q9SZB9


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

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Entry information
Entry name PER47_ARATH
Primary accession number Q9SZB9
Secondary accession numbers None
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 56)
Name and origin of the protein
Protein name Peroxidase 47 [Precursor]
Synonyms Atperox P47
EC 1.11.1.7
ATP32
Gene name
Name: PER47
Synonyms: P47
OrderedLocusNames: At4g33420
ORFNames: F17M5.180
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]
DEVELOPMENTAL STAGE.
STRAIN=cv. Columbia;
Zhu T., Budworth P., Han B., Brown D., Chang H.-S., Zou G., Wang X.;
"Toward elucidating the global gene expression patterns of developing Arabidopsis: parallel analysis of 8300 genes by a high-density oligonucleotide probe array.";
Plant Physiol. Biochem. 39:221-242(2001).
[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
AF451951; AAL40837.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL035678; CAB38800.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL161583; CAB80059.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T05993; T05993.
3D structure databases
HSSP Q39034; 1QGJ. [HSSP ENTRY / PDB]
ModBase Q9SZB9.
Protein family/group databases
PeroxiBase 213; AtPrx47.
Organism-specific databases
GeneFarm 1879; 61.
TAIR At4g33420; -.
Gene expression databases
GermOnline AT4G33420; 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 Q9SZB9.
Genome annotation databases
GenomeReviews CT486007_GR; AT4G33420.
NMPDR fig|3702.1.peg.21384; -.
Other
ProtoNet Q9SZB9.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Calcium; Complete proteome; Glycoprotein; Heme; Iron; Metal-binding; Oxidoreductase; Peroxidase; Secreted; Signal.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
SIGNAL   1    25  25     Potential. 
CHAIN   26   314  289     Peroxidase 47. PRO_0000023713
ACT_SITE   66    66        Proton acceptor (By similarity). 
METAL   67    67        Calcium 1 (By similarity). 
METAL   72    72        Calcium 1; via carbonyl oxygen (By similarity). 
METAL   74    74        Calcium 1 (By similarity). 
METAL   76    76        Calcium 1 (By similarity). 
METAL   191   191        Iron (heme axial ligand) (By similarity). 
METAL   192   192        Calcium 2 (By similarity). 
METAL   235   235        Calcium 2 (By similarity). 
METAL   237   237        Calcium 2 (By similarity). 
METAL   242   242        Calcium 2 (By similarity). 
BINDING   161   161        Substrate; via carbonyl oxygen (By similarity). 
SITE   62    62  1     Transition state stabilizer (By similarity). 
CARBOHYD   166   166        N-linked (GlcNAc...) (Potential). 
DISULFID   35   114        By similarity. 
DISULFID   68    73        By similarity. 
DISULFID   120   310        By similarity. 
DISULFID   198   224        By similarity. 
Sequence information
Length: 314 AA [This is the length of the unprocessed precursor] Molecular weight: 34585 Da [This is the MW of the unprocessed precursor] CRC64: EF500FACD2FDA692 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MVRANIVSMV LLMHAIVGFP FHARGLSMTY YMMSCPFAEQ IVKNSVNNAL QADPTLAAGL 

        70         80         90        100        110        120 
IRMLFHDCFI EGCDASILLD STKDNTAEKD SPANLSLRGY EIIDDAKEKI ENRCPGVVSC 

       130        140        150        160        170        180 
ADIVAMAARD AVFWAGGPYY DIPKGRFDGK RSKIEDTRNL PSPFLNASQL IQTFGQRGFT 

       190        200        210        220        230        240 
PQDVVALSGA HTLGVARCSS FKARLTVPDS SLDSTFANTL SKTCSAGDNA EQPFDATRND 

       250        260        270        280        290        300 
FDNAYFNALQ MKSGVLFSDQ TLFNTPRTRN LVNGYALNQA KFFFDFQQAM RKMSNLDVKL 

       310 
GSQGEVRQNC RSIN 

Q9SZB9 in FASTA format

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