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UniProtKB/Swiss-Prot entry Q93V93


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

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Entry information
Entry name PER44_ARATH
Primary accession number Q93V93
Secondary accession number Q9SZH5
Integrated into Swiss-Prot on December 6, 2002
Sequence was last modified on December 1, 2001 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 59)
Name and origin of the protein
Protein name Peroxidase 44 [Precursor]
Synonyms Atperox P44
EC 1.11.1.7
ATP35
Gene name
Name: PER44
Synonyms: P44
OrderedLocusNames: At4g26010
ORFNames: F20B18.120
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
AF452386; AAL40850.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL049483; CAB39666.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL161564; CAB79456.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF412066; AAL06519.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF428430; AAL16199.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY090260; AAL90921.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T04256; T04256.
RefSeq NP_567738.1; -.
UniGene At.2955
3D structure databases
HSSP Q39034; 1QGJ. [HSSP ENTRY / PDB]
ModBase Q93V93.
Protein family/group databases
PeroxiBase 210; AtPrx44.
Organism-specific databases
GeneFarm 1874; 61.
TAIR At4g26010; -.
Gene expression databases
ArrayExpress Q93V93; -.
GermOnline AT4G26010; 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; FALSE_NEG.
PS00436; PEROXIDASE_2; 1.
PS50873; PEROXIDASE_4; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q93V93.
Genome annotation databases
GeneID 828707; -.
GenomeReviews CT486007_GR; AT4G26010.
KEGG ath:AT4G26010; -.
NMPDR fig|3702.1.peg.20518; -.
Other
ProtoNet Q93V93.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Calcium; Complete proteome; 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    20  20     Potential. 
CHAIN   21   310  290     Peroxidase 44. PRO_0000023710
ACT_SITE   62    62        Proton acceptor (By similarity). 
METAL   63    63        Calcium 1 (By similarity). 
METAL   66    66        Calcium 1 (via carbonyl oxygen) (By similarity). 
METAL   68    68        Calcium 1 (via carbonyl oxygen) (By similarity). 
METAL   70    70        Calcium 1 (By similarity). 
METAL   72    72        Calcium 1 (By similarity). 
METAL   187   187        Iron (heme axial ligand) (By similarity). 
METAL   188   188        Calcium 2 (By similarity). 
METAL   229   229        Calcium 2 (By similarity). 
METAL   232   232        Calcium 2 (By similarity). 
METAL   237   237        Calcium 2 (By similarity). 
BINDING   156   156        Substrate; via carbonyl oxygen (By similarity). 
SITE   58    58  1     Transition state stabilizer (By similarity). 
MOD_RES   21    21        Pyrrolidone carboxylic acid (By similarity). 
DISULFID   31   110        By similarity. 
DISULFID   64    69        By similarity. 
DISULFID   116   305        By similarity. 
DISULFID   194   218        By similarity. 
Sequence information
Length: 310 AA [This is the length of the unprocessed precursor] Molecular weight: 33806 Da [This is the MW of the unprocessed precursor] CRC64: E14CEB2BA47B5550 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MRSITALFFL FCFLAPSALA QLRTGFYSRS CPRAESIVAS VVANRFRSDK SITAAFLRMQ 

        70         80         90        100        110        120 
FHDCFVRGCD ASLLIDPRPG RPSEKSTGPN ASVRGYEIID EAKRQLEAAC PRTVSCADIV 

       130        140        150        160        170        180 
TLATRDSVAL AGGPRFSVPT GRRDGLRSNP NDVNLPGPTI PVSASIQLFA AQGMNTNDMV 

       190        200        210        220        230        240 
TLIGGGHSVG VAHCSLFQDR LSDRAMEPSL KSSLRRKCSS PNDPTTFLDQ KTSFTVDNAI 

       250        260        270        280        290        300 
YGEIRRQRGI LRIDQNLGLD RSTSGIVSGY ASSNTLFRKR FAEALVKMGT IKVLTGRSGE 

       310 
IRRNCRVFNN 

Q93V93 in FASTA format

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