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UniProtKB/Swiss-Prot entry Q9FG34


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

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Entry information
Entry name PER54_ARATH
Primary accession number Q9FG34
Secondary accession number P93729
Integrated into Swiss-Prot on December 6, 2002
Sequence was last modified on March 1, 2001 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 66)
Name and origin of the protein
Protein name Peroxidase 54 [Precursor]
Synonyms Atperox P54
EC 1.11.1.7
ATP29a
Gene name
Name: PER54
Synonyms: P54
OrderedLocusNames: At5g06730
ORFNames: MPH15.9
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 [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/35048507; PubMed=11130714 [NCBI, ExPASy, EBI, Israel, Japan]
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
Nature 408:823-826(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
DOI=10.1126/science.1071006; PubMed=11910074 [NCBI, ExPASy, EBI, Israel, Japan]
Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T., Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K., Shinagawa A., Shinozaki K.;
"Functional annotation of a full-length Arabidopsis cDNA collection.";
Science 296:141-145(2002).
[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]
NUCLEOTIDE SEQUENCE [MRNA] OF 212-358.
STRAIN=cv. Columbia;
TISSUE=Root;
Welinder K.G., Jespersen H.M., Kjaersgaard I.V.H., Justesen A.F., Oestergaard L., Abelskov A.K., Jensen R.B., Hansen L.N., Rasmussen S.K.;
"From expressed sequence tags to structure, function, evolution and expression of 28 ER-targeted Arabidopsis peroxidases.";
Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
[6]
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
AP002032; BAB09807.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK118827; BAC43417.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT008584; AAP40411.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY088509; AAM66044.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Y11794; CAA72490.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_196291.1; -.
UniGene At.90
3D structure databases
HSSP Q42578; 1PA2. [HSSP ENTRY / PDB]
SMR Q9FG34; 32-335.
ModBase Q9FG34.
Protein family/group databases
PeroxiBase 220; AtPrx54.
Organism-specific databases
GeneFarm 1908; 61.
TAIR At5g06730; -.
Gene expression databases
ArrayExpress Q9FG34; -.
GermOnline AT5G06730; 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 Q9FG34.
Genome annotation databases
GeneID 830562; -.
GenomeReviews BA000015_GR; AT5G06730.
KEGG ath:AT5G06730; -.
NMPDR fig|3702.1.peg.22804; -.
Other
ProtoNet Q9FG34.
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; Pyrrolidone carboxylic acid; Secreted; Signal; Vacuole.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
SIGNAL   1    31  31     Potential. 
CHAIN   32   358  327     Peroxidase 54. PRO_0000023719
ACT_SITE   73    73        Proton acceptor (By similarity). 
METAL   74    74        Calcium 1 (By similarity). 
METAL   77    77        Calcium 1; via carbonyl oxygen (By similarity). 
METAL   79    79        Calcium 1; via carbonyl oxygen (By similarity). 
METAL   81    81        Calcium 1 (By similarity). 
METAL   83    83        Calcium 1 (By similarity). 
METAL   200   200        Iron (heme axial ligand) (By similarity). 
METAL   201   201        Calcium 2 (By similarity). 
METAL   252   252        Calcium 2 (By similarity). 
METAL   255   255        Calcium 2 (By similarity). 
METAL   260   260        Calcium 2 (By similarity). 
BINDING   170   170        Substrate; via carbonyl oxygen (By similarity). 
SITE   69    69  1     Transition state stabilizer (By similarity). 
MOD_RES   32    32        Pyrrolidone carboxylic acid (By similarity). 
CARBOHYD   34    34        N-linked (GlcNAc...) (Potential). 
CARBOHYD   44    44        N-linked (GlcNAc...) (Potential). 
CARBOHYD   103   103        N-linked (GlcNAc...) (Potential). 
CARBOHYD   161   161        N-linked (GlcNAc...) (Potential). 
CARBOHYD   166   166        N-linked (GlcNAc...) (Potential). 
CARBOHYD   178   178        N-linked (GlcNAc...) (Potential). 
CARBOHYD   218   218        N-linked (GlcNAc...) (Potential). 
CARBOHYD   228   228        N-linked (GlcNAc...) (Potential). 
CARBOHYD   242   242        N-linked (GlcNAc...) (Potential). 
CARBOHYD   298   298        N-linked (GlcNAc...) (Potential). 
DISULFID   42   122        By similarity. 
DISULFID   75    80        By similarity. 
DISULFID   128   330        By similarity. 
DISULFID   207   239        By similarity. 
CONFLICT   21    21        I -> V (in Ref. 4; AAM66044). 
CONFLICT   28    28        T -> A (in Ref. 4; AAM66044). 
CONFLICT   189   189        K -> N (in Ref. 4; AAM66044). 
Sequence information
Length: 358 AA [This is the length of the unprocessed precursor] Molecular weight: 37290 Da [This is the MW of the unprocessed precursor] CRC64: F9841562BAC5106B [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAVTSSSSTC DGFFIISLIV IVSSLFGTSS AQLNATFYSG TCPNASAIVR STIQQALQSD 

        70         80         90        100        110        120 
ARIGGSLIRL HFHDCFVNGC DGSLLLDDTS SIQSEKNAPA NANSTRGFNV VDSIKTALEN 

       130        140        150        160        170        180 
ACPGIVSCSD ILALASEASV SLAGGPSWTV LLGRRDGLTA NLSGANSSLP SPFEGLNNIT 

       190        200        210        220        230        240 
SKFVAVGLKT TDVVSLSGAH TFGRGQCVTF NNRLFNFNGT GNPDPTLNST LLSSLQQLCP 

       250        260        270        280        290        300 
QNGSNTGITN LDLSTPDAFD NNYFTNLQSN NGLLQSDQEL FSNTGSATVP IVNSFASNQT 

       310        320        330        340        350 
LFFEAFVQSM IKMGNISPLT GSSGEIRQDC KVVNGQSSAT EAGDIQLQSD GPVSVADM 

Q9FG34 in FASTA format

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