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UniProtKB/Swiss-Prot entry Q9FUZ2


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

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Entry information
Entry name DEFC_ARATH
Primary accession number Q9FUZ2
Secondary accession numbers Q8LEH0 Q949U8 Q9LYJ4
Integrated into Swiss-Prot on December 5, 2001
Sequence was last modified on December 15, 2003 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 55)
Name and origin of the protein
Protein name Peptide deformylase, chloroplastic [Precursor]
Synonyms PDF
EC 3.5.1.88
Polypeptide deformylase
Gene name
Name: PDF1B
OrderedLocusNames: At5g14660
ORFNames: T15N1_150
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].
DOI=10.1093/emboj/19.21.5916; PubMed=11060042 [NCBI, ExPASy, EBI, Israel, Japan]
Giglione C., Serero A., Pierre M., Boisson B., Meinnel T.;
"Identification of eukaryotic peptide deformylases reveals universality of N-terminal protein processing mechanisms.";
EMBO J. 19:5916-5929(2000).
[2]
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).
[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.
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
AF269165; AAG33980.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL163792; CAB87633.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY050879; AAK92816.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY096673; AAM20307.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY085417; AAM62644.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T48639; T48639.
RefSeq NP_196970.1; -.
NP_850821.1; -.
UniGene At.5087
3D structure databases
HSSP Q9I7A8; 1N5N. [HSSP ENTRY / PDB]
ModBase Q9FUZ2.
Organism-specific databases
TAIR At5g14660; -.
Gene expression databases
ArrayExpress Q9FUZ2; -.
GermOnline AT5G14660; Arabidopsis thaliana.
Ontologies
GO
GO:0009507; Cellular component: chloroplast (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR000181; Fmet_deformylase.
Graphical view of domain structure.
Gene3D G3DSA:3.90.45.10; Fmet_deformylase; 1.
PANTHER PTHR10458; Fmet_deformylase; 1.
Pfam PF01327; Pep_deformylase; 1.
Pfam graphical view of domain structure.
PRINTS PR01576; PDEFORMYLASE.
ProDom PD003844; Fmet_deformylase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR00079; pept_deformyl; 1.
BLOCKS Q9FUZ2.
ProtoNet Q9FUZ2.
Genome annotation databases
GeneID 831318; -.
GenomeReviews BA000015_GR; AT5G14660.
KEGG ath:AT5G14660; -.
NMPDR fig|3702.1.peg.23602; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Chloroplast; Complete proteome; Hydrolase; Iron; Metal-binding; Plastid; Protein biosynthesis; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1     ?        Chloroplast (Potential). 
CHAIN   ?   273        Peptide deformylase, chloroplastic. PRO_0000006732
ACT_SITE   214   214        By similarity. 
METAL   171   171        Iron (By similarity). 
METAL   213   213        Iron (By similarity). 
METAL   217   217        Iron (By similarity). 
CONFLICT   48    48        T -> N (in Ref. 4; AAM62644). 
CONFLICT   205   205        R -> S (in Ref. 1; AAG33980). 
Sequence information
Length: 273 AA [This is the length of the unprocessed precursor] Molecular weight: 30610 Da [This is the MW of the unprocessed precursor] CRC64: 25CDA90ED6D9603E [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAVCNCFLQA PPLSRILLPV LSRRATTLSA GYGRLKSTVT FCSTVNRTSP LTSSVRAEVK 

        70         80         90        100        110        120 
RVSRKDDKVA SATDVQFETP LKIVEYPDPI LRAKNKRIDI FDENLKNLVD AMFDVMYKTD 

       130        140        150        160        170        180 
GIGLSAPQVG LNVQLMVFNP AGEPGEGKEI VLVNPKIKKY SDKLVPFDEG CLSFPGIYAE 

       190        200        210        220        230        240 
VVRPQSVKID ARDITGERFS ISLSRLPARI FQHEYDHLEG VLFFDRMTDQ VLDSIREELE 

       250        260        270 
ALEKKYEEKT GLPSPERVEA RQKRKAGVGF GKR 

Q9FUZ2 in FASTA format

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BLAST logo BLAST submission on ExPASy/SIB
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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