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Reviewed, UniProtKB/Swiss-Prot B6RGY0 (DEF1A_ORYSJ)

Last modified October 13, 2009. Version 8. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Peptide deformylase 1A, chloroplastic
      Short name=PDF 1A
      Short name=OsPDF1A
    EC=3.5.1.88
Gene names
Name: PDF1A
Ordered Locus Names: Os01g0555800, LOC_Os01g37510
ORF Names: OsJ_002139
OrganismOryza sativa subsp. japonica (Rice)
Taxonomic identifier39947 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladeEhrhartoideaeOryzeaeOryza

Protein attributes

Sequence length260 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Removes the formyl group from the N-terminal Met of newly synthesized proteins.

Catalytic activity

Formyl-L-methionyl peptide + H2O = formate + methionyl peptide.

Cofactor

Binds 1 Zinc ion per subunit By similarity.

Enzyme regulation

Inhibited by actinonin.

Subunit structure

Homodimer By similarity.

Subcellular location

Plastidchloroplast stroma. Ref.1

Tissue specificity

Mainly expressed in roots. Lower expression in shoots, mature panicles at flowering stages and mature leaves. Ref.1

Sequence similarities

Belongs to the polypeptide deformylase family.

Sequence caution

The sequence BAF05237.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence EAZ12314.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentChloroplast
Plastid
   DomainTransit peptide
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Gene Ontology (GO)
   Biological processtranslation

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentchloroplast stroma

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioniron ion binding

Inferred from electronic annotation. Source: InterPro

peptide deformylase activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4343Chloroplast Potential
Chain44 – 260217Peptide deformylase 1A, chloroplastic
PRO_0000369420

Regions

Region114 – 1174Substrate binding By similarity
Region182 – 1876Dimerization By similarity
Region227 – 24519Dimerization By similarity
Compositional bias47 – 504Poly-Gly
Compositional bias57 – 637Poly-Gly

Sites

Active site2221 By similarity
Metal binding1791Zinc By similarity
Metal binding2211Zinc By similarity
Metal binding2251Zinc By similarity
Binding site1781Substrate; via carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
B6RGY0-1 [UniParc].

Last modified December 16, 2008. Version 1.
Checksum: A0CEB3C83E884CCE

FASTA26027,493
        10         20         30         40         50         60 
MEAHLRPLSA AALLLSPAAP LPTAVAASAR RASPGGRRWS SVRASAGGGG WLSGLLGGKG 

        70         80         90        100        110        120 
GGGAPTAMTV TPGTVKAGDP VLHEPAQDVA PGDIPSEKVQ GVIDRMVAVM RKAPGVGLAA 

       130        140        150        160        170        180 
PQIGVPLKII VLEDTQEYIS YAPKKDIEAQ DRRPFDLLVI INPKLKTTSK RTALFFEGCL 

       190        200        210        220        230        240 
SVDGYRALVE RHLDVEVSGL DRNGRPIKVE ASGWQARILQ HECDHLEGTL YVDTMVPRTF 

       250        260 
RIVDNLDLPL PVGCPPIGAR 

« Hide

References

« Hide 'large scale' references
[1]"Rice peptide deformylase PDF1B is crucial for development of chloroplasts."
Moon S., Giglione C., Lee D.-Y., An S., Jeong D.-H., Meinnel T., An G.
Plant Cell Physiol. 49:1536-1546(2008) [PubMed: 18718933] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
Strain: cv. Dongjin.
[2]"The map-based sequence of the rice genome."
International rice genome sequencing project (IRGSP)
Nature 436:793-800(2005) [PubMed: 16100779] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Nipponbare.
[3]"Curated genome annotation of Oryza sativa ssp. japonica and comparative genome analysis with Arabidopsis thaliana."
The rice annotation project (RAP)
Genome Res. 17:175-183(2007) [PubMed: 17210932] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: cv. Nipponbare.
[4]"The genomes of Oryza sativa: a history of duplications."
Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S., Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L. expand/collapse author list , Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J., Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X., Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y., Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L., Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H., Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z., Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L., Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.
PLoS Biol. 3:266-281(2005) [PubMed: 15685292] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Nipponbare.

Cross-references

Sequence databases

EU213045 mRNA. Translation: ABY64739.1.
AP008207 Genomic DNA. Translation: BAF05237.1. Sequence problems.
CM000138 Genomic DNA. Translation: EAZ12314.1. Sequence problems.
RefSeqNP_001043323.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID4324565.
GenomeReviewsGene locus PDF1A in contig AP008207_GR.
KEGGosa:4324565.

Family and domain databases

InterProIPR000181. Fmet_deformylase.
[Graphical view]
Gene3DG3DSA:3.90.45.10. Fmet_deformylase. 1 hit.
PANTHERPTHR10458. Fmet_deformylase. 1 hit.
PfamPF01327. Pep_deformylase. 1 hit.
[Graphical view]
PRINTSPR01576. PDEFORMYLASE.
TIGRFAMsTIGR00079. pept_deformyl. 1 hit.
ProtoNetSearch...

Entry information

Entry nameDEF1A_ORYSJ
AccessionPrimary (citable) accession number: B6RGY0
Secondary accession number(s): A2ZUB7, Q0JLZ1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: December 16, 2008
Last modified: October 13, 2009
This is version 8 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

Oryza sativa (rice)

Index of Oryza sativa entries and their corresponding gene designations

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents