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Q5LNI7 (Q5LNI7_SILPO) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Peptide deformylase RuleBase RU003335
Gene names
Name:def-1 EMBL AAV96452.1
Ordered Locus Names:SPO3217
OrganismSilicibacter pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) [Complete proteome] [HAMAP]
Taxonomic identifier246200 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRuegeria

Protein attributes

Sequence length165 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

Formyl-L-methionyl peptide + H2O = formate + methionyl peptide. SAAS SAAS000181

Sequence similarities

Belongs to the polypeptide deformylase family. RuleBase RU003335

Ontologies

Keywords
   Biological processProtein biosynthesis SAAS SAAS000181
   LigandMetal-binding SAAS SAAS000181
   Molecular functionHydrolase SAAS SAAS000181 EMBL AAV96452.1
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processtranslation

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functioniron ion binding

Inferred from electronic annotation. Source: InterPro

peptide deformylase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequences

Sequence LengthMass (Da)Tools
Q5LNI7 [UniParc].

Last modified February 1, 2005. Version 1.
Checksum: 64FF8A665B073A4F

FASTA16518,556
        10         20         30         40         50         60 
MTVRRCLPWP DKHLRTRAAE VSEITDEIRA IWTDMIDTME AMPGVGLAAP QIGVMLRLAV 

        70         80         90        100        110        120 
VDGSSERGRA VRLANPEILH ASIELREHDE ASPNLPGVSA KLKRPRAVTV RFLNEQGQVD 

       130        140        150        160 
RRDFVGIEAT SVQHQIDHLN GRMYFDNLSK VKRDMLLRKA RKLGG 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000031 Genomic DNA. Translation: AAV96452.1.
RefSeqYP_168420.1. NC_003911.11.

3D structure databases

ProteinModelPortalQ5LNI7.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3194969.
GenomeReviewsGene locus SPO3217 in contig CP000031_GR.
KEGGsil:SPO3217.
NMPDRfig|246200.3.peg.3590.
PATRIC23379881. VBIRuePom114501_3284.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG665227.
OMAQHQIDHL.
ProtClustDBCLSK934097.

Enzyme and pathway databases

BioCycRPOM246200:SPO_3217-MONOMER.

Family and domain databases

HAMAPMF_00163. Pep_deformylase.
[Tree]
InterProIPR000181. Fmet_deformylase.
IPR023635. Peptide_deformylase.
[Graphical view]
Gene3DG3DSA:3.90.45.10. Fmet_deformylase. 1 hit.
KOK01462.
PANTHERPTHR10458. Fmet_deformylase. 1 hit.
PfamPF01327. Pep_deformylase. 1 hit.
[Graphical view]
PIRSFPIRSF004749. Pep_def. 1 hit.
PRINTSPR01576. PDEFORMYLASE.
SUPFAMSSF56420. Fmet_deformylase. 1 hit.
TIGRFAMsTIGR00079. Pept_deformyl. 1 hit.
ProtoNetSearch...

Entry information

Entry nameQ5LNI7_SILPO
AccessionPrimary (citable) accession number: Q5LNI7
Entry history
Integrated into UniProtKB/TrEMBL: February 1, 2005
Last sequence update: February 1, 2005
Last modified: December 14, 2011
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)