Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q70PU2 (PGSC1_DROSI) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peptidoglycan-recognition protein SC1a/b

EC=3.5.1.28
Gene names
Name:PGRP-SC1a
AND
Name:PGRP-SC1b
OrganismDrosophila simulans (Fruit fly)
Taxonomic identifier7240 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length185 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

N-acetylmuramyl-L-alanine amidase involved in innate immunity by degrading bacterial peptidoglycans (PGN). Plays a scavenger role by digesting biologically active PGN into biologically inactive fragments. Has no direct bacteriolytic activity By similarity.

Catalytic activity

Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.

Cofactor

Zinc By similarity.

Subcellular location

Secreted Potential.

Sequence similarities

Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.

Ontologies

Keywords
   Biological processImmunity
Innate immunity
   Cellular componentSecreted
   DomainSignal
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
   PTMDisulfide bond
Gene Ontology (GO)
   Biological_processinnate immune response

Inferred from electronic annotation. Source: UniProtKB-KW

peptidoglycan catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionN-acetylmuramoyl-L-alanine amidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 185164Peptidoglycan-recognition protein SC1a/b
PRO_0000023911

Sites

Metal binding521Zinc By similarity
Metal binding861Zinc By similarity
Metal binding1601Zinc By similarity
Metal binding1681Zinc By similarity

Amino acid modifications

Disulfide bond58 ↔ 64 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q70PU2 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: F6368B74A378FC1E

FASTA18520,366
        10         20         30         40         50         60 
MVSKVALLLA VLVCSQYMAQ GVYVVSKAEW GGRGAKWTVA LGNYLSYAII HHTAGSYCET 

        70         80         90        100        110        120 
RAQCNAVLQS VQAYHMDSLG WPDIGYNFLI GGDGNVYEGR GWNNMGAHAA EWNPYSIGIS 

       130        140        150        160        170        180 
FLGNYNWDTL EPNMISAAQQ LLNDAVNRGQ LSSGYILYGH RQVSATECPG THIWNEIRGW 


SHWSG 

« Hide

References

[1]"The evolution of parasite recognition genes in the innate immune system: purifying selection on Drosophila melanogaster peptidoglycan recognition proteins."
Jiggins F.M., Hurst G.D.D.
J. Mol. Evol. 57:598-605(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: C167.4.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ556587 Genomic DNA. Translation: CAD89152.1.
AJ556610 Genomic DNA. Translation: CAD89175.1.

3D structure databases

ProteinModelPortalQ70PU2.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

FlyBaseFBgn0068646. Dsim\PGRP-SC1a.
FBgn0067515. Dsim\PGRP-SC1b.

Phylogenomic databases

OrthoDBEOG757CZ5.

Family and domain databases

Gene3D3.40.80.10. 1 hit.
InterProIPR002502. Amidase_domain.
IPR017331. Peptidoglycan_recognition.
IPR015510. PGRP.
IPR006619. PGRP_domain_met/bac.
[Graphical view]
PANTHERPTHR11022. PTHR11022. 1 hit.
PfamPF01510. Amidase_2. 1 hit.
[Graphical view]
PIRSFPIRSF037945. PGRPs. 1 hit.
SMARTSM00644. Ami_2. 1 hit.
SM00701. PGRP. 1 hit.
[Graphical view]
SUPFAMSSF55846. SSF55846. 1 hit.
ProtoNetSearch...

Entry information

Entry namePGSC1_DROSI
AccessionPrimary (citable) accession number: Q70PU2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: July 5, 2004
Last modified: November 13, 2013
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase