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Q7YT16 (LYS1_MUSDO) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Lysozyme 1

EC=3.2.1.17
Alternative name(s):
1,4-beta-N-acetylmuramidase 1
OrganismMusca domestica (House fly)
Taxonomic identifier7370 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaMuscoideaMuscidaeMusca

Protein attributes

Sequence length141 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May not function as a self-defense protein, but as a digestive enzyme, probably in the gut of the insect body. Inactive towards Micrococcus luteus. Active toward glycol chitin.

Catalytic activity

Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.

Sequence similarities

Belongs to the glycosyl hydrolase 22 family.

Biophysicochemical properties

pH dependence:

Active at acidic pHs. Inactive above pH 7.

Ontologies

Keywords
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processcell wall macromolecule catabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular_functionlysozyme activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Ref.2
Chain20 – 141122Lysozyme 1
PRO_0000018508

Sites

Active site511 By similarity
Active site691 By similarity

Amino acid modifications

Glycosylation651N-linked (GlcNAc...) Potential
Glycosylation1041N-linked (GlcNAc...) Potential
Disulfide bond25 ↔ 140 By similarity
Disulfide bond46 ↔ 130 By similarity
Disulfide bond81 ↔ 97 By similarity
Disulfide bond93 ↔ 111 By similarity

Secondary structure

....................... 141
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q7YT16 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: C640C6407AD80F0E

FASTA14115,733
        10         20         30         40         50         60 
MKFFIVLVAA LALAAPAMGK TFTRCSLARE MYALGVPKSE LPQWTCIAEH ESSYRTNVVG 

        70         80         90        100        110        120 
PTNSNGSNDY GIFQINNYYW CQPSNGRFSY NECHLSCDAL LTDNISNSVT CARKIKSQQG 

       130        140 
WTAWSTWKYC SGSLPSINDC F 

« Hide

References

[1]"Cloning, sequencing and characterization of a digestive lysozyme from Musca domestica midgut."
Chimoy P., Marana S.R., Ferreira C., Terra W.R.
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Midgut epithelium.
[2]"Insect lysozyme from house fly (Musca domestica) larvae: possible digestive function based on sequence and enzymatic properties."
Ito Y., Nakamura M., Hotani T., Imoto T.
J. Biochem. 118:546-551(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 20-141.
Tissue: Larva.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY344589 mRNA. Translation: AAQ20048.1.
PIRPC4062.
RefSeqXP_005181668.1. XM_005181611.1.
XP_005185827.1. XM_005185770.1.
XP_005185828.1. XM_005185771.1.
XP_005185831.1. XM_005185774.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2FBDX-ray1.90A/B20-141[»]
2H5ZX-ray1.92A/B20-141[»]
ProteinModelPortalQ7YT16.
SMRQ7YT16. Positions 20-141.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH22. Glycoside Hydrolase Family 22.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID101892974.
101893151.
101893594.
101895951.

Enzyme and pathway databases

BRENDA3.2.1.17. 3486.

Family and domain databases

InterProIPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
IPR000974. Glyco_hydro_22_lys.
IPR023346. Lysozyme-like_dom.
[Graphical view]
PfamPF00062. Lys. 1 hit.
[Graphical view]
PRINTSPR00137. LYSOZYME.
PR00135. LYZLACT.
SMARTSM00263. LYZ1. 1 hit.
[Graphical view]
SUPFAMSSF53955. SSF53955. 1 hit.
PROSITEPS00128. LACTALBUMIN_LYSOZYME_1. 1 hit.
PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ7YT16.

Entry information

Entry nameLYS1_MUSDO
AccessionPrimary (citable) accession number: Q7YT16
Secondary accession number(s): Q7M437
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: October 1, 2003
Last modified: March 19, 2014
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries