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G3XDD8 (LYG_DRONO) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 9. 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:
Lysozyme G

EC=3.2.1.17
Alternative name(s):
1,4-beta-N-acetylmuramidase
OrganismDromaius novaehollandiae (Emu)
Taxonomic identifier8790 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesPalaeognathaeCasuariiformesDromaiidaeDromaius

Protein attributes

Sequence length204 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Has bacteriolytic activity against M.luteus. Ref.1

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. UniProtKB Q90X99

Subcellular location

Secreted By similarity UniProtKB Q90X99.

Sequence similarities

Belongs to the glycosyl hydrolase 23 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 204185Lysozyme G
PRO_5000795990

Sites

Active site921 By similarity UniProtKB P00718
Active site1051 By similarity UniProtKB P00718

Amino acid modifications

Disulfide bond23 ↔ 79 By similarity UniProtKB P00718
Disulfide bond37 ↔ 48 By similarity UniProtKB P00718

Sequences

Sequence LengthMass (Da)Tools
G3XDD8 [UniParc].

Last modified December 14, 2011. Version 1.
Checksum: 4061327BB92C820C

FASTA20422,493
        10         20         30         40         50         60 
MHLMLVLLGL AALLGTSQSQ TGCYGVVNRI DTTGASCETA KPEKLNYCGV AASRMIAERD 

        70         80         90        100        110        120 
LRSMDRYKTL IKKVGQKLCV DPAVIAGIIS RESHAGKALK NGWGDNGNGF GLMQVDKRSH 

       130        140        150        160        170        180 
TPVGEWNGER HLTQGTEILI SMIKKIQKKF PRWTKEQQLK GGISAYNAGS GNVRSYERMD 

       190        200 
IGTTHNDYAN DVVARAQYYK QHGY 

« Hide

References

[1]"Molecular characterization of goose- and chicken-type lysozymes in emu (Dromaius novaehollandiae): evidence for extremely low lysozyme levels in emu egg white."
Maehashi K., Matano M., Irisawa T., Uchino M., Kashiwagi Y., Watanabe T.
Gene 492:244-249(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, TISSUE SPECIFICITY.
Tissue: Ovary and Oviduct.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB451700 mRNA. Translation: BAL03618.1.
AB462632 Genomic DNA. Translation: BAL03619.1.

3D structure databases

ProteinModelPortalG3XDD8.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR002152. Glyco_hydro_23.
IPR023346. Lysozyme-like_dom.
IPR008258. TGlycosylase-like_SLT.
[Graphical view]
PfamPF01464. SLT. 1 hit.
[Graphical view]
PIRSFPIRSF001065. Lysozyme_g. 1 hit.
PRINTSPR00749. LYSOZYMEG.
SUPFAMSSF53955. SSF53955. 1 hit.
ProtoNetSearch...

Entry information

Entry nameLYG_DRONO
AccessionPrimary (citable) accession number: G3XDD8
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2012
Last sequence update: December 14, 2011
Last modified: June 11, 2014
This is version 9 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries