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Q90X99 (LYG_EPICO) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Protein attributes

Sequence length194 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Has lytic activity against M.lysodeikticus, V.alginolyticus from Epinephelus fario, V.vulnificus from culture water, A.hydrophila from soft-shell turtle, A.hydrophila from goldfish and V.parahaemolyticus, P.fluorescens and V.fluvialis from culture water.

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.

Tissue specificity

Expressed in intestine, liver, spleen, anterior kidney, posterior kidney, heart, gill, muscle and leukocytes. Ref.1

Sequence similarities

Belongs to the glycosyl hydrolase 23 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 194194Lysozyme g
PRO_0000193518

Sites

Active site711 By similarity
Active site841 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q90X99 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 8A12197359127023

FASTA19421,179
        10         20         30         40         50         60 
MGYGNIMNVE TTGASWQTAQ QDKLGYSGVR ASHTMANTDS GRMERYRSKI NSVGAKYGID 

        70         80         90        100        110        120 
PALIAAIISE ESRAGNVLHD GWGDYDSNRG AYNAWGLMQV DVNPNGGGHT ARGAWDSEEH 

       130        140        150        160        170        180 
LSQGAEILVY FIGRIRNKFP GWNTEQQLKG GIAAYNMGDG NVHSYDNVDG RTTGGDYSND 

       190 
VVARAQWYKT QKGF 

« Hide

References

[1]"Molecular cloning, expression of orange-spotted grouper goose-type lysozyme cDNA, and lytic activity of its recombinant protein."
Yin Z.X., He J.G., Deng W.X., Chan S.M.
Dis. Aquat. Organ. 55:117-123(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, TISSUE SPECIFICITY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF416458 mRNA. Translation: AAL08021.2.

3D structure databases

ProteinModelPortalQ90X99.
SMRQ90X99. Positions 2-194.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH23. Glycoside Hydrolase Family 23.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG006299.

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_EPICO
AccessionPrimary (citable) accession number: Q90X99
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: December 1, 2001
Last modified: July 9, 2014
This is version 46 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