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Protein

Lysozyme g

Gene
N/A
Organism
Epinephelus coioides (Orange-spotted grouper) (Epinephelus nebulosus)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei71 – 711By similarity
Active sitei84 – 841By similarity

GO - Molecular functioni

  1. lysozyme activity Source: UniProtKB-EC

GO - Biological processi

  1. cell wall macromolecule catabolic process Source: InterPro
  2. cytolysis Source: UniProtKB-KW
  3. defense response to bacterium Source: UniProtKB-KW
  4. peptidoglycan catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Antimicrobial, Bacteriolytic enzyme, Glycosidase, Hydrolase

Protein family/group databases

CAZyiGH23. Glycoside Hydrolase Family 23.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysozyme g (EC:3.2.1.17)
Alternative name(s):
1,4-beta-N-acetylmuramidase
OrganismiEpinephelus coioides (Orange-spotted grouper) (Epinephelus nebulosus)
Taxonomic identifieri94232 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiNeoteleosteiAcanthomorphataEupercariaPerciformesSerranoideiSerranidaeEpinephelinaeEpinepheliniEpinephelus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 194194Lysozyme gPRO_0000193518Add
BLAST

Expressioni

Tissue specificityi

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

Structurei

3D structure databases

ProteinModelPortaliQ90X99.
SMRiQ90X99. Positions 2-194.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 23 family.Curated

Phylogenomic databases

HOVERGENiHBG006299.

Family and domain databases

InterProiIPR002152. Glyco_hydro_23.
IPR023346. Lysozyme-like_dom.
IPR008258. TGlycosylase-like_SLT.
[Graphical view]
PfamiPF01464. SLT. 1 hit.
[Graphical view]
PIRSFiPIRSF001065. Lysozyme_g. 1 hit.
PRINTSiPR00749. LYSOZYMEG.
SUPFAMiSSF53955. SSF53955. 1 hit.

Sequencei

Sequence statusi: Complete.

Q90X99-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGYGNIMNVE TTGASWQTAQ QDKLGYSGVR ASHTMANTDS GRMERYRSKI
60 70 80 90 100
NSVGAKYGID PALIAAIISE ESRAGNVLHD GWGDYDSNRG AYNAWGLMQV
110 120 130 140 150
DVNPNGGGHT ARGAWDSEEH LSQGAEILVY FIGRIRNKFP GWNTEQQLKG
160 170 180 190
GIAAYNMGDG NVHSYDNVDG RTTGGDYSND VVARAQWYKT QKGF
Length:194
Mass (Da):21,179
Last modified:November 30, 2001 - v1
Checksum:i8A12197359127023
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF416458 mRNA. Translation: AAL08021.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF416458 mRNA. Translation: AAL08021.2.

3D structure databases

ProteinModelPortaliQ90X99.
SMRiQ90X99. Positions 2-194.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH23. Glycoside Hydrolase Family 23.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG006299.

Family and domain databases

InterProiIPR002152. Glyco_hydro_23.
IPR023346. Lysozyme-like_dom.
IPR008258. TGlycosylase-like_SLT.
[Graphical view]
PfamiPF01464. SLT. 1 hit.
[Graphical view]
PIRSFiPIRSF001065. Lysozyme_g. 1 hit.
PRINTSiPR00749. LYSOZYMEG.
SUPFAMiSSF53955. SSF53955. 1 hit.
ProtoNetiSearch...

Publicationsi

  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(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiLYG_EPICO
AccessioniPrimary (citable) accession number: Q90X99
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 9, 2004
Last sequence update: November 30, 2001
Last modified: October 28, 2014
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.