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P81711

- LYSC_SYRSO

UniProt

P81711 - LYSC_SYRSO

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Protein

Lysozyme C

Gene

LYZ

Organism
Syrmaticus soemmerringii (Copper pheasant) (Phasianus soemmerringii)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents.PROSITE-ProRule annotation

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 sitei35 – 351PROSITE-ProRule annotation
Active sitei52 – 521PROSITE-ProRule annotation

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
Complete GO annotation...

Keywords - Molecular functioni

Antimicrobial, Bacteriolytic enzyme, Glycosidase, Hydrolase

Protein family/group databases

CAZyiGH22. Glycoside Hydrolase Family 22.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysozyme C (EC:3.2.1.17)
Alternative name(s):
1,4-beta-N-acetylmuramidase C
CPL
Gene namesi
Name:LYZ
OrganismiSyrmaticus soemmerringii (Copper pheasant) (Phasianus soemmerringii)
Taxonomic identifieri9067 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeSyrmaticus

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 129129Lysozyme CPRO_0000208872Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi6 ↔ 127PROSITE-ProRule annotation
Disulfide bondi30 ↔ 115PROSITE-ProRule annotation
Disulfide bondi64 ↔ 80PROSITE-ProRule annotation
Disulfide bondi76 ↔ 94PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP81711.

Interactioni

Subunit structurei

Monomer.By similarity

Structurei

3D structure databases

ProteinModelPortaliP81711.
SMRiP81711. Positions 1-129.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 22 family.PROSITE-ProRule annotation

Phylogenomic databases

HOVERGENiHBG052297.

Family and domain databases

InterProiIPR001916. Glyco_hydro_22.
IPR000974. Glyco_hydro_22_lys.
IPR023346. Lysozyme-like_dom.
[Graphical view]
PfamiPF00062. Lys. 1 hit.
[Graphical view]
PRINTSiPR00137. LYSOZYME.
PR00135. LYZLACT.
SMARTiSM00263. LYZ1. 1 hit.
[Graphical view]
SUPFAMiSSF53955. SSF53955. 1 hit.
PROSITEiPS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P81711-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
KVYGRCELAA AMKRLGLDNF RGYSLGNWVC AAKFESNFNT HATNRNTDGS
60 70 80 90 100
TDYGILQINS RWWCNDGRTP GSRNLCNIPC SALLSSDTIA SVNCAKKIVS
110 120
DGNGMNAWVA WRKRCKGTDV NAWTRGCRL
Length:129
Mass (Da):14,286
Last modified:December 1, 2000 - v1
Checksum:iF0EC776CEFAC7611
GO

Sequence databases

PIRiJC2144.

Cross-referencesi

Sequence databases

PIRi JC2144.

3D structure databases

ProteinModelPortali P81711.
SMRi P81711. Positions 1-129.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH22. Glycoside Hydrolase Family 22.

Proteomic databases

PRIDEi P81711.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOVERGENi HBG052297.

Family and domain databases

InterProi IPR001916. Glyco_hydro_22.
IPR000974. Glyco_hydro_22_lys.
IPR023346. Lysozyme-like_dom.
[Graphical view ]
Pfami PF00062. Lys. 1 hit.
[Graphical view ]
PRINTSi PR00137. LYSOZYME.
PR00135. LYZLACT.
SMARTi SM00263. LYZ1. 1 hit.
[Graphical view ]
SUPFAMi SSF53955. SSF53955. 1 hit.
PROSITEi PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The amino acid sequence of copper pheasant lysozyme."
    Araki T., Kuramoto M., Torikata T.
    Biosci. Biotechnol. Biochem. 58:794-795(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
    Tissue: Egg white.

Entry informationi

Entry nameiLYSC_SYRSO
AccessioniPrimary (citable) accession number: P81711
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: December 1, 2000
Last modified: November 26, 2014
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Lysozyme C is capable of both hydrolysis and transglycosylation; it shows also a slight esterase activity. It acts rapidly on both peptide-substituted and unsubstituted peptidoglycan, and slowly on chitin oligosaccharides (By similarity).By similarity

Keywords - Technical termi

Direct protein sequencing

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