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Protein

Lysozyme C-1

Gene
N/A
Organism
Capra hircus (Goat)
Status
Reviewed-Annotation score: 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.

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.

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)DescriptionActionsGraphical viewLength
Active sitei35PROSITE-ProRule annotation1
Active sitei53PROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAntimicrobial, Bacteriolytic enzyme, Glycosidase, Hydrolase
Biological processDigestion

Protein family/group databases

CAZyiGH22. Glycoside Hydrolase Family 22.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysozyme C-1 (EC:3.2.1.17)
Alternative name(s):
1,4-beta-N-acetylmuramidase C-1
OrganismiCapra hircus (Goat)
Taxonomic identifieri9925 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeCaprinaeCapra

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002088471 – 129Lysozyme C-1Add BLAST129

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi6 ↔ 127PROSITE-ProRule annotation
Disulfide bondi30 ↔ 115PROSITE-ProRule annotation
Disulfide bondi65 ↔ 81PROSITE-ProRule annotation
Disulfide bondi77 ↔ 95PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Monomer.By similarity

Structurei

3D structure databases

ProteinModelPortaliP37713.
SMRiP37713.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

HOVERGENiHBG052297.

Family and domain databases

CDDicd00119. LYZ1. 1 hit.
InterProiView protein in InterPro
IPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
IPR000974. Glyco_hydro_22_lys.
IPR023346. Lysozyme-like_dom.
PfamiView protein in Pfam
PF00062. Lys. 1 hit.
PRINTSiPR00137. LYSOZYME.
PR00135. LYZLACT.
SMARTiView protein in SMART
SM00263. LYZ1. 1 hit.
SUPFAMiSSF53955. SSF53955. 1 hit.
PROSITEiView protein in PROSITE
PS00128. LACTALBUMIN_LYSOZYME_1. 1 hit.
PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.

Sequencei

Sequence statusi: Complete.

P37713-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
KVFERCELAR TLKKLGLDDY KGVSLANWLC LTKWESGYNT KATNYNPGSE
60 70 80 90 100
STDYGIFQIN SKFWCNDGKT PDAVDGCHVS CSELMENDIE KAVACAKHIV
110 120
SEQGITAWVA WKSHCRDHDV SSYVEGCTL
Length:129
Mass (Da):14,433
Last modified:October 1, 1994 - v1
Checksum:iDA7FD76F890AFE91
GO

Cross-referencesi

3D structure databases

ProteinModelPortaliP37713.
SMRiP37713.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH22. Glycoside Hydrolase Family 22.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG052297.

Family and domain databases

CDDicd00119. LYZ1. 1 hit.
InterProiView protein in InterPro
IPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
IPR000974. Glyco_hydro_22_lys.
IPR023346. Lysozyme-like_dom.
PfamiView protein in Pfam
PF00062. Lys. 1 hit.
PRINTSiPR00137. LYSOZYME.
PR00135. LYZLACT.
SMARTiView protein in SMART
SM00263. LYZ1. 1 hit.
SUPFAMiSSF53955. SSF53955. 1 hit.
PROSITEiView protein in PROSITE
PS00128. LACTALBUMIN_LYSOZYME_1. 1 hit.
PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiLYSC1_CAPHI
AccessioniPrimary (citable) accession number: P37713
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: March 15, 2017
This is version 73 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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

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 one 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.