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P79158

- LYSC_CALJA

UniProt

P79158 - LYSC_CALJA

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Protein
Lysozyme C
Gene
LYZ, LZM
Organism
Callithrix jacchus (White-tufted-ear marmoset)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at transcript 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.

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 sitei53 – 531 By similarity
Active sitei71 – 711 By 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
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
Gene namesi
Name:LYZ
Synonyms:LZM
OrganismiCallithrix jacchus (White-tufted-ear marmoset)
Taxonomic identifieri9483 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniPlatyrrhiniCebidaeCallitrichinaeCallithrix
ProteomesiUP000008225: Chromosome 9

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818 By similarity
Add
BLAST
Chaini19 – 148130Lysozyme C
PRO_0000018459Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi24 ↔ 146 By similarity
Disulfide bondi48 ↔ 134 By similarity
Disulfide bondi83 ↔ 99 By similarity
Disulfide bondi95 ↔ 113 By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP79158.

Interactioni

Subunit structurei

Monomer.

Structurei

3D structure databases

ProteinModelPortaliP79158.
SMRiP79158. Positions 19-148.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000037357.
HOVERGENiHBG052297.
OMAiLQDNIAD.
OrthoDBiEOG7BW0M5.
TreeFamiTF324882.

Family and domain databases

InterProiIPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
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.
PROSITEiPS00128. LACTALBUMIN_LYSOZYME_1. 1 hit.
PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P79158-1 [UniParc]FASTAAdd to Basket

« Hide

MKVLIILGLV LLSVMVQGKV FERCELARTL KRFGLDGYRG ISLANWMCLA    50
KWESDYNTRA TNYNPGDQST DYGIFQINSH YWCNNGRTPG AVNACHISCN 100
ALLQDDITEA VACAKRVVRD PQGIRAWVAW KAHCQNRDVS QYVQGCGV 148
Length:148
Mass (Da):16,602
Last modified:May 1, 1997 - v1
Checksum:iC79BB37557B1E951
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U76923 mRNA. Translation: AAB41203.1.
RefSeqiXP_002752792.1. XM_002752746.2.

Genome annotation databases

EnsembliENSCJAT00000003379; ENSCJAP00000003201; ENSCJAG00000001788.
GeneIDi100393686.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U76923 mRNA. Translation: AAB41203.1 .
RefSeqi XP_002752792.1. XM_002752746.2.

3D structure databases

ProteinModelPortali P79158.
SMRi P79158. Positions 19-148.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH22. Glycoside Hydrolase Family 22.

Proteomic databases

PRIDEi P79158.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSCJAT00000003379 ; ENSCJAP00000003201 ; ENSCJAG00000001788 .
GeneIDi 100393686.

Organism-specific databases

CTDi 4069.

Phylogenomic databases

HOGENOMi HOG000037357.
HOVERGENi HBG052297.
OMAi LQDNIAD.
OrthoDBi EOG7BW0M5.
TreeFami TF324882.

Family and domain databases

InterProi IPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
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 PS00128. LACTALBUMIN_LYSOZYME_1. 1 hit.
PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Episodic adaptive evolution of primate lysozymes."
    Messier W., Stewart C.B.
    Nature 385:151-154(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Blood.

Entry informationi

Entry nameiLYSC_CALJA
AccessioniPrimary (citable) accession number: P79158
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 1, 1997
Last modified: February 19, 2014
This is version 75 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.

Keywords - Technical termi

Complete proteome, Reference proteome

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

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