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P50717

- LYS_HYPCU

UniProt

P50717 - LYS_HYPCU

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Protein
Lysozyme
Gene
N/A
Organism
Hyphantria cunea (Fall webworm moth)
Status
Reviewed - Annotation score: 3 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
Complete GO annotation...

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 (EC:3.2.1.17)
Alternative name(s):
1,4-beta-N-acetylmuramidase
OrganismiHyphantria cunea (Fall webworm moth)
Taxonomic identifieri39466 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaLepidopteraGlossataDitrysiaNoctuoideaArctiidaeHyphantria

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020 Reviewed prediction
Add
BLAST
Chaini21 – 142122Lysozyme
PRO_0000018507Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi27 ↔ 142 By similarity
Disulfide bondi48 ↔ 131 By similarity
Disulfide bondi83 ↔ 97 By similarity
Disulfide bondi93 ↔ 111 By similarity

Keywords - PTMi

Disulfide bond

Structurei

3D structure databases

ProteinModelPortaliP50717.
SMRiP50717. Positions 25-142.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

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.

P50717-1 [UniParc]FASTAAdd to Basket

« Hide

MQKLAVFLFA IAAVCIHCEA KYYSTRCDLV RELRKQGFPE NQMGDWVCLV    50
ENESGRKTDK VGPVNKNGSK DYGLFQINDK YWCSNTRTPG KDCNVTCADL 100
LLDDITKAST CAKKIFKRHN FRAWYGWRNH CDGKTLPDTS NC 142
Length:142
Mass (Da):16,241
Last modified:October 1, 1996 - v1
Checksum:i7A565C7748D4C127
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U23786 mRNA. Translation: AAA84747.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U23786 mRNA. Translation: AAA84747.1 .

3D structure databases

ProteinModelPortali P50717.
SMRi P50717. Positions 25-142.
ModBasei Search...

Protein family/group databases

CAZyi GH22. Glycoside Hydrolase Family 22.

Protocols and materials databases

Structural Biology Knowledgebase Search...

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. Park S.-S., Shin S.W., Park D.S., Kim M.K., Oh H.W., Park H.Y.
    Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiLYS_HYPCU
AccessioniPrimary (citable) accession number: P50717
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: October 16, 2013
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

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

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