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Database: UniProt
Entry: A0A8K0C867_IGNLU
LinkDB: A0A8K0C867_IGNLU
Original site: A0A8K0C867_IGNLU 
ID   A0A8K0C867_IGNLU        Unreviewed;       105 AA.
AC   A0A8K0C867;
DT   03-AUG-2022, integrated into UniProtKB/TrEMBL.
DT   03-AUG-2022, sequence version 1.
DT   28-JAN-2026, entry version 10.
DE   RecName: Full=lysozyme {ECO:0000256|ARBA:ARBA00012732};
DE            EC=3.2.1.17 {ECO:0000256|ARBA:ARBA00012732};
DE   Flags: Fragment;
GN   ORFNames=ILUMI_25588 {ECO:0000313|EMBL:KAF2880577.1};
OS   Ignelater luminosus (Cucubano) (Pyrophorus luminosus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Elateriformia; Elateroidea;
OC   Elateridae; Agrypninae; Pyrophorini; Ignelater.
OX   NCBI_TaxID=2038154 {ECO:0000313|EMBL:KAF2880577.1, ECO:0000313|Proteomes:UP000801492};
RN   [1] {ECO:0000313|EMBL:KAF2880577.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=TRF0915ILg1 {ECO:0000313|EMBL:KAF2880577.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KAF2880577.1};
RG   Photinus pyralis genome working group;
RA   Fallon T.R., Sander Lower S.E., Weng J.-K.;
RT   "The genome of the North American firefly Photinus pyralis.";
RL   Submitted (AUG-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic
CC         acid and N-acetyl-D-glucosamine residues in a peptidoglycan and
CC         between N-acetyl-D-glucosamine residues in chitodextrins.;
CC         EC=3.2.1.17; Evidence={ECO:0000256|ARBA:ARBA00000632};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KAF2880577.1}.
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DR   EMBL; VTPC01090949; KAF2880577.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A8K0C867; -.
DR   OrthoDB; 6337871at2759; -.
DR   Proteomes; UP000801492; Unassembled WGS sequence.
DR   GO; GO:0003796; F:lysozyme activity; IEA:UniProtKB-EC.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.530.10; -; 1.
DR   InterPro; IPR008597; Invert_lysozyme.
DR   Pfam; PF05497; Destabilase; 1.
DR   PROSITE; PS51909; LYSOZYME_I; 1.
PE   4: Predicted;
KW   Antimicrobial {ECO:0000256|ARBA:ARBA00022529};
KW   Bacteriolytic enzyme {ECO:0000256|ARBA:ARBA00022638};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR608597-3};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000801492};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..105
FT                   /note="lysozyme"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5035450789"
FT   DISULFID        41..47
FT                   /evidence="ECO:0000256|PIRSR:PIRSR608597-3"
FT   DISULFID        84..90
FT                   /evidence="ECO:0000256|PIRSR:PIRSR608597-3"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KAF2880577.1"
SQ   SEQUENCE   105 AA;  12033 MW;  4F98FA51FAA7AECF CRC64;
     MRTFNKSLFI LTIFCLAIAN NAYMMRHLIG SEIQECLNCL CHARSGCWNR LNCANYSITK
     TYWEKSGSPT NGNYLNSDES FKFCMQDENC ILNAVKGYTE SFGEK
//
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