ID M7ANB9_CHEMY Unreviewed; 287 AA.
AC M7ANB9;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=lysozyme {ECO:0000256|ARBA:ARBA00012732};
DE EC=3.2.1.17 {ECO:0000256|ARBA:ARBA00012732};
GN ORFNames=UY3_16889 {ECO:0000313|EMBL:EMP26024.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP26024.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
CC {ECO:0000256|RuleBase:RU004440}.
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DR EMBL; KB584993; EMP26024.1; -; Genomic_DNA.
DR AlphaFoldDB; M7ANB9; -.
DR eggNOG; ENOG502SR6Z; Eukaryota.
DR Proteomes; UP000031443; Unassembled WGS sequence.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
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 GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR CDD; cd16897; LYZ_C; 1.
DR Gene3D; 1.10.530.10; -; 2.
DR InterPro; IPR001916; Glyco_hydro_22.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR PANTHER; PTHR11407; LYSOZYME C; 1.
DR PANTHER; PTHR11407:SF28; LYSOZYME C; 1.
DR Pfam; PF00062; Lys; 1.
DR PRINTS; PR00135; LYZLACT.
DR SMART; SM00263; LYZ1; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 2.
DR PROSITE; PS51348; GLYCOSYL_HYDROL_F22_2; 1.
PE 3: Inferred from homology;
KW Antimicrobial {ECO:0000256|ARBA:ARBA00022529};
KW Bacteriolytic enzyme {ECO:0000256|ARBA:ARBA00022638};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000031443}.
FT REGION 1..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 287 AA; 31505 MW; 3E713A1F92612C11 CRC64;
MHGLELSPRE QEDCERQREP EKELQKQQQH ELAVGERRGL GDLPGSALTP VSLPCSDSGQ
VHGGHSTELQ QQHPEVRVLD SLQDQNHQGG TEGAGPRTRR PCPGMRALAL LPVLACLSAG
ARGEVLSRCE LARLLQRGGL DGFMGYRLDN WLCLAFYASR FNTGTVTENS DGSSDYGIFQ
VNSRRWCSDQ RSRTLDLCQT RCRVRLPPDP SPVGMGVLGL VTLLACLSAG GRGKIFTRCE
LAQELQENGM DGYEGYSLAN YLLNPDIKDD INCAKRVVQD PQGMEAL
//
