ID   CHI11_METAN             Reviewed;         522 AA.
AC   O74199;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Endochitinase 11;
DE            EC=3.2.1.14;
DE   AltName: Full=Chitinase 11;
DE   Flags: Precursor;
GN   Name=chi11;
OS   Metarhizium anisopliae (Entomophthora anisopliae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX   NCBI_TaxID=5530;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9742698; DOI=10.1111/j.1574-6968.1998.tb13156.x;
RA   Kang S.C., Park S., Lee D.G.;
RT   "Isolation and characterization of a chitinase cDNA from the
RT   entomopathogenic fungus, Metarhizium anisopliae.";
RL   FEMS Microbiol. Lett. 165:267-271(1998).
RN   [2]
RP   SUBCELLULAR LOCATION, FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
RX   PubMed=10222181; DOI=10.1006/jipa.1999.4843;
RA   Kang S.C., Park S., Lee D.G.;
RT   "Purification and characterization of a novel chitinase from the
RT   entomopathogenic fungus, Metarhizium anisopliae.";
RL   J. Invertebr. Pathol. 73:276-281(1999).
CC   -!- FUNCTION: Secreted chitinase involved in the degradation of chitin, a
CC       component of the cell walls of fungi and exoskeletal elements of some
CC       animals (including worms and arthropods). Participates in the infection
CC       process and directly acts in the penetration process of the host
CC       cuticle. {ECO:0000269|PubMed:10222181}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide
CC         (1->4)-beta-linkages in chitin and chitodextrins.; EC=3.2.1.14;
CC         Evidence={ECO:0000269|PubMed:10222181};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 5.0. {ECO:0000269|PubMed:10222181};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10222181}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC       class V subfamily. {ECO:0000305}.
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DR   EMBL; AF036320; AAC33265.1; -; mRNA.
DR   AlphaFoldDB; O74199; -.
DR   SMR; O74199; -.
DR   CAZy; GH18; Glycoside Hydrolase Family 18.
DR   CLAE; CHI18K_METAN; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004568; F:chitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR001223; Glyco_hydro18_cat.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF00704; Glyco_hydro_18; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS51910; GH18_2; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Chitin degradation; Chitin-binding; Glycoprotein;
KW   Glycosidase; Hydrolase; Polysaccharide degradation; Secreted; Signal;
KW   Virulence.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..522
FT                   /note="Endochitinase 11"
FT                   /id="PRO_0000429872"
FT   DOMAIN          235..522
FT                   /note="GH18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   ACT_SITE        346
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   CARBOHYD        148
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        275
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        455
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        519
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   522 AA;  57454 MW;  8A01FE69689FD162 CRC64;
     MLFSMVMFTE RWWVGSKDCP RVPALENSNN PWRLERTATA AELSQYGNPT TCEIDNGGVI
     VADGFQASKG YTGDSIVDYN DAHYKTSVDQ DAWGFVRAAY NRGRNTNRQS SGPHPLCTRK
     CIAWLLMGRL MNAVLTQSDN PALVPNQNAT GSNSRPWKPL GKAQSYSNEE LNNAPQFNPE
     TLYASDTLIR FNGVNYISQS KEQKVSPSDS NPWRVFVDWT GTKERVGTPK KAWPKHVYAP
     YVDFTLNTIP DLRALAKNHN VNHFTLAFVV SKDANTTCGT AYGMQNYAQY SKIKALREAG
     GDVMLSIGGA NNAPLAASCK NVDDLMQHYY DIVDNLNLKV LDFDIEGTWV AVQASIERRN
     LAVKKVQDKW KSEGKDIAIW YTLPILPTGL TPEGMNVLSD AKAKGVELAG VNVMTMDYGN
     AICQSANTEG QNIHGKCATS AIAFLHSQLK GLHPNKSDAE IDAMMGTTPM VGVNDVQGEV
     FYLSDARLVM QDAQKRNLGM VGIWSIARDL PAALTCLRNS TA