ID   CHI4_METAN              Reviewed;         282 AA.
AC   C9WJD0;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   24-NOV-2009, sequence version 1.
DT   25-MAY-2022, entry version 34.
DE   RecName: Full=Endochitinase 4;
DE            EC=3.2.1.14;
DE   AltName: Full=Chitinase 4;
DE   Flags: Fragment;
GN   Name=chi4;
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 [GENOMIC DNA].
RC   STRAIN=ARSEF 7524;
RX   PubMed=19682457; DOI=10.1016/j.jip.2009.08.006;
RA   Enkerli J., Ghormade V., Oulevey C., Widmer F.;
RT   "PCR-RFLP analysis of chitinase genes enables efficient genotyping of
RT   Metarhizium anisopliae var. anisopliae.";
RL   J. Invertebr. Pathol. 102:185-188(2009).
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 (By similarity). {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC       class V subfamily. {ECO:0000305}.
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DR   EMBL; FJ609317; ACU30521.1; -; Genomic_DNA.
DR   AlphaFoldDB; C9WJD0; -.
DR   SMR; C9WJD0; -.
DR   CAZy; GH18; Glycoside Hydrolase Family 18.
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; IPR001579; Glyco_hydro_18_chit_AS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF00704; Glyco_hydro_18; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS01095; GH18_1; 1.
DR   PROSITE; PS51910; GH18_2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Chitin degradation; Chitin-binding; Glycoprotein;
KW   Glycosidase; Hydrolase; Polysaccharide degradation; Secreted; Virulence.
FT   CHAIN           1..282
FT                   /note="Endochitinase 4"
FT                   /id="PRO_0000429870"
FT   DOMAIN          <1..>282
FT                   /note="GH18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   ACT_SITE        112
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   CARBOHYD        265
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
FT   NON_TER         282
SQ   SEQUENCE   282 AA;  29690 MW;  0E7DEFA8AB0FFF89 CRC64;
     GAKNGVHPPL GWIPIQDARI RQHGYNVISA AFPVILPDGT ALWEDGMDAN VKVATPAEMC
     QAKAAGATMV MSIGGAAAAI DLSSSSVADK FVSTIVPILK RYNFDGVDID IEAGLSGSGT
     FGTLSASQAN LVRIIDGILA QMPSNFGLTM APETAYVTGG SVTYGSIWGA YLPIIKKYAD
     NGRLWWLNMQ YYNGAMYGCS GDSYEAGTVK GFVAQTDCLD KGLVIQGTTI RVPYDKQVPG
     LPAQSGAGGG YMSPSLVGQA WDHYNGSLKG LMTWSINWDG SK