ID   CHI3_METRA              Reviewed;         317 AA.
AC   E9ENC6;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 1.
DT   25-MAY-2022, entry version 42.
DE   RecName: Full=Endochitinase 3;
DE            EC=3.2.1.14;
DE   AltName: Full=Chitinase 3;
DE   Flags: Precursor;
GN   Name=chi3; ORFNames=MAA_01212;
OS   Metarhizium robertsii (strain ARSEF 23 / ATCC MYA-3075) (Metarhizium
OS   anisopliae (strain ARSEF 23)).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX   NCBI_TaxID=655844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 23 / ATCC MYA-3075;
RX   PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA   Gao Q., Jin K., Ying S.-H., Zhang Y., Xiao G., Shang Y., Duan Z., Hu X.,
RA   Xie X.-Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S.,
RA   Zhong Y., Ma L.-J., St Leger R.J., Zhao G.-P., Pei Y., Feng M.-G., Xia Y.,
RA   Wang C.;
RT   "Genome sequencing and comparative transcriptomics of the model
RT   entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL   PLoS Genet. 7:E1001264-E1001264(2011).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ARSEF 23 / ATCC MYA-3075;
RX   PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA   Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA   St Leger R.J., Wang C.;
RT   "Trajectory and genomic determinants of fungal-pathogen speciation and host
RT   adaptation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
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. Involved in heat-shock adaptation (By similarity).
CC       {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 III subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EFZ04138.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; ADNJ02000008; EFZ04138.2; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_007817401.2; XM_007819210.2.
DR   AlphaFoldDB; E9ENC6; -.
DR   SMR; E9ENC6; -.
DR   CAZy; GH18; Glycoside Hydrolase Family 18.
DR   EnsemblFungi; EFZ04138; EFZ04138; MAA_01212.
DR   GeneID; 19255498; -.
DR   KEGG; maj:MAA_01212; -.
DR   HOGENOM; CLU_007818_2_1_1; -.
DR   Proteomes; UP000002498; Unassembled WGS sequence.
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   CDD; cd02877; GH18_hevamine_XipI_class_III; 1.
DR   InterPro; IPR045321; Cts1-like.
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; Signal;
KW   Virulence.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..317
FT                   /note="Endochitinase 3"
FT                   /id="PRO_0000429869"
FT   DOMAIN          29..317
FT                   /note="GH18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   ACT_SITE        170
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   CARBOHYD        25
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        49
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        169
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        245
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   317 AA;  34157 MW;  58EAE71E549E9399 CRC64;
     MFVRNALVVT GLLAALTQAA PAERNTSRHK LTVYWGAEDD TTTLDDVCND SSYDVVNLAF
     LSHFFSGGGY PRMSIGNLDG PSRAQKKAGA TGLQDGSSLV KSIKNCQSKG KPVILSMGGA
     TDYSDVQLHS DAQGQQIANT VWDLFLGGTD HKELRPFGDV KLDGVDLDNE TNDGTGYLAM
     AKQFKANFQK DTSKKYYITA APQCPYPDQS EPLDVCRLLD WVQVQFYNNG NCNIAQSGFA
     TAVKNWSRGI GSGVQLYIGA LASGADGDEG YVDAAVLNRA IDQVKAMDLP NFGGAMLWEA
     QLAVNNGNYQ KEIKANL