ID   CHI2_METRA              Reviewed;         419 AA.
AC   E9F9R9;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   04-MAR-2015, sequence version 2.
DT   25-MAY-2022, entry version 43.
DE   RecName: Full=Endochitinase 2;
DE            EC=3.2.1.14;
DE   AltName: Full=Chitinase 2;
DE   Flags: Precursor;
GN   Name=chi2; ORFNames=MAA_09018;
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 (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 III subfamily. {ECO:0000305}.
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DR   EMBL; ADNJ02000006; EFY95562.2; -; Genomic_DNA.
DR   RefSeq; XP_007825207.2; XM_007827016.2.
DR   AlphaFoldDB; E9F9R9; -.
DR   SMR; E9F9R9; -.
DR   CAZy; GH18; Glycoside Hydrolase Family 18.
DR   EnsemblFungi; EFY95562; EFY95562; MAA_09018.
DR   GeneID; 19263304; -.
DR   KEGG; maj:MAA_09018; -.
DR   HOGENOM; CLU_007818_6_1_1; -.
DR   Proteomes; UP000002498; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030248; F:cellulose binding; IEA:InterPro.
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; IPR035971; CBD_sf.
DR   InterPro; IPR000254; Cellulose-bd_dom_fun.
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; PF00734; CBM_1; 1.
DR   Pfam; PF00704; Glyco_hydro_18; 1.
DR   SMART; SM00236; fCBD; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF57180; SSF57180; 1.
DR   PROSITE; PS51164; CBM1_2; 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..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..419
FT                   /note="Endochitinase 2"
FT                   /id="PRO_0000429867"
FT   DOMAIN          35..343
FT                   /note="GH18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   DOMAIN          383..419
FT                   /note="CBM1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT   REGION          350..386
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        173
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   CARBOHYD        153
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        237
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        256
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   419 AA;  43619 MW;  9C8BB689E70EFB3B CRC64;
     MHHLRALVGV GLAGLAAGVP LTDKISVKPR QAPGAQNVVY WGQNGGGTIE NNDLAAYCQP
     NSGIDVLVLA FLYQFGNGGN IPSGTIGQSC YISTSGQGQN CEALTAAIHT CQSAGVKIIL
     SLGGATSSYS LQTQAQAEQI GQYLWDSYGN SGNKTVQRPF GSNFVNGFDF DIEVNGGSSQ
     YYQYMIAKLR SNFASDKSNT YLITGAPQCP IPEPNMGVII SNSVFDHLYV QFYNNNNYTV
     PCALGINGNA PFNYNNWTSF IADTPSAGAK IFIGVPASPL ASTGTPSGAQ YYAAPDQLAA
     IVGEYRSDAH FGGIMMWSAG FSDANVNNGC TYAQQAKSIL VNGAPCASSG PPSSTPATAP
     APTATTMPSS TSVSSPAASP TGGTVPQWGQ CGGEGYSGPT QCVAPYQCVK QGDWWSSCR