ID   CHI4_METRA              Reviewed;         345 AA.
AC   E9F7R6;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 1.
DT   25-MAY-2022, entry version 33.
DE   RecName: Full=Endochitinase 4;
DE            EC=3.2.1.14;
DE   AltName: Full=Chitinase 4;
DE   Flags: Precursor;
GN   Name=chi4; ORFNames=MAA_08315;
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 V subfamily. {ECO:0000305}.
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DR   EMBL; ADNJ02000001; EFY96204.1; -; Genomic_DNA.
DR   RefSeq; XP_007824504.1; XM_007826313.1.
DR   AlphaFoldDB; E9F7R6; -.
DR   SMR; E9F7R6; -.
DR   CAZy; GH18; Glycoside Hydrolase Family 18.
DR   EnsemblFungi; EFY96204; EFY96204; MAA_08315.
DR   GeneID; 19262601; -.
DR   KEGG; maj:MAA_08315; -.
DR   HOGENOM; CLU_019399_1_2_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   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..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..345
FT                   /note="Endochitinase 4"
FT                   /id="PRO_0000429871"
FT   DOMAIN          41..345
FT                   /note="GH18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   ACT_SITE        163
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   CARBOHYD        29
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        89
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        316
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   345 AA;  36501 MW;  B019F097F6DFAB4F CRC64;
     MAPLLNTGLV ILPLIVSTLL GPMPAFAQNE TCATKGKPAG KVLQGYWENW DGAKNGVHPP
     FGWTPIQDAQ IRQHGYNVIS AAFPVILPNG TALWEDGMDA NVKVATPAEM CQAKAAGATI
     VMSIGGATAA IDLSSSSVAD KFVSTIVPIL KRYNFDGVDI DIEAGLSGSG TIGTLSTSQA
     NLVRIIDGIL AQMPSNFGLT MAPETAYVTG GSVTYGAIWG AYLPIIKKYA DNGRLWWLNM
     QYYNGDMYGC SGDSYKAGTV EGFVAQTDCL NKGLVIQGTT IRVPYDKQVP GLPAQSGAGG
     GYMSPSLVGQ AWDHYNGSLK GLMTWSINWD GSKGWTFGDN VKGRL