ID   CHI2_ARTBC              Reviewed;         332 AA.
AC   D4AVJ0;
DT   09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT   09-DEC-2015, sequence version 2.
DT   25-MAY-2022, entry version 48.
DE   RecName: Full=Probable class II chitinase ARB_00204 {ECO:0000305};
DE            EC=3.2.1.14 {ECO:0000250|UniProtKB:Q9BZP6};
DE   Flags: Precursor;
GN   ORFNames=ARB_00204;
OS   Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS   mentagrophytes).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4681 / CBS 112371;
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(2011).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX   PubMed=21919205; DOI=10.1002/pmic.201100234;
RA   Sriranganadane D., Waridel P., Salamin K., Feuermann M., Mignon B.,
RA   Staib P., Neuhaus J.M., Quadroni M., Monod M.;
RT   "Identification of novel secreted proteases during extracellular
RT   proteolysis by dermatophytes at acidic pH.";
RL   Proteomics 11:4422-4433(2011).
CC   -!- FUNCTION: Degrades chitin and chitotriose.
CC       {ECO:0000250|UniProtKB:Q9BZP6}.
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:0000250|UniProtKB:Q9BZP6};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21919205}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC       class II subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EFE32746.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; ABSU01000013; EFE32746.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_003013386.1; XM_003013340.1.
DR   AlphaFoldDB; D4AVJ0; -.
DR   SMR; D4AVJ0; -.
DR   STRING; 663331.D4AVJ0; -.
DR   PRIDE; D4AVJ0; -.
DR   EnsemblFungi; EFE32746; EFE32746; ARB_00204.
DR   GeneID; 9519422; -.
DR   KEGG; abe:ARB_00204; -.
DR   eggNOG; ENOG502S0WK; Eukaryota.
DR   HOGENOM; CLU_019399_1_2_1; -.
DR   Proteomes; UP000008866; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008061; F:chitin binding; IEA:InterPro.
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; IPR011583; Chitinase_II.
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   SMART; SM00636; Glyco_18; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS01095; GH18_1; 1.
DR   PROSITE; PS51910; GH18_2; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Chitin degradation; Glycoprotein; Glycosidase;
KW   Hydrolase; Polysaccharide degradation; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..332
FT                   /note="Probable class II chitinase ARB_00204"
FT                   /id="PRO_0000434917"
FT   DOMAIN          19..331
FT                   /note="GH18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   ACT_SITE        118
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   CARBOHYD        245
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   332 AA;  36173 MW;  7765FFA7BC385DEB CRC64;
     MKTPFTILAA LTVATTLADV PDEWDIIELS FGEPTSVDSG EIKFAMCPKT ECPNVESEEE
     FKAAIKAKRA KGKKVLLSIG GQNGQVQLKT TEARDKFVSS VGGIIDKYGL DGLDIDFEGH
     SLYLDQGDTD FKNPKTSVVV NLIAALKSLK EKYGKAFVLT MAPETFFVQL GYSSYGPSNG
     NDARAGSYLP VIHAMRDDLT VLQVQNYNSG PIIGLDDQYH NVGTPDFLIA MADMLKAGFP
     VAKTNNTFPP LREDQIAIGL PSTVSAGNGF VDEKGVQDAL NCLMKGESCG TYKPRGGKSP
     SFRGLMAWSI NWDKFSNWGF LNPHRKYLDS FP