ID   CHI33_ARTBC             Reviewed;         330 AA.
AC   D4B4X4;
DT   11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT   11-NOV-2015, sequence version 2.
DT   25-MAY-2022, entry version 48.
DE   RecName: Full=Class III chitinase ARB_03514 {ECO:0000305};
DE            EC=3.2.1.14 {ECO:0000250|UniProtKB:Q12713};
DE   AltName: Full=Endochitinase ARB_03514 {ECO:0000305};
DE   Flags: Precursor;
GN   ORFNames=ARB_03514;
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: 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) (By similarity). Plays a
CC       morphogenetic role during apical growth, cell division and
CC       differentiation (cell wall morphogenesis) (By similarity).
CC       {ECO:0000250|UniProtKB:Q12713}.
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:Q12713};
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q12713}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21919205}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC       class III subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EFE29619.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; ABSU01000035; EFE29619.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_003010259.1; XM_003010213.1.
DR   AlphaFoldDB; D4B4X4; -.
DR   SMR; D4B4X4; -.
DR   STRING; 663331.D4B4X4; -.
DR   EnsemblFungi; EFE29619; EFE29619; ARB_03514.
DR   GeneID; 9525527; -.
DR   KEGG; abe:ARB_03514; -.
DR   eggNOG; KOG4701; Eukaryota.
DR   HOGENOM; CLU_007818_3_0_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: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   1: Evidence at protein level;
KW   Carbohydrate metabolism; Chitin degradation; Chitin-binding; Glycoprotein;
KW   Glycosidase; Hydrolase; Polysaccharide degradation; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..330
FT                   /note="Class III chitinase ARB_03514"
FT                   /id="PRO_0000434775"
FT   DOMAIN          23..314
FT                   /note="GH18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   ACT_SITE        155
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   CARBOHYD        61
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        135
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        278
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        302
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   330 AA;  35423 MW;  6E6EEABD59B5CBDD CRC64;
     MSSVKNILSF VALFAGVKTA YAGLNSPGHN NVAIYWGADV DVIPLAFAVS IKGPGGVPQI
     NFSNQGDPCK PFPGTDLLHC PQIGEDIKTC QKKGKTILLS IGGATYSEGG FRSAEDAVAG
     ANLLWDTFGP VKSSNSSVLR PFDDAVIDGF DLDFEATVLN MVPFAKQLRT LYDAEKSKTF
     YLTAAPQCPY PDLYNKEMLE GGVKFDALFI QFYNNFCGLN NFVLGSQSQD KFNFAEWDNF
     AKKVSANPDV KIMVGAPANK GAASSGYIDA QTLVSVINWS KTFSSFGGVM MWDASQAWAN
     GNFTSAVKGA LSAGNSRVVR MSYAGYHSGY