ID   CSNC_ASPOR              Reviewed;         389 AA.
AC   Q2U5P1;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 50.
DE   RecName: Full=Endo-chitosanase C;
DE            EC=3.2.1.132;
DE   Flags: Precursor;
GN   Name=csnC; ORFNames=AO090113000063;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
CC   -!- FUNCTION: Chitosanase catalyzing the endo-type cleavage of chitosan,
CC       the deacylated form of chitin. Chitosanase may be crucial in the
CC       degradation of the deacetylated portion of chitin in the fungal cell
CC       wall. Chitoolisaccharides produced by the hydrolysis of partially N-
CC       acetylated chitosan are known to have many biological activities,
CC       including antibacterial activity, immune-enhancing effects, and
CC       elicitor activity (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of beta-(1->4)-linkages between D-glucosamine
CC         residues in a partly acetylated chitosan.; EC=3.2.1.132;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- DOMAIN: The C-terminal R3 domain contains 3 tandem repeats required for
CC       the binding to insoluble chitosan. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 75 family. {ECO:0000305}.
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DR   EMBL; AP007166; BAE63124.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2U5P1; -.
DR   STRING; 510516.Q2U5P1; -.
DR   CAZy; GH75; Glycoside Hydrolase Family 75.
DR   EnsemblFungi; BAE63124; BAE63124; AO090113000063.
DR   HOGENOM; CLU_041930_0_0_1; -.
DR   Proteomes; UP000006564; Chromosome 5.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016977; F:chitosanase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR009939; Chitosanase_fungal.
DR   PANTHER; PTHR42061; PTHR42061; 1.
DR   Pfam; PF07335; Glyco_hydro_75; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..389
FT                   /note="Endo-chitosanase C"
FT                   /id="PRO_0000429640"
FT   REPEAT          280..313
FT                   /note="R3-1"
FT   REPEAT          320..350
FT                   /note="R3-2"
FT   REPEAT          357..387
FT                   /note="R3-3"
SQ   SEQUENCE   389 AA;  39844 MW;  D6F3C18849D85C70 CRC64;
     MPIKSFASRL ALSLAICGTA MGQKVNGADY NKPDGGPPAK FFQASSSIPV AAIQAAAAKA
     SKVPSHATYP IGQGSTKSTI HSDWAGFSEG AAFSFIADMD VDCDGLNHGC KGNPDGQKET
     NWGALSAYEV PFIVIPQEFL DANKGTLKGN AVAAVICATS SNGKMFYGIF GDSNGDSPQV
     TGEASWLMAR TCFPEEDLNG NKGHTAADVT YIVFTGDKAV LPSSALNKNY ITNFDTLRSM
     GDSLVGALAK NLNLGGGGGN PPTTLTTTSI PEPTGGSGSC SWPGHCAGFK NKGATCSSND
     DCSDDLACQN GKCASDGSAE TCSWEGHCKG ATCSSNDDCS DELACISGIC SVDNGVETCE
     WEGHCEGASC SSHDDCDGNL ACKNGKCSA