ID   CHI1_APHAL              Reviewed;         423 AA.
AC   P32470;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Chitinase 1;
DE            EC=3.2.1.14;
DE   Flags: Precursor;
GN   Name=CHI1;
OS   Aphanocladium album (Wheat rust fungus) (Acremonium album).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreales incertae sedis; Aphanocladium.
OX   NCBI_TaxID=12942;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ETHM 483;
RX   PubMed=1398137; DOI=10.1016/0378-1119(92)90099-b;
RA   Blaiseau P.-L., Lafay J.-F.;
RT   "Primary structure of a chitinase-encoding gene (chi1) from the filamentous
RT   fungus Aphanocladium album: similarity to bacterial chitinases.";
RL   Gene 120:243-248(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-67, AND PROTEIN SEQUENCE OF 35-67.
RX   PubMed=1735126; DOI=10.1007/bf00318656;
RA   Blaiseau P.-L., Kunz C., Grison R., Bertheau Y., Brygoo Y.;
RT   "Cloning and expression of a chitinase gene from the hyperparasitic fungus
RT   Aphanocladium album.";
RL   Curr. Genet. 21:61-66(1992).
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.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC       class V subfamily. {ECO:0000305}.
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DR   EMBL; X64104; CAA45468.1; -; Genomic_DNA.
DR   EMBL; S81303; AAB21333.1; -; Genomic_DNA.
DR   PIR; JQ1975; JQ1975.
DR   PIR; S26859; S26859.
DR   AlphaFoldDB; P32470; -.
DR   SMR; P32470; -.
DR   CAZy; GH18; Glycoside Hydrolase Family 18.
DR   CLAE; CHI18A_APHAL; -.
DR   PRIDE; P32470; -.
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   Gene3D; 3.10.50.10; -; 1.
DR   InterPro; IPR011583; Chitinase_II.
DR   InterPro; IPR029070; Chitinase_insertion_sf.
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   SUPFAM; SSF54556; SSF54556; 1.
DR   PROSITE; PS01095; GH18_1; 1.
DR   PROSITE; PS51910; GH18_2; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Chitin degradation;
KW   Cleavage on pair of basic residues; Direct protein sequencing; Glycosidase;
KW   Hydrolase; Polysaccharide degradation; Secreted; Signal; Zymogen.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..34
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000011922"
FT   CHAIN           35..423
FT                   /note="Chitinase 1"
FT                   /id="PRO_0000011923"
FT   DOMAIN          38..401
FT                   /note="GH18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   ACT_SITE        171
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   BINDING         102..103
FT                   /ligand="chitin"
FT                   /ligand_id="ChEBI:CHEBI:17029"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   BINDING         129..132
FT                   /ligand="chitin"
FT                   /ligand_id="ChEBI:CHEBI:17029"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   BINDING         172
FT                   /ligand="chitin"
FT                   /ligand_id="ChEBI:CHEBI:17029"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   BINDING         237..240
FT                   /ligand="chitin"
FT                   /ligand_id="ChEBI:CHEBI:17029"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   BINDING         378
FT                   /ligand="chitin"
FT                   /ligand_id="ChEBI:CHEBI:17029"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
SQ   SEQUENCE   423 AA;  46059 MW;  55DFB25B73443F31 CRC64;
     MLSFVKKSIA LVAALQAVTA LATPISSEAG VEKRGSGFAN AVYFTNWGIY GRNFQPADLP
     ASEITHVLYS FMNVRADGTI FSGDTYADYE KHYAGDSWND VGTNAYGCVK QLYLLKKQNR
     NMKVMLSIGG WTWSTNFPAA ASSAATRKTF AQSAVGFMKD WGFDGIDIDW EYPADATQAQ
     NMVLLLQAVR SELDSYAAQY AKGHHFLLSI AAPAGPDNYN KLKFAELGKV LDYINLMAYD
     YAGSWSNYTG HDANIYANPQ NPNATPYNTD DAVQAYINGG VPANKIVLGM PIYGRSFQQT
     EGIGKPYNGI GSGSWENGIW DYKALPKAGA TVKCDDTAKG CYSYDPSTKE LISFDTPAMI
     STKVSWLKGK GLGGTMFWEA SASKKGSDSL ISTSHQGLGS QDSTQNYLDY PNSKYDNIKK
     GMN