ID   CHI2_RHIOL              Reviewed;         542 AA.
AC   P29027;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   22-FEB-2023, entry version 105.
DE   RecName: Full=Chitinase 2;
DE            EC=3.2.1.14;
DE   Flags: Precursor;
GN   Name=CHI2;
OS   Rhizopus oligosporus (Rhizopus microsporus var. oligosporus).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX   NCBI_TaxID=4847;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 23-38.
RC   STRAIN=ATCC 22959 / CBS 338.62 / NBRC 8631 / NRRL 2710 / AS 3.4818;
RX   PubMed=1429462; DOI=10.1128/jb.174.22.7398-7406.1992;
RA   Yanai K., Takaya N., Kojima N., Horiuchi H., Ohta A., Takagi M.;
RT   "Purification of two chitinases from Rhizopus oligosporus and isolation and
RT   sequencing of the encoding genes.";
RL   J. Bacteriol. 174:7398-7406(1992).
CC   -!- FUNCTION: Probably involved in the apical growth and branching of
CC       fungal hyphae.
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   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- PTM: O-glycosylated.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC       class III subfamily. {ECO:0000305}.
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DR   EMBL; D10158; BAA01022.1; -; Genomic_DNA.
DR   PIR; B47022; B47022.
DR   AlphaFoldDB; P29027; -.
DR   SMR; P29027; -.
DR   CAZy; CBM19; Carbohydrate-Binding Module Family 19.
DR   CAZy; GH18; Glycoside Hydrolase Family 18.
DR   CLAE; CHI18B_RHIOL; -.
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   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR005089; CBM_fam19.
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   PANTHER; PTHR45708; ENDOCHITINASE; 1.
DR   PANTHER; PTHR45708:SF49; ENDOCHITINASE; 1.
DR   Pfam; PF03427; CBM_19; 1.
DR   Pfam; PF00704; Glyco_hydro_18; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 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;
KW   Direct protein sequencing; Glycoprotein; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Secreted; Signal; Zymogen.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000269|PubMed:1429462"
FT   CHAIN           23..446
FT                   /note="Chitinase 2"
FT                   /id="PRO_0000011932"
FT   PROPEP          447..542
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000011933"
FT   DOMAIN          29..314
FT                   /note="GH18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   REGION          312..356
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          355..406
FT                   /note="Chitin-binding, high affinity"
FT   ACT_SITE        166
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
SQ   SEQUENCE   542 AA;  56528 MW;  3E8F17DA551FD0A7 CRC64;
     MLTRTFLGMA ISAFLASTGV QAAWSSHGPN VMYYWGQNSA GGSNTQASLG TYCESGQVDA
     VLLSFLHVFN VGGIPEINLS SACAGTYFPN TQLLSCPAVG ADIKKCQDKG VKVILSLGGA
     AGVYGFTSDA QGQQFAQTIW NLFGGGNSDT RPFGDAVIDG VDLDIEGGSS TGYVAFVNAL
     RQKFSSNFLI GAAPQCPFPD AILGSVLNSA SFDYVNVQFY NNYCSATGSS FNFDTWDNWA
     KTTSPNKNVK IMFTVPGSST AAGSGYVPMS TLQTIVPSLA SKYSSYGGVS VWDASQAWNN
     GGFNSQLYSL VHSGGSTPPP PSSSSATKTT TKTTATSTKT TTTTAPTATS TPGSCPVANQ
     PCSTQNQYAC TADGKYAVCD HGKWVASSCP SNTVCIPTTD GASIYCGYAT GSGSTCPSVS
     ALEITAASLG SKNGPVPRPY KASKVAAQLA VTSTDKNSFE AVINARRTTL TPFEKSVTIE
     FTTPSNIKFT ESDMGPVRQV GNKVRIQAKN DYNESMTLVV KVKGSINSGV FVAPSTSAWN
     FK
//