ID   A0A1X6N5S1_9APHY        Unreviewed;       442 AA.
AC   A0A1X6N5S1;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE            EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN   ORFNames=POSPLADRAFT_1168110 {ECO:0000313|EMBL:OSX63954.1};
OS   Postia placenta MAD-698-R-SB12.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Postiaceae; Postia.
OX   NCBI_TaxID=670580 {ECO:0000313|EMBL:OSX63954.1, ECO:0000313|Proteomes:UP000194127};
RN   [1] {ECO:0000313|EMBL:OSX63954.1, ECO:0000313|Proteomes:UP000194127}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAD-698-R-SB12 {ECO:0000313|EMBL:OSX63954.1,
RC   ECO:0000313|Proteomes:UP000194127};
RG   DOE Joint Genome Institute;
RA   Gaskell J., Kersten P., Larrondo L.F., Canessa P., Martinez D., Hibbett D.,
RA   Schmoll M., Kubicek C.P., Martinez A.T., Yadav J., Master E.,
RA   Magnuson J.K., James T., Yaver D., Berka R., Labutti K., Lipzen A.,
RA   Aerts A., Barry K., Henrissat B., Blanchette R., Grigoriev I., Cullen D.;
RT   "Genome Sequence of the Model Brown-Rot Fungus Postia placenta SB12.";
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00000822};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family.
CC       {ECO:0000256|RuleBase:RU004453}.
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DR   EMBL; KZ110594; OSX63954.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X6N5S1; -.
DR   OrthoDB; 2783699at2759; -.
DR   Proteomes; UP000194127; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; 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; cd00598; GH18_chitinase-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
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; PF00704; Glyco_hydro_18; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS01095; GH18_1; 1.
DR   PROSITE; PS51910; GH18_2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Chitin degradation {ECO:0000256|ARBA:ARBA00023024};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000489};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000489};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW   Reference proteome {ECO:0000313|Proteomes:UP000194127};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..442
FT                   /note="chitinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010854951"
FT   TRANSMEM        402..423
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          84..372
FT                   /note="GH18"
FT                   /evidence="ECO:0000259|PROSITE:PS51910"
SQ   SEQUENCE   442 AA;  47977 MW;  7139A1EC8B7CB7EB CRC64;
     MVSVSRLLLS AVAFAAAGVL ALPTELSRPA KRAPSAPYWV EYFDASVSEV TGVPPVSDVT
     VCPTHYFHPR GCPLTLDTRA RTHRDTMCCK CRSSRVHRRA TDPRACARPS PHSIIAFLLT
     EGAWDNAEGW ASLSASDRST LKSQYAAAGI SLMVSVFGST DTPTSSGADP TDTANTFAAW
     VQEYDLDGID VDYEDFNAFD AGTAEAWLET FTTQLRNQLP ASDYIITHAP VAPWFSPNYW
     TNGGYIQVDS EVGDLIDWYN IQFYNQGSTE YTTCAGLLTN SSSTWPESAL FQIAASGVPL
     DKLVIGKPAT TGDASTGYMS TSTLATCVEQ AKGEGWEAQG LGLTRAPPGA DAGVMVWEAA
     RVPSLKARDL ISSLDWLNTP LSLRLRTIIF TPHAPVSARW KALIRTLFAF ALFACVWIAW
     ITLQGAVRAH RQGLVWGERL MS
//