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Database: UniProt
Entry: A0A179F4G6_PURLI
LinkDB: A0A179F4G6_PURLI
Original site: A0A179F4G6_PURLI 
ID   A0A179F4G6_PURLI        Unreviewed;       688 AA.
AC   A0A179F4G6;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE            EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN   ORFNames=VFPFJ_11553 {ECO:0000313|EMBL:OAQ60073.1};
OS   Purpureocillium lilacinum (Paecilomyces lilacinus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Purpureocillium.
OX   NCBI_TaxID=33203 {ECO:0000313|EMBL:OAQ60073.1, ECO:0000313|Proteomes:UP000078340};
RN   [1] {ECO:0000313|EMBL:OAQ60073.1, ECO:0000313|Proteomes:UP000078340}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PLFJ-1 {ECO:0000313|EMBL:OAQ60073.1};
RA   Wang G., Liu Z., Lin R., Li E., Mao Z., Ling J., Yin W., Xie B.;
RT   "Biosynthesis of antibiotic leucinostatins and their inhibition on
RT   Phytophthora in bio-control Purpureocillium lilacinum.";
RL   Submitted (FEB-2016) 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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OAQ60073.1}.
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DR   EMBL; LSBI01000045; OAQ60073.1; -; Genomic_DNA.
DR   RefSeq; XP_018172807.1; XM_018328620.1.
DR   AlphaFoldDB; A0A179F4G6; -.
DR   STRING; 33203.A0A179F4G6; -.
DR   GeneID; 28893669; -.
DR   KEGG; plj:VFPFJ_11553; -.
DR   OMA; KCHESTN; -.
DR   OrthoDB; 360175at2759; -.
DR   Proteomes; UP000078340; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
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   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   4: Predicted;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Chitin degradation {ECO:0000256|ARBA:ARBA00023024};
KW   Chitin-binding {ECO:0000256|ARBA:ARBA00022669};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000489};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000489};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078340}.
FT   DOMAIN          17..332
FT                   /note="GH18"
FT                   /evidence="ECO:0000259|PROSITE:PS51910"
FT   REGION          332..449
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          641..661
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   688 AA;  71662 MW;  D4BFF4A542947262 CRC64;
     MSLSVRGVVG ASVGAFGALN GYWGQKDNQG LRAYCDSGVS SVTLGFINSA PEHDKSDLKY
     PGINFSTHCW AETYTDKNGV PSPLYEYCQS LKTDIPYCQD KGVKVILSIG GMYSSANNYK
     VSTTANGVHF ADKLYQIFGP YNPTAGVARP FDSPDRHVAV DGFDFDLEVE LDNKPYIAMI
     NRLRALDNSL IITGAPQCPL STTPNVMAEL LQQASFDALF IQFYNNPVCD YVGDGNGDKF
     NLDEWVSFMA KSNSKSAKLY VGLPGGPTSN SARSGYISPD KVKELVCKYS TKTPNWGGIS
     VWDLDTAAAN VVNGKNFKQH VADALKYGCR PVPTTTSTTA SSTKSSSSST IRASSTTTSS
     TTKVSSTTSS STSSSTSKAS STASSTSVAS STTVSSATDS SSSSTKVLSS SSTKAISSTA
     KPTSATTTDV TSPPVPTSTP VTSIVSSTTK WSNSTITSGT VSMTTSTVYT TSVHTVTKCP
     PYVANCPNGG YVTTETVPLY TTVCPVTKTP KPPQPTQAKT SAAWTTSTVY TTKIHTVTAC
     PPQIANCPVG HVTTETIPWY TTVCPVTETE TGKVPQPTPS VPGDVYPPLL ESTSATLAKS
     SITETVTNPA DVALKPSCSG PGCPGVSSGV VVPTLSWTTT PDAPSQGFTS TPGGPSAVPS
     NPVQAGASTL ALSLSGLVVM AAFQVFAL
//
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