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Database: UniProt
Entry: A0A319DVE4_9EURO
LinkDB: A0A319DVE4_9EURO
Original site: A0A319DVE4_9EURO 
ID   A0A319DVE4_9EURO        Unreviewed;       517 AA.
AC   A0A319DVE4;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   22-FEB-2023, entry version 17.
DE   RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE            EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN   ORFNames=BO71DRAFT_426504 {ECO:0000313|EMBL:PYH98157.1};
OS   Aspergillus ellipticus CBS 707.79.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1448320 {ECO:0000313|EMBL:PYH98157.1, ECO:0000313|Proteomes:UP000247810};
RN   [1] {ECO:0000313|EMBL:PYH98157.1, ECO:0000313|Proteomes:UP000247810}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 707.79 {ECO:0000313|EMBL:PYH98157.1,
RC   ECO:0000313|Proteomes:UP000247810};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (FEB-2018) 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. Chitinase
CC       class V subfamily. {ECO:0000256|ARBA:ARBA00008682}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00261}.
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DR   EMBL; KZ825815; PYH98157.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A319DVE4; -.
DR   STRING; 1448320.A0A319DVE4; -.
DR   Proteomes; UP000247810; Unassembled WGS sequence.
DR   GO; GO:0008061; F:chitin binding; IEA:UniProtKB-UniRule.
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; cd00035; ChtBD1; 1.
DR   Gene3D; 3.10.50.10; -; 1.
DR   Gene3D; 3.30.60.10; Endochitinase-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR001002; Chitin-bd_1.
DR   InterPro; IPR018371; Chitin-binding_1_CS.
DR   InterPro; IPR011583; Chitinase_II.
DR   InterPro; IPR029070; Chitinase_insertion_sf.
DR   InterPro; IPR036861; Endochitinase-like_sf.
DR   InterPro; IPR001223; Glyco_hydro18_cat.
DR   InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR11177; CHITINASE; 1.
DR   PANTHER; PTHR11177:SF373; CHITINASE; 1.
DR   Pfam; PF00187; Chitin_bind_1; 1.
DR   Pfam; PF00704; Glyco_hydro_18; 1.
DR   SMART; SM00270; ChtBD1; 1.
DR   SMART; SM00636; Glyco_18; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF54556; Chitinase insertion domain; 1.
DR   SUPFAM; SSF57016; Plant lectins/antimicrobial peptides; 1.
DR   PROSITE; PS00026; CHIT_BIND_I_1; 1.
DR   PROSITE; PS50941; CHIT_BIND_I_2; 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   Chitin-binding {ECO:0000256|ARBA:ARBA00022669, ECO:0000256|PROSITE-
KW   ProRule:PRU00261};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00261};
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:UP000247810};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..517
FT                   /note="chitinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5016260203"
FT   DOMAIN          67..116
FT                   /note="Chitin-binding type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50941"
FT   DOMAIN          121..480
FT                   /note="GH18"
FT                   /evidence="ECO:0000259|PROSITE:PS51910"
FT   REGION          493..517
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        85..97
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT   DISULFID        90..104
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
SQ   SEQUENCE   517 AA;  56093 MW;  F56C2909DA194148 CRC64;
     MNGWGVFIVL VGLSGLQMIQ ANTPCSATDL CTTGCCGNGG IENNDYICGT GPTFCGEGNC
     TSTCDYKAEC NPGGWPSSMY NDTTCPLNVC CSEYGFCGTT SSFCGDTTVT QPSCDGTSSD
     ARTIGYYEGW SLERSCQTMD PDQIPLGYYT HLNYAFAYID QDLSYIISAM DSTTGSLYQE
     VTALKDKQPD LEVWISVGGW AFNDAGSTEH TFSDLAASET AQDLFFASLI TFMVNNAFDG
     IDIDWEYPVA SDRYGSSVDF DNYVTFLKRL RSALNNSGYL FGISITLPSS YWYMQNFDIV
     SIDPIVDWFN IMTYDLHGVW DGDDPYIGAV ALAHTNLTEI KESLDLLWRN NINPSRVNLG
     LGFYGRSFTM SDPSCMTAGC PFSGGGREGP CTATSGILSD VEIRDIIADG ATVTLDEAAA
     VQIVTWDTNQ WVSYDDATTI KMKIDYANSV CLGGTMVWAV DLDDTNGTSI NYLGSGLNRT
     AATIYNDTSL DTSGDLGSSV ARRSESHLRG HRHHGGL
//
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