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
//