ID A0A2C6A8L9_9HYPO Unreviewed; 404 AA.
AC A0A2C6A8L9;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=CDD83_7517 {ECO:0000313|EMBL:PHH88452.1};
OS Cordyceps sp. RAO-2017.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Cordyceps.
OX NCBI_TaxID=2004951 {ECO:0000313|EMBL:PHH88452.1, ECO:0000313|Proteomes:UP000221130};
RN [1] {ECO:0000313|Proteomes:UP000221130}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1346 {ECO:0000313|Proteomes:UP000221130};
RA de Bekker C., Evans H.C., Brachmann A., Hughes D.P.;
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PHH88452.1, ECO:0000313|Proteomes:UP000221130}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1346 {ECO:0000313|EMBL:PHH88452.1,
RC ECO:0000313|Proteomes:UP000221130};
RA De Bekker C., Evans H.C., Brachmann A., Hughes D.P.;
RT "Ant-infecting Ophiocordyceps genomes reveal a high diversity of potential
RT behavioral manipulation genes and a possible major role for enterotoxins.";
RL Submitted (OCT-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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class V subfamily. {ECO:0000256|ARBA:ARBA00008682}.
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:PHH88452.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NJEV01000443; PHH88452.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C6A8L9; -.
DR STRING; 2004951.A0A2C6A8L9; -.
DR OrthoDB; 3203764at2759; -.
DR Proteomes; UP000221130; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008061; F:chitin binding; IEA:InterPro.
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; 3.10.50.10; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR029070; Chitinase_insertion_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:SF406; GH18 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00636; Glyco_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 Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000221130};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 25..404
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
SQ SEQUENCE 404 AA; 45129 MW; 802828F8AD6B2B6D CRC64;
MRFDSLFTPA SLTIGLAGLA LGDSPVIVGF VQSWLWEERP AIREIDFSSY TYVNMAFSIP
QKDGSSIFEQ EDILPEAVRI IHDKKSKVLM SYGGWTGSAN FSDIVNDDTI CDTFIDNIIA
HTEKHNLDGV DIDWEYPGRE GDDCNVFHKE SDTDKFSAFL TKLRKKMDER FPEPKKIISL
AVATRTFEGP DGPIDDVSAF IDAVDFMAVM LYDMSEGEEL TGPNAPLDFV KDKGTQTSFK
TGLDAWAKAK WPAEKTLAGV GFYGRASIVD EEMTPENVNP FMKKNATVPA GDKDNQEPFD
DPCSNQGPVW SGEYWYRNLL EQKILQDPTT AGKGWIRNVH DPSKTPILRN LASNTLLSYD
DPESITAKVK EASSRGLKGI MIWSIDMDTP DQQMTNAIQK GWET
//
