ID A0A151GAE6_9HYPO Unreviewed; 654 AA.
AC A0A151GAE6;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=DCS_06029 {ECO:0000313|EMBL:KYK54073.1};
OS Drechmeria coniospora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Drechmeria.
OX NCBI_TaxID=98403 {ECO:0000313|EMBL:KYK54073.1, ECO:0000313|Proteomes:UP000076580};
RN [1] {ECO:0000313|EMBL:KYK54073.1, ECO:0000313|Proteomes:UP000076580}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 6962 {ECO:0000313|EMBL:KYK54073.1,
RC ECO:0000313|Proteomes:UP000076580};
RX PubMed=26975455; DOI=10.1038/srep23122;
RA Zhang L., Zhou Z., Guo Q., Fokkens L., Miskei M., Pocsi I., Zhang W.,
RA Chen M., Wang L., Sun Y., Donzelli B.G., Gibson D.M., Nelson D.R.,
RA Luo J.G., Rep M., Liu H., Yang S., Wang J., Krasnoff S.B., Xu Y.,
RA Molnar I., Lin M.;
RT "Insights into Adaptations to a Near-Obligate Nematode Endoparasitic
RT Lifestyle from the Finished Genome of Drechmeria coniospora.";
RL Sci. Rep. 6:23122-23122(2016).
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:KYK54073.1}.
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DR EMBL; LAYC01000003; KYK54073.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151GAE6; -.
DR STRING; 98403.A0A151GAE6; -.
DR InParanoid; A0A151GAE6; -.
DR OrthoDB; 3203764at2759; -.
DR Proteomes; UP000076580; Chromosome 03.
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 CDD; cd06548; GH18_chitinase; 1.
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:SF365; ENDOCHITINASE B; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF54556; Chitinase insertion domain; 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:UP000076580};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 263..627
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..61
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 654 AA; 71618 MW; 875C60EB88885C58 CRC64;
MARRSRRRPN FLDDGSATQD AQELGAAECQ PGCLRRGPGM RAKGSRVDND KMKDETDDGA
SDPAGLQRGN LRCTNVRRAA HKPCMALPGA ASLLVPSNGK RRRPPLCCEA SGCPASTFWR
GPAKHCPLQP LYCSTVMSTL PQALCSPQAL CSPLLPQALL SHPSSSCLGH LLLLSISFTS
RVYLRNPSAN ASLLAGYAPA ASPIIPLRPV GLCPSPYPTS SAEDASAESN PRPRHLAESA
WHRRASLASF VIHREPPCPA ANARLLISSP LRAIYGRKHF PQDLPVENLT HILYAFANVR
PDTSEVHLTD GWADTDIHWD GDSWNDAGTN MYGCLKQLNL HKRRNRNLKV LLSIGGWTYS
ANFKTPAATP QGRETFAKSS LELLKNMGFD GLDIDWEYPQ NADEARDFVE LLATVRRELD
AYSQTLGGGH RFELTVACPA GAQNYGKLDL AAMDRHLDFW NLMAYDYAGS WDQLSGHQAN
LYPSPDNPAC TPFSTAAAVD FYTSHGVAPD RIVVGMPLYG RAFQNTDGLG KPYQDVGEGT
WERGVHDFNK LPLEGAQETY DERAGATYCY DARQRTLVTY DTPQMTRVKA EFIRQRGLGG
AMWWESSADK AGPDSLIGVA VQCLGGADGL LKRDNCIEYP HTKYDNLRAG FPNN
//
