ID A0A168GDG0_CORDF Unreviewed; 423 AA.
AC A0A168GDG0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=LEL_06030 {ECO:0000313|EMBL:OAA76346.1};
OS Akanthomyces lecanii RCEF 1005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Akanthomyces;
OC Cordyceps confragosa.
OX NCBI_TaxID=1081108 {ECO:0000313|EMBL:OAA76346.1, ECO:0000313|Proteomes:UP000076881};
RN [1] {ECO:0000313|EMBL:OAA76346.1, ECO:0000313|Proteomes:UP000076881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 1005 {ECO:0000313|EMBL:OAA76346.1,
RC ECO:0000313|Proteomes:UP000076881};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(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:OAA76346.1}.
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DR EMBL; AZHF01000004; OAA76346.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A168GDG0; -.
DR STRING; 1081108.A0A168GDG0; -.
DR OrthoDB; 3203764at2759; -.
DR Proteomes; UP000076881; 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 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:SF317; CHITINASE 11; 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:UP000076881};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..423
FT /note="chitinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007897083"
FT DOMAIN 38..401
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
SQ SEQUENCE 423 AA; 45914 MW; B7F0685C1E609328 CRC64;
MLSLLKKSMA VAVALQAVTA LATPISNEVG IEKRGSGFAN AVYFTNWGIY GRNFQPADLP
ASEITHVLYS FMNIRSDGTI FSGDTYADYE KHYPGDSWND VGNNAYGCVK QLYLLKKQNR
NLKVMLSIGG WTWSTNFPAA ASSATSRKTF AQSAVGFMKD WGFDGIDIDW EYPADATQAQ
NMVLLLQAVR DELDSYASQY AKGHHFLLSI AAPAGPDNYN KLKLADLGKV LDYVNLMAYD
FAGSWSNFTG HDANMYASKD NANATPFNTN DAVQAYIKGG VPASKIVLGM PIYGRSFEKT
EGIGKPYNGI GSGSWENGVW DYKALPKSGA TVKCDNAVVG CYSYDASTQE LISFDTPAVI
NTKVSWLKGQ GLGGSMFWEA SADKKGADSL ISTSHQGLGS LDSAQNCLDY PNSKYDNIKN
GMK
//
