ID A0A178DJY1_9PLEO Unreviewed; 1163 AA.
AC A0A178DJY1;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=IQ07DRAFT_592860 {ECO:0000313|EMBL:OAL43795.1};
OS Pyrenochaeta sp. DS3sAY3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Cucurbitariaceae;
OC Pyrenochaeta.
OX NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL43795.1, ECO:0000313|Proteomes:UP000077535};
RN [1] {ECO:0000313|EMBL:OAL43795.1, ECO:0000313|Proteomes:UP000077535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL43795.1,
RC ECO:0000313|Proteomes:UP000077535};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) 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; KV441665; OAL43795.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178DJY1; -.
DR STRING; 765867.A0A178DJY1; -.
DR InParanoid; A0A178DJY1; -.
DR OrthoDB; 671410at2759; -.
DR Proteomes; UP000077535; 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; PTHR47700:SF2; CHITINASE; 1.
DR PANTHER; PTHR47700; V CHITINASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G13720)-RELATED; 1.
DR Pfam; PF00187; Chitin_bind_1; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00270; ChtBD1; 2.
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; 2.
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:UP000077535};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1163
FT /note="chitinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008084337"
FT DOMAIN 57..95
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DOMAIN 96..139
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DOMAIN 152..512
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT DISULFID 66..78
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 71..85
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 89..93
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 110..122
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 115..129
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 133..137
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
SQ SEQUENCE 1163 AA; 128423 MW; 3278E4BEB2A2894B CRC64;
MLQRLVVFAL LAAVDVVRAS HGQRHASFHG RRSLDQIDRE SINNETSLSS VLSRRDDYTC
APGRPCKNGA CCGESGNCGY GPVYCGKGCS SNCDATAECG QYSKIPGKTC PLNVCCSEFG
FCGTTSEFCN KKCQSNCIEH PTPPSGGGKA VDRVIGYWEA WNARSNCHNT QASDLPVQAL
THVNYAFAYI DPSTFEITTM DAQTPVSTFK DVIKLKDIKP DLKVFVSIGG WTFSDNDTAT
QPVFGNIART ESNRQKFAGT LLKFMTGYGF DGVDLDWEYP GAPDRGGKPD DTANYVELVK
TLRSAFDKSG RSLEITFTAP SSLWYLRWFD LPAMIKYVDW INLMSYDLHG VWDSTNPIGS
IVQAHTNLTE IKLAAELFWR VNVPPQKIAL GYGFYGRAFT LADPSCTKPS CAFKGGAKKG
VCTGTSGYLA YYEIQDIIKK NQKKRDFTVV HDKEAAVKYF AWDNDQWISY DDADTFKQKK
DWANSVGFSG SLIWASDLDD YDNNAHIAFT GIKNLGSRKE LEKANKYQEH VETTDSFLGQ
GCKFYETVVS DVKSYDCGKD NELVAYDTHG CKGDKNHKDW QCGWPMCCPK KSRMKDKCMW
RGSGGDCNGQ CHANEVKIGG SSWGGYPGEG KTGRCSRGGK ALCCQVDLEA ANEGCYWTKG
CDNKKCAADE ESVAHAYSIN GDECVIELPP LRRRGDELFS LQSRATNSGQ NYCCKKSKKA
FDSCKWVGKG DCAQNTCDRG EVTLATNEYG DIDDNCNWFR KKALCCKPNQ DAINEPLCNT
DLCKGDDCKD DDEGSLTKRS VSDSDHHLDK RVRPAAKRLL DIGAATRLVL TSAPYPNGPS
GELFSGGGLS TLPVKGGFMW ESNVCKAIGA SFKSVGSIPV DLATWSGKRN LWDTEHYRDI
ASLDKLLVTA TTGILLSGKK MKATKMKAED IIKAWNARYP AGAVLHSLGQ AFVTGVKGFG
TPDAFGNDWN NLETPNMRFH TVLGSHAYRY PFTYIPNEMN RWKSSLLVTG RVPIDKTKFN
KAVVKAITET GKAGSDAVSE VLTGLQRTYA TVAFYNDAYL AHYFDKAHKD FHFLADEMAQ
NFQGWTSFPD ILKEFDVDML EFGSANAKDF MTARTGTVIA KFPSKATLDL STYPVHVQQL
YNTIQFYAEQ QSKLTFMQAD GSS
//
