ID A0A423WL25_9PEZI Unreviewed; 1476 AA.
AC A0A423WL25;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=VSDG_00885 {ECO:0000313|EMBL:ROW04029.1};
OS Valsa sordida.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=252740 {ECO:0000313|EMBL:ROW04029.1, ECO:0000313|Proteomes:UP000284375};
RN [1] {ECO:0000313|EMBL:ROW04029.1, ECO:0000313|Proteomes:UP000284375}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YSFL {ECO:0000313|EMBL:ROW04029.1,
RC ECO:0000313|Proteomes:UP000284375};
RA Yin Z., Huang L.;
RT "Host preference determinants of Valsa canker pathogens revealed by
RT comparative genomics.";
RL Submitted (SEP-2015) 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:ROW04029.1}.
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DR EMBL; LJZO01000002; ROW04029.1; -; Genomic_DNA.
DR STRING; 252740.A0A423WL25; -.
DR Proteomes; UP000284375; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
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 CDD; cd02878; GH18_zymocin_alpha; 1.
DR CDD; cd00118; LysM; 2.
DR Gene3D; 3.10.50.10; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 3.10.350.10; LysM domain; 2.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR029070; Chitinase_insertion_sf.
DR InterPro; IPR029226; Ecp2.
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 InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR PANTHER; PTHR47700:SF1; CHITINASE; 1.
DR PANTHER; PTHR47700; V CHITINASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G13720)-RELATED; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR Pfam; PF14856; Hce2; 1.
DR Pfam; PF01476; LysM; 2.
DR SMART; SM00636; Glyco_18; 1.
DR SMART; SM00257; LysM; 2.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF54556; Chitinase insertion domain; 1.
DR SUPFAM; SSF54106; LysM domain; 2.
DR SUPFAM; SSF57016; Plant lectins/antimicrobial peptides; 1.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
DR PROSITE; PS51782; LYSM; 2.
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};
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:UP000284375};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..1476
FT /note="chitinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019235225"
FT DOMAIN 303..348
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 367..415
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 507..883
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 1157..1176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1476 AA; 158090 MW; 2C2E31E7D222B16F CRC64;
MFLHYYWLKI FLGLVLSHRD FYVLSSQTTK SGRSPYYRGL DPCPARCSDA GPSPGNWSLY
HNLDQFVQCP ETIFLDFSLS DEVDDAARKH RLYACSVWGA DWTQTPNTTA PVSVTRVINS
TYELGWWPAP GTGQSGGAST IAAVRALSRQ MRWYLTNGHA PTNKPVYLFA RFFNAAVGLY
VGKGLQNEGT GSTALKLLED ALVSVDPRTA AGGVALQLCP EGSDADHMFG VVASTNGTFS
TTQSALTSLS HAECLSGFIG GMNITAQAYL VSPLVISSSN VTTNSSSIFT NTTSHLSRRA
NCTTIQVVSG DSCASLASKC GIAASDFTDY NPQDDLCSTL QPYQHVCCSD GTLPDFAPQP
NDDGSCATYT IASGDTCSGL AAEYSLTVED LEDFNMNTWA WNGCDDIWVG TIICLSTGDP
PMPAPLANAL CGPQVPGTDK PTDGTALSDL NPCLLNACCD VWGQCGTTSE FCTNTSTGAP
GTAKEGTNGC ISNCGTDIIF SGAPDEFRSV TYFESYGFDR PCLYMDAKQI NTDKYTHVHY
AFATLSDDYE VLTGDAMATY EFGNFKAIRG PKKIVTFGGW DFSTNPNTYY IFRNGVTAAN
RLTMAINIAN FVEENGLDGV DIDWEYPGAS DIPGIPAAST DDGDNYFAFL VVLRNLLGTE
KSISIAVPSS YWYLKGYPIG YMSALVDYFV FMTYDLHGQW DYGNAYSNPG CPTGNCLRSQ
VNLTETINAL SMITKAGVPS NQVVVGVTSY GRSFQMAAAG CYTENCLFTG SSTVSNAEEG
VCTVTAGYIS DAEIKDIIAN GSRVNYNSLD DSSNSNILVY DDIQWVAWMD EDTKAGRAAV
YQLLEMGGTT DWATDLENYQ EAPAGTESWA IFLEKVNSGL DPYEEGNRTG NWTELDCSSQ
GVADVHDLTA KERWEMLDCS NAWQDAIDIW TQIDRPANNL TFSESIANTF HVGENANCGQ
LFMDTNCDNT IVCTQAVGAG TGPAGYVIWN SLVLIHEAYE NYYNALNDAA SSSIFPSFTA
YEDDFTPLPD TTDEKVIQVL LDVVGLLGAL GAGVYFTEYL ESLPSFLAFL DKDTAKDGTL
ALIAAGTSVA KDLMDGDSSV WTATKQHEFE QYMAEFVSGW KAVTEQAVHN LYNGSDDNIN
TLTKLIADGR FIEGSANGHA TGTSDTPGPA PTSNTDLEGN ITTAFWSYTI PVGWTLSGTH
AFVLDSGYGC DTTGNPLDKY LTDKTASATQ GCYNNKLYYL VAAKGDAELC INDGCASSYF
QAPAGLDKLD GTAYGGLTLQ NMITGSIKTY VANGNSNGAS SADFTSSSTL DDLYNTDITT
PGFIRIPVCS AELAYTNWDA VITLNSSLSS ADGFPCNKPQ GEAYCGDSTF VDESSDASPT
VSDCQQIATN IGLGGDWTVD SSGNQHQLVQ YGTCAFGIQG QGRPIGNVDF TIGNQDIIDI
ITTSISMFGG GGKVGAKGTM SCSGDATSQD VLWGLY
//
