ID A0A178DZH1_9PLEO Unreviewed; 1275 AA.
AC A0A178DZH1;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=IQ07DRAFT_569301 {ECO:0000313|EMBL:OAL49054.1};
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:OAL49054.1, ECO:0000313|Proteomes:UP000077535};
RN [1] {ECO:0000313|EMBL:OAL49054.1, ECO:0000313|Proteomes:UP000077535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL49054.1,
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}.
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DR EMBL; KV441647; OAL49054.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178DZH1; -.
DR STRING; 765867.A0A178DZH1; -.
DR InParanoid; A0A178DZH1; -.
DR OrthoDB; 11640at2759; -.
DR Proteomes; UP000077535; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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 Gene3D; 3.10.350.10; LysM domain; 2.
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 InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR PANTHER; PTHR47700:SF2; CHITINASE; 1.
DR PANTHER; PTHR47700; V CHITINASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G13720)-RELATED; 1.
DR Pfam; PF00704; Glyco_hydro_18; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000077535};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1275
FT /note="chitinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008084912"
FT TRANSMEM 1164..1189
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 323..369
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 388..436
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 531..899
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 889..914
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1275 AA; 138601 MW; DA166BF7CD79FCA6 CRC64;
MRPSLSPLFL ALLTLFPFPF PSAHASSPTN PCPIPCSTAG PNPTAWTHLH GERALKRCPE
PVLFDTAIFT GVDDPNTLIT LRSCTASGAN TTQEMDYTPA PFTFGGPLER RQNVSGSVNA
TDVVFSKLAA LAGCNADPEG VKNQTDISIL RWRYSRDGIL ATKAEVATAA QKLRDYLRTQ
PDCKSTIMLA QFRGAVVGLY VGTEVLNADA DVVVDRFLKA LDGAGEVSAL ASEVCREKTP
ASWSVGVYAD FRGNISATQA ALANWVQGKC QAGYDSKEAA QQASITFIRR LSVPQEPVVL
GGFEQTSEPV SDLAKRQTTA TCKYLKVIGG DSCWSLSQQC GISQADLEKF NPQKTNFCNT
LQPDQYVCCN KGSLPDFTPK PNADGSCATY QIQKDDSCYK IGEAHFLTAQ NITDFNKKTW
GWAGCTQIQP GQKICLSKGE PPMPASVENA LCGPTVPGTL RPTDGKALKD LNPCPLNVCC
NVWGQCGLTD DFCVPNPADT GAPGTSKPGK NGCIASCGME ITNNASPPAQ FRKIAYFEAW
NKDRPCLHMD VTDIDKAKFT HVHFAFPDIT VDFKPDVSKL QEQFDKFKGM TGIKRIVSFG
GWAFSTEAAT FNIFRTGVTD ANRATLATNI VDFVNKHGLD GVDFDWEYPA APDIPGIPAG
SLEAGKQYLE FLKLVKRRLS TKEVAIAAPA SYWYLKGMPI KEISQVVDYF VYMTYDLHGQ
WDYGNKWATV GCESGNCLRS HINSTETRIS LAMVTKAGVQ SNKVIVGVAS YGRSFHMEVP
GCTGPDCKFT GSSTESDAMP GECTGTGGYI SNAEIRELIT KGQDERSGYT VKTWHDGASN
SDIMVYNDVE WVAYMSDVTK STRTDWYKGL NFGGTSDWAV DLDKDYGSSG IGEGSTGEPT
EGGGGPKCDQ RDSYDSLEKI SNDNGLNSYC ASIYTLRVLQ GMLHKSIDKY GTVNNGYDSK
FKSYVKYMKK GLPETLRLWA HWLSGDGQVF FDCTFDGNGK KWSGPCPVPR SVRGGLLIGI
WKIEMTLRDA DGFWKALADK TGILQDWIVF DTYKEKTQCA PTPQPAPCNT LELVVTGMPF
LKKDYTIPDP KDIVVKAMSN VGNLDASITA RTFDVATGQW LGSNADVVQS LAIPVFMVEN
AVEGMEDAKE LGEEVEKKEA QNTLLTVLSL IFFIVPFLGQ AAAVAAGLLQ LGRIIAIAGL
AAEAGLTIRE VIENPEMAPF AIMDLLTAGR LKTPREYLDA ANFRRAMQPS DIATLGEKFT
KQDGMIQKIV SACRK
//
