ID W7HXN9_9PEZI Unreviewed; 1237 AA.
AC W7HXN9;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 03-MAY-2023, entry version 34.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=DRE_00961 {ECO:0000313|EMBL:EWC44902.1};
OS Drechslerella stenobrocha 248.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Drechslerella.
OX NCBI_TaxID=1043628 {ECO:0000313|EMBL:EWC44902.1, ECO:0000313|Proteomes:UP000024837};
RN [1] {ECO:0000313|EMBL:EWC44902.1, ECO:0000313|Proteomes:UP000024837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=248 {ECO:0000313|EMBL:EWC44902.1,
RC ECO:0000313|Proteomes:UP000024837};
RA Liu X., Zhang W., Liu K.;
RT "Drechslerella stenobrocha genome reveals carnivorous origination and
RT mechanical trapping mechanism of predatory fungi.";
RL Submitted (MAY-2013) 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; KI966433; EWC44902.1; -; Genomic_DNA.
DR AlphaFoldDB; W7HXN9; -.
DR HOGENOM; CLU_001482_0_0_1; -.
DR Proteomes; UP000024837; 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 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; 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:UP000024837};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1237
FT /note="chitinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004895611"
FT TRANSMEM 1123..1142
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1149..1171
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1177..1193
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 282..327
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 346..394
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 488..850
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
SQ SEQUENCE 1237 AA; 133776 MW; 1F21A0AC6232387A CRC64;
MKHLALSSIF VALAARCIAD DSFISALRAC PQSCSEVGQN PADWTVYDSV ERLNSCNETL
LLDFAIYSPL DDPETTVKIS SCTASGPQKA KRQEIVTNSC QHSDQTDVSI ELQSSGAGIS
VNGPHVVAAA RQIQSYLKST SDCGTFINFG YSNHSVVGVY VGASVENTNV ADTLVQKFID
HIQSNGIANT TIAQYCQGAN SDYTIGIAAS ASGDIAGIQS IVRSWSDSKC VTGLEQKSLD
WAKTTLKIAG SVAVVEDKEF SISGSGQTLR ASSGLVSRAT CKYIKVVSGD SCGSLAGKCK
ITGPKFMEFN TAKNLCATLA VGQPVCCDKG TLPDLKPKPN KDGSCSSYAV IKDDYCAKIA
ASNGLTVQNL EAFNKNTWGW SGCNRLLTGI KICLSTGTPP MPAPVTNAVC GPQKPGSKPP
DAGKSLASLN PCKLNVCCNI WGQCGTTSDF CTVSKSATGA PGTSAPGVSG CISNCGTELV
KSAAPAKFIS VAYFEAWNSK RKCLHMDVDQ IDSKKYTHIH YSFADITKDF KVDVSGVSRD
WEAFKSITDI KKILSFGGWS FSTEQDSYPI FREGVTDANR QTFATNVVNF LKQNNLDGLD
FDWEYPGAPD IPGIPPGGKN DGANYLKFLQ MVRAALPAGK TLSIAAPASF WYLQGFHPLD
QFAKTLDYII YMTYDLHGQW DYGNKWASPG CPAGNCLRSH VNSTETYDSL VMVTKAGVPS
NKVIVGVSSY GRSFKMAQAG CTGPNCPFTG PNSGAKPGRC TETAGYIADA EIDEILKRNP
SAKMWLDKSS NSNIMVYDNT EWVAYMDGPN KAGRTTYYKG LQMGGVSDWA VDLQQFAPPS
KPLPELAACD ARYLSLEDIE RDKDKIPDHC INIYIVQAQV EALNRARRDF NDILNSGYDH
KFDIYLKYLR LHVIPGFERW VLNNANEYFD CGRPFVRNCC HDCKDNACNF CSKCESGLNS
GPFEQSVNCP NLIPIKGAQP TTAFNVNWHL KDKERFVKDL SEKAGIDESW FHYVDKIVDT
PSKFCTDKPE CHFWWRGYPV LTEPVVIPNP KKAIAEALDN LKAMNEAFDD AVIAAQVFGD
MGEMAEVAMA SELPVFMTEV AIDSMRQIVK FADELQEANR KEFILSFVMS FLFLVPMAGS
VVAGLGLRVL GNVIIAIGET AGLAFTVYGI VQDPESAVGA ILGLLVGIGG LRGNKGSMIS
QAAGLRRGMS TADTAKLGPY VVGRTDMLRG LQRSCGL
//
