ID A0A0F9ZRG2_TRIHA Unreviewed; 1500 AA.
AC A0A0F9ZRG2;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, 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=THAR02_05014 {ECO:0000313|EMBL:KKP02892.1};
OS Trichoderma harzianum (Hypocrea lixii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=5544 {ECO:0000313|EMBL:KKP02892.1, ECO:0000313|Proteomes:UP000034112};
RN [1] {ECO:0000313|Proteomes:UP000034112}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T6776 {ECO:0000313|Proteomes:UP000034112};
RX PubMed=26067977; DOI=10.1128/genomeA.00647-15;
RA Baroncelli R., Piaggeschi G., Fiorini L., Bertolini E., Zapparata A.,
RA Pe M.E., Sarrocco S., Vannacci G.;
RT "Draft whole-genome sequence of the biocontrol agent Trichoderma harzianum
RT T6776.";
RL Genome Announc. 3:E0064715-E0064715(2015).
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00261}.
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:KKP02892.1}.
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DR EMBL; JOKZ01000132; KKP02892.1; -; Genomic_DNA.
DR OMA; SFGPDWA; -.
DR OrthoDB; 11640at2759; -.
DR Proteomes; UP000034112; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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 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; IPR001002; Chitin-bd_1.
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; PS50941; CHIT_BIND_I_2; 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, ECO:0000256|PROSITE-
KW ProRule:PRU00261}; Disulfide bond {ECO:0000256|PROSITE-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:UP000034112};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 319..364
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 383..432
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 445..513
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DOMAIN 524..891
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT DISULFID 470..482
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 475..489
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 507..511
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
SQ SEQUENCE 1500 AA; 158738 MW; 79749D3C6223CA5E CRC64;
MPLSNSSAWP RPRDTFLAFL YMALASLSFF VGTSSAITTP LRLPASPGYQ GRSSACPARC
AVTGPNPANW SLYRNFNQFA LCQESIFYSF SFLDPVDDAD EAHRIYACTS FGPDWANLPA
NTSSLSSQSA KAPVLVNGTY EIGSWPSAPG SIVSTSLATI TTQIRHYLSN GFGATDHPTI
LFASFGSTSV GLYIGQGLQN RGIGNIALAY LENSIATSSA SHSAQVAMQF CQPGQTSHHI
FGLIATGNGT FAAVQDALKS WSKAECLTFP VVQNATGTIP LVTPLFTPST NITSNNSSLT
HGNAASVGHR ALTPRANCTT IQVVYGDGCG SLAQRCGITS AQFTQYNPAS NECSSLQPGE
HVCCSAGTLP NYAPPPQADG TCATYTIQPN DDCSTIAATY SLTVTELGNF NNNTWAWGGC
NRPLFPNNII CLSKGNPPMP APVSNALCGP QVPGTPTPPS GTNISTLNPC PLNACCDVWG
QCGTTADFCT NTGTGAPGTA AKGTNGCISN CGTNIVLSSP PATFRSIGFY EGFNLQRSCL
FQDVSQINVD AYTHIYFAFG VLTPSYVVQI PNDTTLYEFN EFKRIVGAKR ILSIGGWDFS
TNPSTYNIFR EGVTAANRLT MATNIANFIN DNDLDGVNID WEYPGAPDIP GIPPASTSDG
TNYLAFLAIL RNLLPSKEIT IAAPASYWYL QGFPIEKMAP LLDYIIYMTY DLHGQWDSQN
AWSQLGCPTG NCLRTDVNLT ETIGALVMIT KAGVPSNKVV VGTTSYGRSF AMAEVGCYGP
DCTFLGSADD SQAAPGICTQ TAGYISNAEI QEILANSSRV NQNFIDPTSN TNILVYDDIQ
WVGWMSNGIK ASRASLYKGL AMGGTTDWAT DLQEYNDPPY TVSNWGILIS DVLLGTDPSE
EGTRHGNWTK LNCSDPAVQG ALFMGCSQRW SQLDCNDAWS DAIAVWNQYD YNRTNFSLSV
MNTFHGSEEI DCGRISPSNC QQTQTCDYIQ GIGDNGGSGV AGYMVYNSFV IINEIYSQFY
NAINYASANY IGNALTDFEN TFAPVPPEED DEWKLILTNL AGLGLTAIAA PFFDGVFGAL
PALAALGEAA ADTVKDVTYA TLAFGAAIIT ITLDGGGETP WSPQSQSLFS DTMGKALGAW
ATIVENQLAA LFNGSEASIA LLGTLIGNGN LIECDGSSPL QNDPSDDSTY QGLENYVTRA
FYGFAIPALW TVSGAAAFVV DSGYPCGTVN PLGLYMSNDT AEATYSCYNG NLYYLVSAAG
DYHGCTGEDI ALTVDTVDPP PPPCTDSLFT APTGLDSLGS KWGGITVSDL IAGSVRTYVA
NGNTNGAPAA NPADSQTLQD LANQDITTPG YITLPVCSPQ VAWASWTNPS QSNATAPGYP
CNPLQGVTKC SSYTYVDQTS SASPTVSDCQ TIIKNIQGTS GSWNTGIGSQ RDIASFGSCH
FGVDNSGVTG DVTYQTGSQD IVNIITQSIA LYGGGGQVGA KGYMECAGDA GSQYVEWGLY
//
