ID A0A2T3ZVA5_TRIHA Unreviewed; 820 AA.
AC A0A2T3ZVA5;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
DE Flags: Fragment;
GN ORFNames=M431DRAFT_99322 {ECO:0000313|EMBL:PTB48755.1};
OS Trichoderma harzianum CBS 226.95.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=983964 {ECO:0000313|EMBL:PTB48755.1, ECO:0000313|Proteomes:UP000241690};
RN [1] {ECO:0000313|EMBL:PTB48755.1, ECO:0000313|Proteomes:UP000241690}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 226.95 {ECO:0000313|EMBL:PTB48755.1,
RC ECO:0000313|Proteomes:UP000241690};
RG DOE Joint Genome Institute;
RA Aerts A., Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B.,
RA Kuo A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y., Rahimi M.J.,
RA Shen Q., Grigoriev I.V., Kubicek C.P., Druzhinina I.S.;
RT "Multiple horizontal gene transfer events from other fungi enriched the
RT ability of initially mycotrophic Trichoderma (Ascomycota) to feed on dead
RT plant biomass.";
RL Submitted (JUL-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 -!- 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}.
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DR EMBL; KZ679697; PTB48755.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T3ZVA5; -.
DR STRING; 983964.A0A2T3ZVA5; -.
DR OrthoDB; 11640at2759; -.
DR Proteomes; UP000241690; 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; 1.
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; 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 Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000241690};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..820
FT /note="chitinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015556583"
FT DOMAIN 267..312
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 331..379
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 474..820
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT NON_TER 820
FT /evidence="ECO:0000313|EMBL:PTB48755.1"
SQ SEQUENCE 820 AA; 87574 MW; B4657A4C7D41ED9F CRC64;
MTKLTWAVVV LNLLHCTFGS EFISQLQQCP NDCTNLGPNP SNWTFIHYLE KLNSCNHTVL
FDLSLHNDVA DHSTHTTIRA CTVAVGDDPK TNTIPVAKQA NSTSFSASIL GAQSGKNVQF
NQDEFEGLSG AIQQHVIALD ENAPTIILGK IENLVMGFFA GGSIDSSRSI AAIIHELTSQ
VKAVGLSETT LVQRCGQDLN GNHTVGLVVN TDGNVASVQN TLLTWSNATC VQDLEVIRHS
NITMFSKPTI KSQFSRRGIN SRDGTCSTVQ VVSGDSCGSL ATECGISAQD LATFNPASDL
CSTLAVGQYI CCTSGSLPDL SPKPNPDGSC AQYAVQPNDY CALIASENSI TITDIENWNQ
DTWGWQGCDN VQLGQVICLS TGTPPFPASV SNAICGPQVP GTQPPADFST LTDLNPCPLN
SCCDIYGQCG ITPDFCTISK STTGAPGTSA PGTAGCISNC GTEITNNSEG PSEFIKVGYW
ESFNLDRPCL QMPVSAIPSG YTHIHYAFAT LTEDFLVDVS ADQDAFNDFA AATGFKRILS
FGGWSFSTDV DSFPIFRDSV TSANRLTFAQ SVVDIVNQHN LDGVDFDWEY PGAPDIPGIP
PGSPNDGANY LAFLQTLRNI LPEGKTLSLA APASYWSRIR YLRGFPIADM AQVLDYIVYE
TYDLHGQWDY ANAFSNPGCP TGNCLRSHVN LTETDFALAM ITKAGVPTNK ITVGVTSYGR
SFGMVDPSCT SVDCLFSGPD SSAIPGACTQ TAGYLADAEI YQLIGQGAIQ SRDDASDSDI
VTYQDTWVAY MTPATKASRI SSYQAANFAG SVDWAIDLEA
//
