ID   Q8TFB3_HYPVI            Unreviewed;       527 AA.
AC   Q8TFB3;
DT   01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2002, sequence version 1.
DT   22-FEB-2023, entry version 93.
DE   RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE            EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN   Name=ech3 {ECO:0000313|EMBL:AAL84698.1};
OS   Hypocrea virens (Gliocladium virens) (Trichoderma virens).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=29875 {ECO:0000313|EMBL:AAL84698.1};
RN   [1] {ECO:0000313|EMBL:AAL84698.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Kim D.-J., Baek J.-M., Uribe P., Kenerley C.M., Cook D.R.;
RL   Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AAL84698.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=11919676; DOI=10.1007/s00294-001-0267-6;
RA   Kim D.J., Baek J.M., Uribe P., Kenerley C.M., Cook D.R.;
RT   "Cloning and characterization of multiple glycosyl hydrolase genes from
RT   Trichoderma virens.";
RL   Curr. Genet. 40:374-384(2002).
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; AF397019; AAL78812.1; -; mRNA.
DR   EMBL; AF395759; AAL84698.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8TFB3; -.
DR   CAZy; GH18; Glycoside Hydrolase Family 18.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008061; F:chitin binding; IEA:InterPro.
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; cd06548; GH18_chitinase; 1.
DR   Gene3D; 3.10.50.10; -; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR011583; Chitinase_II.
DR   InterPro; IPR029070; Chitinase_insertion_sf.
DR   InterPro; IPR001223; Glyco_hydro18_cat.
DR   InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR11177; CHITINASE; 1.
DR   PANTHER; PTHR11177:SF384; CHITINASE; 1.
DR   Pfam; PF00704; Glyco_hydro_18; 1.
DR   SMART; SM00636; Glyco_18; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF54556; Chitinase insertion domain; 1.
DR   PROSITE; PS01095; GH18_1; 1.
DR   PROSITE; PS51910; GH18_2; 1.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Chitin degradation {ECO:0000256|ARBA:ARBA00023024};
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   Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..527
FT                   /note="chitinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007714634"
FT   DOMAIN          142..505
FT                   /note="GH18"
FT                   /evidence="ECO:0000259|PROSITE:PS51910"
FT   REGION          36..136
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        121..136
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   527 AA;  58125 MW;  4F5D78ACE33E0E97 CRC64;
     MLASKPLTMF KLLCVVLAVA ARVAVANPAT LSARCDDPKA HLSSLTEPVP TIPTADLPID
     LPPIELEPIS PEDIEEAGQP VPPSWLTEPS PVPVDSESPV LDSSPTSPQD PKPKLPGLNV
     PTNDDDDDGH SSRKGYSESF RRKNVVYFTD WSIYGAGFLP QNLPADDITH LLYAFAGIAA
     DGSVVVYDPW ADEQKLLGKR NTQGESVHGA VEQVFLLKNK YRHMKTLLSI GGWTASQEGK
     FGPAISSPEG RRRFAETAVR LLADWGFDGL DVDYEYPANP QDAQNFVLLL QECRRALDEY
     AGRNGQNYHY LLTVATPAGP EHYSLLDMRA MDQYVDAWHL MAYDYAGSWD TVSGQQANLY
     PDLENPDSTK FNTDQAVGDY IARGIDPRKI VLGLPLYGRS FTNTDGLGRP YSGIGQGSIE
     PGVWLYRDLP RPGATVYVNS YTVSAYTYDP ATRELVSYDN VETARLKAEY LQSRGLGGAV
     FWEAAGDRTG EESLVRTLAR EMGHLDNSIN MVHYPESRYT NIQNPSW
//