ID Q8NJT8_9HYPO Unreviewed; 423 AA.
AC Q8NJT8;
DT 01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2002, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
OS Stachybotrys elegans.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Stachybotryaceae; Stachybotrys.
OX NCBI_TaxID=80388 {ECO:0000313|EMBL:AAM70478.1};
RN [1] {ECO:0000313|EMBL:AAM70478.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12892640; DOI=10.1016/S1087-1845(03)00050-1;
RA Morissette D.C., Driscoll B.T., Jabaji-Hare S.;
RT "Molecular cloning, characterization, and expression of a cDNA encoding an
RT endochitinase gene from the mycoparasite Stachybotrys elegans.";
RL Fungal Genet. Biol. 39:276-285(2003).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF516397; AAM70478.1; -; mRNA.
DR AlphaFoldDB; Q8NJT8; -.
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:SF317; CHITINASE 11; 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..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..423
FT /note="chitinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004311843"
FT DOMAIN 37..400
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
SQ SEQUENCE 423 AA; 46189 MW; EA2B98D2BD06040B CRC64;
MLPFIAKSLT ALVSLQASLG FASPVSNKEV GKRADGYLNS VYFTNWGIYG RNFQPADLPV
SEISHVIYSF LNLRQDGTVF SGDTYADIEK HYPTDSWNDV GNNVYGCVKQ LYLLKKANRN
LKIMLSIGGW TWSTNFPAAA STAAGRSNFA RSSVAFMKDW GFDGIDVDWE YPANEAEASN
MILLLQAVRD ELDRYAAQYA PGHHSQLSIA APAGPSNYEK LHLRELGQVL DHINLMAYDY
AGSWDARSGH QANLFANPSN PGATPYNTEQ AIRAYIAGGV PASKLVLGMP IYGRAFQATS
GIGQPFTGIG QGSWEAGIWD YKDLPKAGAT VQCDNVAQGC YTYDASTREL ISFDTPDMIR
TKVTYLKSRG LGGSMFWEAS ADKRGADSLI STSINSLGAL DTTQNWLSYP NSQYDNMRAG
IPS
//
