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Database: UniProt
Entry: G0RVZ9_HYPJQ
LinkDB: G0RVZ9_HYPJQ
Original site: G0RVZ9_HYPJQ 
ID   G0RVZ9_HYPJQ            Unreviewed;       411 AA.
AC   G0RVZ9;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE            EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN   Name=chi18-14 {ECO:0000313|EMBL:EGR44650.1};
GN   ORFNames=TRIREDRAFT_124043 {ECO:0000313|EMBL:EGR44650.1};
OS   Hypocrea jecorina (strain QM6a) (Trichoderma reesei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=431241 {ECO:0000313|Proteomes:UP000008984};
RN   [1] {ECO:0000313|EMBL:EGR44650.1, ECO:0000313|Proteomes:UP000008984}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QM6a {ECO:0000313|EMBL:EGR44650.1,
RC   ECO:0000313|Proteomes:UP000008984};
RX   PubMed=18454138; DOI=10.1038/nbt1403;
RA   Martinez D., Berka R.M., Henrissat B., Saloheimo M., Arvas M., Baker S.E.,
RA   Chapman J., Chertkov O., Coutinho P.M., Cullen D., Danchin E.G.,
RA   Grigoriev I.V., Harris P., Jackson M., Kubicek C.P., Han C.S., Ho I.,
RA   Larrondo L.F., de Leon A.L., Magnuson J.K., Merino S., Misra M., Nelson B.,
RA   Putnam N., Robbertse B., Salamov A.A., Schmoll M., Terry A., Thayer N.,
RA   Westerholm-Parvinen A., Schoch C.L., Yao J., Barabote R., Nelson M.A.,
RA   Detter C., Bruce D., Kuske C.R., Xie G., Richardson P., Rokhsar D.S.,
RA   Lucas S.M., Rubin E.M., Dunn-Coleman N., Ward M., Brettin T.S.;
RT   "Genome sequencing and analysis of the biomass-degrading fungus Trichoderma
RT   reesei (syn. Hypocrea jecorina).";
RL   Nat. Biotechnol. 26:553-560(2008).
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 III subfamily. {ECO:0000256|ARBA:ARBA00025727}.
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DR   EMBL; GL985086; EGR44650.1; -; Genomic_DNA.
DR   RefSeq; XP_006969397.1; XM_006969335.1.
DR   AlphaFoldDB; G0RVZ9; -.
DR   STRING; 431241.G0RVZ9; -.
DR   EnsemblFungi; EGR44650; EGR44650; TRIREDRAFT_124043.
DR   GeneID; 18483795; -.
DR   KEGG; tre:TRIREDRAFT_124043; -.
DR   VEuPathDB; FungiDB:TRIREDRAFT_124043; -.
DR   eggNOG; KOG4701; Eukaryota.
DR   HOGENOM; CLU_007818_6_1_1; -.
DR   OrthoDB; 360175at2759; -.
DR   Proteomes; UP000008984; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030248; F:cellulose binding; IEA:InterPro.
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; cd02877; GH18_hevamine_XipI_class_III; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR035971; CBD_sf.
DR   InterPro; IPR000254; Cellulose-bd_dom_fun.
DR   InterPro; IPR045321; Cts1-like.
DR   InterPro; IPR001223; Glyco_hydro18_cat.
DR   InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR45708; ENDOCHITINASE; 1.
DR   PANTHER; PTHR45708:SF49; ENDOCHITINASE; 1.
DR   Pfam; PF00734; CBM_1; 1.
DR   Pfam; PF00704; Glyco_hydro_18; 1.
DR   SMART; SM00236; fCBD; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF57180; Cellulose-binding domain; 1.
DR   PROSITE; PS00562; CBM1_1; 1.
DR   PROSITE; PS51164; CBM1_2; 1.
DR   PROSITE; PS01095; GH18_1; 1.
DR   PROSITE; PS51910; GH18_2; 1.
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   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
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:UP000008984};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..411
FT                   /note="chitinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003409071"
FT   DOMAIN          32..339
FT                   /note="GH18"
FT                   /evidence="ECO:0000259|PROSITE:PS51910"
FT   DOMAIN          375..411
FT                   /note="CBM1"
FT                   /evidence="ECO:0000259|PROSITE:PS51164"
FT   REGION          343..382
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        357..371
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   411 AA;  42561 MW;  40B34A8F2DEE362D CRC64;
     MFFTKAVGGL GLLASLASSA PNPIARRQAP GAQNVVYWGQ NGGGTVENND LSAYCTPTSG
     IDIIVLSFLY QWGQGSSALG GTIGQSCGIT TSGEPQNCDA LTAAITKCKT AGVKIILSLG
     GASAFSSFQT ADQAAQAGQY LWNAYGGGSG VTRPLGNNVM DGFDLDIESN PGTNENYAAL
     VSALRSNFAS DPSRQYVISG APQCPLPEPN MGVIIQNAQF DYLWVQFYNN NEYPGDPCSL
     GLPGDAPFNF NNWTTFIQST PSKDAKVFVG VPAAPLAANG APSGEVYYAT PSQLADIVND
     VKSNPAFGGI MMWSAGFSDT NVNDGCNYAQ EAKNILLTGS PCSSGPVSVS RPPVSSPTIT
     SSPPGTSPAP PSQTGSVPQW GQCGGNGYTG PTQCVAPFKC VATSEWWSQC E
//
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