ID A0A2T3A8Z1_9PEZI Unreviewed; 416 AA.
AC A0A2T3A8Z1;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=BD289DRAFT_367785 {ECO:0000313|EMBL:PSR86968.1};
OS Coniella lustricola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Schizoparmaceae; Coniella.
OX NCBI_TaxID=2025994 {ECO:0000313|EMBL:PSR86968.1, ECO:0000313|Proteomes:UP000241462};
RN [1] {ECO:0000313|EMBL:PSR86968.1, ECO:0000313|Proteomes:UP000241462}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B22-T-1 {ECO:0000313|EMBL:PSR86968.1,
RC ECO:0000313|Proteomes:UP000241462};
RA Raudabaugh D.B., Iturriaga T., Carver A., Mondo S., Pangilinan J.,
RA Lipzen A., He G., Amirebrahimi M., Grigoriev I.V., Miller A.N.;
RT "Coniella lustricola, a new species from submerged detritus.";
RL Mycol. Prog. 17:191-203(2018).
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.
CC {ECO:0000256|RuleBase:RU004453}.
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DR EMBL; KZ678435; PSR86968.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T3A8Z1; -.
DR STRING; 2025994.A0A2T3A8Z1; -.
DR InParanoid; A0A2T3A8Z1; -.
DR Proteomes; UP000241462; 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 Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR035971; CBD_sf.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
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 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:UP000241462};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..416
FT /note="chitinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015538289"
FT DOMAIN 19..330
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT DOMAIN 380..416
FT /note="CBM1"
FT /evidence="ECO:0000259|PROSITE:PS51164"
FT REGION 351..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 416 AA; 43724 MW; 3CBDD262CB050BC1 CRC64;
MLSTLATLLP LAGLVSAVGQ NVVYWGQNGG GTIENNDLST YCTSTSGIDI LILAFLYEFG
ISTGDIPSGT IGQSCFISSI NGEGQNCDAL AAAIATCQDA GVTIILSIGG ASGSYSLENN
AQAEAIGQYL WDSYGNSGNT TVERPFGDVF VNGFDFDIEL NNGYSQYYPA MIDTLRANFE
TDPGNTYYIT GAPQCPIPEP NMGVIIGNAT FDYLWVQWYN NNNYSVDPCA LPFNGNAPFN
YDDWVAYTAT TPSANAEIFI GVPAAPLAAN GGPSGETYYI TPDQLAELVD EYDDATRFGG
VMMWSAGFSD SNVNNGCTYA QEAHAILEYG SPCVNGPSSV SIGTATATST ATRTTLTTST
TKPVTTSATT TTTSTAATGT PLPQWSQCGG EGYTGSTNCA SPYSCVCLSV WWCQCD
//