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Database: UniProt
Entry: M7SBM0_EUTLA
LinkDB: M7SBM0_EUTLA
Original site: M7SBM0_EUTLA 
ID   M7SBM0_EUTLA            Unreviewed;       374 AA.
AC   M7SBM0;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE            EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN   ORFNames=UCREL1_9471 {ECO:0000313|EMBL:EMR63579.1};
OS   Eutypa lata (strain UCR-EL1) (Grapevine dieback disease fungus) (Eutypa
OS   armeniacae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Diatrypaceae; Eutypa.
OX   NCBI_TaxID=1287681 {ECO:0000313|EMBL:EMR63579.1, ECO:0000313|Proteomes:UP000012174};
RN   [1] {ECO:0000313|Proteomes:UP000012174}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCR-EL1 {ECO:0000313|Proteomes:UP000012174};
RX   PubMed=23723393; DOI=10.1128/genomeA.00228-13;
RA   Blanco-Ulate B., Rolshausen P.E., Cantu D.;
RT   "Draft genome sequence of the grapevine dieback fungus Eutypa lata UCR-
RT   EL1.";
RL   Genome Announc. 1:E0022813-E0022813(2013).
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; KB707201; EMR63579.1; -; Genomic_DNA.
DR   RefSeq; XP_007797322.1; XM_007799131.1.
DR   AlphaFoldDB; M7SBM0; -.
DR   STRING; 1287681.M7SBM0; -.
DR   KEGG; ela:UCREL1_9471; -.
DR   eggNOG; KOG2806; Eukaryota.
DR   HOGENOM; CLU_002833_1_2_1; -.
DR   OMA; KSCQRGV; -.
DR   OrthoDB; 3203764at2759; -.
DR   Proteomes; UP000012174; Unassembled WGS sequence.
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   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:SF228; CHITINASE; 1.
DR   Pfam; PF00704; Glyco_hydro_18; 1.
DR   SMART; SM00636; Glyco_18; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 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   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:UP000012174}.
FT   DOMAIN          7..374
FT                   /note="GH18"
FT                   /evidence="ECO:0000259|PROSITE:PS51910"
SQ   SEQUENCE   374 AA;  41194 MW;  DFD86F019EA3CABF CRC64;
     MSETRDFING AYYPSWRVYR QLPPSALQFD CLNRVYYAFV LANEDGTLRF LDEYADCQIS
     ADGTTGCLSA LSSNVKQQQQ RQLQQLEQQR APNNSSLTTT KALVSIGGGS GSKEFPALAA
     HSSSRLRFAR ACRELVDRFG LDGVDVDWEH PQSDVDGKNY VALLEAVRAE LPAPRYELTT
     ALPVGEYVLQ HIDLARAAGS LDYLNLMCYD FNGPWTKVCG HQSKLFPLAS SSNQRDIHPE
     LRRSGKGAVE YVIARGFPAR KIVLGIPAYA RTFGGARGPG QPFQSSSEID YVDLPREWVH
     GAKIDQSVGA AFYVDPCQDQ GGKGFVTFDV PETVRHKAEY VKSQGLGGLF YWTGVGDIKG
     PESLVRAGYE ALNT
//
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