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Database: UniProt
Entry: M2TFS1_COCSN
LinkDB: M2TFS1_COCSN
Original site: M2TFS1_COCSN 
ID   M2TFS1_COCSN            Unreviewed;       488 AA.
AC   M2TFS1;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   03-MAY-2023, entry version 32.
DE   RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE            EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN   ORFNames=COCSADRAFT_167354 {ECO:0000313|EMBL:EMD68086.1};
OS   Cochliobolus sativus (strain ND90Pr / ATCC 201652) (Common root rot and
OS   spot blotch fungus) (Bipolaris sorokiniana).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX   NCBI_TaxID=665912 {ECO:0000313|EMBL:EMD68086.1, ECO:0000313|Proteomes:UP000016934};
RN   [1] {ECO:0000313|EMBL:EMD68086.1, ECO:0000313|Proteomes:UP000016934}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ND90Pr / ATCC 201652 {ECO:0000313|Proteomes:UP000016934};
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA   Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA   LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA   Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA   Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA   Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT   genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
RN   [2] {ECO:0000313|Proteomes:UP000016934}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ND90Pr / ATCC 201652 {ECO:0000313|Proteomes:UP000016934};
RX   PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA   Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA   Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA   Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA   LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA   Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT   "Comparative genome structure, secondary metabolite, and effector coding
RT   capacity across Cochliobolus pathogens.";
RL   PLoS Genet. 9:E1003233-E1003233(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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family.
CC       {ECO:0000256|RuleBase:RU004453}.
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DR   EMBL; KB445638; EMD68086.1; -; Genomic_DNA.
DR   RefSeq; XP_007695789.1; XM_007697599.1.
DR   AlphaFoldDB; M2TFS1; -.
DR   STRING; 665912.M2TFS1; -.
DR   GeneID; 19132509; -.
DR   KEGG; bsc:COCSADRAFT_167354; -.
DR   eggNOG; KOG2806; Eukaryota.
DR   HOGENOM; CLU_002833_2_2_1; -.
DR   OMA; MDMDWEY; -.
DR   OrthoDB; 671410at2759; -.
DR   Proteomes; UP000016934; Unassembled WGS sequence.
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; cd00598; GH18_chitinase-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR011583; Chitinase_II.
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:SF333; 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:UP000016934}.
FT   DOMAIN          35..317
FT                   /note="GH18"
FT                   /evidence="ECO:0000259|PROSITE:PS51910"
SQ   SEQUENCE   488 AA;  54822 MW;  096728B393EF059C CRC64;
     MLPKCSAARG LPKDVTTTGP LKRPSCSKYG TSVNKRSIGY YETWASTRPC SAVALEQLNL
     QGLTHINFAS MFFEPDTFEL THMDRNAGSL ISRFTKLKER KPGLETWVSV AGKYQQAFSI
     ISNTAANRRK FINNLIKFMQ TYGFDGMDMD WEYPIADDRG GKPEDKANFV LLSRDIYNAF
     EKEGYGYSLT LPASYWYLQH FDLTKLQPYG HWFNLMSSFL RDMSTYVAIT FTSMPRCSRV
     SGILNLQEIF DIINDKKLKL THDKKAGWVS YDDDKTLMQK REFRVSRCLG GMMIWALHQI
     DQDTPIGGSL SPEEMEETEA IYQDAAAKGV CYTSMYDDKC RNGDYEAAQM REQPGFLSTM
     SRCSKHQVRC FCCSKGATMG TCKWRGFRGL GLSCTGGCHG DETEVTINTN YVEKNEDQTC
     IGGTKSYCCS GFKPPISREQ VSEKIKDEAA DLALAAAETL AMGIAAKAFC RVAIMAETLP
     LRIIPFVG
//
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