ID M2T8Y9_COCSN Unreviewed; 930 AA.
AC M2T8Y9;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=COCSADRAFT_198637 {ECO:0000313|EMBL:EMD65716.1};
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:EMD65716.1, ECO:0000313|Proteomes:UP000016934};
RN [1] {ECO:0000313|EMBL:EMD65716.1, 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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004609};
CC Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}. Membrane
CC {ECO:0000256|ARBA:ARBA00004589}; Lipid-anchor, GPI-anchor
CC {ECO:0000256|ARBA:ARBA00004589}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class III subfamily. {ECO:0000256|ARBA:ARBA00025727}.
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DR EMBL; KB445641; EMD65716.1; -; Genomic_DNA.
DR RefSeq; XP_007698786.1; XM_007700596.1.
DR AlphaFoldDB; M2T8Y9; -.
DR STRING; 665912.M2T8Y9; -.
DR GeneID; 19134066; -.
DR KEGG; bsc:COCSADRAFT_198637; -.
DR eggNOG; KOG4701; Eukaryota.
DR HOGENOM; CLU_009107_0_0_1; -.
DR OMA; NGPYIAM; -.
DR OrthoDB; 360175at2759; -.
DR Proteomes; UP000016934; Unassembled WGS sequence.
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; 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:SF47; ENDOCHITINASE A; 1.
DR Pfam; PF00704; Glyco_hydro_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 Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Chitin degradation {ECO:0000256|ARBA:ARBA00023024};
KW Chitin-binding {ECO:0000256|ARBA:ARBA00022669};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00022622};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000489};
KW GPI-anchor {ECO:0000256|ARBA:ARBA00022622};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000489};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000016934};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..930
FT /note="chitinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004025727"
FT DOMAIN 30..350
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 365..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 480..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 534..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 608..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..649
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 930 AA; 95572 MW; 6944DB08AA2B6AF3 CRC64;
MVASIFSRVA FATGLLASTA SAAYDASAKS NVAVYWGQGS NQMTLLEVCL DPNVDIVNIG
FVNKFPKKRG EYPGTNHANA CGDATYTDPT TNQPSKLLSS CPGVGEAINA CKRRGKKVML
SLGGGWPTDY YLPTPDVANW FAEFLLGAYG PPTAEWKAAG KPRPFGDAYV DGFDLDLEAA
EWDVPSADML YANYDVFGKY IKAHSKMLLS GAPQCVVPDA RIFLALKEVP FDFLFTQFYN
TWTCSAAKAV QDMKNNAEST FTFNTWISWL KNNSKNPDIK LYLGLAAGED GLPTHKDHYL
APEDANMLVQ SLQGDSMFGG IMLWEATVSK NNPTYDQSYG TWMKYAVQGT FKDKYHPVVS
SSSVVSSTIT PSSTPASSIS ASSTPASSTP ASSIPASSIP ASSIPASSVP ASSVPASSTP
ASSTPASSTP ISSVSASSYP ASSVSASSTP GSSISASSIP VSSTPISSVS ASSIPASSYP
ASSVSASSTP GSSISASSIP VSSTPISSVS ASSIPASSIP ASNSVTMVSS SSIEISSSTP
VGPSSVPTVS APESIGSSVV VPSGSETSTS CSTSNGAYPT GVNSSYGVYP TESAVYPIET
YSASKGAEYP AESSKGYGEY PAASSTGYDS TPSVTKKPEQ SEYPTVPTGS TTSVVTTTYV
DVCPTGLTTV TATYVATVCT KCAKPTGTAD VPEGWTTSVY TASTLTVTIT KPVATVTAVP
EYPSSAPSVV YPAEYSATPI SSGKPAYPAV PEASKVAYPT IPEVSKAAYP AVPEVSKAAY
PAVPEVSKVA EYPVAPASSA APEYPAHSMP SVPSAAQPAS SPAAEYPSYP VGTGYPKKPV
EHEVVSSMHV TLSKVAVSTY IPAPYPSAGV PYIPAGPAKN ATSVYVPMPT GTGKPVTPLP
SMPPQFEGVA SRASVGFMMF VGAVGAVFAM
//
