ID E5ACE4_LEPMJ Unreviewed; 679 AA.
AC E5ACE4;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 28-JUN-2023, entry version 57.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=LEMA_P009330.1 {ECO:0000313|EMBL:CBY02146.1};
OS Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS (Blackleg fungus) (Phoma lingam).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC Plenodomus; Plenodomus lingam/Leptosphaeria maculans species complex.
OX NCBI_TaxID=985895 {ECO:0000313|EMBL:CBY02146.1, ECO:0000313|Proteomes:UP000002668};
RN [1] {ECO:0000313|Proteomes:UP000002668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8
RC {ECO:0000313|Proteomes:UP000002668};
RX PubMed=21326234; DOI=10.1038/ncomms1189;
RA Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT "Effector diversification within compartments of the Leptosphaeria maculans
RT genome affected by Repeat-Induced Point mutations.";
RL Nat. Commun. 2:202-202(2011).
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DR EMBL; FP929139; CBY02146.1; -; Genomic_DNA.
DR RefSeq; XP_003845625.1; XM_003845577.1.
DR AlphaFoldDB; E5ACE4; -.
DR STRING; 985895.E5ACE4; -.
DR CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR EnsemblFungi; CBY02146; CBY02146; LEMA_P009330.1.
DR GeneID; 13286785; -.
DR eggNOG; KOG2806; Eukaryota.
DR HOGENOM; CLU_404927_0_0_1; -.
DR InParanoid; E5ACE4; -.
DR OMA; MAYYAKW; -.
DR OrthoDB; 1449869at2759; -.
DR Proteomes; UP000002668; Genome.
DR GO; GO:0008061; F:chitin binding; IEA:InterPro.
DR GO; GO:0004568; F:chitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd00035; ChtBD1; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 2.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR11177; CHITINASE; 1.
DR PANTHER; PTHR11177:SF337; CHITINASE; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000002668};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..679
FT /note="chitinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003194956"
FT DOMAIN 20..424
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 420..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 654..679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..479
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..508
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 679 AA; 73006 MW; 0243B83E55F5CFD5 CRC64;
MRFSSVEFLA SSFLAASASA RFVMYADEWH PTRPTTPADR AGIDHVVLAF AMANATAQFQ
PKVPITTIRS EYPNAKVMIA VGGWGDDIGF AEASRSDATI AKFAADIATM LTNTGADGVD
IDWEYPGGNG ADYKQVPNSE KVYQIEAYPK TLAAVRTAIG DKLLSIAVPG KKGDMIGFTQ
ETGPKIWPSV DYINVMSYDL ANRRDTVTKH HSSVAGSEDT IKNYLAIGAP PAKINLGFAY
YAKYFTTQGD CTANPLGCPI MAAEDQVTGK DLLTSGAWTF EPSHMKPVDS SALPISYDGT
CGPDKGTKCA SGCCSQYGNC GTSPEHCSGA CWHAFGVGCT DSDVAGSWQL AAKNGVTDET
EGGQYYFDNT NNLFWTWDTP KLITRKFEDI VKKYKLGGVM AWSLGEDSYD WSHIRQMASQ
LQGTSPGGDS PTPEEDQPMQ PTEPMLPAAE FDEASGQYNP VPDTQQRRPR PSHRPQPSLS
ASPYDIVFVD GTENGPSDQP SNEPGSPPDF SVDYNDGQRI QPPSNDEVDS FVAPAEPSIY
DLPNADPEDV NTVPDQPYIE PLDSNAPPAK LPLDIVAPVP IPAPVPTPLT QPFEPDFVPD
PGYINPNWHP EAQAQSAPVV ADARVAAKAA ASLAALPIEG EVSTDMEDAA IWAKPMTNSR
PESVACGARR RRKAKRGSQ
//
