ID V2XAS2_MONRO Unreviewed; 441 AA.
AC V2XAS2;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Glycoside hydrolase family 18 protein {ECO:0000313|EMBL:ESK96283.1};
GN ORFNames=Moror_7069 {ECO:0000313|EMBL:ESK96283.1};
OS Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS (Crinipellis roreri).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK96283.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK96283.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK96283.1,
RC ECO:0000313|Proteomes:UP000017559};
RX PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT mechanisms of the biotrophic and necrotrophic phases.";
RL BMC Genomics 15:164-164(2014).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ESK96283.1}.
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DR EMBL; AWSO01000050; ESK96283.1; -; Genomic_DNA.
DR RefSeq; XP_007844323.1; XM_007846132.1.
DR AlphaFoldDB; V2XAS2; -.
DR STRING; 1381753.V2XAS2; -.
DR KEGG; mrr:Moror_7069; -.
DR HOGENOM; CLU_002833_6_1_1; -.
DR OrthoDB; 3203764at2759; -.
DR Proteomes; UP000017559; 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 Gene3D; 3.20.20.80; Glycosidases; 2.
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:SF406; GH18 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF54556; Chitinase insertion domain; 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:UP000017559};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..441
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004711692"
FT DOMAIN 52..435
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
SQ SEQUENCE 441 AA; 46656 MW; C0D95A549B511314 CRC64;
MYFHLAAIFL TFLLTTVLSA PTCGLAPPPK DTNVSSTSSS TTGCSNLAAA DALLTGWYPG
WLGNQSPPQN ISWSKYTALT FAFGVTTPNG GVSLDDISTQ VLPEFVASAK EHNVQALLSI
GGWTGSRYFS SAVATQESRT AFVKTIVDLV NQYDLDGIDF DWEYPNKQGI GCNQQSPDDA
ANFLSFLEQL RSDPVGSKLT LSAAVGIAPF VGSDGVPMTD VSGFAKVLDH IGIMNYDVWG
SWSPSVGPNA PLDDTCAPTK AGSAVSAVKA WTDAGFPADQ IALGVAAYGH SFHVAQTAAL
NAQSNTLQLY PAFDKALQPH GDSQDGEAGV DQCGNPVPVG GIFNFWGLVD GGFLNQDGTA
DTQAGIVYRY DNCSQTPYVY NPTNQVMVSY DDATSFAVKG KWINENGLKG FAMWHVLGDF
DDILLDAISE AMGVDVEPCS A
//
