ID A7F134_SCLS1 Unreviewed; 393 AA.
AC A7F134;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=SS1G_11304 {ECO:0000313|EMBL:EDN95426.1};
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079 {ECO:0000313|EMBL:EDN95426.1, ECO:0000313|Proteomes:UP000001312};
RN [1] {ECO:0000313|Proteomes:UP000001312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1 {ECO:0000313|Proteomes:UP000001312};
RX PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
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. Chitinase
CC class V subfamily. {ECO:0000256|ARBA:ARBA00008682}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH476637; EDN95426.1; -; Genomic_DNA.
DR RefSeq; XP_001588061.1; XM_001588011.1.
DR AlphaFoldDB; A7F134; -.
DR STRING; 665079.A7F134; -.
DR EnsemblFungi; EDN95426; EDN95426; SS1G_11304.
DR GeneID; 5484074; -.
DR KEGG; ssl:SS1G_11304; -.
DR VEuPathDB; FungiDB:sscle_12g086860; -.
DR eggNOG; KOG2806; Eukaryota.
DR HOGENOM; CLU_002833_1_0_1; -.
DR InParanoid; A7F134; -.
DR OMA; SYPESKY; -.
DR OrthoDB; 3203764at2759; -.
DR Proteomes; UP000001312; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0008061; F:chitin binding; IBA:GO_Central.
DR GO; GO:0004568; F:chitinase activity; IBA:GO_Central.
DR GO; GO:0006032; P:chitin catabolic process; IBA:GO_Central.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd06548; GH18_chitinase; 1.
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:SF365; ENDOCHITINASE B; 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:UP000001312}.
FT DOMAIN 7..372
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
SQ SEQUENCE 393 AA; 44484 MW; BB0E7B288024822A CRC64;
MGGGDGYRAV AYFVNWAIYG RKHFPQELPA EKLTHVLYAF ANVRPESGEV YMTDGWADTD
IHFEGDSWND VGTNLYGCLK QLNILKSRNR SLKILLSIGG WTYSSNFAQP ASTESGRRRF
AESAVDLIRN LGFDGIDIDW EYPKNTDEAR DYVLLLRECR EAMDRYSSTL SNFHHFELTV
ACPAGPQNYN NMDVRSMNEY IDFWNLMAYD YAGSWDSVAG HQANLHPSES NPDSTPFNTE
HAVRAYEARG VQGHKIVLGM PIYGRAFQGT EGLGKPFNGV GEGTWENGVH DFKKLPQEGA
EEIVDEETCA SYSYNEDTKT LITYDTVEIA RRKAYYIKER GLGGAMWWES SADHPEREKS
LIHNVVDVLG ILEGSDNCLE YPESKYDNLR NGF
//
