ID A7E9Z8_SCLS1 Unreviewed; 1677 AA.
AC A7E9Z8;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=SS1G_02128 {ECO:0000313|EMBL:EDN99276.1};
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:EDN99276.1, 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}.
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DR EMBL; CH476623; EDN99276.1; -; Genomic_DNA.
DR RefSeq; XP_001595914.1; XM_001595864.1.
DR EnsemblFungi; EDN99276; EDN99276; SS1G_02128.
DR GeneID; 5492994; -.
DR KEGG; ssl:SS1G_02128; -.
DR eggNOG; KOG2806; Eukaryota.
DR HOGENOM; CLU_241609_0_0_1; -.
DR InParanoid; A7E9Z8; -.
DR OrthoDB; 1771043at2759; -.
DR Proteomes; UP000001312; 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; cd00035; ChtBD1; 1.
DR CDD; cd02878; GH18_zymocin_alpha; 1.
DR CDD; cd00118; LysM; 1.
DR Gene3D; 3.10.50.10; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 3.10.350.10; LysM domain; 1.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR029070; Chitinase_insertion_sf.
DR InterPro; IPR036861; Endochitinase-like_sf.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR PANTHER; PTHR47700:SF2; CHITINASE; 1.
DR PANTHER; PTHR47700; V CHITINASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G13720)-RELATED; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00636; Glyco_18; 1.
DR SMART; SM00257; LysM; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF54556; Chitinase insertion domain; 1.
DR SUPFAM; SSF57016; Plant lectins/antimicrobial peptides; 1.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
DR PROSITE; PS51782; LYSM; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Chitin degradation {ECO:0000256|ARBA:ARBA00023024};
KW Chitin-binding {ECO:0000256|ARBA:ARBA00022669};
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 832..880
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 974..1354
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1677 AA; 183058 MW; D551D46CB375DD61 CRC64;
MSSVAGAAAL SHKEKREQKR AKVRLEKRNK PILLSPGCGG IHWNEPVEKH TITEGILVIV
QFKLLHGLTV HDTSSPAGKL WLATLEYIST IHGCAIRYWG TETTQGQESI FLLVQSENAK
QWVSEKVLKN WRKWEIRWRH EGIEVFGNWL EDDAAQYMAE LADLIPAAVK GQHKVFLVLA
WNRDEESEIV QNDATVLEAE FKEEMMTDGV KEFMMNEFLI PKSIQINIKT EKNDSFPDAK
PQYTADSLAS LLRLSPPRRH SETPVGNSPY FSFCTDTTHI ESIYDAAVGK RQFPGPRGFF
MKMGTFHKNE YINPESNRSI RLQRPPKMDF LWLKFEPGRL DTGKSISESL VELRKSIKED
VGYRASLYWG RSLDDSDEWV LMIEWYKKKD RLQENLESVD IASTSQTVQN HLRDFEFYNS
YEEGIMGMEC SWVSLLRDDP PDPASVPVKQ AGINLHYFFH NYPSSSPVLN NEVAEAQTPN
RSYFTAITMW RSKDAMREWY TDSASQCEDY ERLGHRLDQL RIFCENLEVV DSKVFDMVGD
CYEISKPPMP KYFVSDQGRS TEIISGYPTP ISDLPRGDNF LEIESFALNR CPASCSEAGN
NPANWTAYHD TRRLAVCNET MLLDFTIYNS LNDSNTQTTI YACKTNSTQS ERSSLSRRDT
ACPLSNNSKN AKVSLELGWS GASSQNNTSD VVSAAEQLKT YVTLKEDNCG ETSAFAYAGT
VAIGIYVGSR IQDASSILED FIVEVTKNGV FDTIFVQHCA GNGLNSNYAF GIVARMDGSL
ADVQGTVKTW RDSGCITSST LCSTLAVGQH VCCSDGNLPD YSPQPNANGT CATYTVVTND
SCSQLAALNS ITVDDIESFN RQTWGWMGCA DLQAGYNICL STGNPPMPAT VANAICGPQV
PGTIQSTSGL NFSLYNQCNM NACCDVWGQC GTTAEFCTET QSPTRAPGTA AAGTNGCISN
CGTEIVVGNP PAEFKKVGYW EGYNFDRPCL NKPITSINTT AGYTHVHLAF ATITTDFEVD
VSSIQEAFSD FLSMSGLGFK RILSFGGWDF STDVATYQIF RDAMAPANSK KFAANVAAFV
KKYDLDGVDF DWEYPGEPDI PGIPAGSLDD GVNYVRFFDE LAAVLPAGTT QSVTAPTSYW
YLAPFLILEL SLIVDYVIYM TYDLHGQWDY GSAFSDASCP AGNCLRSGAN LTETLESLSM
ITKAGVASNK VIVGVTSYGR SFQMATPGCY LDSCTYTGPT SGAYAGACTQ TPANAEIDSI
ISGNATVLGT DGSSVRVTGT PFVYLDDSYS NIVVYNDDQW ISYMNDANKI VRTALYKHYN
FGGTADWAVD LQSYDGDNGS GSDGSSIVYV DQSIWTDGPS STGVGGSDGT IGTSGASDNL
SLTCEPPCII VLPPFPLGTT TIFQVASPNQ QRPRPDMEVV NVESSDANHP ADCLAVMVDV
ESLGVVVAAV HLDVRGTAPL VYVEVLAVLE EHVDLLDPTT IIIMITECEE TVACTAEDTR
TTTTATTGYP VTTASMTGFY DSDPTSINTN YDAIASSIIQ AGLKYYGFLK STATMATASP
TATVVTITSN IVATPTPEAI VPQAVCLLVA DVLWYSVQII TNGFETDLGA AIKKQEGGCG
DLLSWEASDV SIPEGFATWT GTREYSFTLP LTIKAGCVER AIASAGGPSG LSCDNVL
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