ID A7E5V2_SCLS1 Unreviewed; 485 AA.
AC A7E5V2;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=SS1G_00677 {ECO:0000313|EMBL:EDN91274.1};
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:EDN91274.1, 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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class V subfamily. {ECO:0000256|ARBA:ARBA00008682}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00261}.
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DR EMBL; CH476621; EDN91274.1; -; Genomic_DNA.
DR RefSeq; XP_001598588.1; XM_001598538.1.
DR AlphaFoldDB; A7E5V2; -.
DR STRING; 665079.A7E5V2; -.
DR EnsemblFungi; EDN91274; EDN91274; SS1G_00677.
DR GeneID; 5494897; -.
DR KEGG; ssl:SS1G_00677; -.
DR eggNOG; KOG2806; Eukaryota.
DR HOGENOM; CLU_002833_2_0_1; -.
DR InParanoid; A7E5V2; -.
DR OMA; WTQNRAP; -.
DR OrthoDB; 671410at2759; -.
DR Proteomes; UP000001312; Unassembled WGS sequence.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-UniRule.
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; 3.10.50.10; -; 1.
DR Gene3D; 3.30.60.10; Endochitinase-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001002; Chitin-bd_1.
DR InterPro; IPR018371; Chitin-binding_1_CS.
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; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR11177; CHITINASE; 1.
DR PANTHER; PTHR11177:SF333; CHITINASE; 1.
DR Pfam; PF00187; Chitin_bind_1; 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 SUPFAM; SSF57016; Plant lectins/antimicrobial peptides; 1.
DR PROSITE; PS00026; CHIT_BIND_I_1; 1.
DR PROSITE; PS50941; CHIT_BIND_I_2; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 3: Inferred from homology;
KW Chitin-binding {ECO:0000256|ARBA:ARBA00022669, ECO:0000256|PROSITE-
KW ProRule:PRU00261};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00261}; Reference proteome {ECO:0000313|Proteomes:UP000001312}.
FT DOMAIN 34..88
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DOMAIN 104..458
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 454..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..485
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 48..60
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 53..67
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
SQ SEQUENCE 485 AA; 52167 MW; E778C3086B532906 CRC64;
MLLWVSFLIG KCDFESANCT KTSTSNHFPY RRDVPQCGRN APQGNQICPL NTCCSGNGYC
GTTSAYCINA DPVNGNTPCQ TGYGACGVIN YPNCGSGSTT ATNGRKVAYW QINSATRSCN
ALPIPLINTQ GLTHLIFAFM SISPNTFHVV PFDTTAVPLM HPFTLLASTT LATYMAIGGG
GSSGLSQVWS QMVKSVGSRA VFIGSVEGWL SSFGFQGVDL DWEFPGSLDD RDGFVALVRE
MRESFNENFP EKNWGISVVL PPDISALQFF DPINLEPYTT FFNFMSYDLH GPWESTNPSL
GAYIRPQTSL LDINSVLSPL WFAGVDPSKL NLGLAAYGRG YTLSNPGCHE QGCAYTGPSI
PGPCTTQMGI LSMREIEVLV LREGLGVSWV GGEAAGQEGD EAVKQIVFGG GRQWMGFDDF
ETWGLKRKFA DGLCMGGTVV WSLDLQGVGT GDGNFGPGVL RSGGMDGDSE EENEKQNKKG
HKTEA
//
