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Database: UniProt
Entry: F9WYS0_ZYMTI
LinkDB: F9WYS0_ZYMTI
Original site: F9WYS0_ZYMTI 
ID   F9WYS0_ZYMTI            Unreviewed;       441 AA.
AC   F9WYS0;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=Glycosidase {ECO:0000256|PIRNR:PIRNR037299};
DE            EC=3.2.-.- {ECO:0000256|PIRNR:PIRNR037299};
GN   ORFNames=MYCGRDRAFT_102047 {ECO:0000313|EMBL:EGP92697.1};
OS   Zymoseptoria tritici (strain CBS 115943 / IPO323) (Speckled leaf blotch
OS   fungus) (Septoria tritici).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX   NCBI_TaxID=336722 {ECO:0000313|EMBL:EGP92697.1, ECO:0000313|Proteomes:UP000008062};
RN   [1] {ECO:0000313|EMBL:EGP92697.1, ECO:0000313|Proteomes:UP000008062}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 115943 / IPO323 {ECO:0000313|Proteomes:UP000008062};
RX   PubMed=21695235; DOI=10.1371/journal.pgen.1002070;
RA   Goodwin S.B., Ben M'barek S., Dhillon B., Wittenberg A.H.J., Crane C.F.,
RA   Hane J.K., Foster A.J., Van der Lee T.A.J., Grimwood J., Aerts A.,
RA   Antoniw J., Bailey A., Bluhm B., Bowler J., Bristow J., van der Burgt A.,
RA   Canto-Canche B., Churchill A.C.L., Conde-Ferraez L., Cools H.J.,
RA   Coutinho P.M., Csukai M., Dehal P., De Wit P., Donzelli B.,
RA   van de Geest H.C., van Ham R.C.H.J., Hammond-Kosack K.E., Henrissat B.,
RA   Kilian A., Kobayashi A.K., Koopmann E., Kourmpetis Y., Kuzniar A.,
RA   Lindquist E., Lombard V., Maliepaard C., Martins N., Mehrabi R.,
RA   Nap J.P.H., Ponomarenko A., Rudd J.J., Salamov A., Schmutz J.,
RA   Schouten H.J., Shapiro H., Stergiopoulos I., Torriani S.F.F., Tu H.,
RA   de Vries R.P., Waalwijk C., Ware S.B., Wiebenga A., Zwiers L.-H.,
RA   Oliver R.P., Grigoriev I.V., Kema G.H.J.;
RT   "Finished genome of the fungal wheat pathogen Mycosphaerella graminicola
RT   reveals dispensome structure, chromosome plasticity, and stealth
RT   pathogenesis.";
RL   PLoS Genet. 7:E1002070-E1002070(2011).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family.
CC       {ECO:0000256|PIRNR:PIRNR037299}.
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DR   EMBL; CM001196; EGP92697.1; -; Genomic_DNA.
DR   RefSeq; XP_003857721.1; XM_003857673.1.
DR   AlphaFoldDB; F9WYS0; -.
DR   STRING; 336722.F9WYS0; -.
DR   EnsemblFungi; Mycgr3T102047; Mycgr3P102047; Mycgr3G102047.
DR   GeneID; 13403292; -.
DR   KEGG; ztr:MYCGRDRAFT_102047; -.
DR   VEuPathDB; FungiDB:ZTRI_1.206; -.
DR   eggNOG; ENOG502QVQI; Eukaryota.
DR   HOGENOM; CLU_040459_0_0_1; -.
DR   InParanoid; F9WYS0; -.
DR   OMA; WNATANQ; -.
DR   OrthoDB; 337487at2759; -.
DR   Proteomes; UP000008062; Chromosome 1.
DR   GO; GO:0000144; C:cellular bud neck septin ring; IEA:EnsemblFungi.
DR   GO; GO:0009277; C:fungal-type cell wall; IEA:EnsemblFungi.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008061; F:chitin binding; IEA:InterPro.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:EnsemblFungi.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006037; P:cell wall chitin metabolic process; IEA:EnsemblFungi.
DR   GO; GO:0031505; P:fungal-type cell wall organization; IEA:EnsemblFungi.
DR   CDD; cd02183; GH16_fungal_CRH1_transglycosylase; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   InterPro; IPR018371; Chitin-binding_1_CS.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000757; GH16.
DR   InterPro; IPR017168; Glyco_hydro_16_CRH1_prd.
DR   PANTHER; PTHR10963:SF22; GLYCOSIDASE CRH2-RELATED; 1.
DR   PANTHER; PTHR10963; GLYCOSYL HYDROLASE-RELATED; 1.
DR   Pfam; PF00722; Glyco_hydro_16; 1.
DR   PIRSF; PIRSF037299; Glycosidase_CRH1_prd; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   PROSITE; PS00026; CHIT_BIND_I_1; 1.
DR   PROSITE; PS51762; GH16_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR037299};
KW   Membrane {ECO:0000256|PIRNR:PIRNR037299};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008062};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..441
FT                   /note="Glycosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003391132"
FT   DOMAIN          75..277
FT                   /note="GH16"
FT                   /evidence="ECO:0000259|PROSITE:PS51762"
FT   REGION          340..419
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        340..368
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        379..419
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        163
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037299-1"
FT   ACT_SITE        167
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037299-1"
SQ   SEQUENCE   441 AA;  46188 MW;  7E88185D7EAA7D15 CRC64;
     MKHTFSAAAA LIATFSLVAA QSAPKCGPGN NCPSDAPCCS QYGQCGAGAY CLGGCDPEHS
     FSLKSCMAAP TCKSADYKMD SIDDIAKNTV YLGDASKANW VSSGTVVEYN DDSVLLTMAP
     STVGTLLSST HYVWYGKISA TMTTSQGQGV VTAFILMSDV KDEIDFEWVG DDVTSAQSNY
     YYQGITNYQN MVPLKVSDTR QNTHTYEIDW TPDKVTWSID GNVMRTLNRD DTYNETTKGY
     NFPQTPARVQ LSLWPAGLPS NGEGTIEWAG GLVNWDSNYM QNGYYYAMIK DVTVECYKPP
     SGSGNGDAYY YTSVAGTEGD VQIGNNDTVL SSFLATGENP KFGGSSDTSS ASAQPTQQVE
     TVPGISGGGN VASSGRAPVD TGGDNSGTSA GDGNTALSSG SGGNTFSQGM SSDGTNTSEA
     PKLAAGSVVA LLGFFVAALT L
//
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