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Database: UniProt
Entry: F9XKH7_ZYMTI
LinkDB: F9XKH7_ZYMTI
Original site: F9XKH7_ZYMTI 
ID   F9XKH7_ZYMTI            Unreviewed;       992 AA.
AC   F9XKH7;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   16-JAN-2019, entry version 43.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   Name=MgLAC1 {ECO:0000313|EMBL:EGP84525.1};
GN   ORFNames=MYCGRDRAFT_75961 {ECO:0000313|EMBL:EGP84525.1};
OS   Zymoseptoria tritici (strain CBS 115943 / IPO323) (Speckled leaf
OS   blotch fungus) (Septoria tritici).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Dothideomycetidae; Capnodiales; Mycosphaerellaceae;
OC   Zymoseptoria.
OX   NCBI_TaxID=336722 {ECO:0000313|EMBL:EGP84525.1, ECO:0000313|Proteomes:UP000008062};
RN   [1] {ECO:0000313|EMBL:EGP84525.1, 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.,
RA   Crane C.F., Hane J.K., Foster A.J., Van der Lee T.A.J., Grimwood J.,
RA   Aerts A., Antoniw J., Bailey A., Bluhm B., Bowler J., Bristow J.,
RA   van der Burgt A., Canto-Canche B., Churchill A.C.L., Conde-Ferraez L.,
RA   Cools H.J., Coutinho P.M., Csukai M., Dehal P., De Wit P.,
RA   Donzelli B., van de Geest H.C., van Ham R.C.H.J., Hammond-Kosack K.E.,
RA   Henrissat B., Kilian A., Kobayashi A.K., Koopmann E., Kourmpetis Y.,
RA   Kuzniar A., Lindquist E., Lombard V., Maliepaard C., Martins N.,
RA   Mehrabi R., Nap J.P.H., Ponomarenko A., Rudd J.J., Salamov A.,
RA   Schmutz J., Schouten H.J., Shapiro H., Stergiopoulos I.,
RA   Torriani S.F.F., Tu H., de Vries R.P., Waalwijk C., Ware S.B.,
RA   Wiebenga A., Zwiers L.-H., Oliver R.P., Grigoriev I.V., Kema G.H.J.;
RT   "Finished genome of the fungal wheat pathogen Mycosphaerella
RT   graminicola reveals dispensome structure, chromosome plasticity, and
RT   stealth pathogenesis.";
RL   PLoS Genet. 7:E1002070-E1002070(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing beta-D-galactose
CC         residues in beta-D-galactosides.; EC=3.2.1.23;
CC         Evidence={ECO:0000256|RuleBase:RU000675,
CC         ECO:0000256|SAAS:SAAS01116863};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000256|RuleBase:RU003679, ECO:0000256|SAAS:SAAS00534244}.
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DR   EMBL; CM001204; EGP84525.1; -; Genomic_DNA.
DR   RefSeq; XP_003849549.1; XM_003849501.1.
DR   ProteinModelPortal; F9XKH7; -.
DR   EnsemblFungi; Mycgr3T75961; Mycgr3P75961; Mycgr3G75961.
DR   GeneID; 13402355; -.
DR   KEGG; ztr:MYCGRDRAFT_75961; -.
DR   InParanoid; F9XKH7; -.
DR   Proteomes; UP000008062; Chromosome 9.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.102.20.10; -; 1.
DR   Gene3D; 2.60.120.260; -; 2.
DR   Gene3D; 2.60.390.10; -; 1.
DR   InterPro; IPR018954; Betagal_dom2.
DR   InterPro; IPR037110; Betagal_dom2_sf.
DR   InterPro; IPR025972; BetaGal_dom3.
DR   InterPro; IPR036833; BetaGal_dom3_sf.
DR   InterPro; IPR025300; BetaGal_jelly_roll_dom.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR031330; Gly_Hdrlase_35_cat.
DR   InterPro; IPR019801; Glyco_hydro_35_CS.
DR   InterPro; IPR001944; Glycoside_Hdrlase_35.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR23421; PTHR23421; 1.
DR   Pfam; PF10435; BetaGal_dom2; 1.
DR   Pfam; PF13363; BetaGal_dom3; 1.
DR   Pfam; PF13364; BetaGal_dom4_5; 2.
DR   Pfam; PF01301; Glyco_hydro_35; 1.
DR   PRINTS; PR00742; GLHYDRLASE35.
DR   SMART; SM01029; BetaGal_dom2; 1.
DR   SUPFAM; SSF117100; SSF117100; 1.
DR   SUPFAM; SSF49785; SSF49785; 2.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000008062};
KW   Glycosidase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108869};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008062}.
FT   DOMAIN      368    546       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   992 AA;  108705 MW;  B2DAE80C97FC216A CRC64;
     MIKPYKREVL QDIVTWDEHS IFINGDRVML YSAEFHPFRL PVPSLWLDVF QKIKSMGYNT
     VSVYFDWALV EGKPGNYTAE GIFALEPFFE AAKTAGIYIL ARPGPYINAE VSGGGFPGWL
     QRTPGRLRTT DKGYIDATEN YIANIGKSIA AAQITNGGPV ILVQPENEYS GAAKNVPEFP
     DPVYWSKVEE QLRDSGIVVP FISNDNHNHG YFAPGPPPQN PAVSVDIYGH DGYPLGFDCA
     NPETWPDNHL PTNFGEQHLN QSSSTPFSLV EFQGGSFDPW GGPGFTKCGQ LLGPEFQRVF
     YKNDFSFGVT FFSIYMTYGG TNWGNLGHPG GYTSYDYGAV ISEERLVGQE KYSQAKLLAN
     FLQASPAYLT AAYQNNTYAN GSYTGNSAIA TTALFGEVTK FFVVRHAFFN TLESTDYTIT
     LPTSQGNITI PQLGGSLTLH GRDSKVYATD YDVGGANLLY TTAEIFTWKQ YGDTKVLILY
     GGPDETNEFA VSGCGGAKIA EGEDVKIEAK NEAIVVQYSS SSTRKVVEFD NGLWVYLLDR
     QSAYNYWVVD LPNDDVTANF TNHKHAISAP IIQFGYLVRT VTVDGNNLHL TGDLNATSSL
     EVIGAPHCLE QLTFNGESLD FEEGDSGIVT ATVVYNEPAL VVPDLAKVQW KVLDSLPEVK
     ADYDDSAWTA ADLTQTPNDY RNLTTPTSLY SSDYGYHTGS LIYRGHFTAN GQESSLYLAT
     QGGSAFGHSI WLDDTLVGSF YGADLYMTWN ETYTLPPITS GKTYVLTILV DNMGLDENYN
     TGENQMKAPR GILDYNLSGH SKSDITWKLT GNLGGEDYLD AARGPLNEGG LYAERQGYHL
     PNAPTSSWRD SAGPMEGIAN AGVAFYTTTF DLDMPSGYDI PLSFSFSNAT DGVQDAVPTD
     GQISKYRCQI YVNGYQFGKY VHNIGPQDVF PVPEGIWNYH GSNYVAVSLW ALEASGAKVA
     NLSLVTGPVI QSGFGPVELS PVPAWEQRKG AY
//
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