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Database: UniProt
Entry: N1PHL1_DOTSN
LinkDB: N1PHL1_DOTSN
Original site: N1PHL1_DOTSN 
ID   N1PHL1_DOTSN            Unreviewed;      1011 AA.
AC   N1PHL1;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   16-JAN-2019, entry version 27.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=DOTSEDRAFT_74371 {ECO:0000313|EMBL:EME40786.1};
OS   Dothistroma septosporum (strain NZE10 / CBS 128990) (Red band needle
OS   blight fungus) (Mycosphaerella pini).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Dothideomycetidae; Capnodiales; Mycosphaerellaceae;
OC   Dothistroma.
OX   NCBI_TaxID=675120 {ECO:0000313|EMBL:EME40786.1, ECO:0000313|Proteomes:UP000016933};
RN   [1] {ECO:0000313|Proteomes:UP000016933}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NZE10 / CBS 128990 {ECO:0000313|Proteomes:UP000016933};
RX   PubMed=23209441; DOI=10.1371/journal.pgen.1003088;
RA   de Wit P.J.G.M., van der Burgt A., Oekmen B., Stergiopoulos I.,
RA   Abd-Elsalam K.A., Aerts A.L., Bahkali A.H., Beenen H.G., Chettri P.,
RA   Cox M.P., Datema E., de Vries R.P., Dhillon B., Ganley A.R.,
RA   Griffiths S.A., Guo Y., Hamelin R.C., Henrissat B., Kabir M.S.,
RA   Jashni M.K., Kema G., Klaubauf S., Lapidus A., Levasseur A.,
RA   Lindquist E., Mehrabi R., Ohm R.A., Owen T.J., Salamov A., Schwelm A.,
RA   Schijlen E., Sun H., van den Burg H.A., van Ham R.C.H.J., Zhang S.,
RA   Goodwin S.B., Grigoriev I.V., Collemare J., Bradshaw R.E.;
RT   "The genomes of the fungal plant pathogens Cladosporium fulvum and
RT   Dothistroma septosporum reveal adaptation to different hosts and
RT   lifestyles but also signatures of common ancestry.";
RL   PLoS Genet. 8:E1003088-E1003088(2012).
RN   [2] {ECO:0000313|EMBL:EME40786.1, ECO:0000313|Proteomes:UP000016933}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NZE10 / CBS 128990 {ECO:0000313|Proteomes:UP000016933};
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A.,
RA   Barry K.W., Condon B.J., Copeland A.C., Dhillon B., Glaser F.,
RA   Hesse C.N., Kosti I., LaButti K., Lindquist E.A., Lucas S.,
RA   Salamov A.A., Bradshaw R.E., Ciuffetti L., Hamelin R.C., Kema G.H.J.,
RA   Lawrence C., Scott J.A., Spatafora J.W., Turgeon B.G.,
RA   de Wit P.J.G.M., Zhong S., Goodwin S.B., Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in
RT   the genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
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; KB446543; EME40786.1; -; Genomic_DNA.
DR   EnsemblFungi; EME40786; EME40786; DOTSEDRAFT_74371.
DR   OMA; YFAPGPP; -.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000016933; Unassembled WGS sequence.
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:UP000016933};
KW   Glycosidase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108869, ECO:0000313|EMBL:EME40786.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016933};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     21       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        22   1011       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5004109109.
FT   DOMAIN      396    570       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1011 AA;  111203 MW;  A9E4631FBED7822D CRC64;
     MLFGKLLKAA VLSAMAVQTA ALTIGGKPNT MIKSYKRDTL QDLVTWDDHS LFVRGERVLF
     YSGEFHPFRL PVPSLWLDVF QKIKALGYNG VSVYFDWALL EGKPGSFEAE GIFALEPFFE
     AAQTAGIYLL ARPGPYINAE VSGGGYPGWM QRNPALLRTR DAEYLKATQN YVDSISKPIA
     KAQITNGGPI ILLQPENEYS QATNNVEPFP DPVYFQYVED QFRNNSIVVP FISNDARPQG
     YFAPGPPRQE AAVDIYGHDG YPLGFDCANP YTWPDNALPT NYGDLHHYQS SSTPYSIVEF
     QGGAFDPWGG PGFAKCTALL GSEFERVFYK NDYSFGVTIF NIYMTYGGTN WGNLGHPGGY
     TSYDYGAVIT EERTVEREKY SQAKLQAQFL RASPAYLTAM PQNNSHANGS YTGNGAIATT
     ALFGNVTNFY VVRHASYNSL DTTNYSFNFP TSKGNITIDG LSLHGRDSKI FVSDYDVGGI
     NVLYSTAEIF TWKKYGDKRV LVVYGGPGET NELAVVKSQI GKCVEGQGVR TETKNGLSAI
     RFSTSSQRNV VEVGDDLSVY ILDRNSAYNY WVIDLPDDSV TGNFTNNKHA TSAPIVKVGY
     LLRTIEIHGS SLYLTGDINS TTPVEVIGAP QPLNELTFNG ESLKFAQAKN GVVTATAEYK
     KPELAVPDLS SISWKVIDTL PEIGSNYDDS AWTVADLTYS NNTIRNLTTP TSLYASDYGY
     HTGTLIYRGH FKANGDERDL YLATQGGSAF GHSIWLNGAF VGSFYGADKY YTWNETYTLP
     NTIAGKDYII TVLVDNMGLD ESGTVGSEQM KNPRGVIDYD LKGHNKSGVN WKLTGNLHGE
     DYEDHTRGPL NEGGLYAERQ GYHLPGAPTS DWTDSKTGPM DGINAPGVSF YATTFDLDFP
     QGYDIPLSFA FTNSSTNTSA TTPSYRCQLY VNGYQFGKYI YNIGPQNSFP VPEGIWNYQG
     SNYVAISLWA LEKGGAKVEK LRLVAGTPVQ SGFGPVEPAP QTGWKKREGA Y
//
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