ID N1PHL1_DOTSN Unreviewed; 1011 AA.
AC N1PHL1;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Beta-galactosidase {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|RuleBase:RU000675};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|RuleBase:RU000675};
GN ORFNames=DOTSEDRAFT_74371 {ECO:0000313|EMBL:EME40786.1};
OS Dothistroma septosporum (strain NZE10 / CBS 128990) (Red band needle blight
OS fungus) (Mycosphaerella pini).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; 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., Lindquist E.,
RA Mehrabi R., Ohm R.A., Owen T.J., Salamov A., Schwelm A., Schijlen E.,
RA Sun H., van den Burg H.A., van Ham R.C.H.J., Zhang S., Goodwin S.B.,
RA 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 lifestyles
RT 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., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT 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 residues
CC in beta-D-galactosides.; EC=3.2.1.23;
CC Evidence={ECO:0000256|ARBA:ARBA00001412,
CC ECO:0000256|RuleBase:RU000675};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC {ECO:0000256|ARBA:ARBA00009809, ECO:0000256|RuleBase:RU003679}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KB446543; EME40786.1; -; Genomic_DNA.
DR AlphaFoldDB; N1PHL1; -.
DR STRING; 675120.N1PHL1; -.
DR EnsemblFungi; EME40786; EME40786; DOTSEDRAFT_74371.
DR eggNOG; KOG0496; Eukaryota.
DR HOGENOM; CLU_005732_2_0_1; -.
DR OMA; QTEFPVP; -.
DR OrthoDB; 1032627at2759; -.
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; Beta-galactosidase, domain 2; 1.
DR Gene3D; 2.60.390.10; Beta-galactosidase, domain 3; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 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:SF122; BETA-GALACTOSIDASE A-RELATED; 1.
DR PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1.
DR Pfam; PF13364; BetaGal_ABD2; 2.
DR Pfam; PF10435; BetaGal_dom2; 1.
DR Pfam; PF13363; BetaGal_dom3; 1.
DR Pfam; PF01301; Glyco_hydro_35; 1.
DR PRINTS; PR00742; GLHYDRLASE35.
DR SMART; SM01029; BetaGal_dom2; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF117100; Beta-galactosidase LacA, domain 3; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000675};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000675};
KW Reference proteome {ECO:0000313|Proteomes:UP000016933};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1011
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004109109"
FT DOMAIN 396..570
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000259|SMART: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
//
