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Database: UniProt
Entry: A0A0D1YWS5_9EURO
LinkDB: A0A0D1YWS5_9EURO
Original site: A0A0D1YWS5_9EURO 
ID   A0A0D1YWS5_9EURO        Unreviewed;      1065 AA.
AC   A0A0D1YWS5;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Lactase {ECO:0000256|ARBA:ARBA00032230};
GN   ORFNames=PV11_06841 {ECO:0000313|EMBL:KIV79273.1};
OS   Exophiala sideris.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=1016849 {ECO:0000313|EMBL:KIV79273.1, ECO:0000313|Proteomes:UP000053599};
RN   [1] {ECO:0000313|EMBL:KIV79273.1, ECO:0000313|Proteomes:UP000053599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 121828 {ECO:0000313|EMBL:KIV79273.1,
RC   ECO:0000313|Proteomes:UP000053599};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala sideris CBS121828.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC       {ECO:0000256|ARBA:ARBA00007401, ECO:0000256|RuleBase:RU361154}.
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DR   EMBL; KN846953; KIV79273.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D1YWS5; -.
DR   STRING; 1016849.A0A0D1YWS5; -.
DR   HOGENOM; CLU_002346_0_0_1; -.
DR   OrthoDB; 276651at2759; -.
DR   Proteomes; UP000053599; Unassembled WGS sequence.
DR   GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt.
DR   Gene3D; 2.70.98.10; -; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   InterPro; IPR004199; B-gal_small/dom_5.
DR   InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR014718; GH-type_carb-bd.
DR   InterPro; IPR006101; Glyco_hydro_2.
DR   InterPro; IPR006103; Glyco_hydro_2_cat.
DR   InterPro; IPR023230; Glyco_hydro_2_CS.
DR   InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR   InterPro; IPR006104; Glyco_hydro_2_N.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR032312; LacZ_4.
DR   PANTHER; PTHR46323; BETA-GALACTOSIDASE; 1.
DR   PANTHER; PTHR46323:SF1; LACTASE; 1.
DR   Pfam; PF02929; Bgal_small_N; 1.
DR   Pfam; PF00703; Glyco_hydro_2; 1.
DR   Pfam; PF02836; Glyco_hydro_2_C; 1.
DR   Pfam; PF02837; Glyco_hydro_2_N; 1.
DR   Pfam; PF16353; LacZ_4; 1.
DR   PRINTS; PR00132; GLHYDRLASE2.
DR   SMART; SM01038; Bgal_small_N; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 2.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   PROSITE; PS00719; GLYCOSYL_HYDROL_F2_1; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361154};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361154};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053599}.
FT   DOMAIN          763..1047
FT                   /note="Beta galactosidase small chain/"
FT                   /evidence="ECO:0000259|SMART:SM01038"
SQ   SEQUENCE   1065 AA;  120887 MW;  EF327DFD293A734F CRC64;
     MVQPERYDRS QRKPDYSNER VFQRNKLAAR AYHIPDTSIS LSGAWDFHYA QNPELAPSWD
     DITTQDEFSW QPITVPGHWQ LQGYGIPQYT NVVFPFPVCP PNSPTDNHTG SYLKKFYVPK
     SWSLDSQIRL RFEGVDSAFH LFVNGTEVGY SQGSRNPAEF DISSCVERNT ENQILVRVYQ
     WSDGSYIEDQ DQWWLSGIFR DVYLLAFPEK ARVEDYFIQA ELDNSYQHGN LNVSLDMALQ
     EDCELEIMLQ SPAKGTVLID DRVTVAREES KLRRQFVVEA PAKWTAETPV LYHVELRLLV
     NGECIQTIRH PTGFRKVEIK NGLLTVNGVP LLLRGTNRHE HHPRLGRAVP PEYLRQDLLL
     MKQHNINAIR CSHYPSQPAL YQFADELGFW VLDEADLECH GFSEAVNSSM QIPKDMDYEQ
     RSALLADKAA AFTSDNPDWE AAYVDRMTQL VQRDKNFTSV IVWSLGNEAF YGRNHKAMYE
     YVKRADPSRP VHYEGDRNAV TADMYSYMYP SVQQLITLAK EEGVAPDGSF EKPIILCEYG
     HAMGNGPGLL EDYQAAFRKH ERLQGGFIWE WANHGLLKPS EEVPGRQVYA YGGDFGDVPN
     DGTFVMDGLC YSDHTPTPGL KELKKVVAPI RAWFDEDRNE IVIENGFNFK GLEEHTAKYI
     LEIFTDTPET YVWKSDIPDI KPGRTGTIAL PDFALRYRSF TAAECWVTVS FTLKDSCAWA
     DAGHEVAWFQ HHLNKNAFAP PINTPISNTG NKLDVTTSRQ YTTVTGQDFS ITFDRVHTYI
     SSWVLNGINL LQAPKPSTLP FKLGFWRPPT DNDARGQTQL WQQWGLDTMT TQKRSFDVIR
     ANDEHVELKT VTYLAPPILA WGMQVEATYR ISADGTISIR THITPKGASP ANLPRAGWDI
     QLPQACNRAV YFGLGPGESY HDKKSAQKVG IYHASIDDLH TPYEVPQENG NRMDMRWVKI
     LDERGAGIKA TMTGGKRTPD TFHFAMSKYS AEELERARHG PELIEGDANY LRLDVDVSGV
     GTAACGPGIK DEDFVKCEEM EFEICLEPIF DETLACSNAK ARKEG
//
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