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
//