ID   A0A074W790_9PEZI        Unreviewed;      1069 AA.
AC   A0A074W790;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Lactase {ECO:0000256|ARBA:ARBA00032230};
GN   ORFNames=M437DRAFT_63314 {ECO:0000313|EMBL:KEQ65767.1};
OS   Aureobasidium melanogenum CBS 110374.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX   NCBI_TaxID=1043003 {ECO:0000313|EMBL:KEQ65767.1, ECO:0000313|Proteomes:UP000030672};
RN   [1] {ECO:0000313|EMBL:KEQ65767.1, ECO:0000313|Proteomes:UP000030672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 110374 {ECO:0000313|EMBL:KEQ65767.1,
RC   ECO:0000313|Proteomes:UP000030672};
RX   PubMed=24984952;
RA   Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA   Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA   Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT   "Genome sequencing of four Aureobasidium pullulans varieties:
RT   biotechnological potential, stress tolerance, and description of new
RT   species.";
RL   BMC Genomics 15:549-549(2014).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC       {ECO:0000256|ARBA:ARBA00007401, ECO:0000256|RuleBase:RU361154}.
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DR   EMBL; KL584826; KEQ65767.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A074W790; -.
DR   STRING; 1043003.A0A074W790; -.
DR   HOGENOM; CLU_002346_0_0_1; -.
DR   OrthoDB; 276651at2759; -.
DR   Proteomes; UP000030672; 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; IPR023232; Glyco_hydro_2_AS.
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.
DR   PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 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:UP000030672}.
FT   DOMAIN          779..1064
FT                   /note="Beta galactosidase small chain/"
FT                   /evidence="ECO:0000259|SMART:SM01038"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1069 AA;  121316 MW;  EEF5CFCB8AA3A789 CRC64;
     MSLPGSLTAS DHHSGQSSDL DICNPKIVHR NRLPARSYWI PEKSLLLNGT WGFVYSPTPK
     HAPHPSLYSD GLSSLVDALT VDGEGQTADI KWSSITVPGH WQLQGYGKPH YTNTVYPFPV
     CPPYVPTENP TGTYRRNFFV PSSWSEDSQI RLRFDGVDSA YHVYLNGQKV GYSQGSRNPA
     EFDITNYVNR GEDVNRLIVN VFQFCDGSYI EDQDQWWLSG IFRDVHLICF PSKTRIEDVF
     IKTELDGEYR DAKLHVELDL TIHEAAEAML TLRSPNGSSV INEKIQLSAE SPHSPHVFAV
     SNPVKWTAEA PQLYSLEINL LDSDSDTPVQ TVKQKVGFRC VEIIKGNISV NGKPIFLRGV
     NRHDHHPIFG RAVPLAYMRR DLMIMKQHNI NALRTSHYPA NPKLYELCDE LGLWVMDEAD
     LECHGFFDAV ERPLNLPPDM GYEERKKYTF DKAAKFTSDN EDWKTAYLDR MVQMVERDKN
     HPSIIMWSLG NEAFYGRNHV AMYEWAKSRD PERPVHYEGD VNAASADMFS YMYPSIEKLI
     GHATEEGDDF KKPIVLCEYG HAMGNGPGLL EDYQAAFRKY RRLQGGYIWE WANHGLLKTE
     GDKQFYAYGG DFGDVPNDDT FVMDGLLFSD HTPTPGLTEL KKVIAPVRAW IEGKKLVIKN
     EYEFITLGQF IADYKVEVLG IRPDRVLSGP IQLPHIDPGT EAKIDLPEEI FNVHRPNGTE
     VWLTIDFRLG VATPWAEAGH SITWYQTRLS AKDDDYTYGI ERPIMSSAIT PHETQLHYRF
     IGCDFHFNFS RARGTLVEWV YGGRSVLKKR DTPDDPLLAL GFWRAPTDND AVGMSKEWKR
     YGLDSMTPQL RSFSLEDNGP DKARLTAVYY YSPPVLAWGF TAKVTYEISS AGQLSITIHL
     TPQGNAPTTL PRVGLNLQLD SSFKQATWYG KGPGESYSDK ATSQQLGIWN STIRKLQTPY
     EVPQENGNRI ETRWVKVLNE QGLGIKATYI PRPKEKEFFQ WACCLHDAKV LEEARHPCDL
     VERESPLWRL DADNAGVGTA ACGPGVKKED QVECREREFT FVLEPAIDF
//