ID A0A0F4G9W1_9PEZI Unreviewed; 1062 AA.
AC A0A0F4G9W1;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Lactase {ECO:0000256|ARBA:ARBA00032230};
GN ORFNames=TI39_contig4215g00007 {ECO:0000313|EMBL:KJX94129.1};
OS Zymoseptoria brevis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=1047168 {ECO:0000313|EMBL:KJX94129.1, ECO:0000313|Proteomes:UP000033647};
RN [1] {ECO:0000313|EMBL:KJX94129.1, ECO:0000313|Proteomes:UP000033647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zb18110 {ECO:0000313|EMBL:KJX94129.1,
RC ECO:0000313|Proteomes:UP000033647};
RA Grandaubert J., Bhattacharyya A., Stukenbrock E.H.;
RT "RNA-seq based gene annotation and comparative genomics of four
RT Zymoseptoria species reveal species-specific pathogenicity related genes
RT and transposable element activity.";
RL Submitted (MAR-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KJX94129.1}.
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DR EMBL; LAFY01004174; KJX94129.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F4G9W1; -.
DR STRING; 1047168.A0A0F4G9W1; -.
DR OrthoDB; 276651at2759; -.
DR Proteomes; UP000033647; 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:UP000033647}.
FT DOMAIN 779..1060
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
FT REGION 55..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1062 AA; 119138 MW; 9F0FC5D787B43138 CRC64;
MSSLSSAVLQ DHQGQIPDYN NEQIFQRHRL PARAYHIPKD SLLLNGRWDF HYAPTPLHAP
DPRQNGQYTP ATPDSAVQDG LDTTVDEPAH EWTNIDVPGH WQLQGFGKPH YTNVIYPFPV
NPPHVPTENP AGTYRRRFTV PASWSTNAQL RLRFEGVDSA FHVFVNSSLV GYHQGSRNSS
EFDVTDVVRK DGENEVFVKV YQWCDGSYIE DQDQWWLSGI FRDVYLLALP KTARIEDFFV
KTLLDAKYQD ATLELTLDVN LGSDVDVVVS LKDRKNGDQP VNQESFSAKA QSGQLKHSIP
VSTPKKWSAE TPNLYQLEID LVDVRDRTVL HSIKSQVGFR QVEIKDGLLL VNGKRILLQG
VNRHDHHNKF GRAVPLSYIR EDLLLMKRHN INALRCSHYP PDPKLLDLCD ELGLWVMDEA
DLECHGFYDA VARPLDIPEE MDYEERKLLA FPQAAAYTSD NPRWQGQYVD RIESVVQRDK
NHPSVIIWSL GNEAFYGQNH KAMYDAAKKI DNTRPVHYEG DAKALSADMF SYMYPSVERL
LKLANTEGVI DGKFDKPIVL CEYAHAMGNG PGNLEGYQQA FRDVPRLQGG FIWEWANHGL
WKDGPDGKGF FAYGGDFGDT PNDGTFVMDG LCNSNHTPTP GLIEYKKVIE PLRAAIEDNE
LVVRNLYDFV SLDHLTATYR IESFNEEESI LISSGFFDIT GIGAGQTKRL PLPSSLNNST
LPDETWLSVS FRLGQATNWA DTGHEVAWCQ GCLTANRHQA VEPHKLGPLR VRTSPTSWIV
GSGGFEIIFD RARGVLKSWS SNSKSLLIED PRTHAALMPS VWRAPTDNDR PSDDPYWKRY
GLNDMTSQLR STKIARQSES TVAISSTTYL APPILDWGIE AEISYTIKSN ESVSIEAKLT
PVGSMPTTVP RIGLDLRLNK ALVAAKYHGL GPGESYPDKM MAQRVAIYES PVAQLSYNYD
VPQENGNRMG ARWVKLVDET GFGLQSRRAD SDHPFSWTAS YHRAEMLDAA KHPCDLVEED
ALLLKLDVAT AGVGSAACGP GIGEDVQVKC QATSFAFELR RI
//
