ID A0A364MS15_9PLEO Unreviewed; 1011 AA.
AC A0A364MS15;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
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=DDE83_008912 {ECO:0000313|EMBL:RAR01441.1};
OS Stemphylium lycopersici.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Stemphylium.
OX NCBI_TaxID=183478 {ECO:0000313|EMBL:RAR01441.1, ECO:0000313|Proteomes:UP000249619};
RN [1] {ECO:0000313|Proteomes:UP000249619}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIDEFI 213 {ECO:0000313|Proteomes:UP000249619};
RA Medina R., Franco M.E.E., Lucentini C.G., Saparrat M.C.N., Balatti P.A.;
RT "Draft genome sequence of Stemphylium lycopersici strain CIDEFI 213.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:RAR01441.1}.
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DR EMBL; QGDH01000271; RAR01441.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A364MS15; -.
DR STRING; 183478.A0A364MS15; -.
DR Proteomes; UP000249619; 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:UP000249619};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1011
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016825357"
FT DOMAIN 394..572
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000259|SMART:SM01029"
SQ SEQUENCE 1011 AA; 110197 MW; 8DD5B8F629F37752 CRC64;
MKSFLRLGSA VALGCLAVES AARAVGYSPK EWVKPYRREA LQDIVTWDED SLFVHGERIF
LYSGEVHPYR LPVPDLYIDI FQKIKALGYN GVSFYVDWAL LEGKPGVYRE EGVFDLQPFF
DAAQEAGIYL IARPGPYINA EVSGGGFPGW LQRINGTLRT RAPDFLAATD NYMKHVGAKI
AGAQITNGGP IILVQPENEY TQALGNIQPF PDPVYMNYVE DQIRDAGIIV PLISNDASPK
GYLAPGDPAG VDIYGHDGYP LGFDCANPNT WPDGNLPTNW HDLHEEQSPT TPYSILEFQS
GSFDPWGGPG FDKCGILVGA EFNRVFYKQL YSFGVTILNF YMTYGGTNWG NLGHPGGYTS
YDYAAPIKED RQVDRAKYSE LKLQANFLKV SPAYLTATRG NASNSTWTTT SDLSVTPAYG
EKTNFYFLRH SKYNSLDSTS YKLKISTSAF GNITVPQMNG TSLTLNGRDA KVHVSDYNIG
GTNIAYSTAE IFTWHKYEDK TVVIVYGGSG ETHELAIAAT DANVIEGDVK STTSQGHTIV
GFQIDSTRKV AKFGSDSPIY VYMLDRNEAF NYWSIDQAPH DSSNPVILKA GYLMRTAKAT
GKTLALTGDV NATTPIEIIG GASSDLSKLT FNGKDLDFEV SKEGSLTANI DFPKLNLDIP
QLSELEWKYV DSLPEIQPGY DDSEWTVADL KKTYNSLRPL DTPVSLYSSD YGYHTGTLLF
RGTFTATGNE SSFSLTTQGG SAFGSSAWVG DQFLGSWRGY DAAINGSATF TMPNLTKGKT
YTITVVVDNQ GLDENWTIGT ESMKNPRGIL DYKLSGHAAS DVNWKLTGNL GGEDYKDISR
GPLNEGGLYV ERQGLHLPGA LSASDAKWEK SAGPVADGIT APGIGFFATE FDLNMPSGYD
IPLSFTFSNG TSSGNGTSGS GVAAYRVQLY VNGWQYGKYV NNVGPQTKFP VTEGVLNYNG
TNYLGVSLWG LDAGATKIEG LELTVDAEIW SGLDGVATVQ GQRYEEREGA Y
//
