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Database: UniProt
Entry: A0A1V6QMD6_9EURO
LinkDB: A0A1V6QMD6_9EURO
Original site: A0A1V6QMD6_9EURO 
ID   A0A1V6QMD6_9EURO        Unreviewed;      1008 AA.
AC   A0A1V6QMD6;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   16-JAN-2019, entry version 10.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=PENSOL_c058G06268 {ECO:0000313|EMBL:OQD90341.1};
OS   Penicillium solitum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=60172 {ECO:0000313|EMBL:OQD90341.1, ECO:0000313|Proteomes:UP000191612};
RN   [1] {ECO:0000313|EMBL:OQD90341.1, ECO:0000313|Proteomes:UP000191612}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 29525 {ECO:0000313|EMBL:OQD90341.1,
RC   ECO:0000313|Proteomes:UP000191612};
RA   Nielsen J.C., Nielsen J.;
RT   "Uncovering the secondary metabolism of Penicillium species provides
RT   insights into the evolution of 6-MSA pathways.";
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing beta-D-galactose
CC         residues in beta-D-galactosides.; EC=3.2.1.23;
CC         Evidence={ECO:0000256|RuleBase:RU000675,
CC         ECO:0000256|SAAS:SAAS01116863};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000256|RuleBase:RU003679, ECO:0000256|SAAS:SAAS00534244}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OQD90341.1}.
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DR   EMBL; MDYO01000058; OQD90341.1; -; Genomic_DNA.
DR   Proteomes; UP000191612; 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; -; 1.
DR   Gene3D; 2.60.120.260; -; 2.
DR   Gene3D; 2.60.390.10; -; 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; PTHR23421; 1.
DR   Pfam; PF10435; BetaGal_dom2; 1.
DR   Pfam; PF13363; BetaGal_dom3; 1.
DR   Pfam; PF13364; BetaGal_dom4_5; 2.
DR   Pfam; PF01301; Glyco_hydro_35; 1.
DR   PRINTS; PR00742; GLHYDRLASE35.
DR   SMART; SM01029; BetaGal_dom2; 1.
DR   SUPFAM; SSF117100; SSF117100; 1.
DR   SUPFAM; SSF49785; SSF49785; 2.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000191612};
KW   Glycosidase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108869};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191612};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     18       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        19   1008       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5012890050.
FT   DOMAIN      396    576       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1008 AA;  109835 MW;  16D9914BC6F2E09F CRC64;
     MKFSSSWAFA CLAAQAAGAA ISHSVNGFTF TEHPDPVKRD LLQKYVTWDD KSLFVNGERL
     MLFSGEIHPY RLPVPSLWID VLQKVKALGF NCVSFYIDWA LLEGKPGEYT AEGIFALEPF
     FDAAKEAGIY LLARPGPYIN AEASGGGFPG WLQRVNGTLR TSDEAYLKAT DNYISHVATT
     MAKGQITNGG PIILYQPENE YSGACCGYND FPDGAYMQYV EDQARKAGIV VPLISNDASP
     GGHNAPGTGE GAVDIYGHDS YPLGFDCANP TTWPAGDLPT DFYTTHMNQS PSTPYSLIEF
     QGGAFDPWGG VGFTKCAALL NHEFERVFYK NNLSFRVAFL NLYMIFGGTN WGNLGHPGGY
     TSYDYGSPIT ESRNITREKY SELKLIGNFA RVSPAYLVST PGSLTTSKYT TSSDLAVTPL
     LGGNNTASSF FVVRHSDYSS QASVDYKLKV PTSVGEVTIP QLGGSLTLSG RDSKIHVVDY
     DVAGKNILYS SAEVFTWTES GKSKILVLYG GPGEHHELAV SSTLKASVIE GSSSSITTKQ
     VDKAVVIGWD VSTTRRIVQV GDLQIVLLDR NSAYNYWVPQ LPTTGTSPGY SSQKVTASSL
     IVKAGYLVRT AYVQGSDLHL TADFNATTPI EVIGAPSNAK NLVINGKKAQ VKVDKNGIWS
     SSVSYTAPKI ELPTLKDLKW KSIDTLPEIQ DSYDDSAWVS ADKPTQNSIH KLKTPTSLFS
     SDYGFHTGTL LFRGHFVATS DEKTFFVQTQ GGSAFGSAVW LNENHIGSWG GISIDADHNG
     TYTLPTLKKG KSYVFTVVVD NLGLNENWIV GEDQMKNPRG ILNYELSGRS ASDITWKLTG
     NLGGEDYLDK VRGPLNEGGL YAERQGFHQP QPPTQNWKST SPFDGLSAPG INFYSASFDL
     NIEKGWDVPL YFNFGNTTSP AAYRAQLYVN GYQYAKYVNN IGPQTSFPVP EGILNYRGTN
     YLGLSLWVLE SDGAKLEGLD LIHTTPVLTA LKVGSVEQPK YNKRKGAY
//
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