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Database: UniProt
Entry: A0A135LNY7_PENPA
LinkDB: A0A135LNY7_PENPA
Original site: A0A135LNY7_PENPA 
ID   A0A135LNY7_PENPA        Unreviewed;      1009 AA.
AC   A0A135LNY7;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   16-JAN-2019, entry version 12.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=PGRI_044390 {ECO:0000313|EMBL:KXG50672.1};
OS   Penicillium patulum (Penicillium griseofulvum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=5078 {ECO:0000313|EMBL:KXG50672.1, ECO:0000313|Proteomes:UP000070168};
RN   [1] {ECO:0000313|EMBL:KXG50672.1, ECO:0000313|Proteomes:UP000070168}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PG3 {ECO:0000313|EMBL:KXG50672.1,
RC   ECO:0000313|Proteomes:UP000070168};
RX   PubMed=26729047; DOI=10.1186/s12864-015-2347-x;
RA   Banani H., Marcet-Houben M., Ballester A.R., Abbruscato P.,
RA   Gonzalez-Candelas L., Gabaldon T., Spadaro D.;
RT   "Genome sequencing and secondary metabolism of the postharvest
RT   pathogen Penicillium griseofulvum.";
RL   BMC Genomics 17:19-19(2016).
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:KXG50672.1}.
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DR   EMBL; LHQR01000045; KXG50672.1; -; Genomic_DNA.
DR   EnsemblFungi; KXG50672; KXG50672; PGRI_044390.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000070168; 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:UP000070168};
KW   Glycosidase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108869, ECO:0000313|EMBL:KXG50672.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070168};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     19       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        20   1009       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5007800721.
FT   DOMAIN      396    576       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1009 AA;  109846 MW;  A800F480C56E1FE4 CRC64;
     MKLLSSWAIA YLAAQAAGAA ISHSWNGYTI TEHPDPVKRD LLQKHVTWDD KSLFVNGERI
     MIFSGEIHPY RLPVPSLWID VLQKVKSLGF NCVSFYIDWA LLEGKPGQYT AEGIFALEPF
     FDAAKEAGIY LLARPGPYIN AEVSGGGFPG WLQSVNGTLR SGDEDFLKAT DNYMANVAAT
     MAKGQITNGG PIILFQPENE YSGACCGYED FPDGAYMQYV QDQAHRAGIV VPIISNDAGT
     DGHNAPGTGE GEVDIYGHDN YPLGFDCSNP STWPAGKLPT DFYKIHMETS PATPYSLVEF
     QGGAFDPWGG AGLDKCAALL NHEFERVFYK NNLSFRVAIF NLYMIFGGTN WGNLGHPGGY
     TSYDYGSAIT ESRNITREKY SELKLIGNFA RASSAYLLST PGELTTSKYT TSSDLAVTPL
     LGGKNTASSF FVVRHSDYSS QASVDYKLKV PTSAGEVTIP QLGGSLTLSG RDSKIHVVDY
     DVADTNVLYS SAEVFTWTKS GKSKILVLYG GPGEHHELAV SSNSKASVIE GSSSSITTKK
     VGKAVVIGWD VSTTRRIVQV GDLKIVLLDR NSAYNYWVPQ LPAKGESPGY STQKTAPSSL
     IVKAGYLVRT AFVKGNDLHL TADFNATTPI EVLGAPSNAK NLVINGKKAN VKVDKNGIWS
     TSVAYTAPKV ELPTLKSLKW KSIDTLPELQ ASYDDSKWVS ADKPTKNSGH ALKTPTSLYS
     SDYGFHTGTL LFRGHFVATG NEKTFSLQTQ GGSAFGSSVW LNENHIGSWS GIGPDADHNG
     TYNLPTLKKG KSYVFTVVVD NMGLNENWIV GEDQMKLPRG ILNYELSGHP ASDIAWKLTG
     NLGGEDYLDQ VRGPLNEGGL YAERQGFHQP KPPTQKWESG SPFEGLSKPG IKFYTTSFDL
     DMEKGWDVPV YFNFGNSTSS PAYRAQLYVN GYQYAKYVSN IGPQTSFPVP EGILNYRGTN
     YLALSLWALD SKGAKLESLD MVHTTPVLTA LDEVKPAGQP EYEKRKGAY
//
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