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Database: UniProt
Entry: A0A2H3J3M7_9EURO
LinkDB: A0A2H3J3M7_9EURO
Original site: A0A2H3J3M7_9EURO 
ID   A0A2H3J3M7_9EURO        Unreviewed;      1010 AA.
AC   A0A2H3J3M7;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   16-JAN-2019, entry version 6.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=PENO1_024800 {ECO:0000313|EMBL:PCH05034.1};
OS   Penicillium occitanis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=290292 {ECO:0000313|EMBL:PCH05034.1, ECO:0000313|Proteomes:UP000218381};
RN   [1] {ECO:0000313|EMBL:PCH05034.1, ECO:0000313|Proteomes:UP000218381}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CL100 {ECO:0000313|EMBL:PCH05034.1,
RC   ECO:0000313|Proteomes:UP000218381};
RX   PubMed=28951729; DOI=.3389/fmicb.2017.01627;
RA   Bravo-Ruiz G., Sassi A.H., Marcet-Houben M., Di Pietro A.,
RA   Gargouri A., Gabaldon T., Roncero M.I.G.;
RT   "Regulatory Mechanisms of a Highly Pectinolytic Mutant of Penicillium
RT   occitanis and Functional Analysis of a Candidate Gene in the Plant
RT   Pathogen Fusarium oxysporum.";
RL   Front. Microbiol. 8:1627-1627(2017).
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:PCH05034.1}.
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DR   EMBL; NPFK01000046; PCH05034.1; -; Genomic_DNA.
DR   Proteomes; UP000218381; 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:UP000218381};
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:PCH05034.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000218381};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     20       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        21   1010       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5013890935.
FT   DOMAIN      396    577       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1010 AA;  109414 MW;  8FA42EEF80A189D7 CRC64;
     MKVLETTAVA LACLSGQVLG RAVSHRGGAL NVFENSGVEQ RALLQDVVTW DNQSLYIHGE
     RLMIFSGEVH PFRLPVSSLY IDIFQKIKAL GFNTVSFYVD WALLEGKPGS YRADGIFDLQ
     PFFDAAKQAG IYLLARPGPY INAEVSGGGF PGWLQRVNGT LRTRDPGYWD ATENYANHIG
     ATIAANQITK GGPIILYQPE NEYSGFATGY SDDAQYMQDI MDTARNAGVI IPFISNDAWA
     GGHNAPGSGV GAVDIYGHDS YPLGFDCANP STWPSGGLPT YFREDHVEQS PSTPFSLVEF
     QGGAFDPWQG SGFENCVALL GPEFERVFYK NNIAAGVAFL NLYMTFGGTN WGNLGYPDGY
     TSYDYGAAIS ESRSITREKY SQLKLLGNFL KASPSYLDVV PGSASNGTYT STTALTVTPL
     IGRSTKSSFY VVRHADYTSL DSTGYTLKVP TSAGTLTLPQ LGGSLTLNGR DSKIHVTDYD
     VAGTNILYST AEVFTWKNFS DYKALVLYGG AGEHHELAIS SSSSAKISIV DGSKSGVTTK
     TQNGQAIIAW DVSSSRRIVK VDDLLVFLLD RNSAYDYWVP QVGTSNSSIG FTTQETVASS
     IIVNAGYLVR YAWLQGSELH LSADFNATTT VEVIGVPKAA TSLYVNGVLY SHTKTSNGFW
     TASVKYSAPK ISLPDFSKLT WKYVDSLPEI QSTYDDSAWV SADHDWTNNT ANPLKTPVSL
     YASDYGFNTG HLLYRGHFVA NGNEKTFYVE TIGGSGFGSS VWLNGTLLGS WAGNANNDSA
     ASTYTLPTLK SGSSYTLTIL TSNTGLEEDW TVGTETMKTP RGILDFDLSG HSQSDVTWKI
     TGNLGGEDYV DLARGPLNEG GLYAERQGWH QPSPPSSDWK TSSPFEGISQ AGVGFYSTSF
     TLDLPQGYDI PLSFTFGDSS GSSYRVQLYV NGYQYGTYVP QLGPQTQFPV PQGILNYQGE
     NWVAITLWAQ ESSGAKVDRF ELTYTTPVLT ALTGIESSPQ PAYSQRAGAY
//
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