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Database: UniProt
Entry: B2AT20_PODAN
LinkDB: B2AT20_PODAN
Original site: B2AT20_PODAN 
ID   B2AT20_PODAN            Unreviewed;      1082 AA.
AC   B2AT20;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   13-FEB-2019, entry version 76.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=PODANS_1_14400 {ECO:0000313|EMBL:CAP67543.1};
OS   Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS   (Pleurage anserina).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Sordariomycetidae; Sordariales; Lasiosphaeriaceae;
OC   Podospora.
OX   NCBI_TaxID=515849 {ECO:0000313|EMBL:CAP67543.1};
RN   [1] {ECO:0000313|EMBL:CAP67543.1, ECO:0000313|Proteomes:UP000001197}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC   {ECO:0000313|Proteomes:UP000001197}, and S mat+
RC   {ECO:0000313|EMBL:CAP67543.1};
RX   PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA   Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O.,
RA   Porcel B.M., Couloux A., Aury J.-M., Segurens B., Poulain J.,
RA   Anthouard V., Grossetete S., Khalili H., Coppin E.,
RA   Dequard-Chablat M., Picard M., Contamine V., Arnaise S., Bourdais A.,
RA   Berteaux-Lecellier V., Gautheret D., de Vries R.P., Battaglia E.,
RA   Coutinho P.M., Danchin E.G.J., Henrissat B., El Khoury R.,
RA   Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
RA   Debuchy R., Wincker P., Weissenbach J., Silar P.;
RT   "The genome sequence of the model ascomycete fungus Podospora
RT   anserina.";
RL   Genome Biol. 9:R77.1-R77.22(2008).
RN   [2] {ECO:0000313|EMBL:CAP67543.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=S mat+ {ECO:0000313|EMBL:CAP67543.1};
RA   Genoscope - CEA;
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000001197}
RP   GENOME REANNOTATION.
RC   STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC   {ECO:0000313|Proteomes:UP000001197};
RX   PubMed=24558260; DOI=10.1534/genetics.113.159988;
RA   Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E.,
RA   Benkhali J.A., Couloux A., Wincker P., Debuchy R., Silar P.;
RT   "Maintaining two mating types: Structure of the mating type locus and
RT   its role in heterokaryosis in Podospora anserina.";
RL   Genetics 197:421-432(2014).
RN   [4] {ECO:0000313|EMBL:CDP23804.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Genoscope - CEA;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000313|EMBL:CDP23804.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Grognet P., Bidard F., Kuchly C., Chan Ho Tong L., Coppin E.,
RA   Ait Benkhali J., Couloux A., Wincker P., Debuchy R., Silar P.;
RT   "Maintaining two mating types: Structure of the mating type locus and
RT   its role in heterokaryosis in Podospora anserina.";
RL   Submitted (SEP-2014) 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}.
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DR   EMBL; CU633899; CAP67543.1; -; Genomic_DNA.
DR   EMBL; FO904936; CDP23804.1; -; Genomic_DNA.
DR   RefSeq; XP_001906872.1; XM_001906837.1.
DR   STRING; 515849.XP_001906872.1; -.
DR   CAZy; GH35; Glycoside Hydrolase Family 35.
DR   EnsemblFungi; CAP67543; CAP67543; PODANS_1_14400.
DR   GeneID; 6191490; -.
DR   KEGG; pan:PODANSg3905; -.
DR   eggNOG; KOG0496; Eukaryota.
DR   eggNOG; COG1874; LUCA.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000001197; Chromosome 1.
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:UP000001197};
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:CDP23804.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001197};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     22       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        23   1082       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5007638991.
FT   DOMAIN      455    630       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1082 AA;  121129 MW;  C60AF6A396E21A62 CRC64;
     MARLPSIIAM ISALSLMAPA LATIHYVMPN YTWQLNHTIS SGPGGGLPLP QLPVNSSTST
     PVSNPITNST SNFYTSSPFS YYNYNQERIK VRPEGWQGPA VTYDNNSLSV YGERIMLYSG
     EFHYFRLPRS PELWCDVLVK IKAMGFNAVS IYVPWMMLEP LRGEWDEVGW FDLDLFIGFA
     QTNGLYVIAR PGPYINGEVT GGGLPGWLQR TTPTLRTADL EFLQAAENYV VRVANLMAKW
     QVDNGGPVIL YQVENEYTMS TDSYKGFPDN GYMQWLIEKA KNASITIPII NNDAWPAGNS
     RPGIGVGEVD IYGHDLYPFG LDCSAKDWPE NATYTDLWSK HIGMSPGTPY TIPEGGAYDT
     WGSVGYDECV KLFDDVQARV LFKNSYAAGV KVFNVYMIFG GTNWGNLGDP YVYTSYDYGA
     AIAEDRTIGR PKYSELKLQA NFFKVSPGYL AAMPFENMTE GIVGFQMNST DDKLVATQLT
     GDFGTFYVIR HRDYRQTDDV AFTLKLPTAS GRWHLPAKSA NFVLSGRDSK LLVTDYPFGG
     FFMTYCSAEI LTWNSYNKTT IVIYGNIGEY HELRFTHPWT DPILESSGVN LFADINTTAA
     QWTIGPDRQW AVINNYVYMH FENRKSAYKY WTVDLVPAYS EGASSIIVYG GYLIRSAAET
     WLEGGITTGL ILMGDFNETT TLEIMNVPLL ARTLTVNSDP VNYTVNEHGN WVVTIDYKSA
     DNTGTPDLVT GIEWNYRDCL PEIQSDYNDS GWLRSVLMTN NTDTAPAYTP TSLYGSDYGF
     HTGVLLFRGH FQAARVKAAL NLYTQGGPGF AVSVWLNDQF LYSFDGNLGT EGNDTLYYLP
     DLEVNYDNLV NYNLTVLVDN MGLEENLIVG ANRMKSPRGI MNYGIFDETV HNIVMAIDWK
     LTGNWKGEYY ADKVRGPLNE GGLFAERMGY HLPGAPLSGD TSKNPFKDGL DKPGVGFWSA
     KLTINWDRIY DTPLSFVFQE TDESKRAANG CRAWLYVNGY QFGRYIPKFG PQNEFHVPDG
     IIYTNGTENH IAIAMWAPNE GGAKLPWLTL KSGHPVRSTR IWPGDMNSFV AESYYDGREG
     SY
//
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