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Database: UniProt
Entry: E5A3W5_LEPMJ
LinkDB: E5A3W5_LEPMJ
Original site: E5A3W5_LEPMJ 
ID   E5A3W5_LEPMJ            Unreviewed;      1014 AA.
AC   E5A3W5;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   16-JAN-2019, entry version 52.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=LEMA_P093980.1 {ECO:0000313|EMBL:CBX97989.1};
OS   Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race
OS   Av1-4-5-6-7-8) (Blackleg fungus) (Phoma lingam).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Pleosporomycetidae; Pleosporales; Pleosporineae;
OC   Leptosphaeriaceae; Leptosphaeria;
OC   Leptosphaeria maculans species complex.
OX   NCBI_TaxID=985895 {ECO:0000313|Proteomes:UP000002668};
RN   [1] {ECO:0000313|Proteomes:UP000002668}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8
RC   {ECO:0000313|Proteomes:UP000002668};
RX   PubMed=21326234; DOI=10.1038/ncomms1189;
RA   Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA   Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA   Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA   Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA   Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA   Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA   Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA   Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT   "Effector diversification within compartments of the Leptosphaeria
RT   maculans genome affected by Repeat-Induced Point mutations.";
RL   Nat. Commun. 2:202-202(2011).
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; FP929133; CBX97989.1; -; Genomic_DNA.
DR   RefSeq; XP_003841468.1; XM_003841420.1.
DR   STRING; 5022.CBX97989; -.
DR   CAZy; GH35; Glycoside Hydrolase Family 35.
DR   EnsemblFungi; CBX97989; CBX97989; LEMA_P093980.1.
DR   GeneID; 13285937; -.
DR   InParanoid; E5A3W5; -.
DR   OMA; PDETHEM; -.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000002668; Genome.
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:UP000002668};
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:UP000002668};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     19       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        20   1014       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5003195076.
FT   DOMAIN      392    569       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1014 AA;  111072 MW;  F0E0707928F11691 CRC64;
     MRVTDVLFSL ALASVHTQAV IARALSGKPA DFIIADKRAP LQDVVTWDEH SLFVHGERVI
     FWGGEFHPFR LPVPGLWLDI FQKIRALGYN GVSLYSAWVL HEPKRGDFSA EGLFDWEPYF
     DAAKKAGVYL VARPGPYINA EVSGGGFPGW LQRISGNLRT PDADYQEASK NYIESITPII
     AKAQITNGGP VILFQPENEY TMGMNNVTFP DADYMNGLMR QFRDLGIVVP LINNVAFPNG
     INAPGTDAPV DIYGHDSYPL GMNCTDPTYW IDDSLPTNWR ELHLNQSAST PYMLVEYQGG
     AFQPWGGDGF EKCAEFTNHE FERVFYKNNI AAGATIFNVY MTFGGTNWGN LGHAQGYTSY
     DYGATITEER QVYREKYSEA KLIAHFVQSS PALASAVPGY NTTGVYADNT AITITPLFSE
     KTSFYVSRQT KYNAVGSESY KLKLRTSAGN ITVPQLGGNL SIHGRDSKIH VADYEVGDFN
     VLYSTAEIFT WKRYGSRTVL VVYGGPNEIH ELAVSETSGG TVAEGSGVNL SNRNGNTILH
     WSSSPNRRVV RIGSDLYIVI LDRNSAYNYW TVNTLGDEAY SHEATPSSEL IIHAGYLIRN
     ATVAEGKINL VGDVNVTTTI EVIGGAHESI TGLTFNGVDV TAKLDRNGFL SGVVDFSVPA
     LTLPAMDSLA WKYIDTMPEI SNSYDDSLWT DADHTETNNT YWPLTTPTVL WGAEYGYNGG
     SLITRGHFTA TGNESVIHLN VSGGNAFAFT AWVNKTFIGS WPATGEAAIA NVTMNMPMLN
     RGEHYVLTVL SDHMGHNGNW FAGYNEMKTP RGIIGYDFPG HTVSSSNASR ANDGIKWKIT
     GNLGGEDLRD RTRGPLNEGA LWVERNGFHL PSAPTAEWAT STGPASGLSH PGVGFYIANL
     PLDMPSGWDI PLSFVFHGDA FNGQGKGWRA QLWVNGYHFG KFANGVGPQR RFPVPEGILN
     YQGDNMIAVS IWALEEGGAK PDGFELIAGM PVKSGYGLVP RAPMSSWEKR EAAY
//
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