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Database: UniProt
Entry: A0A194V1C2_9PEZI
LinkDB: A0A194V1C2_9PEZI
Original site: A0A194V1C2_9PEZI 
ID   A0A194V1C2_9PEZI        Unreviewed;       985 AA.
AC   A0A194V1C2;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   16-JAN-2019, entry version 13.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=VP1G_04969 {ECO:0000313|EMBL:KUI57656.1};
OS   Valsa mali var. pyri.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX   NCBI_TaxID=694573 {ECO:0000313|EMBL:KUI57656.1, ECO:0000313|Proteomes:UP000078576};
RN   [1] {ECO:0000313|Proteomes:UP000078576}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SXYL134 {ECO:0000313|Proteomes:UP000078576};
RA   Yin Z., Liu H., Gao X., Li Z., Song N., Ke X., Dai Q., Wu Y., Sun Y.,
RA   Xu J.-R., Kang Z.K., Wang L., Huang L.;
RT   "Genome Sequence of Valsa Canker Pathogens Uncovers a Specific
RT   Adaption of Colonization on Woody Bark.";
RL   Submitted (DEC-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; KN714702; KUI57656.1; -; Genomic_DNA.
DR   EnsemblFungi; KUI57656; KUI57656; VP1G_04969.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000078576; 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:UP000078576};
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:UP000078576};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     19       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        20    985       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5008266066.
FT   DOMAIN      388    566       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   985 AA;  106733 MW;  8EE77B925E5EF7AF CRC64;
     MRLTDILSVA ALALQGSNAL QGRPDQLFHP ERRELLQDVV TFDNYSLIIN GERVMIYSGE
     VHPFRLPVPS LWPDVFEKVK GLGLNTISVY IHWGALEGKS GDFIAEGPLA IEPFFQAAQE
     AGLYIIARPG PYINAEATGG GFPGWLQRIE GKLRTNATDY LSATDNYMAN VGALLAKYQI
     TNGGPVILVQ VENEYTIAVD GVVFPNGYYM LYIEDQLRNA GIVVPLINND ASPDGHDLPG
     TLGGVDIYGH DGYPLGFDCA NPSSWPSGAL PTYYRETHLE QSPATPYLIP EFQGGSFDPP
     GGVGFEKCAA LLNMEFERVF YKNNYAAGIT ILNLYMLFGG TNWGNIGHPG GYTSYDYGSV
     IREDRAVDRE KYSELKLQAN FLKVSPGYLL AAAANSSSTG IYNTNSDIVT TPVIGVNGTG
     SFFIVRHSDY TSESSSTYNL SLPTSQGDIS IPQLGGSLSL NGRDSKVHVT DYPVGDSKLL
     YSTAEIFTWQ AYDDKKVLVV YGGPNELHEL AVLGASNGTL VEGDGVKIQK TNSSTVAQWQ
     TSTDRRVLQV GNLYIYILDR NSAYNYWVAE TTDGAVIVNG PYLVRSASVD GTTLSLRADF
     NKTTTIEIIS APSAITALQV NNVTLNYTAA VGIQTYSPPD FNIPDLSTAT WYYIDSLPEI
     STGYDDSAWP DANHTNTTNP IGSPLLTPVS LYGSDYGFNT GSLLFRGHFT AAGNESTIAL
     WTQGGEAYGA SVWLNGTFIG SWAGTAPAED QNSTFTLPNL TAGKEYVFTI LIDNMGLDEN
     YDVGADEEKD PRGILDYDFA SDITWKITGN LGGEDYADRV RGPLNEGGLF VERQGYHQPA
     PPVEEEFTSG KSPYEGISSA GVAYYTTNFT LSIPSDKWDV PLSLVFTNDT SAAADAPYRA
     LIYVNGYQFG RYTSNIGPQT AFPVPEGVLD YNGENWLGIT LWALGSDGAT VPGLNWTIGS
     TPVLTGRKTP TLVEQPAWSE RPGAY
//
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