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Database: UniProt
Entry: G2WQS5_VERDV
LinkDB: G2WQS5_VERDV
Original site: G2WQS5_VERDV 
ID   G2WQS5_VERDV            Unreviewed;       889 AA.
AC   G2WQS5;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   16-JAN-2019, entry version 40.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=VDAG_00717 {ECO:0000313|EMBL:EGY14035.1};
OS   Verticillium dahliae (strain VdLs.17 / ATCC MYA-4575 / FGSC 10137)
OS   (Verticillium wilt).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Glomerellales;
OC   Plectosphaerellaceae; Verticillium.
OX   NCBI_TaxID=498257 {ECO:0000313|Proteomes:UP000001611};
RN   [1] {ECO:0000313|Proteomes:UP000001611}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VdLs.17 / ATCC MYA-4575 / FGSC 10137
RC   {ECO:0000313|Proteomes:UP000001611};
RX   PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA   Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA   Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA   Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R.,
RA   Santhanam P., Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z.,
RA   Inderbitzin P., Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R.,
RA   Galagan J., Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT   "Comparative genomics yields insights into niche adaptation of plant
RT   vascular wilt pathogens.";
RL   PLoS Pathog. 7:E1002137-E1002137(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; DS572695; EGY14035.1; -; Genomic_DNA.
DR   RefSeq; XP_009650389.1; XM_009652094.1.
DR   EnsemblFungi; EGY14035; EGY14035; VDAG_00717.
DR   GeneID; 20702180; -.
DR   KEGG; vda:VDAG_00717; -.
DR   InParanoid; G2WQS5; -.
DR   OMA; YFAPGPP; -.
DR   Proteomes; UP000001611; 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; -; 1.
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; 1.
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; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000001611};
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:UP000001611}.
FT   DOMAIN      417    586       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   889 AA;  99034 MW;  CEDAA7B39A9CA0EE CRC64;
     MSICRTDQNR WRWTVPEIDE PFSACQFRRY ATTCMDMILP LLASTWLSGV SAVAADAGIQ
     SLHERQQKIV TYDGNSVLIN GERLMLFSAE FHAFRMPVPS LWLDILQKIK AMGYNCVSFY
     VNWGLVEAKP GEVRAEGIFS LEPLFEAAQK AGLYLFARPG PYVNAEVTGG GFPGWLQRVQ
     GALRTSDEAY LKATDNYTSE IGRIIADAQI TNGGPVILFQ MENEYMFAVE PYPFPDFDYW
     NYVDNQFRSV GVVVPYVNNE AWKLGGVTPT TPASVDIYGF DSYPLGFDCW NPNQWPAQGL
     PTDWLQRHRE ISPNTPFTIV EFQGGGFQPW GGAGFESCAG LLNHEFERVL FKHAYAAGAT
     LFNVYMTWGG TNWGNLGHSD GYTSYDYGAQ ITEERLVNRE KYSESKLQAN FFHVSPAYLE
     AERHFASLDW TDNAAITVTP ATTNTTKFYF TRHTQYSSLE TVAYKLTVDT VEYGNLTVPQ
     LSESLFLTRR DSKIHVSDYA VGDKTLVYST AEIFTWKQYK DKTVLVVYGG PNEHHELAVE
     GKGDAEVIEG SDVETDQKDG YTILNWEVTE DRKVVRVHKD LYAYNYWVPP TEADLGTADV
     IVKAGYLVRT VSIDGSSLSF VGDVNATTPI EVIGGAPTSL KALEFNGKAL DFEQDDSGVV
     SAVIEFKTPD IKLPCLSRLK WKYLDSLPEI QSDYSDDAWL DADRDTLNIA NPLDTPKSLY
     GGDYGFHTGS LLFRGRFTAN GEEASSGNAL DLTTQGGNAY GTSVWLNDQF IGSWVGNAVA
     PAHNSTFDLP KLTEGEEYII TVVVDHMGMN GNWVVAEEQQ KNPRGILNYA LSGHKQSDIA
     WKITGNLGGE DYADDDRGPL NEGGLFAERQ GYHWPQPPSD SWDDSKGHD
//
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