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Database: UniProt
Entry: G2X3Z7_VERDV
LinkDB: G2X3Z7_VERDV
Original site: G2X3Z7_VERDV 
ID   G2X3Z7_VERDV            Unreviewed;       999 AA.
AC   G2X3Z7;
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_04734 {ECO:0000313|EMBL:EGY23296.1};
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; DS572702; EGY23296.1; -; Genomic_DNA.
DR   RefSeq; XP_009652633.1; XM_009654338.1.
DR   ProteinModelPortal; G2X3Z7; -.
DR   EnsemblFungi; EGY23296; EGY23296; VDAG_04734.
DR   GeneID; 20706197; -.
DR   KEGG; vda:VDAG_04734; -.
DR   InParanoid; G2X3Z7; -.
DR   OMA; GGEDYVD; -.
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; -; 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: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};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     21       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        22    999       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5003439081.
FT   DOMAIN      392    571       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   999 AA;  110028 MW;  89D078502DC724D2 CRC64;
     MQLKSLRALF LGLALATSVG AKGLGQNVHD IKQMGSRQAQ DIVTWDDHSL FINGERLMVF
     SGEFHPFRLP VQSLWLDILQ KIKASGYNCV SIYINWHLIE AERGQIRMDG IFDLNPFFEA
     AKKAGLYVLP RPGPYINAEV AGGGFPGWLT RTRGALRTYN EAFFNATDLY TREIGKVIAA
     HQITNGGPVI LFQPENEYQN TIDQELYPMP DYDYWKRVQN QYRDAGVIVP YINNEAHMNG
     YITAHTPASV DIYGHDSYPL GFDCENPTVW PDDGLPTDWL AINNAIAPDT PYTIPEYQGG
     GFQHWGDAGF ENCALLLNME FERVLYKNNY AVGATIFNIY MTYGGTNWGN LGHAEGFTSY
     DYGAQITEER LLWREKYSEV KLQANFFHVS PAFLEAERFN SSLDFTDNPG VTVTPARTNT
     TKFYISRHTQ YGTVDRVPYK LTVETAEHGD LVIPQLGDSL YLTRRDSKIH VSDYPVGDHT
     LIYSSAEVFT WKKYDEKTVL VLYGGPDEHH EIAIEGAGSA DSEVLEGSGV KIEDGDGQTI
     VAWDATTDRK LVRVHQNFYI YLVVRNEAYN FWVPPTGSGG DYGTSDVIVK AGYLVRTANV
     DASTLALVGD VNATTSIEIV GGAPAGLKTL TWNGQELSFE QSSHGVITAT VDFSPPEIKL
     PCFSQLKWKT IDSLPEIQPS YDDSLWADAN LTTSPNDKFP IKTPVSLYAS DYGFHTGSVI
     YRGHFTATTA ESTLNITLQG GHAFGASIWL DDQHLGSWPG SPSAPSGTLT MALPSLKPNT
     SHVLTVLIDL MGLNGNYVLG EDNLKTPRGI LAYSLSGHEP DAVKWKLTGN LGGERYADKK
     RGPLNEGGLF AERQGYHQPS PPSSSWAAGG PTSGRAAPGV SFYTAEFALD LPRGYDVPLA
     VRFGMSGEGN GAYRVQLFVN GFQFGKFVPH IGPQARFPVP EGILDYHGTN TVGITLWAME
     EGGARVEGMA WDVAMVTASG FGDVELTEAP IWEKREGAY
//
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