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Database: UniProt
Entry: A0A1L9VUK8_ASPGL
LinkDB: A0A1L9VUK8_ASPGL
Original site: A0A1L9VUK8_ASPGL 
ID   A0A1L9VUK8_ASPGL        Unreviewed;      1006 AA.
AC   A0A1L9VUK8;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   16-JAN-2019, entry version 10.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=ASPGLDRAFT_163873 {ECO:0000313|EMBL:OJJ87580.1};
OS   Aspergillus glaucus CBS 516.65.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1160497 {ECO:0000313|EMBL:OJJ87580.1, ECO:0000313|Proteomes:UP000184300};
RN   [1] {ECO:0000313|Proteomes:UP000184300}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 516.65 {ECO:0000313|Proteomes:UP000184300};
RX   PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA   de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA   Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K.,
RA   Battaglia E., Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C.,
RA   Canovas D., Cerqueira G.C., Chen F., Chen W., Choi C., Clum A.,
RA   Dos Santos R.A., Damasio A.R., Diallinas G., Emri T., Fekete E.,
RA   Flipphi M., Freyberg S., Gallo A., Gournas C., Habgood R., Hainaut M.,
RA   Harispe M.L., Henrissat B., Hilden K.S., Hope R., Hossain A.,
RA   Karabika E., Karaffa L., Karanyi Z., Krasevec N., Kuo A., Kusch H.,
RA   LaButti K., Lagendijk E.L., Lapidus A., Levasseur A., Lindquist E.,
RA   Lipzen A., Logrieco A.F., MacCabe A., Maekelae M.R., Malavazi I.,
RA   Melin P., Meyer V., Mielnichuk N., Miskei M., Molnar A.P., Mule G.,
RA   Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P., Overkamp K.M.,
RA   Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F., Ramon A.,
RA   Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA   Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E.,
RA   Sanguinetti M., Schuetze T., Sepcic K., Shelest E., Sherlock G.,
RA   Sophianopoulou V., Squina F.M., Sun H., Susca A., Todd R.B., Tsang A.,
RA   Unkles S.E., van de Wiele N., van Rossen-Uffink D., Oliveira J.V.,
RA   Vesth T.C., Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B.,
RA   Baker S.E., Benoit I., Brakhage A.A., Braus G.H., Fischer R.,
RA   Frisvad J.C., Goldman G.H., Houbraken J., Oakley B., Pocsi I.,
RA   Scazzocchio C., Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S.,
RA   Grigoriev I.V.;
RT   "Comparative genomics reveals high biological diversity and specific
RT   adaptations in the industrially and medically important fungal genus
RT   Aspergillus.";
RL   Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
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; KV878890; OJJ87580.1; -; Genomic_DNA.
DR   EnsemblFungi; OJJ87580; OJJ87580; ASPGLDRAFT_163873.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000184300; 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:UP000184300};
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:UP000184300};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     18       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        19   1006       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5012544301.
FT   DOMAIN      395    572       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1006 AA;  110754 MW;  276610439F857B0D CRC64;
     MKLLTLCAVA SLATQAVGAA IKHKLNGFTI TEHPDPVKRD LLQKYVTWDD KSLSINGERI
     MIFSGEFHPY RLPVPSLWLD VLQKVKALGF NCISFYTDWA LLEGKPGDYR AEGIFALEPF
     FEAAKEAGIY LLARPGPYVN AESSGGGFPG WLQRVNGTLR TADRGFLDAT DNYIATIGAS
     IAKAQITNGG PVILYQPENE YTNGCCGEEF PDPDYFQYVI DQARDAGIVV PMISNDASPD
     GHNAPSTGKG AADIYGHDSY PLGFDCANPS VWPEDNLPTN FWTLHEEQSP TTPYSLVEFQ
     AGAYDPWGGP GFAACADLVN HEFERVFYKN NFSFRVAISN LYMIFGGTNW GNLGHPGGYT
     SYDYGSVLSE TRNITREKYS ELKLFGNFVK VSPSYLLADP GNQTTGYTDT SSLTVTPLKA
     DGSTSYYVVR HTDYSSQAST PYKLRLAISS GNVTVPQLGG ELSLNGRDSK VHVADYDVSG
     TNIVYSTAEI FTWKKFADSK VLVLYGGPGE HHELAIASKS EASVIEGSQS DIKSKRIGSS
     VVISWDVSST RRIVQVDNLK IFLLDRNTAY NYWVPELPAE GTTPGYSNKK NTASSIIVKA
     GYLVRTAYLK DSDLHLTADF NTTTPIEVIG APENAQTLYI NNEKVSHKVD KNGIWTSEVE
     FTAPKIDLPS LEDLEWKYLD TLPEIQSSYD DSAWSKADKP TTDNDHRPLD TPTSLYSSDY
     GFHTGYLVYR GSFIAQGNES TFFIHTQGGQ AFGSSVWLNQ TLLGSWTGLN QDSDNNSTYK
     LPSLQQGKNY VFTVVVDNMG LDENLDVGAD VMKNPRGILN YSVSGRSLDA IKWKLTGNLG
     GEDYQDKVRG PLNEGGIYAE RYGFHQPEPP SADWKSSSPL DGLSQPGIGF YSTNFDLSIP
     SGYDVPIYFN FGNTTDPAPF RAQLYVNGYQ YGKYISNIGP QTSFPVPEGI LNHRGTNWVA
     VSLWALGEEG AKLSSFEFSH ERPVRTGLKE VEAAEQPKYE AREGVY
//
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