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Database: UniProt
Entry: A0A1L9U2X3_9EURO
LinkDB: A0A1L9U2X3_9EURO
Original site: A0A1L9U2X3_9EURO 
ID   A0A1L9U2X3_9EURO        Unreviewed;      1020 AA.
AC   A0A1L9U2X3;
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=ASPBRDRAFT_138831 {ECO:0000313|EMBL:OJJ66046.1};
OS   Aspergillus brasiliensis CBS 101740.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=767769 {ECO:0000313|EMBL:OJJ66046.1, ECO:0000313|Proteomes:UP000184499};
RN   [1] {ECO:0000313|Proteomes:UP000184499}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 101740 {ECO:0000313|Proteomes:UP000184499};
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; KV878702; OJJ66046.1; -; Genomic_DNA.
DR   EnsemblFungi; OJJ66046; OJJ66046; ASPBRDRAFT_138831.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000184499; 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:UP000184499};
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:UP000184499};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     19       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        20   1020       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5012408797.
FT   DOMAIN      398    579       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1020 AA;  112687 MW;  70AA05EE6FB1C3FD CRC64;
     MNWVYQLLLS FLWHVLLFAI STDQSRLHIP HTPDPLAEQP TGLVTWDEYS IFVRGERILL
     FSGEFHPFRL PSPGLWLDVF QKIRALGYSA VSFYLMWGLL EGAPEHFHSD GVFDLQPFFD
     AASQAGIYLI ARPGPYINAE VSGGGLPGWL QRLRGDVRSV APDYLNATRN YITRTGEIIA
     RAQITNGGPV ILFQPENEYT MCSGFTSVGE ISACLDGNYM SGVEAQYREA GIVVPFISND
     AVPLGNWAPG TGKGAMDIYG YDDYPFGWGT GCQDPYNWTR ILDPLTLSNF STHLAMSPDT
     PYAILEYQGG APDPWGGNGV STCAAMIGAE FARVFYKVNF SLRATIVNLY MMFGGTNWGN
     LGYPSGYTSY DVGAPISEDR LLAREKYHEI KLQAQFVQSS PAYMVSRPLL APSRYSNASN
     LDIAVLHGDP TKFYTVRHAN YGELASTYYH INLETSFGNF TVPTLGGSLV LHGWDSKIHV
     TDYQMGDISL VYSSAEIYTW KRSGHKTILL MYGGEAEQHE FAVPIPSDYV KVLEGNETTY
     RGSDNLTFVQ WTVSLTRQVI SFSDKLDVYL LWRNDAYNYW VIDLPLPPPV GLHVSPSREN
     TSVIVKGGYL IRNATISGDV LSLTGDLNAT TEIEVVAAPS GCCSGLVFNG ETVKTSVENG
     RLKGLLKYQA PAIALPDLAT ANWQYLDSLP ELGPRYDDST WTLCDHVSTN NPRRLSTPTS
     LYASDYGYHA GSILYRGHFV ANGAESSFSL SSQGGYAFAH SVWLNSTFLG AWPGDPAVQT
     YNQTLQFPNR LEFGVPYVLT VLIDNMGLDA NFYANLQTMK NPRGILDYRL SGHEDKADII
     WRITGNYEGE RRRDLSRGPL NEGATFAERQ GFHLPGTPTQ GWQHSSPLDG LSGPGVGFYA
     TTFNLSFPYG YDIPTSVIFA NSSAIGDHTT AGRFRISLYV NGWQFGKYVN NIGPQTSYPI
     PEGILNHHGE NYLALVFWAL DRNGAKLGDI QIGTSAIIQT GYSLPNMVRA SEYAIRGDSH
//
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