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Database: UniProt
Entry: A0A1L9WZ41_ASPAC
LinkDB: A0A1L9WZ41_ASPAC
Original site: A0A1L9WZ41_ASPAC 
ID   A0A1L9WZ41_ASPAC        Unreviewed;      1010 AA.
AC   A0A1L9WZ41;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, 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=ASPACDRAFT_1866893 {ECO:0000313|EMBL:OJK01423.1};
OS   Aspergillus aculeatus ATCC 16872.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=690307 {ECO:0000313|EMBL:OJK01423.1, ECO:0000313|Proteomes:UP000184546};
RN   [1] {ECO:0000313|Proteomes:UP000184546}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 16872 {ECO:0000313|Proteomes:UP000184546};
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; KV878974; OJK01423.1; -; Genomic_DNA.
DR   RefSeq; XP_020057762.1; XM_020197887.1.
DR   SMR; A0A1L9WZ41; -.
DR   EnsemblFungi; OJK01423; OJK01423; ASPACDRAFT_1866893.
DR   GeneID; 30971701; -.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000184546; 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:UP000184546};
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:UP000184546};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     19       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        20   1010       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5012499408.
FT   DOMAIN      395    576       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1010 AA;  110050 MW;  A46CAF9F889084FD CRC64;
     MRFLAVCGAA LLAVHAAGAA VKHRFNGFTL TEHPDAAKRD LSQKYVTWDD KSLFINGERI
     MIFSGEVHPY RIPVPTLYID IFQKIKALGF NTVSFYVDWA LLEGKPGEYR ADGVFALEPF
     FEAAAEAGIY LLARPGPYIN AEVSGGGFPG WLQRVDGILR SSDKPYLEAT DNYIAHVAAT
     IAKYQITNGG PIILYQPENE YSGSSGNVTF PDPVYMQYVL DQARNAGIVV PFISNDASAS
     GHNAPGTGEG SVNIYGHDSY PLGFDCANPS TWPAGNLPTN FRTLHLEQSP TTPYSIVEFQ
     AGAFDPWGGP GFAKCAALVN HEFERVFYKN DFSFGVAILN LYMTFGGTNW GNLGYANGYT
     SYDYGSPLTE SRNLTREKYS ELKLLGNFAK ASPGYLLATP GNLTTSGYAD TSDITVTPLL
     GSNNTGSFFV VRHSDYTSQA STSYMLKVPT SAGSLTIPQL GGSLSLNGRD SKIHVVDYDV
     SGTNILYSTA EVFTWKKFSD GKVLVLYGGA DEHHELAITT KSNVTVVEGK ASAISSKQTG
     KSLVIGWDVS STRQIIKVGD LQIHLLGIDR NSAYNYWVPQ VGKDSTSTEF STQAAVASSI
     IVKAGYLVRT AYVKGNGLYL TADFNATTPI EVFGAPATTR NLYINGEKTS HTVAKNGAWT
     TEVEYSAPKI SLPSLKGLSW KYLDTLPEIQ SSYDDSLWIA ADLSETKNTF RSLTTPTSLY
     SSDYGFHTGY LIYRGRFVAT GDETTFTVDT QGGTAFGSSI WLNDTFLGSF TGLFIYADYN
     QTVTLPKLKS GKEYVFTVVV DNLGLDEDWT VGSELMKAPR GILNYDLAGH DASDISWKLT
     GNLGGEDYQD KTRGPLNEGG LYAERQGYHQ PQPPSQKWKS ASPLDGLSKP GIGFYSAEFE
     LDLPTGWDVP LFFNFANSTT PDAYRAQLYV NGYQYGKYVS NIGPQTSFPV PQGILNYQGT
     NWIALSVWAQ NEGGAKVEGL ELSYETPVLT ALKGVKSVDQ PKYKARKGAY
//
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