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Database: UniProt
Entry: A0A1R3S1E1_ASPC5
LinkDB: A0A1R3S1E1_ASPC5
Original site: A0A1R3S1E1_ASPC5 
ID   A0A1R3S1E1_ASPC5        Unreviewed;      1213 AA.
AC   A0A1R3S1E1;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   16-JAN-2019, entry version 11.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=ASPCADRAFT_511526 {ECO:0000313|EMBL:OOG00557.1};
OS   Aspergillus carbonarius (strain ITEM 5010).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=602072 {ECO:0000313|EMBL:OOG00557.1, ECO:0000313|Proteomes:UP000188318};
RN   [1] {ECO:0000313|Proteomes:UP000188318}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ITEM 5010 {ECO:0000313|Proteomes:UP000188318};
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; KV907493; OOG00557.1; -; Genomic_DNA.
DR   EnsemblFungi; OOG00557; OOG00557; ASPCADRAFT_511526.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000188318; 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:UP000188318};
KW   Glycosidase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108869, ECO:0000313|EMBL:OOG00557.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000188318};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     19       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        20   1213       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5012661386.
FT   DOMAIN      594    769       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1213 AA;  132775 MW;  9327CB4202AC2941 CRC64;
     MGSGGWGWGV GVGVYVAFGG SVPVLDDVDV DVGGLGGGGG DISHEKDVCE ALVRTVAVEG
     RVFGLGAWGG LSAYGSGGGA GAGDAVGDVH SHSVMWKKRS RSVTAEGPHE IVWPEVHPRD
     QDEEQENDED EGVSPGIRRS ITAEGPHEIV WPERHADEEM VSPKRKEEKK PGTGMGRGRA
     ESAWMVSPFG EMLASNDGDS GDRLLVREID LEDCIRARWD RDEEIVTWDD KSLFVYGERV
     LLLSGEFHPF RLPSPGLWLD VFQKVRAIGY SAVSFYVDWA LLEGQPGHIR TQGVFDLEPF
     FAAAQEAGLY LIARPGPYIN AEVSGGGFPG WLQRLDGPLK RTDSPYLDAI TPYIATVGEI
     IARAQITNGG PVILVQAENE YTLCMTETGY TQMNNETVTA ANNSCLETEY MAYVEDQYRQ
     AGIVVPLIVN DAEPLGDFAP GTGVGAVDIY SFDFYPLQWS TAPRNASDWS SLNNPLEWYN
     YTVHEEQSPT TPVSISEFQG GVPDAWGGVG VDTSAAYIGP EFERVFYKLN YGYRVALQNL
     YMIFGGTNWG NLGHPGGYTS YDVGAAIMED RQVIREKYSE LKLQAGFLQA SPAYLISQPD
     NGTYGVYTNS TMLATTRLHT NTTNFYMVRH GELGANHTIQ YTLQLSTSIG DINIPQLGGS
     LSLHRRDSKI HVVDYDVGGI NLIYSTAEVF SWKKAGNKSV LILYGGEGET HEFAVPSTLS
     PSAVEGDGLL INSSTSTVIQ WSVQPSRRVV HFGDQLEVHL LWRNEAYNYW VLDLPLPGPI
     SRHSSPSRAN SSVIIQAGYL LRTASITGPT LTLTGDLNAT TELEIIAAPS SISTIRFNNQ
     QLTTTTNTHG RLHATVPYQP PAFTLPSLSS LPWHFLDSLP ELHPTYNDTL WTPCNHTTTR
     NPRNLTTPTS LYSSDYGYNT GSLLYRGTFT ATGSETALSL LTEGGYAYGH SIWLNSTFLS
     SWPGSPAEMF HNQSLPLPAL HQGEPYTFTI LIDHMGNDEN FPANGAIMKD PRGILDYTLH
     GRTKDSISWK VTGNLGGEAY LDHSRGPLNE GGLYVERMGY HLPGAPIHHW KKVTSPTDEV
     ISTPGVGLWA THFDLDLPLG YDIPLSVVFT NTSTIVTNTT DVSPAEFRAQ IFINGWQFGK
     YVNHIGPQTH FPIPEGILNY NGSNYLAVTI WAMDTRTFQL AGLEVQAGAV VKSAYRKPGL
     VRGEGYVRRI GEY
//
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