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Database: UniProt
Entry: A0A1L9ULI7_9EURO
LinkDB: A0A1L9ULI7_9EURO
Original site: A0A1L9ULI7_9EURO 
ID   A0A1L9ULI7_9EURO        Unreviewed;       993 AA.
AC   A0A1L9ULI7;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   13-FEB-2019, entry version 9.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OJJ72527.1};
GN   ORFNames=ASPBRDRAFT_74480 {ECO:0000313|EMBL:OJJ72527.1};
OS   Aspergillus brasiliensis CBS 101740.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=767769 {ECO:0000313|EMBL:OJJ72527.1, 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|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; KV878683; OJJ72527.1; -; Genomic_DNA.
DR   EnsemblFungi; OJJ72527; OJJ72527; ASPBRDRAFT_74480.
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; 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.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000184499};
KW   Glycosidase {ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {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    993       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5013267923.
FT   DOMAIN      384    561       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   993 AA;  109970 MW;  700E3757008E569D CRC64;
     MKLPLLLNFA VILASLCQAL SVSNNSTGAV TWDEYSLLVN GERVFINAAE FHYQRLPVPE
     MWLDVLQKLK ANGFNTISVY FFWSYHSASR DAYDFETGAH DIQRLFDMAK QTGLWVIARP
     GPYVNAQTNA GGLALWGSDG SMGKLRTSDE AYHQAWLPYM RKVGQIIAAN QITRGGPVIL
     CQVENELQET SHDPNNTLVT YMKQIELVLK EVGITVPTTH NEKGMRSQSW SRDYENVGGA
     VDIYGLDSYP GGFLVGNKCD GATGFDVVRT YYQWFMNYSW TGPIYLAEFE GGRTLPWGAP
     QNYDECRSEH STNFADIYYK NNVGQRVTLQ SIYEGYGGTN WGHSACPVAY TSNDYMTPLR
     ETREQWAKLW QTKLVQLFSE STPNLLKTYM LGNGSGYSVS TAEAYSWVLK NPDTQATFTV
     LQQNETPSTA TITFSAYLNT SLGNITVPGI QLEGRQSKIV VTDYRFGNQT LLYSSADILT
     NGVFPGYEVL TLYLWEGQSG EFALKTSKNL AYEVYGASTV SSTLLAGYQR IRYTQAAGST
     VLHFSGGVIV LLLDQPTAWY FWAPSTSKYP SPRPDEKFFI LGPYLVRSAS VNDEVLQVSG
     DNNGTTILES FIGDVSIKAI EWNGQRLTAT KTPYGSYTAR IPGTENRSVS LPSLNHWYSA
     DSLPEAQPGY DDSRWTVADK NSTLSPQPPL TLPVLFSSDY GYYTGAKVYR GYFDGSNYTA
     VNITASGGLA FGWNAWLNGH LIGGHTGDPN LSSTNMTLTL PLPFLRTRKN VITVLVDYHG
     HDETSTDDGV ENPRGILGAY LLPGGTRTAT GFQLWKIQGN AGGSKNIDPV RGPMNEGGLY
     AERLGWFLPG FPASDHKDFN SSSSPLDGIS KSGVRFYVTT FDLDIDSDLD APIGISLSAP
     NGTIARVMLW INGYQYGKYV PHIGPQTKFP IPPGIINNRG QNTLALSLWA QTDAGAKLDT
     VELFTYGLYQ TGFQFDRDWS YLQPRWEDRS VYA
//
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