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Database: UniProt
Entry: A0A1L9MY49_ASPTU
LinkDB: A0A1L9MY49_ASPTU
Original site: A0A1L9MY49_ASPTU 
ID   A0A1L9MY49_ASPTU        Unreviewed;       952 AA.
AC   A0A1L9MY49;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   13-FEB-2019, entry version 10.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OJI81931.1};
GN   ORFNames=ASPTUDRAFT_933791 {ECO:0000313|EMBL:OJI81931.1};
OS   Aspergillus tubingensis CBS 134.48.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=767770 {ECO:0000313|EMBL:OJI81931.1, ECO:0000313|Proteomes:UP000184304};
RN   [1] {ECO:0000313|Proteomes:UP000184304}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 134.48 {ECO:0000313|Proteomes:UP000184304};
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; KV878205; OJI81931.1; -; Genomic_DNA.
DR   EnsemblFungi; OJI81931; OJI81931; ASPTUDRAFT_933791.
DR   Proteomes; UP000184304; 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:UP000184304};
KW   Glycosidase {ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00108869};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184304};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     19       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        20    952       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5012318377.
FT   DOMAIN      343    520       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   952 AA;  105462 MW;  FBF654ADAD545EC1 CRC64;
     MRLPVLLKLV VALATLCQAL SVSNNSSGAV TWDEYSLKVN GERVFINVYF FWSYHSASRD
     AYDFETGAHN IQRLFDMAKQ TGLWVIARPG PYVNAQTNAG GLALWGSDGS MGKLRTSDEA
     YHQAWLPYMR KVGQIIAANQ VTKGGPVILF QVENELRETS HKPNDTLVTY MEQLESVIRD
     VGITVPTTHN EQSTRYISWS RDYENVGGAV DIYGFDDYHA GFLVGNKCDG GTGFDVVRTY
     YQWFMNYAWS GPIYLAEFEG GRTLTWGAPQ NYDDCRSEHS TTFVDIYYKN NIGQRVTLQS
     IYEGYGGTNW GYYYMTPLRE TREQWAKLWQ TKLIQLFSGS ALDLLKTKMH GNGSGYSLST
     PDAYSWVLKN PDTQATFTVL QQNETPSTAT ITFSAYLNTS LGNVTVPGIQ LEGRQSKILV
     TDYKFGNQTL LYSSADVLTN AVLPRHDVLT LYLWEGQTGE FALRTSKNLT FEVYGASTVS
     STLHHGYQKI RYTQSTGSTV LRFSNGVIVL LLDQPTAWHF WAPSTSKYPS PRPDQKLFIL
     GPYLVRSASV NNEVLQVSGD NNGTTTLEGF IGSVPIKAIE WNGQLLTATK TPYGSYTAQI
     PGTENRSVTL PPLNHWHSAE SLPEIQPDFD DSRWTVANKN STLSPIAPLT LPVLFSSDYG
     FYAGAKIYRG YFDGIEHTAV NLTASGGLAF GWNAWLNGHL IGGHPGDPDL SATNMTLALP
     ASHLKTRNNV ITVLVDYHGH DETDIPNGAE NPRGILGAYL LRGGTRTATG FQLWKIQGNA
     GGSKNIDPVR GPMNEGGLYA ERLGWFLPGF LASNDKGFKS TSSPLDGISK SGVRFYVTTF
     DLDIDSDLDA PIGVSLSAPN GTIARVMLWA NGYQYGKYVP HIGPQTKFPI PPGIINNRGQ
     NTLALSVWAQ TDAGAKLDTV ELFTYGLYQT DFQFDRDWSY LQPRLEDRSI YS
//
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