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Database: UniProt
Entry: A0A1L9SEX3_9EURO
LinkDB: A0A1L9SEX3_9EURO
Original site: A0A1L9SEX3_9EURO 
ID   A0A1L9SEX3_9EURO        Unreviewed;      1002 AA.
AC   A0A1L9SEX3;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   13-FEB-2019, entry version 12.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OJJ45756.1};
GN   ORFNames=ASPZODRAFT_68809 {ECO:0000313|EMBL:OJJ45756.1};
OS   Penicilliopsis zonata CBS 506.65.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicilliopsis.
OX   NCBI_TaxID=1073090 {ECO:0000313|EMBL:OJJ45756.1, ECO:0000313|Proteomes:UP000184188};
RN   [1] {ECO:0000313|Proteomes:UP000184188}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 506.65 {ECO:0000313|Proteomes:UP000184188};
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; KV878344; OJJ45756.1; -; Genomic_DNA.
DR   EnsemblFungi; OJJ45756; OJJ45756; ASPZODRAFT_68809.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000184188; 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:UP000184188};
KW   Glycosidase {ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00108869};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184188};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     20       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        21   1002       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5012702232.
FT   DOMAIN      397    578       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1002 AA;  109981 MW;  69C67805C7F108F9 CRC64;
     MRPYKWALAL LSCLGAGAVA ENATDSQWPL DNDGLTNVVE WDHYSFLINN ERVFIFSGEF
     HYWRIPVPEL WIDILEKIKA LGFTTFSIYV NWGYHAPNNY TVDFSTEAHD ITPVFELAEK
     VGLYQLVRPG PYINAETNAG GFPLWLTTGA YGTLRDNDTR YIDALEPYWS KISQLTSDYM
     ITEGHNAICY QIENEYSDQW LTDATERVPN ETAIAYMEIL EASARANGIK IPLTVNEANT
     GALSWIPTWS DAGGNVDVTG LDSYPACWTC ATAACGDVVP YEVVDYYAYF QYSQPTLPSF
     MPEFQGGGYN PWGGPEGGCE NATGTEWVNL FYRWNVAQRV TAMSLYMIYG GTNWGATATT
     VTATSYDYSA AISEDRSIGT KYYEIKLLAL FTRSATDLTE TDMIGNGTQY TNNAAIKAFE
     LQNPKTKARF YPTFHNDTTS DTNEVFNLKV NTSEGALTIP RHGNSIRLNG HQSKIIVTDF
     TFGDKTLLYS TAEVLTYAIF DSKPTLVLWV PTGESGEFNI KGAKSGSVER CDGCSGVGFY
     PELGGVTVKF TQSEGMTVLS LNDGTRVVVL DRTTAYYFWA PALTNNPTVP DTESVLVQGP
     YLVRGATLSG STLSITGDVV NATTLEVFAP SSVTTIKWNG RKLSTSATSY GSRQVSLDAA
     PAIKLPALSS WKSNDSLPER FASYDDSGLA WVAADDMTTP NPEAPETLPV LYADQYGFHN
     GVRLWRGYFT GSATGVYLNV QGGEAFGWSA WLNGDLVGSW LGNADDELYN LTLSFSNVTV
     NTDSTNVLLV VHDDTGHDET TGALNPRGIL GAELQGRTNS TQFSHWRVAG TAGGESNLDP
     VRGVYNEDGL YAERVGWHLP GFDDSAWSDT TDPSDGFTGA TVRFYRTVVP LALPTDVDVS
     ISFLLSTVTD NTAFRVQLFV NGYQYGRFNP YIGNQVVFPV PPGILDYQGD NTIGLAVWAQ
     TEAGAQVGLD WRVNYVADSS LDVSFDGSAL RPKWTEERLQ YA
//
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