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Database: UniProt
Entry: A0A1L9SF93_9EURO
LinkDB: A0A1L9SF93_9EURO
Original site: A0A1L9SF93_9EURO 
ID   A0A1L9SF93_9EURO        Unreviewed;       997 AA.
AC   A0A1L9SF93;
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:OJJ45757.1};
GN   ORFNames=ASPZODRAFT_68401 {ECO:0000313|EMBL:OJJ45757.1};
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:OJJ45757.1, 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; OJJ45757.1; -; Genomic_DNA.
DR   EnsemblFungi; OJJ45757; OJJ45757; ASPZODRAFT_68401.
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     23       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        24    997       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5012792795.
FT   DOMAIN      382    559       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   997 AA;  109264 MW;  3B67DB0F4086C984 CRC64;
     MRLSALLSFF LSLLVWRAST VSGTSDGNTT LVTWDEYSLS VRGERVFIFS GEFHYHRLPV
     PEMWLDVLQK LKANGYNAVS VYFLWNYHSA SEGVFDFETG AHDIQRFFDY AKQAGVYIIA
     RPGPYINGET TAGGFALWAA NGKLGDARTS DETYHQAWLP WILEVAKILK ANQITEGGPV
     ILHQNENELQ ETVHSADNTL VLYMEQIIAA YAEAGIVVPS SSNEKGMRSM SWSTDYEDVG
     GAVNVYGLDS YPGGLSCTDV DTGFEVLHTY YEWFQNYSYT QPEYFPEFEG GWFEAWGGSF
     YDTCTSELSP QFADVFYKNN LGQRVTMQSL YMSFGGTNWG HFPAPVVYTS YDYSAPLRET
     RQIRDKLRQI KLIGLFTRVS ADLRKTVMEG NGTTYTNSSS IWTWVIRNPD TQARFYVTQQ
     ADTSTFDSVK FDLNVTTSAG AVTLSDINLD GRQSKIIVTD YTISSSTTLL FSSAEVLTYA
     NLDVDVIAFY LDVGQVGHFA FKDAANLTFT TYGSTSLTTA ASSAHSTVYT YTQGTGVTAV
     KFSNGLVAYL LDRDSAWYFW APPTTSDPNV KPDQHIFVQG PYLVRNASVE GSTVKLVGDN
     ENTTTLEVFA DSSIKTVEWN GNKVSVKKTA YGSLVGSAPG AEDVEVSLPT LDSWKAQDSI
     PEINPAYDDS LWPVCNHTTT LNPVAPLTLP VLYSPDYGYH AGIKVYRGRF DGPTTTAANI
     TGANVTVQNG YAAGWSAWLN GEYVGGSLGG TADVSSTAVL PFNSSSLKAT DNLLTLLLDY
     TGHDEDDVSP AGTQNPRGIL GASLITENNG SITPPNFTSW RIRGNAGGEA NIDPVRGPLN
     EGGLYAERMG WHLPGYPVPT TDSSTDSPLD GVAGAAGRFY LTNFTLDLPA DLDVPLGLQL
     GSPADTAAVV HIYMNGYQFG HYLPHYGPQE VFPFPPGIIN NRGLNTLGIN LWSLTDAGAA
     LDTVQLISYG KYRSGFDFNS DWSYLQPAWK NDREKYA
//
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