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Database: UniProt
Entry: A0A1L9NB59_ASPTU
LinkDB: A0A1L9NB59_ASPTU
Original site: A0A1L9NB59_ASPTU 
ID   A0A1L9NB59_ASPTU        Unreviewed;      1014 AA.
AC   A0A1L9NB59;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   13-FEB-2019, entry version 11.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OJI86526.1};
GN   ORFNames=ASPTUDRAFT_27556 {ECO:0000313|EMBL:OJI86526.1};
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:OJI86526.1, 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; KV878187; OJI86526.1; -; Genomic_DNA.
DR   EnsemblFungi; OJI86526; OJI86526; ASPTUDRAFT_27556.
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     20       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        21   1014       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5012838015.
FT   DOMAIN      402    584       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1014 AA;  111394 MW;  79889667921A4BAA CRC64;
     MTRITKLCAL LLSSTGLLAA AQNQTETGWP LYDDGLTTDI QWDHYSFKVH GERIFVFSGE
     FHYWRIPVPG LWRDILEKIK AAGFTTFSIY SSWAWHAPNN HTVDFSTGAR DITPIFELAK
     ELGMYIIVRP GPYINAEASA GGFPLWLTTG DYGTLRNNDS RYTEAWKPYF EKMTEITSRY
     QVTNGQNTFC YQIENEYGDQ WLSDPSERVP NETAIAYMEL LESSARENGI LVPFTANDPN
     MNAMAWSRDW SNAGGNVDVV GLDSYPSCWT CDVSQCTSTN GEYVAYQVVE YYDYFLDFSP
     TMPSFMPEFQ GGSYNPWAGP EGGCGDDTGV DFVNLFYRWN IAQRVTAMSL YMLYGGTNWG
     AIAAPVTATS YDYSSPISED RSISSKYYET KLLSLFTRSA RDLTMTDLIG NGTQYTNNTA
     VKAYELRNPT TNAGFYVTLH EDSTVGTNEA FSLRVNTSAG NLIVPRLGGS IRLDGHQSKI
     IVTDFTFGSE TLLYSTAEVL TYAVLDKKPT LVLWVPTGES GEFAVKGAKS GSVVSKCQGC
     SAINFHQQGG NLVVGFTQAQ GMSVVQIDND IRVILLDRTA AYEFWAPALT EDPLVPEDEA
     VLIQGPYLVR SASLEKSTLA IKGDSINETA VEIFAPKDVK TVTWNGKQLK TSKSSYGSLK
     ATIAAPVSIQ LPAFTSWKVN DSLPERLPTY DASGPAWVDA NHMTTANPSK PATLPVLYAD
     EYGFHNGVRL WRGYFNGTAS GVFLNVQGGS AFGFSAYLNG HFLGSYLGNA SIEQANQTFV
     FPTNITHQAT QNTLLIIHDD TGHDETTGAL NPRGILEARL LPSSTDNTTS PEFTHWRLAG
     TAGGESNLDP VRGAWNEDGL YAERVGWHLP GFDDSTWPSV SSSSLSFTGA TVKFFRTTIP
     LNIPRGLDVS ISFVLGTPNN APNAYRAQLF VNGYQYGRFN PYIGNQVVFP VPVGVLDYSG
     ENTIGVAVWA QTEDGAEITV DWKVNYVADS SLDVAGLETS GLRPGWSVER LKFA
//
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