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Database: UniProt
Entry: A0A1L9UMX1_9EURO
LinkDB: A0A1L9UMX1_9EURO
Original site: A0A1L9UMX1_9EURO 
ID   A0A1L9UMX1_9EURO        Unreviewed;       994 AA.
AC   A0A1L9UMX1;
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:OJJ73074.1};
GN   ORFNames=ASPBRDRAFT_205377 {ECO:0000313|EMBL:OJJ73074.1};
OS   Aspergillus brasiliensis CBS 101740.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=767769 {ECO:0000313|EMBL:OJJ73074.1, 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; KV878682; OJJ73074.1; -; Genomic_DNA.
DR   EnsemblFungi; OJJ73074; OJJ73074; ASPBRDRAFT_205377.
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    994       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5012521737.
FT   DOMAIN      379    557       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   994 AA;  108671 MW;  D6C3913CEC97F9DA CRC64;
     MKLQFILSCW AILVARIWAI TDGLTDLVAW DPYSLTVNGN RLFVYSGEFH YPRLPVPEMW
     LDVFQKMRAH GFNTVSLYFF WDYHSPINGT YDFETGAHNI QRLFDYAQEA GIYIIARAGP
     YCNAEFNGGG LALYLSDGSG GDLRTSDATY HQAWTPWIER IGKVIADNSI TNGGPVILNQ
     IENELQETTH SASNTLVEYM EQIEEAFRAA GVDVPFTSNE KGQRSRSWST DYEDVGGAVN
     VYGLDSYPGG LSCTNPSSGF SVVRNYYQWF QNTSFTQPEY LPEFEGGWFS AWGAGSFYDQ
     CTSELSPQFA DVYYKNNIGQ RITLQNLYML YGGTNWGHLA APVVYTSYDY SAPLRETRQI
     RDKLSQTKLV GLYTRVSSGL LGVEMEGNGT SYTSTTSAYT WVLRNPNTTA GFYVVQQDTT
     SSQTDITFSL NVNTSAGALT LPNINLQGRQ SKIISTDYPL GHSTLLYVST DIATYGTFGD
     TDVVVLYARS GQEVSFAFKN TTKLTFEEYG DSVNLTSSSG NHTITSYTYT QGSGSSVVKF
     SNGAIFYLLE TETAFRFWAP PTTTDPYVTA EQQIFVLGPY LVRNASISGS VVDLVGDNDN
     ATTVEVFAGS SAKTVKWNGK EITVKKTDYG SLVGSIGGAD SSSITLPSLT GWKVRDSLPE
     TQSSYDDSKW TVCNKTTTLS PVDPLSLPVL FASDYGYYTG IKIYRGRFDG ANVTGANLTA
     QGGLAFGWNV WLNGDLVASL PGDADETSSN AVINFSNHTL KQTDNLLTVV VDYTGHDETS
     TGDGVENPRG LLGATLNGGS FKSWKIQGNA GGAAGAYELD PVRAPMNEGG LLAERQGWHL
     PGYKAKSSDG WTDGSPLDGL NMSGVAFYLT TFTLDLPKNY DVPLGIQFTS PSTVDPVRIQ
     LFINGYQYGK YVPYLGPQTT FPIPPGIINN RDKNTIGLSL WAQTDAGAKL ENIELISYGA
     YESGFDAGDG TGFDLNGAKL GYQPEWTEAR AQYT
//
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