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Database: UniProt
Entry: A0A1L9Q491_ASPVE
LinkDB: A0A1L9Q491_ASPVE
Original site: A0A1L9Q491_ASPVE 
ID   A0A1L9Q491_ASPVE        Unreviewed;      1001 AA.
AC   A0A1L9Q491;
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:OJJ08595.1};
GN   ORFNames=ASPVEDRAFT_66505 {ECO:0000313|EMBL:OJJ08595.1};
OS   Aspergillus versicolor CBS 583.65.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1036611 {ECO:0000313|EMBL:OJJ08595.1, ECO:0000313|Proteomes:UP000184073};
RN   [1] {ECO:0000313|Proteomes:UP000184073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 583.65 {ECO:0000313|Proteomes:UP000184073};
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; KV878140; OJJ08595.1; -; Genomic_DNA.
DR   EnsemblFungi; OJJ08595; OJJ08595; ASPVEDRAFT_66505.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000184073; 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:UP000184073};
KW   Glycosidase {ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00108869};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184073};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     15       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        16   1001       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5012566887.
FT   DOMAIN      393    574       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1001 AA;  110845 MW;  9D6FAB9974D69F9C CRC64;
     MFLFFFLLYE ETSSCSKTEW PIRDTGLGKT VKWDHYSLIY NGERLFSFGG EFHPFRIPVP
     ELWVDILEKT KASGMNTMSF YNHWGFHMPA SNPESLDFES GAHDLGRLYE IAKELGLFVH
     ARPGPYINAE LNAGGMPLWL TTGEFGALRD NDTAWEAKWK PYMDRVAEIT APYQVSRNGT
     VLLFQIENEF PEQWADVEEK VPNPVPIAYM EELFEQMQAK GIEVPLTHNM PGQKYKSWSV
     DYDTVGAGGN VHIYGLDNYP SCWSCMPEDC GTSNPSFTLM DYTAHFNEVA AKQPSMMPEF
     QGGAMNPWDG PAGGCEAKTD DSFVNFYYRD NVAQSVTILG IYMFYGGTNW GWLAAPFVPT
     SYGYSAAIAE NRSIGAKYYE IKSLALFTRS ARDLTKTDLV GNSTSYSDNE AVTTIELRNP
     DTDAGFYAIR HTDPTSNDEQ AFRLSIRTSA GNFTVPALDD GAIALNGHIQ KILVTDFPFG
     SRNLIYSTAE VLTYGIFDEQ PTLALWVPNG EGGEFFVQGA RSGKVIAGGK SDVRFSRSQK
     GLIVSFKEHK GMAVILLDGD VRVVVMDRDT AHRFWAPALT NDPRVPANQV AFVQGPYLVR
     SAVFDNHTLS LLGDSSEATD IEVFTESRVR TIKWNGRTLR TYKTKYNTLK ASIDGPAEWS
     PPSFRAWKVH DSLPERFANY SDSGPAWANA DHMTTVSKYD EATKPYLYAD EYGFHAGVQL
     WRGYFSGSAG SVYLDVQGGT AHGWSAWLNG DFIGSFLGDL DSSSGSKELE LPSKSVKSGE
     NVLLVMQDNS GHDQGSGSLN VRGIINATLI DNKSGRFSAW KVAGTAGGAS NTTIDPVRTY
     YNEGGLTAER LGWHLPGFDD SGWSTSTPSD GFSGAGAKFY RGILPLDTPE GHDVALSVKI
     SFDEEASEKS TFRAYLYVNG YQYGRYYPYI NSAVNTFPVP PGIWDYSGDN VVGLAVWNQG
     DGEVKLDVDV QVDYVLASAL DVKFDGQYLR PGWDESRAEY I
//
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