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Database: UniProt
Entry: A0A074YXC0_9PEZI
LinkDB: A0A074YXC0_9PEZI
Original site: A0A074YXC0_9PEZI 
ID   A0A074YXC0_9PEZI        Unreviewed;      1011 AA.
AC   A0A074YXC0;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   16-JAN-2019, entry version 21.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=AUEXF2481DRAFT_60882 {ECO:0000313|EMBL:KER00795.1};
OS   Aureobasidium subglaciale EXF-2481.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Dothideomycetidae; Dothideales; Saccotheciaceae;
OC   Aureobasidium.
OX   NCBI_TaxID=1043005 {ECO:0000313|EMBL:KER00795.1, ECO:0000313|Proteomes:UP000030641};
RN   [1] {ECO:0000313|EMBL:KER00795.1, ECO:0000313|Proteomes:UP000030641}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EXF-2481 {ECO:0000313|EMBL:KER00795.1,
RC   ECO:0000313|Proteomes:UP000030641};
RX   PubMed=24984952;
RA   Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J.,
RA   Zalar P., Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y.,
RA   Lipzen A., Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT   "Genome sequencing of four Aureobasidium pullulans varieties:
RT   biotechnological potential, stress tolerance, and description of new
RT   species.";
RL   BMC Genomics 15:549-549(2014).
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|RuleBase:RU000675,
CC         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; KL584749; KER00795.1; -; Genomic_DNA.
DR   RefSeq; XP_013349309.1; XM_013493855.1.
DR   EnsemblFungi; KER00795; KER00795; AUEXF2481DRAFT_60882.
DR   GeneID; 25369399; -.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000030641; 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; IPR019801; Glyco_hydro_35_CS.
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.
DR   PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000030641};
KW   Glycosidase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108869, ECO:0000313|EMBL:KER00795.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030641};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     22       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        23   1011       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5001704798.
FT   DOMAIN      402    579       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1011 AA;  109535 MW;  A3C1C0E2B7075C91 CRC64;
     MLGNTLLKAA ALVAALATSS DALALKKPNY NELIKPYKRE LLQDLVSWDE HSLYVRGERI
     MIYSGEVHPF RLPVPSLWLD VLQKIKALGY NAVSFYVNWA LHEGKQGEFN AEGVFAWEPF
     FEAAQEAGIY LIARPGPYIN AEVTGGGFPG WLARNPGIPR TRDPNFLNAT DYYSRAIGEI
     IAKAQITEGG PIILYQPENE YSQAVPSDPE FPDPVYFGAV EQKFRDAGIV VPSISNDAYP
     HGYFAPGQAA AVDIYGHDAM LIFLQGYPLG FDCANPTTWP DNALPTYYGD LHAEQSPSTP
     YSILEFQGGS FDPWGGLGFA QCAELLNTEF QRVFYKNDYS FGVTIFNIYM TYGGTNWGGL
     SHPGGYTSYD YGAVITEDRL VSREKYSEAK LEANFLQASP AYLTAIPQNN THANGSYTNN
     ADIAVTALLG NRTNFFVIRH AAYNSRASTE FKLHLPTSQG NITIPQLNGS LVLNGRDSKF
     AVTDYDAAGT NLLYSSAEIF TQKSYGDKQV LIVYAGPNEN HELALTLSCS SEVIEGSGVN
     IVKKKGTTIL GFKSSSERRI VKIGDLYIYI LDRNDAYNYW VLDLPSSTSS AAIIKAGYLL
     RTVEISGNSM HLTGDLNATT DVEIVGGAPS KLTELTFNSK SIKFAQDSCS GVVTGSVAYV
     EPSFSIPDLS TVGWQVIDSL PEIAAGYDDS LWTSADLTYS NNTQRNLTTS VSLYAQDYGY
     LTGNLLYRGH FVAAGNESSI YLQTQGGSAF GMSAWLNSTF LGSARGIDAA SNANSTFTLP
     NVAAGSSYVL TILLDHMGLQ ENGQGGSSEM KTPRGILNYS LSGRDASAIT WKLTGNLGGE
     SYKDRTRGPL NEGGLYVERQ GYHLPGAPTS SWANSTGPMT GISYPGVAFY ATTFDLDMPA
     GYDIPIAISF SNATSSSNGS TPVAYRSQIY VNGYQFGKYV SNIGPQDVFP VPQGIFNYNG
     PNYFGVSLWA LDEGGAKISN LSLVAGPVIQ SGYGPIELSP MTGWSKREGA Y
//
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