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Database: UniProt
Entry: A0A0D2HL97_9EURO
LinkDB: A0A0D2HL97_9EURO
Original site: A0A0D2HL97_9EURO 
ID   A0A0D2HL97_9EURO        Unreviewed;      1011 AA.
AC   A0A0D2HL97;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, 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=Z520_01166 {ECO:0000313|EMBL:KIY02701.1};
OS   Fonsecaea multimorphosa CBS 102226.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Fonsecaea.
OX   NCBI_TaxID=1442371 {ECO:0000313|EMBL:KIY02701.1, ECO:0000313|Proteomes:UP000053411};
RN   [1] {ECO:0000313|EMBL:KIY02701.1, ECO:0000313|Proteomes:UP000053411}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 102226 {ECO:0000313|EMBL:KIY02701.1,
RC   ECO:0000313|Proteomes:UP000053411};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Fonsecaea multimorphosa CBS 102226.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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; KN848063; KIY02701.1; -; Genomic_DNA.
DR   RefSeq; XP_016636823.1; XM_016771684.1.
DR   EnsemblFungi; KIY02701; KIY02701; Z520_01166.
DR   GeneID; 27706912; -.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000053411; 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:UP000053411};
KW   Glycosidase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108869};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053411};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     18       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        19   1011       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5002243403.
FT   DOMAIN      396    576       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1011 AA;  110204 MW;  66F2AB20EC7DC7B1 CRC64;
     MRLSVVSVLA CLAARAAGLA FPGHSFGGLN IIEHPDPEKR QLLQDIVTWD ETSLFIYGQR
     IMIFSGEFHP FRLPVPSLWL DVFQKIKALG FNCVSFYLDW AILEGKPGNF SAEGVFALEP
     FFEAASAAGV YLIARPGPYI NAEASGGGFP GWLARLPGRL RTTDPGYLAS TENYVRNVAS
     SIAAAQITNG GPVILYQPEN EYSQACCGVE FPDGQYMQDV MDQARQAGVV VPMISNDARP
     SGDNAPGTGI GAVDIYGHDG YPLGFDCSHP TVWPDGALPT TYWQTHLNES PTTPYSIDEF
     QGGSFDPWGG PGFGKCEILV NYEFVRVFYR NIIASGAKIF NIYMIFGGTN WGNLGHDGGY
     TSYDYAAAIS ENRQVDRQKY SETKLISNFI KASPAYLTAE PRQLNTTSVF TNTSDLTVTS
     VGGNGSATTF YIVRHYNYSD LSPTFYKLSL PTSSGNLTIP QLGGTLTLGG RDSKVHVADF
     DLAGVSLVYC TAEIFTWKNF GDRTVLILYG GEEEHHELCV ASSSAPSVIE GDSSTVTTNQ
     TGSGIIVAWD TSSSRRVVQV GQLEVFLLDK NSAYDYWVLD LSTIGFGNSF ASANTTASSI
     ILKTGYLARE AHIKGDELHL RADFNDTTPI EVIGVPSIAN ALFVNDLPVQ YDVNSQGDWS
     AIFNYTEPNI SLPDLQSLEW KYIDSLPEIQ PDYDDSGWTN ADLPTTNNTV RNLTTPTSLY
     ASDYGYHAGS LTYRGHFTAQ ESSTNLSLNT QGGWAFGHSV WLNQSFLGSY DGVSTENNTN
     ATYALSALQT GSGYVLTVLI DHMGLEENGY VGSDQMKTPR GILDYKLAGY EDDAITWKLT
     GNLGGEDYVD RSRGPLNEGS LYAERQGWHL PNPPSQSWES RSPLDGITDP GVGFFSTSFD
     LAIPEGWDLP VSFTFGNTTS PPEPYRAQLF VNGFQYGKYV NHIGPQTSYP VPQGILNFNG
     TNWLALTLWS QQPGGAKLDS FELVCDRPVA TALTGVHFVE GSVYTPRQGA Y
//
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