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Database: UniProt
Entry: A0A178E6T0_9PLEO
LinkDB: A0A178E6T0_9PLEO
Original site: A0A178E6T0_9PLEO 
ID   A0A178E6T0_9PLEO        Unreviewed;      1007 AA.
AC   A0A178E6T0;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   16-JAN-2019, entry version 13.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=IQ07DRAFT_642632 {ECO:0000313|EMBL:OAL51706.1};
OS   Pyrenochaeta sp. DS3sAY3a.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Pleosporomycetidae; Pleosporales; Pleosporineae;
OC   Cucurbitariaceae; Pyrenochaeta.
OX   NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL51706.1, ECO:0000313|Proteomes:UP000077535};
RN   [1] {ECO:0000313|EMBL:OAL51706.1, ECO:0000313|Proteomes:UP000077535}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL51706.1,
RC   ECO:0000313|Proteomes:UP000077535};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L.,
RA   Chaput D.L., Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-2016) 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; KV441642; OAL51706.1; -; Genomic_DNA.
DR   EnsemblFungi; OAL51706; OAL51706; IQ07DRAFT_642632.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000077535; 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:UP000077535};
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:UP000077535};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     22       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        23   1007       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5008085083.
FT   DOMAIN      399    578       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1007 AA;  112023 MW;  B92A3B3E64B4A55B CRC64;
     MRLARLSNLL ALGASLVTTS WQQQQQWPLH DNGLNQVVQW DHHSFMVNGE RLFLWSGELH
     LWRLPVPDLW EDILQKLKAA GFNTIAIYEH WGWHAPNNET LDFSSGAHDF TPIFEIAARV
     GVYIVYRPGP YSNAEANGGG FPGWLTTGEY GPLRDDDPRY TGAWTRYWSH VADIVRPHLI
     TNGGPVLLWQ LENEYGVQFL DPELKTPNRS AINYMETLDN TTRGWNIDVP FTANNPNMWT
     RSWSKDYSDV GGEVDLYGLD HYPACWSCNL DECTNVNGAP EPFTVFNYYD HFQSVSWTQP
     SFLMEFQGGS YNPWNGPTGG CIENMAAPWV NLFFRHNLAQ KVSAVNIYMA YGGTNWGNIG
     YPNVGTSYDY SAPVQENRMI SDKFQETKLF GLFTRIARDF TKVDRVGNST DYSTNPAVFV
     TELRNPDNGA AFYVTRHDYS PSTDSTRFRL NIKTSIGDLV VPEFGSITLN GTESKVLVSD
     FRIGGSGKVL AYSTIELLTI ADFQERQVVV LWAPNGQNGE FLLKGATTVN ASQGSIDNQA
     AKPDGLVVSF TTGHDPIVLD FDIGVQAVIV DRESAYKLWA PTLGNSPFAW ENETVIVTGP
     YLVRHVELDS GKLNIYGDWN QETSIEVWAP PEVQSITFNG EGLDATKSPY GTFIAKLAAA
     EFTVERVQAS IPALHWKAAD ALPEAAAEYD DSRWTAADHM STPHFVPPDT YPVLFADEYG
     YQAGNILWRG RFDYSPDENL SAVYLRVIGG AGFGWSTYLN GEFLGSYLGD PKEKAGNLTL
     NFENHTLNTD RENVVFVIQD TMGKEQREGA LDPRGILNAT LITQSGAPKN FTSWKVSGNA
     GGNHLLDPIK GTYNEGGLHA ERLGWHLPGF DDSAWQIGNP NEGFIGATAR FYRTNVTLSI
     PRGHDASMAF ELVPTTRAKL RAQLYVNGYQ YGKIIPVFGN QVEFPVPPGI LNYSGDNTIG
     LSIWAMDVAG GAVDVQLKVL GVYRSSYDVL FDASELHPVW TDRSQYA
//
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