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Database: UniProt
Entry: A0A178E5I3_9PLEO
LinkDB: A0A178E5I3_9PLEO
Original site: A0A178E5I3_9PLEO 
ID   A0A178E5I3_9PLEO        Unreviewed;      1007 AA.
AC   A0A178E5I3;
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_508852 {ECO:0000313|EMBL:OAL50621.1};
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:OAL50621.1, ECO:0000313|Proteomes:UP000077535};
RN   [1] {ECO:0000313|EMBL:OAL50621.1, ECO:0000313|Proteomes:UP000077535}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL50621.1,
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; KV441644; OAL50621.1; -; Genomic_DNA.
DR   EnsemblFungi; OAL50621; OAL50621; IQ07DRAFT_508852.
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_5008085112.
FT   DOMAIN      394    573       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1007 AA;  110067 MW;  E2C9CED1D24D3B2E CRC64;
     MKTFVRLGSA VALSCLALQT AARAVGYSPK DWIAPYRREV LQDIVTWDEH SLFVHGERIF
     LYSGEVHPYR LPVPDLYLDI FQKIKALGFN GVSFYVDWAL LEGKPGEYRA EGVFDLKPFF
     DAATKAGIYL IARPGPYINA EVSGGGFPGW IQRINGTLRT RATDFLEATD NYMKNIGATI
     ASAQITNGGP IILVQPENEY TQATSAIKPF PDPVYMQYVE DQLRNAGIVV PLINNDASPK
     GHNAPGQSAA VDIYAHDGYP VGFNCANPTV WNDGSLPTNW LQLHQQQSPT TPYSILEFQA
     GSFDPWGGPG FDKCYVLVGP EFERVFYKQL YSFGVTILNL YMTYGGTNWG NLGHPGGYTS
     YDYASPIREA RQVDREKYSE LKLQSSFFKV SSEYLTAKRE SPSNSTWTTN KDITVARASG
     ESTKFYFVKH SKYNSLASTN YKLTVPTSAF GNITIPQING TSLTLNGRDS KIHVTDYSIG
     SATLVYSTAE IYTWHKYTDK TVLVVYGGPG ETHELVLAVT GLEVLEGNVE SISTRGYTLL
     NFKADGTRKV AKVGVGSNFI YVYMLDRYEA YNYWTVDQAA HDSSNPVILK AGYLTRTAQV
     SGDTLALTGD LNATTPIEIL GGAPSSLSKL TFNGDEFDFT VSKDGVVSAS VDFPRPKFKV
     PELSELTWKY IDSLPELQPG YDDSKWTKAE LKTTSNSLRP LTTPVSLYSS DYGYHTGTLL
     YRGTFTATGN ETTFFVSTQG GSAFGHSAWI GDHFLGSWRG YDAAVSGNNT FTLPNLTAGK
     TYTITVVIDN QGLDENWTIG TETMKNPRGV LDYKLAGHAQ SDVSWKLTGN VGGEDYLDHS
     RGPLNEGGLF VERQGLHLPG ALASSTAAWK PSKGPVADGI SAPGIGFFAA EFQLSLPSGY
     DIPLSFTFSN GTSTSGGTPA YRVQLYVNGW QYGKYVSNVG PQTKFPVPEG ILNYRGTNYL
     GVSVWGLDGG ATKVEGLELS VDGLVWSGLG QVRTVEGEVY KSREGAY
//
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