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Database: UniProt
Entry: R7S3W7_PUNST
LinkDB: R7S3W7_PUNST
Original site: R7S3W7_PUNST 
ID   R7S3W7_PUNST            Unreviewed;      1054 AA.
AC   R7S3W7;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   16-JAN-2019, entry version 31.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=PUNSTDRAFT_146007 {ECO:0000313|EMBL:EIN05080.1};
OS   Punctularia strigosozonata (strain HHB-11173) (White-rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Corticiales; Punctulariaceae; Punctularia.
OX   NCBI_TaxID=741275 {ECO:0000313|EMBL:EIN05080.1};
RN   [1] {ECO:0000313|EMBL:EIN05080.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=HHB-11173 SS5 {ECO:0000313|EMBL:EIN05080.1};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Floudas D., Binder M., Riley R., Barry K., Blanchette R.A.,
RA   Henrissat B., Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S.,
RA   Aerts A., Benoit I., Boyd A., Carlson A., Copeland A., Coutinho P.M.,
RA   de Vries R.P., Ferreira P., Findley K., Foster B., Gaskell J.,
RA   Glotzer D., Gorecki P., Heitman J., Hesse C., Hori C., Igarashi K.,
RA   Jurgens J.A., Kallen N., Kersten P., Kohler A., Kues U., Kumar T.K.,
RA   Kuo A., LaButti K., Larrondo L.F., Lindquist E., Ling A., Lombard V.,
RA   Lucas S., Lundell T., Martin R., McLaughlin D.J., Morgenstern I.,
RA   Morin E., Murat C., Nagy L.G., Nolan M., Ohm R.A., Patyshakuliyeva A.,
RA   Rokas A., Ruiz-Duenas F.J., Sabat G., Salamov A., Samejima M.,
RA   Schmutz J., Slot J.C., St Johnn, F, Stenlid J., Sun H., Sun S.,
RA   Syed K., Tsang A., Wiebenga A., Young D., Pisabarro A., Eastwood D.C.,
RA   Martin F., Cullen D., Grigoriev I.V., Hibbett D.S.;
RT   "The Paleozoic origin of enzymatic mechanisms for decay of lignin
RT   reconstructed using 31 fungal genomes.";
RL   Submitted (MAY-2012) 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; JH687551; EIN05080.1; -; Genomic_DNA.
DR   RefSeq; XP_007387483.1; XM_007387421.1.
DR   ProteinModelPortal; R7S3W7; -.
DR   EnsemblFungi; EIN05080; EIN05080; PUNSTDRAFT_146007.
DR   GeneID; 18881558; -.
DR   KEGG; psq:PUNSTDRAFT_146007; -.
DR   OMA; GGEDYVD; -.
DR   OrthoDB; 179316at2759; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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   Glycosidase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108869}; Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     46     70       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      438    621       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1054 AA;  115207 MW;  7BB55D27F88EFB63 CRC64;
     MFLRRAFCRE MPAIRDGVRS RTRYLSSSTD ESIRSEKSDV VQTGRFIMLL VRLLASVSVA
     LTWFSLLIAA TRPRSGRRLV LDTRQVQTDG YQDVVTWDEY SLMINGTRLF IWGGEVHPYR
     MPVQSLHLDV FQKIKAMGLN AVSFYVFWGI HEPKRGEISW EGFRDLQPFI DAAMEAGLYL
     IARPGPYINA ETTAGGFPGW GTYTPGLWRT ENATYYDAWQ EYMAQVGGII AKNQISNGGP
     IILTQLENEY SLAQAPLTED FTYERQLIDA IRAAGVTVPT THNDAWPHGS NDMVDIYGYD
     SYPNGFDCAH PYTWASDAVA NTEYFWGAHL EYNPEDPNAV YEFQGGAFDP WGGSGYENCA
     VLLGPEFERV FYKHELAMST TLLNLYMAYG GTNWGGIAHP GVYTSYDYGS AIAEDRTLRE
     KYYELKLQAS FISVSPAFLT GRPQNVNAAQ AAFTGNPALT THQVLDVVGN QTGFYIVAQN
     DTSSTTSVSY RLTVPSSKGS LSIPQLGGSL TLNGRDSKIH VVDYSAGSTT LLYSTAEIMT
     WATIGNRDVV VLYGNSGELH ETAIKASSAA NAKVVSGTGN VKQANRNGTL VIQYTTSGQT
     VVEIGSSVLL YILDRTEAYE FWILHTPGTG AYAAFNAENP VIVKGGYLLR SVSASDGTLA
     LKGDLNGTTS FEIIAPSAIT KRITFNGDSL SLTKTKYGTL VAKKNARLPA VTLPHLATAA
     TWKTANSLPE ISSAYSDAPW TTADHNSTVN PTQSLTPVVL YAGDYGYHTG NILWRAHFNA
     SGAERGITLN VQGGSAFGYS VWLDSSFLGS WEGNAVNSSW EQTFPFKSTT IRSRSTHVIT
     ILQDHMGYEE DWTSASDDFK TPRGILSYSF VGSNSTVVGT WKVTGNLGGE SYADSARGPL
     NEGGLFAERQ GWHLPGFDDS KWAAGKPTSG ISQAGVAFYR TTFSLDVPTG VDYPIGISIT
     NSTRTSHFRA QLYVNGYQFG KYVNHIGPQS VFPVPEGILN YHGENTLAVS LWAQDASGAK
     LESIDLQVLA KLDSSMPAVT NQPMPKWSKR PGAY
//
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