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Database: UniProt
Entry: R7S0V0_PUNST
LinkDB: R7S0V0_PUNST
Original site: R7S0V0_PUNST 
ID   R7S0V0_PUNST            Unreviewed;      1019 AA.
AC   R7S0V0;
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_128595 {ECO:0000313|EMBL:EIN03838.1};
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:EIN03838.1};
RN   [1] {ECO:0000313|EMBL:EIN03838.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=HHB-11173 SS5 {ECO:0000313|EMBL:EIN03838.1};
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; JH687558; EIN03838.1; -; Genomic_DNA.
DR   RefSeq; XP_007388896.1; XM_007388834.1.
DR   EnsemblFungi; EIN03838; EIN03838; PUNSTDRAFT_128595.
DR   GeneID; 18878160; -.
DR   KEGG; psq:PUNSTDRAFT_128595; -.
DR   OMA; EFEGGWF; -.
DR   OrthoDB; 179316at2759; -.
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, ECO:0000313|EMBL:EIN03838.1};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     24       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        25   1019       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5004455416.
FT   DOMAIN      392    575       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1019 AA;  110022 MW;  62E9D778B1FEDDC1 CRC64;
     MVASLSHLFG ASVLLFSTVW CALATPQLLP RNSTGLRNAV TWDEHSLFIN GVRTFILSAE
     YHPWRLPNPN LWSDVFQKIK ANGFNTVSFY VDWAVHFPTP DTNGGAGDWQ AGTYRDLQRF
     IDDAKDAGLW LIARPGPYIN AETSGGGFPG WLGNIEGALR TDAEDYHQAW VPYLTAVSKI
     IAKNQVTNGG PIILVQAENE FSEGSTRSPY MQQVIDLHRA NGVVVPIIHN DQHGGTTGNF
     SPDQPGEGDV NIYCGDSYPQ GTTRWNQVQP YSYYYGGHKA VAPSNPLCLA EFGGGWLQGW
     QGTTRGGTGY ERFTYDLTGP NYEDIFYKEN YAQTATILNI YMLFGGTNWG HTYEPTVYSS
     YDYGAGINEN RIATQKMNEM RTQGYFLRVS PDLLASNFNG NGTNYTTNSL LYAVELRNPD
     TGAAFYFVRH SDSTSTAVTS GQLSVNTLEG VFTVPQNGSL TISGREYKIL PTDYIFGSQK
     TKIIYTTAEI LTWTTMDSTD FLILYAPKGE TGETVFSFAS APRVDLSSAP GASSRFANST
     LRLNYVLNGL GVIKFNHGQK QTVIILMDKD AAFTWSAPVL AGSGPFGSHF GVGTNATVFV
     GGPYLVRTAT TSGGTLKLTG DNNGTTSIEF FAPSAVSRLS WNSKSVPVSR TPYGSYKGTL
     GTVKTVTPPS LGSWKVIGSL PEVEPGFDDS SFITCSQTAT NYTLAPLAGD KVLYSQQYGI
     YGGNLIWRGH FNASGQEQAV NLTVQSGFGH GYSTWLNGVF LGSSQGNSTV SLTTDIWNIP
     NGTLRIGQDN VLTVLQDHMG IVETSTNSGK EPRGIRGYSI IGGNTTFNTW KLQGNQGGAA
     GTPDTFRGYM NEGGLYAERI GAHLPGFPDA AWAAGSPLAI SGGGLSGPGV NFYRTQFNLN
     LPSHTDVPIR LSIAPSDITS NFRVQIYLNG WMLGKYINNF GPQTDFVLPA GILLPNAENT
     LAISLWSLDS AGASLAGLSL ISDGTFATSL GSEIADWTAA PNYAAQKSKR PSPTYVKPL
//
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