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Database: UniProt
Entry: R7SKT8_DICSQ
LinkDB: R7SKT8_DICSQ
Original site: R7SKT8_DICSQ 
ID   R7SKT8_DICSQ            Unreviewed;      1017 AA.
AC   R7SKT8;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   13-FEB-2019, entry version 33.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EJF56350.1};
GN   ORFNames=DICSQDRAFT_71631 {ECO:0000313|EMBL:EJF56350.1};
OS   Dichomitus squalens (strain LYAD-421) (Western red white-rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Polyporales; Polyporaceae; Dichomitus.
OX   NCBI_TaxID=732165 {ECO:0000313|EMBL:EJF56350.1};
RN   [1] {ECO:0000313|EMBL:EJF56350.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LYAD-421 SS1 {ECO:0000313|EMBL:EJF56350.1};
RX   PubMed=22745431; DOI=10.1126/science.1221748;
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 John 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 lignin decomposition reconstructed
RT   from 31 fungal genomes.";
RL   Science 336:1715-1719(2012).
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|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; JH719474; EJF56350.1; -; Genomic_DNA.
DR   RefSeq; XP_007370918.1; XM_007370856.1.
DR   EnsemblFungi; EJF56350; EJF56350; DICSQDRAFT_71631.
DR   GeneID; 18843803; -.
DR   KEGG; dsq:DICSQDRAFT_71631; -.
DR   OMA; GYQITEG; -.
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; 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.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00108869};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     29       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        30   1017       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5004444218.
FT   DOMAIN      400    566       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1017 AA;  111564 MW;  3C9F80C46D2E4561 CRC64;
     MFQLLSTVWA RLRPALLVSL LVAWSSILCS KTSPSVFEGT SAVVAANPPR QSNGFTDVVQ
     WDNYTLFLHD QRLFIHAGEF HTFRLPVPEL WLDIFQKMVA AGFNGVSIYI HMGVINPSPG
     ILDFNDWRSL QAIYEAAKVA GIFVILRPGP YINGETTSGG IAHWITSQVA GTVRTNATDW
     TAAYQPYISG IINESVRYQV TEGGPLLAVQ IDNENRNSPD PSTQEYFAQL ENQYREGGIV
     VPLTYNDPGM RSGFINGTGH VDIYGLDAYP QGFNCSTPRT WSHVTTNYHQ YHKANNPSEP
     WYMPEFQGGS FDPWGGPGYD ACELLTGPDF QDVFYKHNWA ANVKMISYYM LYGGTSWGGI
     PFPGVYTSYD YGSSIRENRA LTDKFDEVKR QGMFIRSSPQ FLKTDWIGNS SLGIPGVTLN
     GSAAFVTSLR NPDSNTWFHV TRQADSTSTA NISFALTVPT SQGMLTLPRT TDSIALNGRQ
     SKLIITDYSF GVHGSLLYST ASVFFAGTIG SRDVLFLYGF ADQSHEFALN MTGNGVRTSS
     SRVQFGTSDT INDLTTVAIV PGSAGLLTIW DSDKQLILFS EPVTAASFWA PAIRAETSST
     VAGLESYWWF GTNTTVLVGG PYLVRNATLS RDRNTLALRG DLNVSVPLIV IAPPSVRAVS
     WNGNPVAMRS DGRGVLTGNL QLNADIENAK VPRLKGWRYK DSLPEIQPGF DDSDWVVANH
     TTTNIFQKPL FGDGRVLYGI YASCENTVLW RGHFNGTGSE TSVNLTIYGG TFFASSVWIN
     DKFIGTVTSS ADHVNGLFPF PEGAVITGLN NVITVIQENM GNDEQANIKP ARGIAGFQLD
     SGNFTTWKVQ GKIGGYTNYP DKVRGVLNEG GLFGERHGWH LPGFDTSDWT LRDLSEGLPG
     SSAGVGFFVT TFDLAFPEDT DPFVSFQFEM KNTQPYRALL FVNGWMFGKR VANLGPQTKF
     PVPPGILDCN GKNTVAIVLW ALEDTSVFPT LDLIVDDVLH GGVGPIPLHS PAWKLRE
//
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