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Database: UniProt
Entry: R7SMX4_DICSQ
LinkDB: R7SMX4_DICSQ
Original site: R7SMX4_DICSQ 
ID   R7SMX4_DICSQ            Unreviewed;      1004 AA.
AC   R7SMX4;
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:EJF56352.1};
GN   ORFNames=DICSQDRAFT_174984 {ECO:0000313|EMBL:EJF56352.1};
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:EJF56352.1};
RN   [1] {ECO:0000313|EMBL:EJF56352.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LYAD-421 SS1 {ECO:0000313|EMBL:EJF56352.1};
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; EJF56352.1; -; Genomic_DNA.
DR   RefSeq; XP_007370920.1; XM_007370858.1.
DR   EnsemblFungi; EJF56352; EJF56352; DICSQDRAFT_174984.
DR   GeneID; 18840062; -.
DR   KEGG; dsq:DICSQDRAFT_174984; -.
DR   OMA; RYDNTTE; -.
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     30       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        31   1004       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5004455658.
FT   DOMAIN      381    568       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1004 AA;  110771 MW;  7B822464594175A7 CRC64;
     MSLRRCKSWV FLALLAVYLF FLTSSPTAPA READPVRRSN GYSDIVQWDN YTLWIHNQRI
     FLHSGEFHTF RLPVRELWLD IFQKMVAAGL NGYLLGLTNP SRGVVDFKDW RALKPMYNAA
     SEAGLFIVLR PGPYINAETS AGGIAHWITT ETAGEVRTNA TDWVEAYEPY IDGVIKESVD
     YQITNGGPII AVQIDNEYDQ SISHQLYFQR LENQYREGSI VVPLTYNDPN EREAFINGTG
     AVDIYGMDAY PQAFDCSNPL VWKNVSMNYH AYHEKVNPSQ PWYMPEFQAG AFDPWAGPGY
     EACAVLTGPD FEDVFYKHNW AANEKLVNYY MIYGGTNWGG IPFPGVYTSY DYGAPIRENR
     LLTDKYDEVK RQGIFLRSSP EFRKTDWIGD SASGIPEVTI DNGLVYGTYL RNPDTGTGFL
     ITRQNDSTSA ANVAFTVSLP TSQGILTLPT TADSIVLHGR QSKLITTDYT FGTKGALLYT
     TTSIFFAGTI GPRDVIFLYG HVGQSHEFSF IPLGDGVGTT SSLVQLSKLA RRPATTVTIL
     PGVQGLITVW ESPEQLVLYS DPVTAATFWA PPIRSPSVDI IEGLETFWQF GTNTTVLVGG
     PYLVRNASLE DSGTTLALVG DLNASVPLTV FAPQEVTAVT WNGEPVGTMT QSRSSGLRGM
     LVLKSGIRDV KVPELTGWRY ADSLPEVKKG YDDTEWVVAD KKSTNIPIKP VFGDGRVLYG
     CDYGFCENIV LWRGHFNATG LETGANLTIY GGECFAASVW INDKFISSVY SPSEHVNHLF
     KFPEDALIVG EDNVMTVIQD NMGLDEDDNE KSARGIAGFA LVGGNTTFGT WKVQGKVGGY
     LNYPDKVRGL FNEGGLHGER KGWHLPGFDT SGPEWTLREL SDGLPGGSAG VGFFVTTFEL
     DIPGFTDTPI SFQFEETNDQ PYRALLFVNG WQYGKRAANI GPQTRFTVPQ GILDYTGENW
     VAIALWALND TAVSPTLQLA VDAIIEGGVG PIASNNPVWR SLRP
//
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