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Database: UniProt
Entry: M2QWN1_CERS8
LinkDB: M2QWN1_CERS8
Original site: M2QWN1_CERS8 
ID   M2QWN1_CERS8            Unreviewed;      1071 AA.
AC   M2QWN1;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   13-FEB-2019, entry version 29.
DE   SubName: Full=Glycoside hydrolase family 35 protein {ECO:0000313|EMBL:EMD41518.1};
GN   ORFNames=CERSUDRAFT_110070 {ECO:0000313|EMBL:EMD41518.1};
OS   Ceriporiopsis subvermispora (strain B) (White-rot fungus) (Gelatoporia
OS   subvermispora).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Polyporales; Gelatoporiaceae; Gelatoporia.
OX   NCBI_TaxID=914234 {ECO:0000313|EMBL:EMD41518.1, ECO:0000313|Proteomes:UP000016930};
RN   [1] {ECO:0000313|EMBL:EMD41518.1, ECO:0000313|Proteomes:UP000016930}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B {ECO:0000313|EMBL:EMD41518.1,
RC   ECO:0000313|Proteomes:UP000016930};
RX   PubMed=22434909; DOI=10.1073/pnas.1119912109;
RA   Fernandez-Fueyo E., Ruiz-Duenas F.J., Ferreira P., Floudas D.,
RA   Hibbett D.S., Canessa P., Larrondo L.F., James T.Y., Seelenfreund D.,
RA   Lobos S., Polanco R., Tello M., Honda Y., Watanabe T., Watanabe T.,
RA   Ryu J.S., Kubicek C.P., Schmoll M., Gaskell J., Hammel K.E.,
RA   St John F.J., Vanden Wymelenberg A., Sabat G., Splinter BonDurant S.,
RA   Syed K., Yadav J.S., Doddapaneni H., Subramanian V., Lavin J.L.,
RA   Oguiza J.A., Perez G., Pisabarro A.G., Ramirez L., Santoyo F.,
RA   Master E., Coutinho P.M., Henrissat B., Lombard V., Magnuson J.K.,
RA   Kuees U., Hori C., Igarashi K., Samejima M., Held B.W., Barry K.W.,
RA   LaButti K.M., Lapidus A., Lindquist E.A., Lucas S.M., Riley R.,
RA   Salamov A.A., Hoffmeister D., Schwenk D., Hadar Y., Yarden O.,
RA   de Vries R.P., Wiebenga A., Stenlid J., Eastwood D., Grigoriev I.V.,
RA   Berka R.M., Blanchette R.A., Kersten P., Martinez A.T., Vicuna R.,
RA   Cullen D.;
RT   "Comparative genomics of Ceriporiopsis subvermispora and Phanerochaete
RT   chrysosporium provide insight into selective ligninolysis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:5458-5463(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; KB445791; EMD41518.1; -; Genomic_DNA.
DR   EnsemblFungi; EMD41518; EMD41518; CERSUDRAFT_110070.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000016930; Unassembled WGS sequence.
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; 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   Complete proteome {ECO:0000313|Proteomes:UP000016930};
KW   Glycosidase {ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00108869,
KW   ECO:0000313|EMBL:EMD41518.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016930};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     56     75       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      468    641       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1071 AA;  116009 MW;  A9371115C246BC1F CRC64;
     MAPNSPEKHA LPSYGSRWGG DNKISRWPDE LPDSVHSTGP KSRPTRVKML WHRHSSWALP
     ACVTFLLVLL TWPLTAHTDA RSLRMRDSVS QIRVAATDPP RKSDNFTEVV QWDNYTIFLN
     EQRMFLYSGE FHTFRLPVPD LWLDIFQKMV AAGLNGVSIY IHWALTNPAP GVLDFNDWRA
     LAPIYEAADQ AGIFIVLRPG PYINAETTAG GIAHWVTSRT AGELRTNATD FAATWPDYIN
     EIIEQTKPAQ VTAGGPVLAI QVDNEYSQSP IERAEYFAEL EAAYRAGGIV VPLTYNDPGE
     GSNFVNGTGA VDIYGLDSYP QGFDCSNPTQ WASVVTNYHT YHEEVNPGEP WYMPEFQGGS
     FDPWGGPGYD ACEVLTGPDF QDVFYKQNWA SNVKLISYYM VYGGTSWGGL PEPGVYTSYD
     YGASIRESRA LSAKFDELKR QAIFLRSSPS FRKTDFIGDS SSSIPGVSLG GGEGSAAFAT
     FLKNPDTGTG FFILRQSDST STTNINFTIT IPTSDGTLTL PRTLAGIALA GRQSKLVLTD
     YPFGVSSSVL YTTASVFFAG TIGSRDVLFL FGDADQGHEL ALSLKGAQGT RLDSSRVQFA
     SDGTSGSTTV TILPGSTGLL TLWDSETQLV LFSDPVTAAT FWAPPIPTGA SSFTNYWQFG
     TNTTALIGGP NLVRNASIDG STLALRGDLN ASVTLTVIAP PQVKSVSWNG ALVPVESNAR
     SGLGSGILTG TLELPNSVKS ITAPKLTNWK FNNSLPEVTA SFDDSNWIVA NHTQTNITAP
     LYGDGRVLYG CDYGFCENIV LWRGHFNGTG SETSVNLTIN GSTAFAASVW LNDQFLNSTE
     DVNAEQTTVL YTFPEGAVNI DEDNVITVIQ DGMGNDEDAG ERSPRGIPGF LLNTGNFTTW
     KVQGKLGGYT GYPDKVRGVL NEGGLFGERE GWHLPGFDTS KWTTRDLSEG LPSGEAGIGF
     FITTFKLSFP EDTDVMMSFQ FDTESQPYRA LLFVNGWQFG KRAANIGPQT KFPVPPGILD
     YHGTNTVAVA LWALDNTSVS PTLEVVVDGA LQGGVGPVAL NNPPWSPRTA A
//
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