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Database: UniProt
Entry: A0A2H3JE85_WOLCO
LinkDB: A0A2H3JE85_WOLCO
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ID   A0A2H3JE85_WOLCO        Unreviewed;      1053 AA.
AC   A0A2H3JE85;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   13-FEB-2019, entry version 7.
DE   SubName: Full=Glycoside hydrolase family 35 protein {ECO:0000313|EMBL:PCH40562.1};
GN   ORFNames=WOLCODRAFT_24188 {ECO:0000313|EMBL:PCH40562.1};
OS   Wolfiporia cocos (strain MD-104) (Brown rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Polyporales; Wolfiporia.
OX   NCBI_TaxID=742152 {ECO:0000313|EMBL:PCH40562.1, ECO:0000313|Proteomes:UP000218811};
RN   [1] {ECO:0000313|EMBL:PCH40562.1, ECO:0000313|Proteomes:UP000218811}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MD-104 {ECO:0000313|EMBL:PCH40562.1,
RC   ECO:0000313|Proteomes:UP000218811};
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; KB468053; PCH40562.1; -; Genomic_DNA.
DR   EnsemblFungi; PCH40562; PCH40562; WOLCODRAFT_24188.
DR   OMA; WMMGKRV; -.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000218811; Unassembled WGS sequence.
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:UP000218811};
KW   Glycosidase {ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00108869,
KW   ECO:0000313|EMBL:PCH40562.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000218811}.
FT   DOMAIN      447    626       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1053 AA;  114964 MW;  142910E4EBC3D949 CRC64;
     MSPRIPGRDV LLSYEKNAFD DHKTAIPEFE GPRWVKMLWH RYSPWALTAL LSLVLVVLTP
     TLTQTSGASD VTESVHLSED AALASQTPLK SDNYTDVVQW DNYTILLDGQ RMFLHAGEFH
     TFRLPVPDLW LDIFQKMVAA GLNGASIYIH WTLTNPAPGV LDFEYWRALQ PIYDAAKQAG
     IFIVLRPGPY INAETTAGGI ALWATSLVAG ELRTNASDYR AAWTPYVEEI ASSVVPNQVS
     NGGPILFVQI DNEYYQDAVT GEYFVELEEA YRQAGVVIPL TYNDPGEGKN FVNGTGAVNI
     YGLDSYPQGF DCSDPEVWSP VVTNYHYYHE TTNPGEPWYM PEFQGGSFDP WGGTGYNNCE
     ILTGPDFQDV FYKHNWASNV KLISYYMLYG GTNWGGLAEP GVYTSYDYGS SIRENRALSD
     KYDELKRQGI FLRSSPEFYK TDWVGDTNST MPGVTVNGSE VYVTWLRNPD SGAGFYIVRQ
     TNSSSLANVT FTLSVPTSAG TLSIPQISGA IAINGRESKI ILTDYSFGAQ SSVLYSTASV
     FFAGTIGSRD VLFLYNDIDE SSEVALSLTG TGARAQSSSV TYTNTTSANG QVSTFTLLPG
     IEGLVTLWES DTQLILYSDP GTAATFWAPI IPSTTATEFA NYWQFGSNTT VLVGGPYLVR
     NATISGSALA LRGDLNRSAT LTVIAPHDVT SVTWNGEPVE AITASGGVLY GSLQMSVTAS
     SITVPALTGW QYADSLPEVL SNFSDAEWTL ADHNTTNISP GMLYGDGRVL FGCDYGFCEN
     IVLWRGHFVG TGSETSVNLT INGGTAFAGS VWINDYFIES TWSVYDEQTT TVYTFPEGSV
     RVGEDNVITI IQDGMGNDES PDEKSPRGIP GFQLNSGNFT EWRVQGKLGG YTAYPDRARG
     VLNEGGLYGE REGWQLPGFD TSNWEERDLS EGLPSGGAGV GFFVTTFNLS IPQETDVLMS
     FQFDTTNQTY RALLFVNGWN YGKRVANIGP QTKFPVPQGI LNYQGTNTVA VALWALENEV
     VSPSLELVVD TVIEGGVGPI AVNNPVWTPR AES
//
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