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Database: UniProt
Entry: A0A165HWQ4_9APHY
LinkDB: A0A165HWQ4_9APHY
Original site: A0A165HWQ4_9APHY 
ID   A0A165HWQ4_9APHY        Unreviewed;      1053 AA.
AC   A0A165HWQ4;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   13-FEB-2019, entry version 13.
DE   SubName: Full=Glycoside hydrolase family 35 protein {ECO:0000313|EMBL:KZT12288.1};
GN   ORFNames=LAESUDRAFT_746914 {ECO:0000313|EMBL:KZT12288.1};
OS   Laetiporus sulphureus 93-53.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Polyporales; Laetiporus.
OX   NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT12288.1, ECO:0000313|Proteomes:UP000076871};
RN   [1] {ECO:0000313|EMBL:KZT12288.1, ECO:0000313|Proteomes:UP000076871}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-53 {ECO:0000313|EMBL:KZT12288.1,
RC   ECO:0000313|Proteomes:UP000076871};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K.,
RA   Labutti K., Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T.,
RA   Yoshinaga Y., Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi
RT   Provides Insights into the Origins of Lignocellulose Decay
RT   Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
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; KV427606; KZT12288.1; -; Genomic_DNA.
DR   EnsemblFungi; KZT12288; KZT12288; LAESUDRAFT_746914.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000076871; 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:UP000076871};
KW   Glycosidase {ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00108869,
KW   ECO:0000313|EMBL:KZT12288.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076871};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     46     64       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      444    626       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1053 AA;  115222 MW;  00B0C28D4D721B1A CRC64;
     MLVDRPWENV LLSYRQAGLL RHYKDSGPET VGCRRARMVS SRCSRWAFPA LLSLLLVLLT
     WPITRTTSAL SFRKNVRKAL QDVVTASEPT RKSDNYTDIV QWDNYTIFLN DQRMFLHSGE
     FHTFRLPVPD LWLDIFQKMV AAGLNGVSIY VHWTLTNPAP GVLDFNDWRA LQPVFDAAKQ
     AGIFVTLRPG PYINAETNAG GIALWATSLV AGELRTNATD YMEAWMPYVK EVAASVVPNQ
     VTGGGPILLL QIDNEYEQNA VTGEYFVELE NTYREAGVVV PLTYNDPGEG QNFINGTGAV
     DIYGLDSYPQ GFDCSDPIVW SSVVANYHQY HEETDPGEPW YMPEFQGGSF DPWGGTGYNN
     CEILTGVDFE DVFYKQNWAS NVKMISYYMV YGGTSWGGLP YPGVYTSYDY GSSIRENRVL
     SDKYDELKRQ GLFLRSSPEF RKTDWIGDTD TGMPGVVVNG SEAYVTWLRN PDSGTGFYIV
     RQSNSSSMAD ITFRISVPTS EGTLSIPRTI DSIAINGRQS KVLVVDYSYG ANSSVLYSTA
     SVFFAGTIGS RDVLFLYGDT DQSNEIALTL KGSGTKASSS QVSISNAGTG GYSTITLLAG
     IEGLIPLYES DSQLILYSDP VTAATYWAPV IPSTTATSFE NYWQFGSNST ILVGGPYLVR
     NASLSSGHLA LRGDLNKSII LTVVAPEEVT SISWNGVEVD AVNIADGILS GNLTISSSLK
     SITVPSLAGW RYADSLPEVL SNFSDADWII ANHTTTNITP GPLYGDGRVL FGCDYGFCEN
     IVLWRGHFNG TGSETSANLT INGGDAFAGS VWINDRFINS TWDVSAEQTT ALYTFPEESV
     RIEEDNVITV IQDGMGNDEN PDEKSPRGIP GFLLTGGSFT EWKVQGKMGG YTNYPDKVRG
     VLNEGGLYGE REGWHLPGYD TSSWEERDLS DGLPSGGAGV GFFVTTFDLS IPEGTDVLIS
     FQFDTMDQPY RATLFVNGWN YGKRVANIGP QSKFPVHQGL LDYSGTNTVA VALWALQDTA
     VSPTLELVVD TVIEGGVGEI GVNNPGWSAR VIA
//
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