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Database: UniProt
Entry: A0A165SND5_9HOMO
LinkDB: A0A165SND5_9HOMO
Original site: A0A165SND5_9HOMO 
ID   A0A165SND5_9HOMO        Unreviewed;      1056 AA.
AC   A0A165SND5;
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:KZT25419.1};
GN   ORFNames=NEOLEDRAFT_1065215 {ECO:0000313|EMBL:KZT25419.1};
OS   Neolentinus lepideus HHB14362 ss-1.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Gloeophyllales; Gloeophyllaceae; Neolentinus.
OX   NCBI_TaxID=1314782 {ECO:0000313|EMBL:KZT25419.1, ECO:0000313|Proteomes:UP000076761};
RN   [1] {ECO:0000313|EMBL:KZT25419.1, ECO:0000313|Proteomes:UP000076761}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB14362 ss-1 {ECO:0000313|EMBL:KZT25419.1,
RC   ECO:0000313|Proteomes:UP000076761};
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; KV425572; KZT25419.1; -; Genomic_DNA.
DR   EnsemblFungi; KZT25419; KZT25419; NEOLEDRAFT_1065215.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000076761; 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:UP000076761};
KW   Glycosidase {ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00108869,
KW   ECO:0000313|EMBL:KZT25419.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076761};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     25     46       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      426    611       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1056 AA;  115646 MW;  21079E6826E91DD9 CRC64;
     MPSSTECALP DCSRKAPTVK RTVHGAWLIV ACLLSALAFF SPASYITPRR NGVPLTDSSE
     LTARSVKEAA LVSQYPQLSN NGRTDVVQWD NYSLVLNGQR IFLYSGEFHT WRLPVPFLWP
     DILQKIKAAG LNGISVYTHW GLNNPSPGVI DFDDYRALQP LFGAAKEAGI WIVLRPGPYI
     NAETTAGGIA HWVTSQVAGM LRTNASDYTA SWQDYIHGII SETTNYQVTE GGPVIDNEYT
     QYGVTGGAGY FADLEADYHN SSIVVPLTYN DPGEGKNFVN GTGAVDVYGL DSYPQRFDCS
     NPEVWNPVVT NWHDYHENTN PSQPWYFPEF QAGAFDAWGP TAPGYESCRV LTGADFENVF
     YHTLWASNAK LLSFYMVYGG TSWGALPFHG VYTSYDYGSA IAENRTLTDK YTELKRQGLF
     LRSSPEFYKT DWVGNSSTDA VTVSNPAAFA VYLVNPDTGA GFYIVRQENS TSMATTSFKL
     DIQTSAGSLT VPQTVPNITL GGRQSKVIVT DYTFGSSSKV LYSTAFVLYA GVIGDRDVLF
     LYGDSNQEHE AAITFTGTPF PKASNSRVAL ECKSNQETTI GFLAGINGLV TVYDSTTQLI
     LFADTVTAGT FWSPVIPGTS GDFPNYWQFG TNTSILVGGP YLVRNATING RTLALRGDLE
     TGVRLTVIAH PDLDEITWND VPVSADVQAT SDLSSVGGFV GQLETKQVIA GISVPPLTNW
     KYADSLPEIQ TSFLDANWTL ANHTTTNIPF PPYYGDGRIL YGCDYEYCEN IVLWRGHFNA
     TGNEKWVNLS INGGEAFAAS VWVNNHFLNT SYGNSTNDRN ILEETDDKFY FPQGSLLPDQ
     DNVITIVQIL QDNMGLNETG ETPDASKSPR GVRGFQLDIG NFSEWRVQGK IGGYTNYPDR
     LRGVFNEGGL FGERQGWHLP GYNTSSWASR DLSQGLPNAM AGVGFFVTTF NLSIPSGYDV
     PISFNFDNGI QPYRVYLYVN GWMMGKRVAN LGPQIKFPVQ EGILNYNGIN TAAVALWAME
     ATTVSPTLEL AIDGIYEGGI GGVVSNNPPY SSTGRL
//
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