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Database: UniProt
Entry: A0A165D0B5_9BASI
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ID   A0A165D0B5_9BASI        Unreviewed;      1140 AA.
AC   A0A165D0B5;
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:KZT51795.1};
GN   ORFNames=CALCODRAFT_503076 {ECO:0000313|EMBL:KZT51795.1};
OS   Calocera cornea HHB12733.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Dacrymycetes; Dacrymycetales; Dacrymycetaceae; Calocera.
OX   NCBI_TaxID=1353952 {ECO:0000313|EMBL:KZT51795.1, ECO:0000313|Proteomes:UP000076842};
RN   [1] {ECO:0000313|EMBL:KZT51795.1, ECO:0000313|Proteomes:UP000076842}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB12733 {ECO:0000313|EMBL:KZT51795.1,
RC   ECO:0000313|Proteomes:UP000076842};
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; KV424090; KZT51795.1; -; Genomic_DNA.
DR   EnsemblFungi; KZT51795; KZT51795; CALCODRAFT_503076.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000076842; 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:UP000076842};
KW   Glycosidase {ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00108869,
KW   ECO:0000313|EMBL:KZT51795.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076842};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    103    120       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    126    149       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      510    698       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1140 AA;  124087 MW;  0E9A7495AB1E4C77 CRC64;
     MAPPEEPRRS SHQSPDEEVQ QQDASNTLAH HDVHSRSAPS ISSGEEDEKV EGSRQEEKRR
     LETASEHLLL PQHAMISPSG KSFSSKGISH IYRPRPRNGG TRALLCGGIL LLLLSAVYVQ
     ESHMRFTGLL TTALSLLGLS GLQAALGIAP RAPALVSNNL TNLVQWDPYS LYVLGQRTFL
     WSGEFHTWRL PVPDLWTDIL QKAKAAGMNA MSIYVHWGLT NPSNGTIDFT GVRALAPLFE
     AASASGLWVV VRPGPYINAE TTAGGIAHWV TSEVAAHLRT NETEYENAWV PYIKGIIEQV
     KPYQITEGGP VIAVQIDNEY TQADSPGWPG KAGYFVQLED LYRSEGIVVP LTYNDPGMGD
     NFATGTGAVD IYGLDSYPQS FDCSQPYVWN SVVTNYYTYH MGVSPEEPFY IPEFQGGAFD
     PWGPNAPGYA NCRILTDSDF EQIFYLNLWA NNVKMANFYM LYGGTSWGYL AFHGVYTSYD
     YGASIAETRM LTPKYAELKR EGLFLRSVPD FYKTDVIGNS STSAVNVSSP LIFGTYLRNP
     DTGAGFYIIR QQNSSSLDTV SFTLQANTSE GVLSLPQDGS NITLTGRASK LIAHDIYFGS
     SHLLYSTASI LFAGTIGGRD VLFLHGPSSD SHEAAFKLAG ATSAAVQVSG DLNIRTATIM
     DGTHTLVDVV PGSSGISYIW DSPSSLVLFA DSDTAGTFWA PTVAKSSTSQ FQHYYQFGTN
     ETVLIGGPYL VRNASISGDT LALRGDLNET TYLTVLAPTS VRRVTWNGYE VELDATAKAP
     PASGILTATI TPKFTASSFS LPALNTWKYA NSLPEVSGSY DDSYWTTADK YATNIPYKPL
     YGDGPILYGC DYGYCEGAVL WRGHFEGTGN ETGVELLING GEAFAASVWL NSNFLGTTYG
     NSSNNMNILE ETNTLFPFNG GVLTGQDNIV TIIQDNMGLN ETQDDNGDTS KSPRGIRGYE
     IHGHNYFTSW KVQGKLGGYT NFPDKTRGIF NEGGFYAERA GWHLPGFDDS AWETKPLSTG
     LEKAGVGMFR TTFDLNVPTG MDVSLSFDFD PTPQAYRALL FVNGWQVGRR VANLGPQYSF
     PVHEGILDYS GTNTVAVLLW AMENTGAYAS LNMTVNGVFD GGVGPIALDN PGWSSRGQHI
//
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