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Database: UniProt
Entry: A0A0D7B9U1_9AGAR
LinkDB: A0A0D7B9U1_9AGAR
Original site: A0A0D7B9U1_9AGAR 
ID   A0A0D7B9U1_9AGAR        Unreviewed;      1046 AA.
AC   A0A0D7B9U1;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   13-FEB-2019, entry version 19.
DE   SubName: Full=Glycoside hydrolase family 35 protein {ECO:0000313|EMBL:KIY66929.1};
GN   ORFNames=CYLTODRAFT_21176 {ECO:0000313|EMBL:KIY66929.1};
OS   Cylindrobasidium torrendii FP15055 ss-10.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Agaricomycetidae; Agaricales; Physalacriaceae;
OC   Cylindrobasidium.
OX   NCBI_TaxID=1314674 {ECO:0000313|EMBL:KIY66929.1, ECO:0000313|Proteomes:UP000054007};
RN   [1] {ECO:0000313|EMBL:KIY66929.1, ECO:0000313|Proteomes:UP000054007}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FP15055 ss-10 {ECO:0000313|EMBL:KIY66929.1,
RC   ECO:0000313|Proteomes:UP000054007};
RX   PubMed=25683379; DOI=10.1016/j.fgb.2015.02.002;
RA   Floudas D., Held B.W., Riley R., Nagy L.G., Koehler G., Ransdell A.S.,
RA   Younus H., Chow J., Chiniquy J., Lipzen A., Tritt A., Sun H.,
RA   Haridas S., LaButti K., Ohm R.A., Kues U., Blanchette R.A.,
RA   Grigoriev I.V., Minto R.E., Hibbett D.S.;
RT   "Evolution of novel wood decay mechanisms in Agaricales revealed by
RT   the genome sequences of Fistulina hepatica and Cylindrobasidium
RT   torrendii.";
RL   Fungal Genet. Biol. 76:78-92(2015).
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; KN880540; KIY66929.1; -; Genomic_DNA.
DR   EnsemblFungi; KIY66929; KIY66929; CYLTODRAFT_21176.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000054007; 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:UP000054007};
KW   Glycosidase {ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00108869,
KW   ECO:0000313|EMBL:KIY66929.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054007};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     36     53       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      422    603       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1046 AA;  115561 MW;  A8287C9B909578C6 CRC64;
     MDDDALKTRH LSMEFPPDSK SSNLAPYKHA KTATRWSIRL WILALLLSSI AIFKSSPLKT
     NIKVPMDAQN GWGTDEVSFD SYSLSLRGQR VFVNSGEFHT FRLPVPDLWP DILQKFKAAG
     LNAVSLYTHM AIINPSRGVL DFDDWRALAP FYEACKAAGI WVVLRPGPYI NAETTAGGIA
     HWATSEVAGT LRTNASDWHE VWKVYVDGII KESAPYQITH GGPIIAIQLD NEYEQWLGGE
     YFEDLKDAYH NSEIVVPLTY NDPSARRNFI NGTGAVDLYG MDSYPQRFDC SNPHQWNPVD
     LTYHQYHIEV NPSQPWYIPE FQAGAFDAWG PTSPGYGACN VLTGPDFMSV FNLQLWASNA
     KLINYYMVYG GTSWGGIPFP GVYTSYDYGS AIDEQRALTP KYDELKLQGV FLRSSPEFYK
     TDWLGDSSTG AIAASNPEVF VTQLQNPDSK ANFYIVRHNN SSSTDSTDFR IDVATSQGTL
     SLPQVISPLV LGGRQSKLIV TDYAFGASSR VLYSTAQVFY AGIIDGRDVL FLYGDASQQH
     EAAIEFTGTP NKVQLDTDAF STQAGQSGVT IVSFLDGIEG LVTVYDSDTQ LVLYSDRSTA
     ATFWAPTLAG PKENDLANFW SFGTNSSILV GGPYLVRSAS LEDGRLALQG DLKDEARLML
     IAPKGIRSIT WNGQVVAGDV QLLGSSVLRL SLAKRATAMR GIEVPKLTAW RYKDSLPEIS
     KDYDDARWTL ANHTETNIPQ KPYYGDGRML YGCDYGFCEN TVLWRGHFTG VEGQSSVNLS
     INGGEAFAAT VWLNDAFMNT SYGNSTNNRN ILEETDDVFT FPEGSLNISG DNVITIVQDN
     MGLNETEGDN PDSSKGPRGV RGFKLNKGHF EDWKVQGKLG GYLDFPDKTR GVLNEGGLFG
     ERAGYHLPGF DTSDWAKRDL SAGLPNGKAG VGFFVTTFKL DIPTGFDVPI SFVFKEPLGQ
     PYRVFLFVNG WMMGKRVGNL GPQAKFPIQE GILDYRGENT VAVALWAMEE DADIHPELEI
     MIDGVYDGGV GQVRVNNPGY EQREVY
//
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