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Database: UniProt
Entry: A0A168FAA9_CORDF
LinkDB: A0A168FAA9_CORDF
Original site: A0A168FAA9_CORDF 
ID   A0A168FAA9_CORDF        Unreviewed;      1006 AA.
AC   A0A168FAA9;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   13-FEB-2019, entry version 15.
DE   SubName: Full=Beta-galactosidase lacA {ECO:0000313|EMBL:OAA74885.1};
GN   ORFNames=LEL_06873 {ECO:0000313|EMBL:OAA74885.1};
OS   Cordyceps confragosa RCEF 1005.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Cordycipitaceae;
OC   Cordyceps.
OX   NCBI_TaxID=1081108 {ECO:0000313|EMBL:OAA74885.1, ECO:0000313|Proteomes:UP000076881};
RN   [1] {ECO:0000313|EMBL:OAA74885.1, ECO:0000313|Proteomes:UP000076881}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCEF 1005 {ECO:0000313|EMBL:OAA74885.1,
RC   ECO:0000313|Proteomes:UP000076881};
RX   PubMed=27071652; DOI=10.1093/gbe/evw082;
RA   Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT   "Divergent and convergent evolution of fungal pathogenicity.";
RL   Genome Biol. Evol. 8:1374-1387(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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OAA74885.1}.
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DR   EMBL; AZHF01000005; OAA74885.1; -; Genomic_DNA.
DR   EnsemblFungi; OAA74885; OAA74885; LEL_06873.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000076881; 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:UP000076881};
KW   Glycosidase {ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00108869};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076881};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     18       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        19   1006       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5007896773.
FT   DOMAIN      394    570       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1006 AA;  110861 MW;  40151F01F272F1F3 CRC64;
     MKLSAFVAQL ALSSLAAAAA IQGNRFGPFK VISDVEQRDA HQDVVTWDAH SLFIRGERAM
     IYSGEFHPFR LPVPSLWLDV FQKIKALGFN TVSFYVDWAL LEAKEGEYRA EGIFDLDPFF
     KAAETAGIFL IARPGPYINA EVSGGGFPGR LQRLAGQLRT KSPDFLNATE NYMSNIVPLI
     AKYQITNGGA VILYQAENEY SASNGKVPFP DGEYMQDVID QARRLGIVVP IVNNDASKDG
     HNRPGTGAGA VDIYGYDAYP LGFDCSNPTY WRSDALPVDY HEVHMRNSPN TPFLINEFGG
     GSYDPYGGVG YDKCAALTNH EYERVFNKDT LAGGIGILSV YMIFGGTNWG NLGHSKGYTS
     YDYGSAIRED RYLDREKYSE LKLEAHFNRA SPSYLLTTPG ALSTTAYTNN PNIAVTPLQS
     NGTGDFYVVR HSDYQLTASA SYKLHLPTSN GTLTVPQTGG SLTLPGRDTK IHVTDYPVGN
     YTMHYCTAEI FTWQKTGDQT ILVLYGGLGE FHELAFQESH KVTQLEGNKV QTSASYVNTV
     ISWTVETKRQ VVQINDLTIY LLDRNSAYNY WAPVLPTGKN GNFGSSIMNP DAVIVNGPYL
     VRSADVSDST LNIQADFNKT AEFEVIGAPK GVSKLSINGK TTKFTKSKQG NWLAKPSITF
     PDFKLPDLKS LDWMSMDSLP EIQPGYDDSL WTRAQNFTRN SAWPLSTPVS LYGGDYGYNT
     GTLLFRGRFN ATGSENSLFL RTMGGLAFAS SVWLDGKFVG AKLAQADNDA ANSTYTIPQL
     DPGTLHVLTI VVDNMGLNED FVIGDEDMKH PRGILSYSLT TSAGHQTDIY SWKITGNLGG
     EDYKDHFRGP LNEGGLFAER QGYHQPNPPK DKFFNKTPFE QHDGAGIQFY TAKFPLDLPA
     KDYDIPLSFV FDNSTSTEPY HGFLYVNGFQ FGKYISYLGP QTSFPVPEGI LNYAGDNWVS
     LAVWALDTAG AVVPGLSMSA RQPVLTGRQP VELVASPKWV KRSDAY
//
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