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Database: UniProt
Entry: A0A168D485_9HYPO
LinkDB: A0A168D485_9HYPO
Original site: A0A168D485_9HYPO 
ID   A0A168D485_9HYPO        Unreviewed;      1009 AA.
AC   A0A168D485;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   16-JAN-2019, entry version 16.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=ISF_01224 {ECO:0000313|EMBL:OAA72151.1};
OS   Cordyceps fumosorosea ARSEF 2679.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Cordycipitaceae;
OC   Cordyceps.
OX   NCBI_TaxID=1081104 {ECO:0000313|EMBL:OAA72151.1, ECO:0000313|Proteomes:UP000076744};
RN   [1] {ECO:0000313|EMBL:OAA72151.1, ECO:0000313|Proteomes:UP000076744}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 2679 {ECO:0000313|EMBL:OAA72151.1,
RC   ECO:0000313|Proteomes:UP000076744};
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|RuleBase:RU000675,
CC         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:OAA72151.1}.
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DR   EMBL; AZHB01000002; OAA72151.1; -; Genomic_DNA.
DR   RefSeq; XP_018707597.1; XM_018844831.1.
DR   EnsemblFungi; OAA72151; OAA72151; ISF_01224.
DR   GeneID; 30017516; -.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000076744; 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; IPR019801; Glyco_hydro_35_CS.
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.
DR   PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000076744};
KW   Glycosidase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108869, ECO:0000313|EMBL:OAA72151.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076744};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     18       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        19   1009       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5007896160.
FT   DOMAIN      392    568       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1009 AA;  110271 MW;  86DBE8C4CB5A5B22 CRC64;
     MKLSFTLLAA VAAPATRCLT LGSRSKSYNV IHEPGKRELL QDLITWDSQS LFIRGERALL
     FSGEVHPFRL PVPSLYLDVL QKIRALGFNT VSFYVDWALL EGKPGEFRAD GIFALEPFFE
     AATKAGIYLL ARPGPYINAE VSGGGYPGWL QRVKGLLRTD APDYLAATDN YMANIGAIIA
     KAQITNGGPV ILFQPENEYS GASVSPFPNK KYMQYVIDQA RKAGIVVPLI DNDSYPGGTG
     APGTGEGEVD IYGFDSYPLG FDCAHPDVWP AGNLPTDLHK THMRLSPSTP FSIVEFQGGS
     YDPFGGYGFD QCYKLVNHEF SRVFDKNNLA AGVNIFNIYM IFGGTNWGNL GHPNGYTSYD
     YGASIREDRY IDREKYSETK LEAQFMRVSP SILETTPGDA TTGVYSDSKD IAITPMLSKK
     AGNYFVVRHA DYQSLNSTSY VVKLPTSQGT LSIPQAGGRL TLSGRDSKFH VTDYVMGDYT
     LLYSTAEIMT WQKFDNRTLV ILYGGAGEMH EFALKNAVRV GDSYGSSVAY QQRNSSVIVQ
     FTPTPERQVI RIGDLTVFML DRNSAYDYWV PVLPKDGSAY GSSVMNPDTI IVNGGYLVRS
     ASVSGATVSI QADFNQTTSL EVIGAPRRAS KLSVNGKPTR FKKTADGTWL STPSIRLPTS
     VPLPDLRALN WHAVDSLPEI RPAYDDALWT RANLTATPNP RGAPLRTPVS LYGADYGFNA
     GALLFRGTFT AAGDEDQLLL TTSGGTAYAA AAWIDDVFVG SFAGRKDWDT VIVTHTIPPQ
     PAGSRHVLTV VVDSMGFNEN LTPGNDDMKA PRGILDYQLH STANSTRGPT PITDWKIAGN
     LGGEDYRDRF RGPLNEGGFF FERSGYHQPS PPLDRFAKAS PFNGTAEAGV SYYAAKFDLD
     LPADEYDIPI AVRFDGDGNA PTYRALLYVN GFQYGRYVSN IGPQTEFPVP EGILNYNGEN
     WLGVAVWAMD SDGARIPGLS LTSRPPVLTS RNKVELVKGP SYTKRDGAF
//
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