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Database: UniProt
Entry: A0A1V1SS22_9FUNG
LinkDB: A0A1V1SS22_9FUNG
Original site: A0A1V1SS22_9FUNG 
ID   A0A1V1SS22_9FUNG        Unreviewed;       990 AA.
AC   A0A1V1SS22;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   13-FEB-2019, entry version 9.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:GAW11390.1};
GN   ORFNames=ANO14919_007340 {ECO:0000313|EMBL:GAW11390.1};
OS   fungal sp. No.14919.
OC   Eukaryota; Fungi.
OX   NCBI_TaxID=1813822 {ECO:0000313|EMBL:GAW11390.1, ECO:0000313|Proteomes:UP000189293};
RN   [1] {ECO:0000313|EMBL:GAW11390.1, ECO:0000313|Proteomes:UP000189293}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=No.14919 {ECO:0000313|EMBL:GAW11390.1,
RC   ECO:0000313|Proteomes:UP000189293};
RG   Technology Reseach Association of Highly Efficient Gene Design;
RA   Itoh H., Matsui M., Shibata T.;
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:GAW11390.1, ECO:0000313|Proteomes:UP000189293}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=No.14919 {ECO:0000313|EMBL:GAW11390.1,
RC   ECO:0000313|Proteomes:UP000189293};
RA   Itoh H., Matsui M., Kumagai T., Arita M., Machida M., Shibata T.;
RT   "Genome Sequence of Fungus Strain No.14919 Producing HMG-CoA Reductase
RT   Inhibitor FR901512.";
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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:GAW11390.1}.
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DR   EMBL; BDMC01000002; GAW11390.1; -; Genomic_DNA.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000189293; 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; 2.
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:UP000189293};
KW   Glycosidase {ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00108869};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189293};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     22       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        23    990       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5013228400.
FT   DOMAIN      370    551       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   990 AA;  109261 MW;  AB6DA0F247D56A4A CRC64;
     MVGFKHILGL LGVSTLGLGA AAQSNSTDWP IHDNGLTDLV KWDHYSFHIN GQRLFIFSGE
     FHYWRYPVPE LWRDLLEKVK AAGFNAFSIY NHWGYHNPLP GVLDFESGAH NFTEILTLAK
     ELGMYMIIRP GPYINAEANA GGFPLWVTTG AYGGLRDNDP RYTEAWTPYM TEISKVIAPH
     LITNGGNVAF FQIENELGNQ WLDIAKRTPN TPVQEYMELL QENARENGID VPLTHNAPNM
     FGYSWSRDFS DAKGNVDVVG LDSYPSCWSC NLSECTSTNG EYVAFQTQNY YDYFTVQSPT
     QPNFMPEFQG GSYNPWGGPQ GGCPGDIGAD FANLFYRNLI YQRVSAISLY MLFGGTSWGW
     HAATVVVAND LAMTDRIGNS TDYSTNPAIA VSELRNPETG ARFYVAMHAY TPSGTSETFR
     LRIDTSEGQL TVPQHGEKIT IDGHQSKILV TDFQYGSKKL LYSTAEILTY AIIDGKEVLV
     LWVPTGESGE FTVKGVKSAK VKSREGGINV KFFPGKSHIT ASFTQNAGMS VVELDDGSRV
     VLLDRSAAYL FWAPSLKNDP IYAPDSTILV QGPYLVRSSN IRGHTLELTG DVANTTTIRV
     FAPKSVRKLK WNGENVKITS TKNGFLTAQL KGAPSYTLPA LTNWKSADGL PEISNDYDDS
     GIAWKVADHT NTSNPTPPAP NNPVLYVDDY GVHAGSHIYR ATFQATQKPP TGIFLDITGG
     LAFGYSVWLN SHFVGSWLGL SYIGKQGLEL SFKNITLNTD RENVLTVLMD NSGHDQRAAA
     LNPRGIGNAT LLGPGTYSFS EWKIAGTARE ENALLDPVRG FLNEGGLYAE RVGMHLPGYA
     DTDWETSDSD SSILSVQGAG VQVFRTQAPL NIPSGIDVSI SFRLTAPSDD TFTSQTGKTN
     QLRALLFVNG YQYGRFNPYI GNQIDFPVPP GILNYNGDNT IAVTVWSQSA DGAEMKFEWN
     VDYVHKSSYD MSFEASYLRP GWDSKRLDYR
//
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