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Database: UniProt
Entry: A0A1S9DP05_ASPOZ
LinkDB: A0A1S9DP05_ASPOZ
Original site: A0A1S9DP05_ASPOZ 
ID   A0A1S9DP05_ASPOZ        Unreviewed;      1211 AA.
AC   A0A1S9DP05;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   13-FEB-2019, entry version 10.
DE   SubName: Full=Glycoside hydrolase family 35 {ECO:0000313|EMBL:OOO10791.1};
GN   ORFNames=OAory_01065990 {ECO:0000313|EMBL:OOO10791.1};
OS   Aspergillus oryzae (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=5062 {ECO:0000313|EMBL:OOO10791.1, ECO:0000313|Proteomes:UP000190312};
RN   [1] {ECO:0000313|EMBL:OOO10791.1, ECO:0000313|Proteomes:UP000190312}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCC7051 {ECO:0000313|EMBL:OOO10791.1,
RC   ECO:0000313|Proteomes:UP000190312};
RA   Thammarongtham C., Vorapreeda T., Nookaew I., Srisuk T., Land M.,
RA   Jeennor S., Laoteng K.;
RT   "Genome sequencing of Aspergillus oryzae BCC7051.";
RL   Submitted (OCT-2016) 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:OOO10791.1}.
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DR   EMBL; MKZY01000004; OOO10791.1; -; Genomic_DNA.
DR   Proteomes; UP000190312; Unassembled WGS sequence.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:InterPro.
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   Gene3D; 3.90.190.10; -; 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   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR026893; Tyr/Ser_Pase_IphP-type.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR000387; TYR_PHOSPHATASE_dom.
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   Pfam; PF13350; Y_phosphatase3; 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   SUPFAM; SSF52799; SSF52799; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000190312};
KW   Glycosidase {ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00108869,
KW   ECO:0000313|EMBL:OOO10791.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000190312};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     23       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        24   1211       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5013340718.
FT   DOMAIN     1086   1155       TYR_PHOSPHATASE_2. {ECO:0000259|PROSITE:
FT                                PS50056}.
SQ   SEQUENCE   1211 AA;  134153 MW;  0370A35705E10C23 CRC64;
     MRLLSFIYLV WLALLTGTPQ VSATDNGKTS DVAWDKYSLS VKGERLFVFS GEFHYQRLPV
     PELWLDVFQK LRANGFNTIS VYFFWSYHSA SEDVFDFTTG AHDIQRLFDY AKQAGLYVIA
     RAGPYCNAET SAGGFALWAA NGQMGSERTS DEAYYKKWKP WILEVGKIIA ANQITNGGPV
     ILNQHENELQ ETTYDSNDTK VIYMEQVAKA FEEAGVVVPS SHNEKGMRTV SWSTDYKNVG
     GAVNVYGLDS YPGSLSCANP NSGFNLLRTY YQWFQNYSYT QPEYLAEFEG GWFQPWGGSF
     YDSCASELSP EFADVYYKNN IGSRVTLHNI YMTFGGTNWG HSAAPVVYTS YDYGSPLRET
     REIRDKLKQT KLLGLFTRVS KDLLKTYMEG NGTSYTSDDS IYTWALRNPD SDAGFYVVAH
     NTSSSREVTT FSLNITTSAG AMTIPDIELD GRQSKIIVTD YSIGSESSLL YSSAEVLTYA
     TLDVDVLVFY LNAGQKGAFV FKDAPADLKY QTYGNSNLSA LETSQGTQYS YTQGEGVTAV
     KFSNGVLVYL LDKETAWNFF APPTVSSPTV APNEHILVFG PYLVRGASIK HDTVEIVGDN
     SNSTSIEIYT GDEHVKKVSW NGNLIDTRAT AYGSLIGTVP GAEDIEISLP SLSSWKAQDT
     LPEISPDYDD SRWTICNKTT SVNSVAPLSL PVLYSGDYGY HTGTKIYRGR FDGQNATGAN
     VTVQNGVAAG WAAWLNGAYV GGFSGDPDKV ASWEVLKFNH SSLRSRDNVL TIITDYTGHD
     QNSQKPIGTQ NPRGIMGATL IGGGNFTLWR IQGNAGGEKN IDPVRGPMNE GGLYGERMGW
     HLPGYQVPES ALDSSPLEGV SGAEGRFYTT SFQLDLEEDL DVPIGLQLSA PAGTEAVVQI
     FMNGYQFGHY LPHIGPQSLF PFPPGVIKNR GQNSLAISMW ALTDAGARLE QVELKAYAKY
     RSGFDFNRDW TYLQPGWKDR TETEHQMATA KLHAETGTST PPNNNNTDHL FQLPHVRRQL
     ISLTGKAFER SLLWRLDWWN FFKVLALAAS GYRNDAVIIV GEQVMSPRGL IGLGLDTLDS
     STAEMKEIFE LFASQNDGAD RTYPALVHCT QGKDRTGLVV LMLLLLTGVV SDEAMTADYV
     RSEPELVVEV EERMKEIRKL GLSEDYTKCP DGFTTEIRRH LQERYGGVDG YLRFVGVEKK
     KLDVIREALV A
//
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