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Database: UniProt
Entry: A0A135T3J9_9PEZI
LinkDB: A0A135T3J9_9PEZI
Original site: A0A135T3J9_9PEZI 
ID   A0A135T3J9_9PEZI        Unreviewed;      1019 AA.
AC   A0A135T3J9;
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=CSIM01_13510 {ECO:0000313|EMBL:KXH42733.1};
OS   Colletotrichum simmondsii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Glomerellales; Glomerellaceae;
OC   Colletotrichum.
OX   NCBI_TaxID=703756 {ECO:0000313|EMBL:KXH42733.1, ECO:0000313|Proteomes:UP000070328};
RN   [1] {ECO:0000313|EMBL:KXH42733.1, ECO:0000313|Proteomes:UP000070328}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS122122 {ECO:0000313|EMBL:KXH42733.1,
RC   ECO:0000313|Proteomes:UP000070328};
RA   Baroncelli R., Thon M.R.;
RT   "The genome sequence of Colletotrichum simmondsii CBS122122.";
RL   Submitted (FEB-2014) 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|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:KXH42733.1}.
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DR   EMBL; JFBX01000293; KXH42733.1; -; Genomic_DNA.
DR   EnsemblFungi; KXH42733; KXH42733; CSIM01_13510.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000070328; 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:UP000070328};
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:KXH42733.1};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     18       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        19   1019       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5007803299.
FT   DOMAIN      401    577       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1019 AA;  110317 MW;  8B4182C28B6565A4 CRC64;
     MRPSLFSIAS LGFGLCSAAS VASNLAAGLR SSLALAPVVR ILDEKRDQLQ DIVTWDEHSL
     FVRGERVMIF SGEIHPFRLP VPSLYLDVFQ KVKALGLNTV SFYVDWALLE GKAGDFTVEG
     VFDLQPFFDA ATKAGIYLIA RPGPYINAEA SGGGFPGWLA RLKAKLRTSD PEFLSATDNY
     MANICGIIAK AQITNGGPVI LFQPENEYTN FEDGSSADGP YFQYVIDQAR KAGIVVPLIS
     NDAKAAGHNA PGTGVGAVDI YGFDAYPLGF NCANPNTWPD NALPTTYHAL HLQTSPSTPF
     TIPEFQGGSF DPYGGPGFEK CAALVNHEFE RVFYKNNFGA GVTIYNIYMI FGGTNWGNLG
     HPGGYTSYDY GSAITEERTV SREKYSELKL EAQFLKVSPA YLTATPGNLT VGVYSATPDI
     TVTPLLGNGN GSFFVVRHSN YNSLATTDYT LRLPTSQGTI TIPQSRDLLQ LTRRDSKIVV
     TDYPVGNTTL LYSTAEIFTW KQYKNQTVLV VYSGPGETHE IAIKSTATPV LVEGTSVDHN
     YVNNTLLLAW ETSSTRRVVK VDNLVIYILD RNSAYNYWVP DKPSGSQPAY GTSIMNPDSL
     IVNGGYLVRS ISIQDGTLRV QADFNRTTEI EIIGVEPEVT KLEVNGKQLD HTTNNLTNWI
     ANPSLAGAAP TVPDLKSLNW TFIDSLPEIR AGYDDSAWPL ADHKTTNNTI ANLTTPVSLF
     ASDYGFHTGT LVFRGYFTSN GTEDKLSITT QGGSAFASSV WLNDTFLGSF ANGPDASGDN
     ASNYPLANLT AGATYVLTVL VDTTGLEENF IIPADVMKTP RGIMDYSITS PSGAQTNVPT
     WKITGNLGGE NYADRARGPL NEGGLFIERQ GYHLPSPLES ALNTQRSPFE GTDAPGVAFY
     AAKLDLQIPA TDLDVPLAFV FDDIAASNGT GAYRAILYVN GFQYGRYVSN IGPQTRFPVP
     EGILRYQGTN YIGLAVWALG NGGARVQNFR LDAGEAVTTG REEVKVVDAP AWSQRAGAY
//
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