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Database: UniProt
Entry: A0A010SHV6_9PEZI
LinkDB: A0A010SHV6_9PEZI
Original site: A0A010SHV6_9PEZI 
ID   A0A010SHV6_9PEZI        Unreviewed;      1004 AA.
AC   A0A010SHV6;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   16-JAN-2019, entry version 25.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=CFIO01_02688 {ECO:0000313|EMBL:EXF84373.1};
OS   Colletotrichum fioriniae PJ7.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Glomerellales; Glomerellaceae;
OC   Colletotrichum.
OX   NCBI_TaxID=1445577 {ECO:0000313|EMBL:EXF84373.1, ECO:0000313|Proteomes:UP000020467};
RN   [1] {ECO:0000313|EMBL:EXF84373.1, ECO:0000313|Proteomes:UP000020467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PJ7 {ECO:0000313|EMBL:EXF84373.1,
RC   ECO:0000313|Proteomes:UP000020467};
RA   Baroncelli R., Thon M.R.;
RT   "The genome sequence of Colletotrichum fioriniae PJ7.";
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:EXF84373.1}.
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DR   EMBL; JARH01000168; EXF84373.1; -; Genomic_DNA.
DR   RefSeq; XP_007591881.1; XM_007591819.1.
DR   EnsemblFungi; EXF84373; EXF84373; CFIO01_02688.
DR   KEGG; cfj:CFIO01_02688; -.
DR   Proteomes; UP000020467; 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:UP000020467};
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:EXF84373.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000020467};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     20       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        21   1004       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5001456636.
FT   DOMAIN      394    569       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1004 AA;  111096 MW;  751A51B29561D721 CRC64;
     MKFPFFLAVA SLFFLSPTDA VLSKSHIRST NVTQDLVRWD EHSLFIRGDR IVILSGEFHP
     WRIPSPGLWL DVLQKIKALG YNAVSFYVNW ALLEGKPGEV RMDNVFDLQP FIEAAVEAGL
     YLIARPGPYI NSELSGGGFP GWLQRNKGEL RSMAPDYTNA TENYISSVLR VISAAQITKG
     GPIILVQPEN EYSLAVGTAN PVESTRLLDP NYMEFMEDQF RRNGIEVPLI GNDAVPLGNW
     APGSGKGELD IYAHDAYPFY KGCDHPTDWT DLTALSLTYT YRNHLQQSPS SPYAVLEYQG
     GAPDPWGGVG LDKCAAKINQ DFTRVFVKEL VSRSIKILNL YMTYGGTNWG NMGHSEGYTS
     YDHGASIREN RGIDREKYSE AKIEAHFLRV SEAYLTAIPQ NATSIEFVST PDLRVVPIVG
     DKTRFYVVRH TDYTSLNRTS YRLNLPTSAG NISVPLLGGD LSLHGRDSKI HITDHDVGGT
     SLIYSSAEIF TWKTYGNKTL LILYGGGGEE HEFAVPSSLG KPQFEGSNAT TRAYGSFRAV
     HWLVQERRQV VHFETLEIHL LWRNDAYRHW ILDLPDADNG LIQPTLGKSS IVAKGPYLLR
     NATFADGVLH LAGDINATTT LEILGGVPPN SGLSFNGRSL SNAQWKNGRL QAELVFESPT
     LNLPVFSELK WHSIDSLPEV SESYDDSAWT KATLEQSNNP RNLTTPTSLY CSDYGFHGGS
     LIYRGHFTAT GNESFFNVTT AGGFAYSHSV WVNETFLGSF PGDPHTANST QVFDLTGLKL
     EGPSVFTVVI DHMGMSMNFW ARSDWMKLPR GIVDFSLGGH QQSDVSWKLT GNLGAEDYID
     KTRGPLNEGA FYAERQGFHL PGASTSDWAP VTPFEGTKTA GVSFYKTEFP LDMPIGYDIP
     LSFIISNVTA STGESSLFRA QLFVNGYQFG KYVNYLGPQT RFPVPEGILN YNGNNTVALT
     LWALDGSGAR LKGFELAVDH IVQSGYRKPG QTPQPSWVKR IGAY
//
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