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Database: UniProt
Entry: A0A135U033_9PEZI
LinkDB: A0A135U033_9PEZI
Original site: A0A135U033_9PEZI 
ID   A0A135U033_9PEZI        Unreviewed;      1003 AA.
AC   A0A135U033;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   16-JAN-2019, entry version 11.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=CSAL01_07694 {ECO:0000313|EMBL:KXH53744.1};
OS   Colletotrichum salicis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Glomerellales; Glomerellaceae;
OC   Colletotrichum.
OX   NCBI_TaxID=1209931 {ECO:0000313|EMBL:KXH53744.1, ECO:0000313|Proteomes:UP000070121};
RN   [1] {ECO:0000313|EMBL:KXH53744.1, ECO:0000313|Proteomes:UP000070121}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 607.94 {ECO:0000313|EMBL:KXH53744.1,
RC   ECO:0000313|Proteomes:UP000070121};
RA   Baroncelli R., Thon M.R.;
RT   "The genome sequence of Colletotrichum salicis CBS 607.94.";
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:KXH53744.1}.
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DR   EMBL; JFFI01001825; KXH53744.1; -; Genomic_DNA.
DR   EnsemblFungi; KXH53744; KXH53744; CSAL01_07694.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000070121; 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:UP000070121};
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:KXH53744.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070121};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     20       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        21   1003       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5007804503.
FT   DOMAIN      397    573       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1003 AA;  110665 MW;  FF1D2DEA57F0C7B3 CRC64;
     MRFHRALTAL IWLFASGAWA TDNGLTDVVS WDKYSLVIND TRTYILSAEF HYQRTPVPEL
     WPDILQKFKA NGFNTVSIYF FWSYHSAAEG VYDFETAGKN IQRLFDYCKE AGLYVIARAG
     PYCNAETNGG GLALWGSDGR FGKIRTSDER YQAGWLPFIT QVGKIIAANQ ITNGGPVILN
     QVENEYQESV YSPDHTSVIY MEQLKKAFHD AGIVVPLTHN EKGMRSRSWS TDYNNVGGAV
     NVYGLDSYPG ALSCTDPTVG FNVVRTYFQW FSNYSFTQPS YLAEFEGGWF SNWGSPTFYD
     QCASEHDPAF ADVYYKNNIG QRVTLLSIYM SYGGTNWGHC ESYTNQDTHY IRLTKVAAAP
     QVYTSYDYSA PLRETREQWT KLFQTKLIGL FTRVSSDLLK VEMIGNGTGY SLSSSSAFSW
     VLRNPDTQAG FTVVQQASTK SMTPVQFDVT LNTTAGPVTV PDVMLNGRQS KILVTDYVFG
     KHTLLYASAD IATYGIFDTE VIVFYLQEGQ TGEFAFKDAG DLTFEVFGDT DLQETTSGNH
     SAFTWKQVAG STVVKFSNGA LIYLLEQKSA WRFWAPPTTS NPTVKANEQL FIQGPYLVRS
     ASISHGVLHV SGDSDKATLI EAYVGDKPIE TIDWNGQRLA ATKTAYGSFT AQIPGAEDRA
     VTLPELSNWR AAEALPEAAP DYDDSRWTVC NKTTTPSPYA PVTLPVLYSS DYGFYSGAKI
     YRGYFDGANA TSVNITASGG LAFGWSAWVN GQFLGGDVGA ASATTTNKTL TFPRSALLEK
     NNVVTVVVDY HGHDQASTAQ GINNPRGILG AQLQPGSTRT NTGFKLWKLA GAAGGEANID
     PVRGPMNEGG LYPERLGWHL PGFTPTGSSW KPESPLVGLS GAGIRFYVTD FTLNIDSDLD
     APLGIEFSAP AGTTARVMFW INGYQYGKYV PHIGPQTRFP VPPGVLNNRG RNTLAVSLWA
     QTDAGAKLDG LKLVRYGQYQ TDFKFNRDWS YLQPGWEDRQ EYA
//
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