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Database: UniProt
Entry: A0A194WC98_9PEZI
LinkDB: A0A194WC98_9PEZI
Original site: A0A194WC98_9PEZI 
ID   A0A194WC98_9PEZI        Unreviewed;      1014 AA.
AC   A0A194WC98;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   16-JAN-2019, entry version 13.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=VM1G_09451 {ECO:0000313|EMBL:KUI73723.1};
OS   Valsa mali.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX   NCBI_TaxID=105487 {ECO:0000313|EMBL:KUI73723.1, ECO:0000313|Proteomes:UP000078559};
RN   [1] {ECO:0000313|EMBL:KUI73723.1, ECO:0000313|Proteomes:UP000078559}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=03-8 {ECO:0000313|EMBL:KUI73723.1,
RC   ECO:0000313|Proteomes:UP000078559};
RA   Yin Z., Liu H., Gao X., Li Z., Song N., Ke X., Dai Q., Wu Y., Sun Y.,
RA   Xu J.-R., Kang Z.K., Wang L., Huang L.;
RT   "Genome Sequence of Valsa Canker Pathogens Uncovers a Specific
RT   Adaption of Colonization on Woody Bark.";
RL   Submitted (DEC-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}.
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DR   EMBL; CM003108; KUI73723.1; -; Genomic_DNA.
DR   EnsemblFungi; KUI73723; KUI73723; VM1G_09451.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000078559; Chromosome 11.
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:UP000078559};
KW   Glycosidase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108869};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078559};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     17       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        18   1014       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5008267399.
FT   DOMAIN      392    573       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1014 AA;  111187 MW;  90302A4CAC401C09 CRC64;
     MKPETVLLGA SLWGSWASSI LAGAPTALKR QNMLQNVVTF DEHSILIHGE RLFLYSGEFH
     PFRLPVPDLW LDVFQKIKSL GFNGVSFYVD WALVEGKQGQ VNLDGIWDLR PFFDAAVEAG
     IYLIARPGPY INAEVSAGGF PGWLLRVECI LRSNCSEYED ATKNYLSTIG KVIADAEVTK
     GGPVILVQPE NEYSTWPDVA ETEFPLDFNI DYMAFVEEQL REAGSTVPFI DNDNKVLGNF
     APGTGLGAVD LYGIDSYPVR YDCSQPDVWP TYRWPVDWQV LHEEQSPSTP FAIPEFQGGT
     ATSWGSVGQD MCAALVGPEA LRVFYKNNYS FGVKIMNIYM TYGGTNWGNL GYMGGDTSYD
     YGASITEGRQ VWREKFSEQK LQANFFKVSP GYLTARPGNE GNGTYAFTSD VGVTPLLGEQ
     GMNFYVVRHA DFTSNTTVKY RLELPTSAGN ITIPQLGGDL SLIGRDAKLI VTDYAVGEIK
     LIYSTADIFT WATGTSGKTV LILYGTAGEL HEFSLPVSSG RPVSLGHDSS VIIKQRTSGW
     VVQWTVTPAQ QVIHVSEAGL EIRLLWRNDA FDYWVLELPK LEPIGNFSSP SKSVAIVKGG
     YLMRTAALDG PTLLLTGDFN ATTDTELVFE PTGKVDSLTI NGEALQTRRS DLGTLVSRVT
     YTPPTIRLPD FAALTWHAID SLPEISPGES YDDSLWTVCN HTTSTNNQRN LSTPTSLYAS
     DYGYHAGSLL YRGHFTSTGS ESELFLNVSG GYAFSHSVLL DSTFLGSWVG SPDNKTYAQT
     FPLPTNTTAG VDHVITVLMD HMGQDEEAPG TDAVKYPMGI LDYALYAHPK GDVQWKLTGN
     LGGEDYVDRT RGPRNEGGMF AERKGYHLPV PPVHDASLGW TVSSPISSGL SGPGVRFYST
     TFELHVPDGY DVPLSFVFAN NTGEVAAYRV QLFVNGYQYG KFIPYMGPQS EFPVPEGILN
     YGGTNYVGLT LWALEEKGAR LGGLSLEASM PVMSSMKRPG LAPQPVWELR PSSY
//
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