GenomeNet

Database: UniProt
Entry: BGALB_SCLS1
LinkDB: BGALB_SCLS1
Original site: BGALB_SCLS1 
ID   BGALB_SCLS1             Reviewed;        1008 AA.
AC   A7EBU5;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   16-JAN-2019, entry version 68.
DE   RecName: Full=Probable beta-galactosidase B;
DE            EC=3.2.1.23;
DE   AltName: Full=Lactase B;
DE   Flags: Precursor;
GN   Name=lacB; ORFNames=SS1G_02781;
OS   Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White
OS   mold) (Whetzelinia sclerotiorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Sclerotinia.
OX   NCBI_TaxID=665079;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18683 / 1980 / Ss-1;
RX   PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA   Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P.,
RA   Couloux A., Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S.,
RA   Fournier E., Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M.,
RA   Pradier J.-M., Quevillon E., Sharon A., Simon A., ten Have A.,
RA   Tudzynski B., Tudzynski P., Wincker P., Andrew M., Anthouard V.,
RA   Beever R.E., Beffa R., Benoit I., Bouzid O., Brault B., Chen Z.,
RA   Choquer M., Collemare J., Cotton P., Danchin E.G., Da Silva C.,
RA   Gautier A., Giraud C., Giraud T., Gonzalez C., Grossetete S.,
RA   Gueldener U., Henrissat B., Howlett B.J., Kodira C., Kretschmer M.,
RA   Lappartient A., Leroch M., Levis C., Mauceli E., Neuveglise C.,
RA   Oeser B., Pearson M., Poulain J., Poussereau N., Quesneville H.,
RA   Rascle C., Schumacher J., Segurens B., Sexton A., Silva E., Sirven C.,
RA   Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA   Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT   "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT   sclerotiorum and Botrytis cinerea.";
RL   PLoS Genet. 7:E1002230-E1002230(2011).
CC   -!- FUNCTION: Cleaves beta-linked terminal galactosyl residues from
CC       gangliosides, glycoproteins, and glycosaminoglycans.
CC       {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000305}.
DR   EMBL; CH476623; EDN99923.1; -; Genomic_DNA.
DR   RefSeq; XP_001596561.1; XM_001596511.1.
DR   ProteinModelPortal; A7EBU5; -.
DR   SMR; A7EBU5; -.
DR   STRING; 5180.EDN99923; -.
DR   EnsemblFungi; EDN99923; EDN99923; SS1G_02781.
DR   GeneID; 5492844; -.
DR   KEGG; ssl:SS1G_02781; -.
DR   EuPathDB; FungiDB:SS1G_02781; -.
DR   InParanoid; A7EBU5; -.
DR   OMA; GHQSKII; -.
DR   Proteomes; UP000001312; Unassembled WGS sequence.
DR   GO; GO:0005618; C:cell wall; IBA:GO_Central.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005773; C:vacuole; IBA:GO_Central.
DR   GO; GO:0004565; F:beta-galactosidase activity; IBA:GO_Central.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
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; 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.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Complete proteome; Disulfide bond;
KW   Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL        1     18       {ECO:0000255}.
FT   CHAIN        19   1008       Probable beta-galactosidase B.
FT                                /FTId=PRO_0000395233.
FT   ACT_SITE    193    193       Proton donor. {ECO:0000255}.
FT   ACT_SITE    305    305       Nucleophile. {ECO:0000255}.
FT   BINDING      87     87       Substrate. {ECO:0000250}.
FT   BINDING     132    132       Substrate. {ECO:0000250}.
FT   BINDING     133    133       Substrate; via amide nitrogen.
FT                                {ECO:0000250}.
FT   BINDING     134    134       Substrate. {ECO:0000250}.
FT   BINDING     192    192       Substrate. {ECO:0000250}.
FT   BINDING     262    262       Substrate. {ECO:0000250}.
FT   BINDING     370    370       Substrate. {ECO:0000250}.
FT   CARBOHYD     20     20       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     23     23       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    108    108       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    208    208       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    269    269       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    453    453       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    594    594       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    624    624       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    681    681       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    703    703       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    782    782       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    788    788       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    816    816       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    826    826       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    879    879       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    268    321       {ECO:0000250}.
SQ   SEQUENCE   1008 AA;  110685 MW;  52E5C90A03793D5E CRC64;
     MLLQSLFAWA LAIGPCIAQN STNSTWPIHN NGLTTQVEWD HYSLMVDGQR FFLWSGEFHY
     WRIPVPELWV DVLQKVKAAG FNTFAIYTHW YFHNPNPNTL DFENAAHNFT KIFDLAKELG
     MFVVFRPGPY VNAESNAGAF PLWLTTGAYG ALRNNDERYT EAWTPFWEKV ASIVAPYQFT
     NGGNVLTYQI ENELGSQWRG TPSNKVPNLS SVEYMEALEA SARAHGITIP FQANDPNLNS
     DSWSKDFYDG YGSVDIYGMD SYPACWTCNL TECDSTNGAY KAFNVIDYYD HFEAISPTQP
     SFLPEFQGGS FNPWGGPEGG CPENSPADFA NLFYRNNVGQ RVTAMSLYMI YGGTNWGWLA
     APVVATSYDY SSPISENRMI NDKYAETKLF GHFLRVAKDL TKTDRIGTGK TASTNPNVVY
     SEIRNPDTNA AFYVTIHKES TVGTREEFYI NANTSKGAFK IPQKAASIVL NGFQSKIIVT
     DFNFGSHSLL YSTAEVLSHS IVDDQDILAL WMPTGEAGEF VVTGAKSGSV SSCGGCSSVG
     FYPQGDDLLV TISQSKGISV LTFDDGLRVL VMDRSFAYEF WVPVLTADPF SPANETVFVQ
     GPSLVRSAAY SSDGSTLDLT GDNNGTSTQI QVFPPKSVSK VTWNGQVITT EKTDYDSLIG
     SLTGPALDSL TLPTISGWKA NDSLPERLPT YDDSWWVAAD HMNTSNPTKP ETLPVLYIDD
     YGYHVGNHLW RGRFEGSASG VYLSVTGGRA FGYSAWLNGE FIGSYLGAAY PDTGKLTLSF
     SNVTVNSNST NILLVLQDNS GHDETSEALN PRGINNATLI SSSTKNFTSW KVTGTAGKPD
     TAIDPVRGIL SEGGLYAERL GWHLPDFDDS EWSSASPSNV SSSAGVTFYR TTVSLAIPTG
     LDVAISFTLK ASPSNAALRV LLFVNGYQYG RFSPWIGNQV EFPVPPGILN YDGDNVIGLS
     VWRQEEGDES MGVNVGWKVT EAFASSFEPI FDAAYLQPGW TDERLQYA
//
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