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Database: UniProt
Entry: K1X9R2_MARBU
LinkDB: K1X9R2_MARBU
Original site: K1X9R2_MARBU 
ID   K1X9R2_MARBU            Unreviewed;      1013 AA.
AC   K1X9R2;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   13-FEB-2019, entry version 35.
DE   SubName: Full=Putative beta-galactosidase A {ECO:0000313|EMBL:EKD21737.1};
GN   ORFNames=MBM_00850 {ECO:0000313|EMBL:EKD21737.1};
OS   Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina
OS   leaf spot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Dermateaceae; Marssonina.
OX   NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD21737.1, ECO:0000313|Proteomes:UP000006753};
RN   [1] {ECO:0000313|EMBL:EKD21737.1, ECO:0000313|Proteomes:UP000006753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MB_m1 {ECO:0000313|EMBL:EKD21737.1,
RC   ECO:0000313|Proteomes:UP000006753};
RX   PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA   Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA   Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA   Huang M.-R., Wu R., Zhou Y.;
RT   "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT   evolution.";
RL   BMC Genomics 13:382-382(2012).
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|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; JH921428; EKD21737.1; -; Genomic_DNA.
DR   RefSeq; XP_007288739.1; XM_007288677.1.
DR   EnsemblFungi; EKD21737; EKD21737; MBM_00850.
DR   GeneID; 18756785; -.
DR   KEGG; mbe:MBM_00850; -.
DR   InParanoid; K1X9R2; -.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000006753; 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; 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   Complete proteome {ECO:0000313|Proteomes:UP000006753};
KW   Glycosidase {ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00108869};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006753};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     18       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        19   1013       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5003855017.
FT   DOMAIN      395    572       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1013 AA;  111557 MW;  F4FAA6C8A6E294D0 CRC64;
     MKLCRAVTAF ALAAQAVARS IQGTQMIMER ESNGLQDIVT WDEHSLMVHG ERVFVFSGEF
     HPFRLPVPDL WLDVFQKVKA LGFNVVSFYV HWALLEGEPG VYTAEGVFAF EPFFEAAKQA
     GIYLLARPGP YINAEATGGG FPGWLSRIKG VLRTQDADFL AATDLYMSKI GAAIAKAQIT
     NDGPVILVQP ENEYSGAVGD IPGGFPDPVY FAYIKKQLRD AGIVVPFINN DAWPAGFFAP
     DYSKNGSRIG NVDIYGHDAY PLGFDCANPS TWPAGNLPNY LHSSHEEQSP STPYAIIEFQ
     GGAFDPWGGL GFEQCSRLLN MEFERVFYKN DFASGVAILN LYMIFGGTNW GNLGHAGGYT
     SYDYGANIAE NREIHREKYS ELKLEANFMR VSPAYLTSTI GTPGNATYTN AASIYTTPLF
     DSDSGTNFYI VRHSDYQTLA SETYKLTVTT SKGALSIPQL GGSLTLSGRD SKWHVTDYDL
     GGTTLLYSSA EIFTWKKFDK KTVLLVYGGP GEQHELAVVS ESVAKKVEGS DVTMKSLNGT
     TILNWQTSPT RRVVQVGSLF VYILDRNSAY NYWVPDFART DKWEAYPSNI GNTTSVIVEA
     GYLVRKVYIN NKALHIDGDL NATVPIKVIG APANLKSLHF NSAKLSYTVD PITGDWSSNL
     AYIAPKISLV DLSSLSWKYF DNLPEIKPTY DDSAWTKADH TASNNPFALL TPTSLFASDY
     GYHSGVLIYR GSFIANGQEK DFYLRTQGGS AFGSSVWLNS TYIGSWVGND KSLENNSTYT
     LPNLTAGKTY VFTILVDNNG LQENWIVGEE QMKWPRGILA YTLSGHDDQS SISWKLTGNL
     GGEKYIDKAR GPLNEGGLYA ERQGFHQPFP PNRNWALGSP EMGTKGAGVA FYQADFKLDL
     PNNYDVPLSF SFGNTTVEGS GGVPAEYRAQ LWVNGWQFGK YINNVGPQTD FPVPQGILNY
     HGQNWLAVEI WAQQATGAHL TDFRLKAGTP VWTSMERPAM APIPSYGERT GAY
//
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