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Database: UniProt
Entry: K2SSA3_MACPH
LinkDB: K2SSA3_MACPH
Original site: K2SSA3_MACPH 
ID   K2SSA3_MACPH            Unreviewed;       997 AA.
AC   K2SSA3;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   16-JAN-2019, entry version 31.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=MPH_03404 {ECO:0000313|EMBL:EKG19540.1};
OS   Macrophomina phaseolina (strain MS6) (Charcoal rot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Dothideomycetes incertae sedis; Botryosphaeriales;
OC   Botryosphaeriaceae; Macrophomina.
OX   NCBI_TaxID=1126212 {ECO:0000313|EMBL:EKG19540.1, ECO:0000313|Proteomes:UP000007129};
RN   [1] {ECO:0000313|EMBL:EKG19540.1, ECO:0000313|Proteomes:UP000007129}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MS6 {ECO:0000313|EMBL:EKG19540.1,
RC   ECO:0000313|Proteomes:UP000007129};
RX   PubMed=22992219; DOI=10.1186/1471-2164-13-493;
RA   Islam M.S., Haque M.S., Islam M.M., Emdad E.M., Halim A.,
RA   Hossen Q.M.M., Hossain M.Z., Ahmed B., Rahim S., Rahman M.S.,
RA   Alam M.M., Hou S., Wan X., Saito J.A., Alam M.;
RT   "Tools to kill: Genome of one of the most destructive plant pathogenic
RT   fungi Macrophomina phaseolina.";
RL   BMC Genomics 13:493-493(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|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:EKG19540.1}.
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DR   EMBL; AHHD01000163; EKG19540.1; -; Genomic_DNA.
DR   EnsemblFungi; EKG19540; EKG19540; MPH_03404.
DR   InParanoid; K2SSA3; -.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000007129; 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:UP000007129};
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:EKG19540.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007129};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     18       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        19    997       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5003865106.
FT   DOMAIN      391    567       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   997 AA;  107854 MW;  27A47F58182DE0C2 CRC64;
     MKLTSSLLAA GLASQALGYV VGGKPKDLIK PYKREALQDI VTWDEHSLFV NGERIIFLSG
     EYHPFRLPVP SLWLDVFHKI KALGFNGVSF YVDWALLEGT PGEFTAEGVF AWEPFFDAAQ
     EAGIYLLARP GPYINAEVSG GGFPGWLQRV NGTLRTDDPG YINATDNYAR SIGEIIAKAQ
     ITNGGPVILF QPENEYTGAT DNVEFPNENY WAIVEKQFRD AGIVVPYINN DASPQGYFAP
     GSNWTPQVDI YGHDGYPLGF DCANPYTWPD GKLPTNWKTL HEQQSPSTPY SVIEFQGGAF
     DPWGGLGFDQ CSVLLNHEFE RVFYKNLQSF GVTILNLYMI FGGTNWGNLG HPGGYTSYDY
     GSVIRETREI NREKYSELKL QGNFLKVSPA YLTAEPGDLS NGSYADTSDI AVTPLLGNTT
     NFFVVRHAAY NSLESTPYTI TLPTSAGDLT IPQLNGTLTL NGRDSKVHVT DYDVGGENLL
     YSTAEIFTWK AYDDKTVLVV YGGPGESHEL AFSSGKNATI VEGSGVTIAP KGGATLLHWS
     VTPTRKVVKV GESLYVYILD RNSAYNYWTH DDIVLKAGYL IRNATVDGTT LSVVGDLNAT
     TTLEVIGGAP SGLTKLTFNG EDVAFNQSSL GNVAATLQYT PPAISLPDLS SLSWKSIDSL
     PEIQTDYDDS AWPAADLPTT YNTLRPITTP TSLYGSDYGY HYGTLLFRGH FTATGSETSL
     SISAQGGFAS GFTVFLNSVA LGSWKGADYA SNGNLTLSIP SSAVPTSGSE AVITVVLDTT
     GISENWVTGA EEAKLPRGIL NYDLAGHDAS DVTWKLTGNL GGEKYIDKSR GPLNEGGLFA
     ERQGYHLPGA PTDDWSASEG PAADGVEGVG VKWYATTIDL DIPTGWDVPI SFSFANSTSN
     ATDADGLAKA YRVQLFVNGW QFGKYVHNIG PQDVFPVPEG IWDYRGSNYV AVSLFSQEES
     GATVDGFELV HGTPVKTGYQ AVEVVQGETF AERAGAY
//
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