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Database: UniProt
Entry: V2X6G9_MONRO
LinkDB: V2X6G9_MONRO
Original site: V2X6G9_MONRO 
ID   V2X6G9_MONRO            Unreviewed;      1073 AA.
AC   V2X6G9;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   13-FEB-2019, entry version 31.
DE   SubName: Full=Glycoside hydrolase family 35 protein {ECO:0000313|EMBL:ESK88391.1};
GN   ORFNames=Moror_14750 {ECO:0000313|EMBL:ESK88391.1};
OS   Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS   (Crinipellis roreri).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Agaricomycetidae; Agaricales; Marasmiaceae;
OC   Moniliophthora.
OX   NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK88391.1, ECO:0000313|Proteomes:UP000017559};
RN   [1] {ECO:0000313|EMBL:ESK88391.1, ECO:0000313|Proteomes:UP000017559}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK88391.1,
RC   ECO:0000313|Proteomes:UP000017559};
RX   PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA   Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA   Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA   Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E.,
RA   Shao J., Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT   "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT   Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT   mechanisms of the biotrophic and necrotrophic phases.";
RL   BMC Genomics 15:164-164(2014).
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}.
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:ESK88391.1}.
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DR   EMBL; AWSO01000652; ESK88391.1; -; Genomic_DNA.
DR   RefSeq; XP_007852295.1; XM_007854104.1.
DR   EnsemblFungi; ESK88391; ESK88391; Moror_14750.
DR   KEGG; mrr:Moror_14750; -.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000017559; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:UP000017559};
KW   Glycosidase {ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00108869,
KW   ECO:0000313|EMBL:ESK88391.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017559};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     46     64       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      441    623       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1073 AA;  117336 MW;  011F67D0688F455E CRC64;
     MDANASNSLY SKDGNEDLED LEDLFLRKRE QKNAMSSKFR LGWKNLQLWA LMGMLSIGFA
     MASWSGKQFG QGFGNEGSVF ARFSGTDDIN FDNYSLILRG QRVFLHSGEF HTFRLPVPSL
     WPDILQKFKA AGLNGVSVYT HMGLINPSRG VVDFDSYRAL KPLYEAAMEA GIWIVLRPGP
     YINAETTAGG LAHWTTTEVA GNLRTNDTDW RAAWQDYILG IINETKGFQI SNGGPVVAIQ
     LDNEYTQRQG GPYFEDLKAV YHDPANGIVV PLTYNDPGQG RNFINGTGAV DIYGLDAYPQ
     RFDCSHPDVW NPVTLNYHQY HAEVNPSQPW YFPEFQGGAF DAWGPSAPGY EACRKLTGPD
     FESVFNLQLW ASNAKLISYY MVYGGTSWGA IPFDGVYTSY DYGASITESR MLTTKYTQLK
     MQGIFLRSSP EFYKTDWIGD TSTNLTEGRV VSVNNTPPAF VTLLKNPDSG AGFWIVRQND
     STSTATSVFN LDVTTNANST TPFRIPYPIT LKGRESKVIV TDYLFGATSR LTYSTANVFF
     AGVIDGRDVL FLYGDSDQAY VASADLTGTA SANFSPKALP PNIQVKLAER MIVVLPGVEG
     IFAVWDSDTQ LVLYADTANA ETFFAPVIAT DSSSSPFGNF WSIGTNETVL AGGPYLVREA
     AFSNDGTQLD LHGDFNITSG APESTRLTVI APGKVTSVTW NGAPVSLDAS FAPGASSVIT
     GTISSIQSLS GVAAPELGPW KFADSLPEIQ EDFDDSTWAE ANHTTTNIPH PMLYGDGRVL
     YGCDYGFCEN IVLWRGHFTG TGEEKSVNLS VNGGEAFAAS VWLNDVFLKT TFGNSTNNQN
     VIVETDEVYT FPEGAVKEGA DNVITIVQDN MGLDEAEANS NSMKSPRGIR GFQLNNGNFT
     SWKVQGKIGG YTNFPDKTRG VLNDGGLFGQ RKGWHLPGFD TSAWESKDEL SLNSKAGVGF
     FVTTFELDTP TGTDVMMSFQ FEEELGLPYR ALLFVNGWMM GKRVGNLGPQ AKFPVHEGIL
     DYHGTNTVAV ALWSMETDVE IVPQLRLVVD GVFEGGVGDV QTNNPGWSSV GRE
//
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