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Database: UniProt
Entry: V2Y5W6_MONRO
LinkDB: V2Y5W6_MONRO
Original site: V2Y5W6_MONRO 
ID   V2Y5W6_MONRO            Unreviewed;      1021 AA.
AC   V2Y5W6;
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:ESK87049.1};
GN   ORFNames=Moror_11961 {ECO:0000313|EMBL:ESK87049.1};
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:ESK87049.1, ECO:0000313|Proteomes:UP000017559};
RN   [1] {ECO:0000313|EMBL:ESK87049.1, ECO:0000313|Proteomes:UP000017559}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK87049.1,
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:ESK87049.1}.
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DR   EMBL; AWSO01000849; ESK87049.1; -; Genomic_DNA.
DR   RefSeq; XP_007853647.1; XM_007855456.1.
DR   EnsemblFungi; ESK87049; ESK87049; Moror_11961.
DR   KEGG; mrr:Moror_11961; -.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000017559; 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:UP000017559};
KW   Glycosidase {ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00108869,
KW   ECO:0000313|EMBL:ESK87049.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017559};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     25       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        26   1021       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5004712600.
FT   DOMAIN      399    553       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1021 AA;  113164 MW;  433B47DAC5CC9BD1 CRC64;
     MMGNKWLNLQ LCIASMALLV ALAMAGVQLE AQADLLARRQ YTGTGDVQFD NYSLILNGQR
     IFLHSSEFHT FRIPIPSLWP DILQKYKAAG LNSISVYEPM VLLNPSRGVV DFDGWRGLKQ
     LYEVAMEIGL WVVMRPGPYI NAEVSAGGVS HWITSEIAGD LRSNDSDWRE AWQDYILGVI
     RETRDYQITN GGPVIAIQLD NEYTAEEGMD YFEDLKRVYQ DPANGIVVPL TYNDPYQGKA
     FINGTGSVDL YGLDSYPQAF DCSHPDLWKP VTPNYHQYHQ EVNPSQPWYI PEFQAGSYDP
     WGPAAPGYEQ CRKLTDADFE SVFNLQLWAS NAKLINYYMV YGGTSWGGIP FHGVYTSYDY
     GAPIAEARTL TPKYTQLKMQ GIFLRSSPEF YKTNWIGDTS TNLTEGGVSA VNNTPPAFVT
     LLRNPDSDAG FWILRQNDST STSTSIFNLD ITTKADSTKP FRLPYPIILQ GRESKVIVTG
     YLFGASSRLT YTTAQVLFAG VIDGRDVLFL YGDSDQAYIT SVNLTGTSSP ARSPFIQVDD
     RRVITILAGA EGLLTVWDSE TQLVLYADTP TAETFYAPAI TVPNSDDNPY SKFWSFGTNE
     TVLVAGPYLV REATYSKDRK QLDLRGDLDI TTNVTNVTLV APKTVTSVTW NGMSVSLDDV
     LGSVMTGTIS SSKSGLLAKD TVVELGPWKY ADSLPEIRGC FDDSGWVEAN HTQTNIPHPM
     LYGDGRVLYG CDYGFCENIA LWRGHFMGTG MEKSVNLSVN GGEAFAASVW LNDVFLKTTY
     GNSTNNNNII AETDEVFAFP EGIVEEGEIN VITIVQDNMG LDEAEDNRNS MKSPRGIRGF
     QLNTGNFLSW KVQGKIGGYT NFPDKVRGLL NEGGLFGERK GWHLPGFDSS TWESRDELSL
     DAEAGVGFFV TTFELDTPCG IDIMMSFVFE EEFGLPYRAL LFVNGWMMGK RVGNLGPQAK
     FPVHEGILNY HGMNTMAIAL WAMEPGIDIV PQLRLVVDSV FEGGVGRIEV NNPGWTAQGR
     E
//
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