ID V2XUR1_MONRO Unreviewed; 469 AA.
AC V2XUR1;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Beta-glucosidase {ECO:0000313|EMBL:ESK96275.1};
GN ORFNames=Moror_7061 {ECO:0000313|EMBL:ESK96275.1};
OS Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS (Crinipellis roreri).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK96275.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK96275.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK96275.1,
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., Shao J.,
RA 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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC {ECO:0000256|RuleBase:RU003690}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ESK96275.1}.
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DR EMBL; AWSO01000050; ESK96275.1; -; Genomic_DNA.
DR RefSeq; XP_007844315.1; XM_007846124.1.
DR AlphaFoldDB; V2XUR1; -.
DR KEGG; mrr:Moror_7061; -.
DR HOGENOM; CLU_001859_1_2_1; -.
DR OrthoDB; 3373839at2759; -.
DR Proteomes; UP000017559; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001360; Glyco_hydro_1.
DR InterPro; IPR018120; Glyco_hydro_1_AS.
DR InterPro; IPR033132; Glyco_hydro_1_N_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR10353; GLYCOSYL HYDROLASE; 1.
DR PANTHER; PTHR10353:SF36; KLOTHO (MAMMALIAN AGING-ASSOCIATED PROTEIN) HOMOLOG; 1.
DR Pfam; PF00232; Glyco_hydro_1; 1.
DR PRINTS; PR00131; GLHYDRLASE1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS00572; GLYCOSYL_HYDROL_F1_1; 1.
DR PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU004468};
KW Hydrolase {ECO:0000256|RuleBase:RU004468};
KW Reference proteome {ECO:0000313|Proteomes:UP000017559}.
FT ACT_SITE 372
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ SEQUENCE 469 AA; 53288 MW; 6455A37A2D14BAE3 CRC64;
MKLPKDFLFG YATASYQIEG SSDVDGRGPS IWDTFSHTPG KIVDGTNGDV ATDSYQRWKD
DVKIVKDYGA NAYRFSISWS RIIPLGGKDD PVNPEGIRFY RTLIEELLNN GITPCVTLYH
WDLPQALHDR YGGWLDRRVI EDFVRYCEIC FEAFGNSVKH WITFNEPWCI SCLGYGYGVF
APGRSSNRNR SEAGDSTREP WIVAHNLLLA HASAVASYRQ KFWPSQAGSI GITLDCVWYM
PYDESNAEDV DAAQRALDTR LGWFADPIYK GHYPTSLKAM LGNRLPEFTT EEQALIKGSS
DFFGLNTYTS NLVQPGGSDE FNGKVKTTHT RADGSQLGKQ AHVPWLQAYP PGFRALLNYL
WKTYGKPIYV TENGFAIKDE NRLPPEDAIH DQDRVDYYRG YTNALAHAAN EDGVDVKAYF
AWSLLDNFEW AEGYQVRFGV TFVDFETQQR YPKDSSKFLA EWYRSSLAK
//
