UniProt: A0A316VQK5

Database: UniProt
Entry: A0A316VQK5_9BASI

LinkDB:  A0A316VQK5_9BASI 
Original site:  A0A316VQK5_9BASI

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (13)   
   InterPro (8)   
   Pfam (3)   
   PROSITE (1)   
   SMART (1)   
Literature (1)   
   PubMed (1)   
All databases (19)   

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ID   A0A316VQK5_9BASI        Unreviewed;       915 AA.
AC   A0A316VQK5;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   28-JUN-2023, entry version 12.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744, ECO:0000256|RuleBase:RU361161};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744, ECO:0000256|RuleBase:RU361161};
GN   ORFNames=FA14DRAFT_177057 {ECO:0000313|EMBL:PWN37775.1};
OS   Meira miltonrushii.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Exobasidiomycetes; Exobasidiales; Brachybasidiaceae; Meira.
OX   NCBI_TaxID=1280837 {ECO:0000313|EMBL:PWN37775.1, ECO:0000313|Proteomes:UP000245771};
RN   [1] {ECO:0000313|EMBL:PWN37775.1, ECO:0000313|Proteomes:UP000245771}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 3882 {ECO:0000313|EMBL:PWN37775.1,
RC   ECO:0000313|Proteomes:UP000245771};
RX   PubMed=29771364; DOI=10.1093/molbev/msy072;
RA   Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA   Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA   Spatafora J.W., Aime M.C.;
RT   "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT   clade Ustilaginomycotina.";
RL   Mol. Biol. Evol. 0:0-0(2018).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal, non-reducing beta-D-glucosyl residues
CC         with release of beta-D-glucose.; EC=3.2.1.21;
CC         Evidence={ECO:0000256|ARBA:ARBA00000448,
CC         ECO:0000256|RuleBase:RU361161};
CC   -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC       {ECO:0000256|RuleBase:RU361161}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC       {ECO:0000256|ARBA:ARBA00005336, ECO:0000256|RuleBase:RU361161}.
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DR   EMBL; KZ819602; PWN37775.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A316VQK5; -.
DR   STRING; 1280837.A0A316VQK5; -.
DR   InParanoid; A0A316VQK5; -.
DR   OrthoDB; 5486783at2759; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000245771; Unassembled WGS sequence.
DR   GO; GO:0008422; F:beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR   Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR026891; Fn3-like.
DR   InterPro; IPR019800; Glyco_hydro_3_AS.
DR   InterPro; IPR002772; Glyco_hydro_3_C.
DR   InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR   InterPro; IPR001764; Glyco_hydro_3_N.
DR   InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR42715:SF12; BETA-GLUCOSIDASE A-RELATED; 1.
DR   Pfam; PF14310; Fn3-like; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   Pfam; PF01915; Glyco_hydro_3_C; 1.
DR   PRINTS; PR00133; GLHYDRLASE3.
DR   SMART; SM01217; Fn3_like; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR   PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361161};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361161};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW   Polysaccharide degradation {ECO:0000256|RuleBase:RU361161};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245771};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           31..915
FT                   /note="beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5016414342"
FT   DOMAIN          824..892
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
FT   REGION          768..796
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   915 AA;  99938 MW;  CB6BAD982BBED008 CRC64;
     MGNDDIHREG EGFIALFGFL TVLFSQQTYA QQLPQGPDQA PFPNSYYPFA SLVNITSVPQ
     GYNITSPPKY PSPWMDGSGD WGWAYKKAEE FVSKLTIPEK VNLTTGGGWQ SDSCVGQTGS
     IPRLGFRSLC LQDSPLGVRD TDYNSVFPAG GTVAASFDRN IWWQRGHAMG SEFRDKGADA
     QLGPVVGPLG RSPEDRRMWE GFSPDPWLTG QAGAQTIYGM QSAGVMATLK HFILNEQEHF
     RQLGEAHQFG YNITEVLSSN VDDTTMHELY LWPFADAVRA GVASVMCSYQ RVNNSAACQN
     SYTLNYLLKG ELGFQGFVMS DWQAQKSGVS SALAGMDMAM PGDTLFATGN AFYGTNSTIA
     ILNGTLPQWR LDDMAMRIMA AYYYVGRDKH QVPINFNSWT TDTDGYIHLI SKTGYGKVND
     HVDVRGNHGK LIRDFAARST VLLKNTNNTL PLKACDEKFT AVFGSDAGNN PDGPNGCSDR
     GCDQGTLGEG WGSGTANYPY LITPLDAISN KVHDEGNGII QGITNDTATS QISALASQAS
     VAIVFVNSDS GEGYISVDGN EGDRNNLTLW HSGEDLIKTV AAQNNRTIVV IHSGGPVLVD
     TFKDHPNVTA IVWAGMPGQE SGNSIVDVLY GKVNPGAKLP FTMGSERQEY TTDILYQPNN
     GELSPQDNFG EGKFIDYRGF DRYNKTPEYE FGYGLSYTTF EYSNLQVDCH QIAQYYPTNR
     KSKKAPTIGR KPGTAEDYLY PTENFDRVQL YIYPYLNSTD LKASAGNADY GEKSEDWLPP
     LSQDGSPYEL PPAGGSPGGN AQLWDVAYTV TAQVKNTGQV EGDEVAQLYV SLGGPLDPPR
     VLRGFDRLTL APGETKTFTA NLTRRDVSNW DPASQNWIIS DHQKTIYVGA SSRKLPLHQE
     FSTSNIGGGG DDSSN
//

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