UniProt: A0A1V8SRR2

Database: UniProt
Entry: A0A1V8SRR2_9PEZI

LinkDB:  A0A1V8SRR2_9PEZI 
Original site:  A0A1V8SRR2_9PEZI

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (18)   
   InterPro (10)   
   Pfam (4)   
   PROSITE (2)   
   SMART (2)   
All databases (23)   

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ID   A0A1V8SRR2_9PEZI        Unreviewed;       848 AA.
AC   A0A1V8SRR2;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=beta-glucosidase {ECO:0000256|RuleBase:RU361161};
DE            EC=3.2.1.21 {ECO:0000256|RuleBase:RU361161};
GN   ORFNames=B0A48_12728 {ECO:0000313|EMBL:OQO01691.1};
OS   Rachicladosporium antarcticum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX   NCBI_TaxID=1507870 {ECO:0000313|EMBL:OQO01691.1, ECO:0000313|Proteomes:UP000192596};
RN   [1] {ECO:0000313|Proteomes:UP000192596}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCFEE 5527 {ECO:0000313|Proteomes:UP000192596};
RA   Coleine C., Masonjones S., Stajich J.E.;
RT   "Genomes of endolithic fungi from Antarctica.";
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00004987, ECO:0000256|RuleBase:RU361161}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC       {ECO:0000256|ARBA:ARBA00005336, ECO:0000256|RuleBase:RU361161}.
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:OQO01691.1}.
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DR   EMBL; NAJO01000030; OQO01691.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V8SRR2; -.
DR   STRING; 1507870.A0A1V8SRR2; -.
DR   InParanoid; A0A1V8SRR2; -.
DR   OrthoDB; 5486783at2759; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000192596; 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; 2.60.120.260; Galactose-binding domain-like; 1.
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   InterPro; IPR037524; PA14/GLEYA.
DR   InterPro; IPR011658; PA14_dom.
DR   PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR42715:SF28; BETA-GLUCOSIDASE-RELATED; 1.
DR   Pfam; PF14310; Fn3-like; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   Pfam; PF01915; Glyco_hydro_3_C; 1.
DR   Pfam; PF07691; PA14; 1.
DR   PRINTS; PR00133; GLHYDRLASE3.
DR   SMART; SM01217; Fn3_like; 1.
DR   SMART; SM00758; PA14; 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.
DR   PROSITE; PS51820; PA14; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW   ECO:0000256|RuleBase:RU361161};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
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|ARBA:ARBA00023326,
KW   ECO:0000256|RuleBase:RU361161};
KW   Reference proteome {ECO:0000313|Proteomes:UP000192596}.
FT   DOMAIN          412..572
FT                   /note="PA14"
FT                   /evidence="ECO:0000259|PROSITE:PS51820"
SQ   SEQUENCE   848 AA;  92105 MW;  712179BFAA97641C CRC64;
     MPGAGPNGAH KVNGDHYIRK DFNVDEVLED LTTTEKISLV SGIDFWHTAS VPRLGIPSLR
     TSDGPNGVRG TKFFDGVPAA CLPCGTGLAA TWDVDLIQRG GALQGKEAIA KGASVLLGPT
     TNMQRSPLGG RGFESFSEDP VLAGNMSAAT VKGIQSTGVA ATIKHFACND LEDKRLSSNS
     ILTERALREI YLMPFQIAQR DAKPLCFMTA YNLINGTHAS ENLKLLQHIL RDEWAFDGLV
     MSDWFGVYST SEAIKAGLDL EMPGPTYIRG GQIDIALRCG KLLIHQLDAR VRNVLNLVKR
     VLPLGIPENA PERTIDSPET ASLLREIGSN GLVLMKNEKK LLPFSKQKST AVIGPNGAFA
     AYCGGGSAAL PAYYTVTPYD GVRTKVPSAE YELGCPAWKR LPLLSNVAKT ESGKPGMSMK
     FYLDPPSIKG REVIDQLRIR DTNILLSDYE NPRVKTDLFW CDIDGKYTPD ETGEYEFSCS
     VAGTAQVFVD GKLVVDNLTR QSPGDSFFGI GTIEELGSIQ LEANKEYNIH VEFGTMPTLT
     YKKDGVTAFG AGGIRLGCFR KVCLKTEIER AIALASEVDQ VIICTGLNGD WESEGYDRPH
     MDLPPGSDDL IEAVLKANPN TAIVVQSGTP VTMPWRDQAP AIVQAWYGGN ETGNAIADVV
     FGDVNPSGKL PLSFPTRNED NPAFLNYISD DNRVLYGEDV FVGYRFYDKT KSTPSFPFGH
     GLSYTTFSLS DLSLTDSNDL ITLTASVKNT GSLPGAEVVQ AYVSARTPSI ARPVKELKGF
     TKTFLQPGES KKVEISFEKK YATSFYAEGR AAWQSEKGVY DVRVGTSSAS LPLKADFEVQ
     KTSWWSGV
//

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