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Database: UniProt
Entry: A0A0W1R2K3_9EURY
LinkDB: A0A0W1R2K3_9EURY
Original site: A0A0W1R2K3_9EURY 
ID   A0A0W1R2K3_9EURY        Unreviewed;       742 AA.
AC   A0A0W1R2K3;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   ORFNames=AUR66_05220 {ECO:0000313|EMBL:KTG07518.1};
OS   Haloferax profundi.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloferax.
OX   NCBI_TaxID=1544718 {ECO:0000313|EMBL:KTG07518.1, ECO:0000313|Proteomes:UP000053157};
RN   [1] {ECO:0000313|EMBL:KTG07518.1, ECO:0000313|Proteomes:UP000053157}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB29 {ECO:0000313|EMBL:KTG07518.1,
RC   ECO:0000313|Proteomes:UP000053157};
RA   Zhang G., Stingl U., Rashid M.;
RT   "Haloferax profundi sp. nov. isolated from the Discovery deep brine-
RT   seawater interface in the Red Sea.";
RL   Submitted (DEC-2015) 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   -!- 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:KTG07518.1}.
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DR   EMBL; LOPV01000716; KTG07518.1; -; Genomic_DNA.
DR   RefSeq; WP_058573905.1; NZ_LOPV01000716.1.
DR   AlphaFoldDB; A0A0W1R2K3; -.
DR   OrthoDB; 30657at2157; -.
DR   Proteomes; UP000053157; 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; 3.40.50.1700; 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; 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; PTHR30620:SF121; PERIPLASMIC BETA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR30620; PERIPLASMIC 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   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.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KTG07518.1}.
FT   DOMAIN          660..729
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   742 AA;  79831 MW;  DDB52BD8A74BB67C CRC64;
     MHTQTRSVLD LLSADRRAEV QERVETVLSE LTLAEKVGQL NQLNADFATG TAVGDMDVEQ
     GVLDGEIGSV LNAADLDEAR RLQTLAVEES DHGVPLLLAL DVIHGYRTIF PIPLGEAASW
     SPEMAELSAR VAATEAAASG VHWTFAPSVD VGRDPRWGRV MEAAGEDPYL SSEISMARVR
     GFQGDDLAAD DSILACAKHY VGYGASEAGR EYNTVDISET NLREVHLPPF EACLEAGVGS
     VMNAFNLYER VPASSNEELV DVILRGELGF EDVVVSDWNS FGELVEHGVA SDLREVARAC
     LEAGSDVDMV SGAYATELVE LVEDGVVDES LVDEAVRRVL TVKGALGLFE DPYRYFDADR
     QSRRVLTDEH REAARDVARE SLVLLKNEGA VLPLDGDEDV ALVGGLADSA TDMLGAWRAE
     GEPDDVTTLK ASLTDRLETL TYVEGCDPDG TVSDEQLEAA VETVESADVA VVAVGERYDQ
     SGEAASRAHI DLPGDQRALL EALVETGTPV AAVLFNGRPL AIDWETEHVP ALLEAWFPGV
     EAGPAISDVL LGAHNPSGRL PMTFPVTEGQ IPVYYNHLKT GRPAEDAGVD LTTPPADHGE
     KYVSRYLDIP NEPLYAFGHG ESYTDFAYTD VSLGAAAITA AEPLSVDVTL ENVGDRAGTE
     VVQVYLSDRV GSRARPVREL VRFENVDLDA GESRTVSFEL TAADLAFWTA DEEYAAEPGE
     FEVQVGHAAD EIAVVETFEL VE
//
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