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Database: UniProt
Entry: M0AYQ6_NATA1
LinkDB: M0AYQ6_NATA1
Original site: M0AYQ6_NATA1 
ID   M0AYQ6_NATA1            Unreviewed;       711 AA.
AC   M0AYQ6;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   ORFNames=C481_05920 {ECO:0000313|EMBL:ELZ03103.1};
OS   Natrialba asiatica (strain ATCC 700177 / DSM 12278 / JCM 9576 / FERM
OS   P-10747 / NBRC 102637 / 172P1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Natrialba.
OX   NCBI_TaxID=29540 {ECO:0000313|EMBL:ELZ03103.1, ECO:0000313|Proteomes:UP000011554};
RN   [1] {ECO:0000313|EMBL:ELZ03103.1, ECO:0000313|Proteomes:UP000011554}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12278 {ECO:0000313|EMBL:ELZ03103.1,
RC   ECO:0000313|Proteomes:UP000011554};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC       {ECO:0000256|ARBA:ARBA00005336}.
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:ELZ03103.1}.
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DR   EMBL; AOIO01000018; ELZ03103.1; -; Genomic_DNA.
DR   RefSeq; WP_006108193.1; NZ_AOIO01000018.1.
DR   AlphaFoldDB; M0AYQ6; -.
DR   STRING; 29540.C481_05920; -.
DR   PATRIC; fig|29540.5.peg.1198; -.
DR   eggNOG; arCOG04634; Archaea.
DR   OrthoDB; 30657at2157; -.
DR   Proteomes; UP000011554; 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; 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: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   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   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011554}.
FT   DOMAIN          630..699
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
FT   REGION          259..282
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          321..344
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          687..711
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        321..336
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   711 AA;  75483 MW;  2DC04F23CDBCD0A3 CRC64;
     MGSDVTALLD ELTLAEKIRL VHGTADPDGT ATGYVPGNDR LGIRPITLVD GPLGVRAMGE
     RATAFPASIA LAASWDPELA REFGTAVGRE TAAHDQDVLL GPGVNIIRTP VGGRNFEYYS
     EDPHLSARTG VGTIEGIQST GVAATVKHYV ANNQETNRYE VSADVSERAL RELYLPAFRA
     AVEEADVDAV MTAYNRVNGV HMSDHEFLLS DVLKDEWDFD GLVVSDWWGT RSTVDAAQAG
     LDLEMPGVEL TEYLPELDAD SFDADPSPPD GTSSDFPPIP DVSAYFGEPL REAIESGEID
     ESILDEKVAR LLSMLESTGR QNVAECETGS PSDDSTGELD TSEHRQLARE IAIEGTVLLT
     NDDVLPLSES DSVAVIGPNA DAAKLGGGGS SEVSPFTETG PLAGIESRAA DASFERGVNP
     IAESSFFADS ESADASEAGT SIDDAVSAAA SADRAVVVAQ DDATEFTDRD SIELPGRQND
     LIDAVAEAAE RTVVVLRTSG PVELPWLDAV DAVLETWYPG QADGEALAAV LFGDADPGGR
     LPVTFGRSAA DYPTADETAF PGTDDVAQYE EGVFVGYRYF DDRDIEPLFP FGHGQSYATF
     EYDDVTVSET DDGCDVTVDL RNSATRTGTE VIQVYVGKSA APVPTPEREL AGFESVELGA
     GDSATVTISL AREDFAYYDE DSGWTVPDGS NTVHVGRSSR DIRATADVDV Q
//
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