ID M0AS18_9EURY Unreviewed; 534 AA.
AC M0AS18;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Glycoside hydrolase family 43 {ECO:0000313|EMBL:ELZ00743.1};
GN ORFNames=C480_18667 {ECO:0000313|EMBL:ELZ00743.1};
OS Natrialba aegyptia DSM 13077.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrialba.
OX NCBI_TaxID=1227491 {ECO:0000313|EMBL:ELZ00743.1, ECO:0000313|Proteomes:UP000011591};
RN [1] {ECO:0000313|EMBL:ELZ00743.1, ECO:0000313|Proteomes:UP000011591}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13077 {ECO:0000313|EMBL:ELZ00743.1,
RC ECO:0000313|Proteomes:UP000011591};
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 -!- PATHWAY: Glycan metabolism; L-arabinan degradation.
CC {ECO:0000256|ARBA:ARBA00004834}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865}.
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:ELZ00743.1}.
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DR EMBL; AOIP01000051; ELZ00743.1; -; Genomic_DNA.
DR AlphaFoldDB; M0AS18; -.
DR PATRIC; fig|1227491.4.peg.3788; -.
DR OrthoDB; 191035at2157; -.
DR Proteomes; UP000011591; 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 CDD; cd18616; GH43_ABN-like; 1.
DR Gene3D; 2.80.10.50; -; 2.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR43301; ARABINAN ENDO-1,5-ALPHA-L-ARABINOSIDASE; 1.
DR PANTHER; PTHR43301:SF3; ARABINOSIDASE-RELATED; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR Pfam; PF14200; RicinB_lectin_2; 1.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:ELZ00743.1}.
FT DOMAIN 374..509
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
FT REGION 509..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..534
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 534 AA; 58128 MW; 74560F94BD333A50 CRC64;
MADFDPVSGP TDRRDVLRAL GGAGTAGLFG SVSMGSVTAQ RGFDEAYYEN PLYGPDFADP
TIQRADDGTW WAYASNMSYI DDADERLVPI LSSPDLVDWT YAGEAFDSRP GWAYGSIWAP
DVHYHDGQWV LFYSLWPRND GEGDQTGIGV ATSDTPDGPF TDHGRLFTNP EHPFPGNTID
PYFVSHQGTP YLFWGNFAGI YYVELTAELQ NYRPGTWGQI VGSAYEGSTI FQRDGYWYFF
GSTGDCCDGF DSTYEIEVGR SENLLGPYAD SDGTPMMERN EWNAGPTHLG DNDRFVAPGH
GDVTVDDDGS YWFVYHAYDT QGLETIDNGW PPARQLFLDR IYWSNGWPVI AGDGTPNATA
PIPNLGQRPA PVAEGTYNVV NVQSGHYLGI AGTGDGATAT VATNDAGFRA AWQLRRLAGG
EYVLNNADSG QTLEVVNADT SDGADVQQWP WNGHPTQRWY CFEESDGTYR MKNACSGKVA
EVANASAAAG ANVQQWTWND GDHQRWRFVP IEDDGSGGSS GSGGTSGSGS STTR
//
