ID M0MRR8_9EURY Unreviewed; 463 AA.
AC M0MRR8;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=PKD domain containing protein {ECO:0000313|EMBL:EMA47434.1};
GN ORFNames=C449_01771 {ECO:0000313|EMBL:EMA47434.1};
OS Halococcus saccharolyticus DSM 5350.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halococcaceae; Halococcus.
OX NCBI_TaxID=1227455 {ECO:0000313|EMBL:EMA47434.1, ECO:0000313|Proteomes:UP000011669};
RN [1] {ECO:0000313|EMBL:EMA47434.1, ECO:0000313|Proteomes:UP000011669}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5350 {ECO:0000313|EMBL:EMA47434.1,
RC ECO:0000313|Proteomes:UP000011669};
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 -!- 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:EMA47434.1}.
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DR EMBL; AOMD01000005; EMA47434.1; -; Genomic_DNA.
DR AlphaFoldDB; M0MRR8; -.
DR STRING; 1227455.C449_01771; -.
DR PATRIC; fig|1227455.4.peg.369; -.
DR InParanoid; M0MRR8; -.
DR Proteomes; UP000011669; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
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; cd12215; ChiC_BD; 2.
DR Gene3D; 2.10.10.20; Carbohydrate-binding module superfamily 5/12; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR003610; CBM_fam5/12.
DR InterPro; IPR036573; CBM_sf_5/12.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR42976; BIFUNCTIONAL CHITINASE/LYSOZYME-RELATED; 1.
DR PANTHER; PTHR42976:SF1; GH18 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF02839; CBM_5_12; 2.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00495; ChtBD3; 2.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51055; Carbohydrate binding domain; 2.
DR PROSITE; PS51910; GH18_2; 1.
DR PROSITE; PS51318; TAT; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000011669}.
FT DOMAIN 188..463
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 77..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 463 AA; 48203 MW; 30273D3A4270260D CRC64;
MRKTTPRTQL MNHTRRSVLR KAAGLSALAI GTSGAASAAT DCSNVPAYDA NTAYSGGDQV
IYEGSLWTAE WWTKGTAPST SENVWTKQGD CGSGGGGGGG SDGGSGGSAA DCSGVPAYDP
NTAYSGGDQV VHNGSLWIAE WWTRGSAPAE SEAVWTLEGS CRSDGGGDGG DGGGDDGDGG
GGGGGGGGGI YSLYAGTWMN RVDGVTSRNL DHVYLTVLGD ATDDGEVNAG WLAGCNTGSC
SQKSLSTQTD TIQALQDNGV EVRVSIGGAD GRVVARDASS ATELKNAYAN ILDTLGVSTL
DIDDENADQR SETLYEMRNE ALAMLKTERP NVTVGFTVSA TADGIVSYGH SRGKTWIKDA
EKKGVGLDYV QPMTMYFQGD ENFDSITQSL EGTVDFLETV YTGKSRSAIW SMVGVTPLLS
QISTQDATQL VDYASQKGMY SIAPWSLNLD TNGEFSDIFK QFG
//