GenomeNet

Database: UniProt
Entry: M0MRR8_9EURY
LinkDB: M0MRR8_9EURY
Original site: M0MRR8_9EURY 
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
//
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