ID M0MLM4_9EURY Unreviewed; 453 AA.
AC M0MLM4;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=PKD domain containing protein {ECO:0000313|EMBL:EMA46582.1};
GN ORFNames=C446_01016 {ECO:0000313|EMBL:EMA46582.1};
OS Halobiforma nitratireducens JCM 10879.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Halobiforma.
OX NCBI_TaxID=1227454 {ECO:0000313|EMBL:EMA46582.1, ECO:0000313|Proteomes:UP000011607};
RN [1] {ECO:0000313|EMBL:EMA46582.1, ECO:0000313|Proteomes:UP000011607}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10879 {ECO:0000313|EMBL:EMA46582.1,
RC ECO:0000313|Proteomes:UP000011607};
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:EMA46582.1}.
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DR EMBL; AOMA01000007; EMA46582.1; -; Genomic_DNA.
DR RefSeq; WP_006671176.1; NZ_AOMA01000007.1.
DR AlphaFoldDB; M0MLM4; -.
DR STRING; 1227454.C446_01016; -.
DR PATRIC; fig|1227454.3.peg.200; -.
DR eggNOG; arCOG07581; Archaea.
DR OrthoDB; 8638at2157; -.
DR Proteomes; UP000011607; 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; 1.
DR CDD; cd00146; PKD; 1.
DR Gene3D; 2.10.10.20; Carbohydrate-binding module superfamily 5/12; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 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; IPR013783; Ig-like_fold.
DR InterPro; IPR022409; PKD/Chitinase_dom.
DR InterPro; IPR000601; PKD_dom.
DR InterPro; IPR035986; PKD_dom_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; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR Pfam; PF18911; PKD_4; 1.
DR SMART; SM00495; ChtBD3; 1.
DR SMART; SM00089; PKD; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51055; Carbohydrate binding domain; 1.
DR SUPFAM; SSF49299; PKD domain; 1.
DR PROSITE; PS51910; GH18_2; 1.
DR PROSITE; PS50093; PKD; 1.
DR PROSITE; PS51318; TAT; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000011607}.
FT DOMAIN 85..163
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 169..453
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
SQ SEQUENCE 453 AA; 49626 MW; 0DD20B46B2058132 CRC64;
MKRTRRDLLR NASALSALTV GVGLSSTVSA REYPEWDPDA VYTSGDRVVH EGYVWEANWW
TRGNEPGEGG EWGPWDQVEP YDPGPTAAFS VSDSSPEPGA EVTFDASDAE GDLESYEWEF
GDDATATGEK VTHAYDATGE YTAELVVTDV DGDTDSTQRT LYVGEVEAPT PSGVYTPYQG
TWYDIVDGTL GRNTDRVIMS FIGDPYRDGE ISPAWLANCN NRNCEGESLD TYASEVQTLQ
DEGIEVGLSI GGWQSPVLAR DADDPEQLKE AYADLLDTFG VTHLDIDDEN AADPDRPDDL
HQLRNEALAL LKDERPEVTV GFTVSATPDG MVSWGESPGE VFIEDAADRG LELDYVQLMT
MHFDGAPENI ETITSSLEGA VDFLETVYPD QSRAELWTMV GVTPYLGEIT TDTASELVEY
ANEKDMYSIA PWVLGEDDDG AFSEVFSEFE SDG
//
