ID M0D8U2_9EURY Unreviewed; 559 AA.
AC M0D8U2;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Carbohydrate binding family 6 {ECO:0000313|EMBL:ELZ30559.1};
GN ORFNames=C475_00405 {ECO:0000313|EMBL:ELZ30559.1};
OS Halosimplex carlsbadense 2-9-1.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Halosimplex.
OX NCBI_TaxID=797114 {ECO:0000313|EMBL:ELZ30559.1, ECO:0000313|Proteomes:UP000011626};
RN [1] {ECO:0000313|EMBL:ELZ30559.1, ECO:0000313|Proteomes:UP000011626}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2-9-1 {ECO:0000313|EMBL:ELZ30559.1,
RC ECO:0000313|Proteomes:UP000011626};
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:ELZ30559.1}.
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DR EMBL; AOIU01000003; ELZ30559.1; -; Genomic_DNA.
DR RefSeq; WP_006881737.1; NZ_AOIU01000003.1.
DR AlphaFoldDB; M0D8U2; -.
DR STRING; 797114.C475_00405; -.
DR PATRIC; fig|797114.5.peg.82; -.
DR eggNOG; arCOG07581; Archaea.
DR eggNOG; arCOG09007; Archaea.
DR OrthoDB; 8638at2157; -.
DR Proteomes; UP000011626; 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; cd00146; PKD; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR018087; Glyco_hydro_5_CS.
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; PTHR34142:SF1; CELLULASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR34142; ENDO-BETA-1,4-GLUCANASE A; 1.
DR Pfam; PF00150; Cellulase; 1.
DR Pfam; PF18911; PKD_4; 2.
DR SMART; SM00089; PKD; 2.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49299; PKD domain; 2.
DR PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
DR PROSITE; PS50093; PKD; 2.
DR PROSITE; PS51318; TAT; 1.
PE 4: Predicted;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW Reference proteome {ECO:0000313|Proteomes:UP000011626}.
FT DOMAIN 426..478
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 477..559
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 559 AA; 61233 MW; A2D1049D70A07AE2 CRC64;
MTAETDPHED GERPTANRSA DERTATRRTV LRTTGAGVAG VALGGFAGTA AASDDGTPSR
LHTDGKWVRD ADGEPVRLRG LATASMGFYA VDGIHPKIPE EVVGWASDPA RGWYPNVVRL
PVTQWDVDQL GVEALVSDVL RPVVDLLGER GTYALIDYHV IHPYTEAAAD DADYDTSPDE
IVRNFWGTVA PAFADDEHVL YELFNEPTYP IFWSDNGESV ESPEAEWLLW RETAQPWVDM
VRESAPETPI VVGSPSWTSR TNFAPEYPFE GENLIYAAHI YPDNGRPEEF DDTYGAPAED
VPVFVTEFGW DPYSDGLDYG TNTDWGRPFR EWVEGYENVG WAAWCFDDSW APAMFDSPGE
GGADEWTLRS APEEHGGFVR QWLAETSAEP IARLHPGKTQ ATAGDWVHFE ARDASGANRH
VSRLAWDLGN GTTGEGWWVD ARYDEPGQYE VELTATNDAG ESTTHGLAIT VTEQTEAVAT
AEPSATEAAV DETVEFEAHD TSGDGRWVDA LAWEFGDGTT AGGWWASHEY GSTGTYTVEL
TATDNTGQTT TDTVEIVVE
//
