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Database: UniProt
Entry: M0CLQ9_9EURY
LinkDB: M0CLQ9_9EURY
Original site: M0CLQ9_9EURY 
ID   M0CLQ9_9EURY            Unreviewed;       665 AA.
AC   M0CLQ9;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   SubName: Full=Carbohydrate-binding family V/XII {ECO:0000313|EMBL:ELZ24186.1};
GN   ORFNames=C475_13092 {ECO:0000313|EMBL:ELZ24186.1};
OS   Halosimplex carlsbadense 2-9-1.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Halosimplex.
OX   NCBI_TaxID=797114 {ECO:0000313|EMBL:ELZ24186.1, ECO:0000313|Proteomes:UP000011626};
RN   [1] {ECO:0000313|EMBL:ELZ24186.1, ECO:0000313|Proteomes:UP000011626}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2-9-1 {ECO:0000313|EMBL:ELZ24186.1,
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:ELZ24186.1}.
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DR   EMBL; AOIU01000031; ELZ24186.1; -; Genomic_DNA.
DR   AlphaFoldDB; M0CLQ9; -.
DR   STRING; 797114.C475_13092; -.
DR   eggNOG; arCOG07581; Archaea.
DR   eggNOG; arCOG09007; Archaea.
DR   Proteomes; UP000011626; Unassembled WGS sequence.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd04080; CBM6_cellulase-like; 1.
DR   CDD; cd00146; PKD; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 3.40.50.1110; SGNH hydrolase; 1.
DR   InterPro; IPR006584; Cellulose-bd_IV.
DR   InterPro; IPR005084; CMB_fam6.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR000601; PKD_dom.
DR   InterPro; IPR035986; PKD_dom_sf.
DR   InterPro; IPR005181; SASA.
DR   InterPro; IPR036514; SGNH_hydro_sf.
DR   InterPro; IPR006311; TAT_signal.
DR   PANTHER; PTHR31988:SF19; 9-O-ACETYL-N-ACETYLNEURAMINIC ACID DEACETYLASE-RELATED; 1.
DR   PANTHER; PTHR31988; ESTERASE, PUTATIVE (DUF303)-RELATED; 1.
DR   Pfam; PF03422; CBM_6; 1.
DR   Pfam; PF18911; PKD_4; 1.
DR   Pfam; PF03629; SASA; 1.
DR   SMART; SM00606; CBD_IV; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF49299; PKD domain; 1.
DR   SUPFAM; SSF52266; SGNH hydrolase; 1.
DR   PROSITE; PS51175; CBM6; 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:UP000011626}.
FT   DOMAIN          392..533
FT                   /note="CBM6"
FT                   /evidence="ECO:0000259|PROSITE:PS51175"
FT   DOMAIN          583..665
FT                   /note="PKD"
FT                   /evidence="ECO:0000259|PROSITE:PS50093"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          314..363
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          536..594
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..39
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   665 AA;  68431 MW;  2C32E32FD5D7B917 CRC64;
     MTTTDDTHDT TGGTDDRQRR TNDGRPASDG NERTNDDGGA LTRRGVLKAG ATLGAGGVVA
     GLADQVSATT PTDPSNLDLY LLFGQSNMEG QGTIGAQDRE TNERIHLLAD LDCPTLEREY
     GEWYLAEPPL NRCSQGLGPG TSFAKTMIEE TPDDRGVGLV PAAVSGADIA LFQKGAPIGR
     NDRNIPSQFD GGYQWLLDLA EQAQEVGTIK GILFHQGETN TGQQEWTSEV QGIVENLRSD
     LGIGTVPFLA GEMLYDSEGG CCASHNSEVN ELPDVIENAH VVSAEGLAGQ DYAHFTTEAY
     RELGRRYANE MLDHVDLGGG SGDDGSGDGG GDGSGDGGSG DDGSGDGGGG GTQQPYNGTP
     HAVPGRIQAE EYDQGGSGVA YSDNTAENEG ASRIQAEEYD QGGSGVAYSD NTAENEGASF
     RTGEAVDISS NSAGSGYSIG YIESGEWVEY TVDVEQSGEY TVDALVASNA GGGSFHVEVN
     GTDVSGAVNV PGTGGWDTWE TVSTSGVSLE AGQQVIRVSM DESWWDLNYL DFSLEGSGGD
     GSGSDGGDGS DGSDGSDGSG DGSSGDGGGD GESGDGSGPS ADLVAEIDPD TTSASVGERV
     AFRVTDTTGS GNWIDSLSWT LGNGETGSGW YVDTTYDSAG SYTVELDATN NEGTTTTDEV
     TVQIS
//
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