ID M0CLP5_9EURY Unreviewed; 588 AA.
AC M0CLP5;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=LPXTG-motif cell wall anchor domain-containing protein {ECO:0000313|EMBL:ELZ24171.1};
GN ORFNames=C475_13017 {ECO:0000313|EMBL:ELZ24171.1};
OS Halosimplex carlsbadense 2-9-1.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Halosimplex.
OX NCBI_TaxID=797114 {ECO:0000313|EMBL:ELZ24171.1, ECO:0000313|Proteomes:UP000011626};
RN [1] {ECO:0000313|EMBL:ELZ24171.1, ECO:0000313|Proteomes:UP000011626}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2-9-1 {ECO:0000313|EMBL:ELZ24171.1,
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:ELZ24171.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AOIU01000031; ELZ24171.1; -; Genomic_DNA.
DR RefSeq; WP_006884275.1; NZ_AOIU01000031.1.
DR AlphaFoldDB; M0CLP5; -.
DR STRING; 797114.C475_13017; -.
DR PATRIC; fig|797114.5.peg.2641; -.
DR OrthoDB; 200966at2157; -.
DR Proteomes; UP000011626; Unassembled WGS sequence.
DR GO; GO:0008810; F:cellulase activity; IEA:InterPro.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd02850; E_set_Cellulase_N; 1.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR004197; Cellulase_Ig-like.
DR InterPro; IPR001701; Glyco_hydro_9.
DR InterPro; IPR018221; Glyco_hydro_9_His_AS.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR PANTHER; PTHR22298; ENDO-1,4-BETA-GLUCANASE; 1.
DR PANTHER; PTHR22298:SF29; ENDOGLUCANASE; 1.
DR Pfam; PF02927; CelD_N; 1.
DR Pfam; PF00759; Glyco_hydro_9; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR PROSITE; PS00592; GH9_2; 1.
PE 4: Predicted;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000011626}.
FT DOMAIN 12..95
FT /note="Cellulase Ig-like"
FT /evidence="ECO:0000259|Pfam:PF02927"
FT DOMAIN 120..579
FT /note="Glycoside hydrolase family 9"
FT /evidence="ECO:0000259|Pfam:PF00759"
FT REGION 331..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 588 AA; 63694 MW; 8AAD6A70AA9FBAAB CRC64;
MSDLERGSER PTERVRVDQV GYLPSAPKRA VVAVESDGST VEAERFAVRD AGDGTVALAG
ALSNPIDSPD AGETVRRADF STLSEPGEYR VAVGRGETAD GDLRETADES VPVRVGTGVY
DGVLADAVRL YTLKRSNTAI DDPVTGLDVP PGHTQDAEAR MYFGDAFREE GQELDVAGGW
YDAGDYGKYV PPAAVTVGQM LLAYERYPAA FEAGQCDLPV ERLGVERSAA DGERESELPD
LLVEAAFELE WLERMQREDG AVYHKVAASE WPAVDEAPTD DDRERYVYGL STFGTAQYAA
AMAMAARVYA DDAPAFAERA LDNARAAHDY LEDNPDPEFR FDAGQDDGSG PYRKDTDREE
RFWAAAELLK TTGDTRYADY LEVRFVDRFD APPRAPVWTD ALSLGQWAYL SADAADDARA
ERLASAFLDY ADDLVADIEA DGYGCALDTE DYHWASTKLA LSKGGMLLLA NAIDSDDRYV
TGALDQLHYA LGRTPTGYSY VTGQGTHPPR NPHDRLVEGT GTSIPGMVVG GANRNGDDET
LAAYIAETDA PPAKCYVDAT ASYSVNEWAI DYTAPVFLLL GHATTMGE
//
