ID A0A2R4X304_9EURY Unreviewed; 502 AA.
AC A0A2R4X304;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Dockerin domain-containing protein {ECO:0000259|PROSITE:PS51766};
GN ORFNames=HARCEL1_10915 {ECO:0000313|EMBL:AWB28180.1};
OS Halococcoides cellulosivorans.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Halococcoides.
OX NCBI_TaxID=1679096 {ECO:0000313|EMBL:AWB28180.1, ECO:0000313|Proteomes:UP000244727};
RN [1] {ECO:0000313|EMBL:AWB28180.1, ECO:0000313|Proteomes:UP000244727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HArcel1 {ECO:0000313|EMBL:AWB28180.1,
RC ECO:0000313|Proteomes:UP000244727};
RA Sorokin D.Y., Toshchakov S.V., Samarov N.I., Korzhenkov A., Kublanov I.V.;
RT "Halococcoides cellulosivorans gen. nov., sp. nov., an extremely halophilic
RT cellulose-utilizing haloarchaeon from hypersaline lakes.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
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; CP028858; AWB28180.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2R4X304; -.
DR KEGG; harc:HARCEL1_10915; -.
DR Proteomes; UP000244727; Chromosome.
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:0000272; P:polysaccharide catabolic process; IEA:InterPro.
DR CDD; cd08547; Type_II_cohesin; 1.
DR Gene3D; 2.60.40.680; -; 1.
DR Gene3D; 1.10.1330.10; Dockerin domain; 1.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR002102; Cohesin_dom.
DR InterPro; IPR002105; Dockerin_1_rpt.
DR InterPro; IPR016134; Dockerin_dom.
DR InterPro; IPR036439; Dockerin_dom_sf.
DR InterPro; IPR006626; PbH1.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR Pfam; PF00963; Cohesin; 1.
DR Pfam; PF00404; Dockerin_1; 1.
DR SMART; SM00710; PbH1; 6.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
DR SUPFAM; SSF63446; Type I dockerin domain; 1.
DR PROSITE; PS00448; CLOS_CELLULOSOME_RPT; 1.
DR PROSITE; PS51766; DOCKERIN; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000244727}.
FT DOMAIN 443..502
FT /note="Dockerin"
FT /evidence="ECO:0000259|PROSITE:PS51766"
FT REGION 285..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 502 AA; 51108 MW; C01CB2BF8FC1E118 CRC64;
MGEMIGIRQA AIVLAVVAVV GGAFAGVASA QSGVSDRIVV DASGNGDYTS IQAAVDNAST
GTTIEIEPGE YSEAVTVGTS NLTIVGTPGE DRPGPGEDAP VMNGTGSDAP AVTLGAGVED
VRIEGLVMED YRAGATFVNG VDAGDHEDVV IAHNRIEAHS GVGVVASDGT TLSDVRVTAN
VVDVTANGVL SKTVDDGSPA VIENLTIERN AFTGGVNGIY LVGSSAGDQR AVSITNNTFQ
NVDVGVELDT EMNASAVTVR ANAFDETDSY GVQNRNTAAN VDATHNDWGA PSGPYNPTTN
PGGAGERVSA NVEYDPWDTR YVELGSASGG SGQNVTVPVT VHSDDIAGYE LEISYDPSVV
RPVGISDGEF ERPVSHIDES HGLINITAAQ ATSASAPTVA QITFEVVGEV NDTATIEVDS
GESAVFGTNG TELDAAYGQS TVSVDLLGDV DDDGRVTAGD AVLLQRHLVG ESVAIDESAA
DVDADGDVDA GDVLALQKRL VA
//
