ID E9SHG0_RUMAL Unreviewed; 660 AA.
AC E9SHG0;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE SubName: Full=Dockerin type I repeat protein {ECO:0000313|EMBL:EGC01289.1};
GN ORFNames=CUS_4663 {ECO:0000313|EMBL:EGC01289.1};
OS Ruminococcus albus 8.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ruminococcus.
OX NCBI_TaxID=246199 {ECO:0000313|EMBL:EGC01289.1, ECO:0000313|Proteomes:UP000004259};
RN [1] {ECO:0000313|EMBL:EGC01289.1, ECO:0000313|Proteomes:UP000004259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8 {ECO:0000313|EMBL:EGC01289.1,
RC ECO:0000313|Proteomes:UP000004259};
RA Nelson K.E., Sutton G., Torralba M., Durkin S., Harkins D., Montgomery R.,
RA Ziemer C., Klaassens E., Ocuiv P., Morrison M.;
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Glycan metabolism; L-arabinan degradation.
CC {ECO:0000256|ARBA:ARBA00004834}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865}.
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:EGC01289.1}.
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DR EMBL; ADKM02000131; EGC01289.1; -; Genomic_DNA.
DR AlphaFoldDB; E9SHG0; -.
DR STRING; 246199.CUS_4663; -.
DR eggNOG; COG1196; Bacteria.
DR eggNOG; COG3507; Bacteria.
DR Proteomes; UP000004259; Unassembled WGS sequence.
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; cd14256; Dockerin_I; 1.
DR CDD; cd18832; GH43_GsAbnA-like; 1.
DR Gene3D; 2.40.128.10; -; 1.
DR Gene3D; 1.10.1330.10; Dockerin domain; 1.
DR InterPro; IPR032291; Abn2_C.
DR InterPro; IPR002105; Dockerin_1_rpt.
DR InterPro; IPR016134; Dockerin_dom.
DR InterPro; IPR036439; Dockerin_dom_sf.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR43301; ARABINAN ENDO-1,5-ALPHA-L-ARABINOSIDASE; 1.
DR PANTHER; PTHR43301:SF3; ARABINAN ENDO-1,5-ALPHA-L-ARABINOSIDASE A-RELATED; 1.
DR Pfam; PF00404; Dockerin_1; 1.
DR Pfam; PF16369; GH43_C; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF63446; Type I dockerin domain; 1.
DR PROSITE; PS51766; DOCKERIN; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000004259};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..660
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003247193"
FT DOMAIN 26..91
FT /note="Dockerin"
FT /evidence="ECO:0000259|PROSITE:PS51766"
FT REGION 92..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 197
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 426
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 364
FT /note="Important for catalytic activity, responsible for
FT pKa modulation of the active site Glu and correct
FT orientation of both the proton donor and substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-2"
SQ SEQUENCE 660 AA; 72221 MW; E03890E61A6198AA CRC64;
MKSRKFAASL AAVMALTAVP YGSALADRKL GDVSGDDIIN VKDISLCAAY VKNVRALDED
SLSAADINGD GKVNITDVSL LAAHVKGVKP IKNKRDDSSC TGSENDVPTS SSPSSYTGSE
NDVPTSSSPS SYTGSENDVP TSSSPSDSDS KSSDDTSSQT DDSSQPDEPY VEPDYDFEMN
YAGIKKRNIP ACAAVHDPSV LKVGDTYYIY GSHMSAAKCD DLMSWQYMAN GYSADNNVYG
QIYDVYDEAF KYAGSPTSIV KTDDADNGGT EHVWAPDVIY NKKMGKYVMY YCTTSNWCTS
NLCYATSDSP EGPFEWQGAF IYSGFYGSTV KYTDVLDYVD LDYASSHYWS GKSYASRQYP
NAIDPTVFYD AEGKMWLTYG SWSGGIFLLE IDEATGLPIH PKANEANGVD PYFGKRIAGG
GGKSGEAPYI LYDEDSGYYY LFISYGALSR EGGYQIRVFR SDKPDGDYVD MNGSELPSGV
DPAGYGLKLS GNYMLPSLNR AYMATGHNSA FVDDDGKKYI VYHTRFDNNT EGHAPRTHQY
LLNAEGWICM LPYQTRGETV SECGYSMAEV EGRYYMTDQG TDISADIAQP VILYLNRDGK
AKTANDEGTW TMEEDSYRMT VTIGGKTYSG VFCKMLDEAQ TEVMTFSAVG SNESIWGVKY
//