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Database: UniProt
Entry: E9SHG0_RUMAL
LinkDB: E9SHG0_RUMAL
Original site: E9SHG0_RUMAL 
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
//
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