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Database: UniProt
Entry: A0A011WT19_RUMAL
LinkDB: A0A011WT19_RUMAL
Original site: A0A011WT19_RUMAL 
ID   A0A011WT19_RUMAL        Unreviewed;       642 AA.
AC   A0A011WT19;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Dockerin domain-containing protein {ECO:0000259|PROSITE:PS51766};
GN   ORFNames=RASY3_06935 {ECO:0000313|EMBL:EXM40160.1};
OS   Ruminococcus albus SY3.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Ruminococcus.
OX   NCBI_TaxID=1341156 {ECO:0000313|EMBL:EXM40160.1, ECO:0000313|Proteomes:UP000021369};
RN   [1] {ECO:0000313|EMBL:EXM40160.1, ECO:0000313|Proteomes:UP000021369}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SY3 {ECO:0000313|EMBL:EXM40160.1,
RC   ECO:0000313|Proteomes:UP000021369};
RA   Dassa B., Borovok I., Lamed R., Flint H., Yeoman C.J., White B.,
RA   Bayer E.A.;
RT   "Rumen cellulosomics: divergent fiber-degrading strategies revealed by
RT   comparative genome-wide analysis of six Ruminococcal strains.";
RL   Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
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:EXM40160.1}.
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DR   EMBL; JEOB01000002; EXM40160.1; -; Genomic_DNA.
DR   RefSeq; WP_037286372.1; NZ_JEOB01000002.1.
DR   AlphaFoldDB; A0A011WT19; -.
DR   PATRIC; fig|1341156.4.peg.1805; -.
DR   Proteomes; UP000021369; 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   Gene3D; 1.10.1330.10; Dockerin domain; 1.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 3.
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; IPR026906; LRR_5.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   PANTHER; PTHR45661:SF3; RICH REPEAT DOMAIN PROTEIN, PUTATIVE-RELATED; 1.
DR   PANTHER; PTHR45661; SURFACE ANTIGEN; 1.
DR   Pfam; PF00404; Dockerin_1; 1.
DR   Pfam; PF13306; LRR_5; 3.
DR   SUPFAM; SSF52058; L domain-like; 2.
DR   SUPFAM; SSF63446; Type I dockerin domain; 1.
DR   PROSITE; PS51766; DOCKERIN; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000021369};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..642
FT                   /note="Dockerin domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001464084"
FT   DOMAIN          578..642
FT                   /note="Dockerin"
FT                   /evidence="ECO:0000259|PROSITE:PS51766"
FT   REGION          558..588
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   642 AA;  69621 MW;  A1B77B77DF323700 CRC64;
     MTKRLITGLI AFVFLFGSTA FPQDKAVIAP CLTANAANTE DGNFQYSYTD TTMSGIEIQN
     YLGSDTNVVI PSEIKGIPVV SIKRYAFMGN TKITSITIPN TVTTISWQAF QDCTSLTSIN
     GAKGLQVLGS FAFKNTALKR LVLPDSITEV GHQAFADCKD LETISFPSSL TDIRGMAFAN
     TKWLRNKQSQ NSVVTVNGIV IDGQKCSGNI TIPNGVIGIG DSAFANNKQI TGVRFPSSLK
     TIGSFAFGCC EYIKDLNVPG SVTTIKYDAF KSCYELENVS IPKSVTYIGG EAFLGTKWLA
     NQQAKDPVVV VNHMVIDGRN CSGRVVIPND VSLICEKAFY KNDRIKDISL PNSLREIGSE
     AFYYCTSIRE IIIPDGVTTI GQGAFNNNLS LKYVDIPNSV TEIGMQAFIE CKALPEITIP
     GSLEEIPIEA FRNCYSLKVL NVESGVRSIS HYAFEGCSAL EELNIAGSVK VIGGYTFKDC
     TGLNEITFNE GLETIAPYAF QNCNNIRTIT LPKSVKAVTT TAFNFSTEGF KIRGYEGTFA
     QKLAKKINVE FEAIEKTDEP DITDDTTTDS ESGSDIPEEP KKGDMTGDGI INVSDISKLA
     AHIKGKRLLS KAVNADINGD GKVNVTDLSK LAAHVKGKRR LF
//
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