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Database: UniProt
Entry: A0A1Y4N843_9FIRM
LinkDB: A0A1Y4N843_9FIRM
Original site: A0A1Y4N843_9FIRM 
ID   A0A1Y4N843_9FIRM        Unreviewed;      1465 AA.
AC   A0A1Y4N843;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Dockerin domain-containing protein {ECO:0000259|PROSITE:PS51766};
GN   ORFNames=B5F08_10280 {ECO:0000313|EMBL:OUP76730.1};
OS   Anaeromassilibacillus sp. An172.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Anaeromassilibacillus.
OX   NCBI_TaxID=1965570 {ECO:0000313|EMBL:OUP76730.1, ECO:0000313|Proteomes:UP000195869};
RN   [1] {ECO:0000313|Proteomes:UP000195869}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An172 {ECO:0000313|Proteomes:UP000195869};
RA   Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA   Rychlik I.;
RT   "Function of individual gut microbiota members based on whole genome
RT   sequencing of pure cultures obtained from chicken caecum.";
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Glycan metabolism. {ECO:0000256|ARBA:ARBA00004881}.
CC   -!- SUBUNIT: Homohexamer; trimer of dimers.
CC       {ECO:0000256|ARBA:ARBA00011165}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 51 family.
CC       {ECO:0000256|ARBA:ARBA00007186}.
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:OUP76730.1}.
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DR   EMBL; NFKS01000023; OUP76730.1; -; Genomic_DNA.
DR   OrthoDB; 9758333at2; -.
DR   Proteomes; UP000195869; Unassembled WGS sequence.
DR   GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IEA:InterPro.
DR   GO; GO:0046373; P:L-arabinose metabolic process; IEA:InterPro.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:InterPro.
DR   CDD; cd14256; Dockerin_I; 1.
DR   Gene3D; 2.60.120.200; -; 2.
DR   Gene3D; 1.20.1270.90; AF1782-like; 1.
DR   Gene3D; 1.10.1330.10; Dockerin domain; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR010720; Alpha-L-AF_C.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR002105; Dockerin_1_rpt.
DR   InterPro; IPR016134; Dockerin_dom.
DR   InterPro; IPR036439; Dockerin_dom_sf.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR006558; LamG-like.
DR   PANTHER; PTHR43576:SF3; ALPHA-L-ARABINOFURANOSIDASE C; 1.
DR   PANTHER; PTHR43576; ALPHA-L-ARABINOFURANOSIDASE C-RELATED; 1.
DR   Pfam; PF00404; Dockerin_1; 1.
DR   Pfam; PF07554; FIVAR; 1.
DR   Pfam; PF13385; Laminin_G_3; 2.
DR   SMART; SM00813; Alpha-L-AF_C; 1.
DR   SMART; SM00560; LamGL; 2.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR   SUPFAM; SSF63446; Type I dockerin domain; 1.
DR   PROSITE; PS51766; DOCKERIN; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000195869};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..1465
FT                   /note="Dockerin domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012373242"
FT   DOMAIN          1400..1465
FT                   /note="Dockerin"
FT                   /evidence="ECO:0000259|PROSITE:PS51766"
SQ   SEQUENCE   1465 AA;  160048 MW;  9345D306963E9D5E CRC64;
     MKRAKKILSV ILALGMISTM CVYSSSAEIT PKADIDSNLT AHWNFEETDA SGNPVNIGSD
     SSIKAVLEGN KVSVKDSGDE TYGKVLHFES KGDAAENSRM FIGDMFNPKQ EDFSVSLWVN
     NSSQQITTQN TIMLQFADKD GATGKTFLYR GTDDKYTVYM NGTDIETSPA TADGKWENIT
     ITKENLDNGK YTLKFYINGE QTYTGECDAS QVIDKVTDLI IGSHKNKTDK DNGQFTGDID
     DLRFYERVLT ADDVMALYNA KTEEAVNSQL EAAISQADSL LKSGKLEITH QAYVLLDNSL
     KKAKAALEAG TTEERQNAIS DLNEKIADFN TAVDGEDALN KGLVGYWTAD SGSLENMAQG
     GTLTATMSGS NLTIAESDIE SMGKMLSFAK KTSGNSSNVT IANGLNSQNE FTITMWVKNS
     EDQKDTTMST VLIQQSTATG RSLLFRTTSG QYGTYISEEN KYFGEATSYN EWQHLALVKS
     NGTDGNYTIA LYLDGVKLGE HTLSKNNATA VTDLIIGSHK QLGNSDQFAG SMDEIRLYTR
     ALSENEVKGI YQLNSAAVNE QKLVALKLQY NELLTKAKEA LSSGDLTEDM PEYIALKEAV
     DHSAEIPENI IYEDMLAEYE ALSTAYDNYQ NASPIVVTIN TDDVTNIIDN GVFGTNHRFG
     FNGYGTFDSE TMTMKQDFVD LYKEAGFGSV RYPGGSISNL FQWKGTLGSK DERLDQVHGY
     YNTNSNGQPQ RGIASNFGIK EVGDFASDVG SEIVYVYGMG RGSASDAADL VEYLNAPNDG
     SNPNGGIDWA AVRAENGHPD PYNVRYFEMG NEMNQGGGKD GDGLWSQGFW TNYVNGKASD
     YAYIEGGTVV CEKQYAVAYD DWNSIESKSD GTANQIFYMR YANPHPALGI ANGDIGLRDI
     TSGNSGVMEQ YNYDPADYAD FKAISSNDET TKVYVGNEEW KVVSDLSTAG ANDKVAKIDY
     ATGGIIFGDG VNGAIPPKDS QIFVSYTVER EGFIDISQAM RDTMEQINNN LKSKGEEEKE
     LYIYTSWETS SFINIMHQKG ADSLYDGMTI HPYAGTPAGG SANEETKKQF YYSTLSLIPG
     TVSRVSNLVN EMRTITGDNT KVPAISEYGI YPSYDTMVRS QTHALYIARV LMEYIRLDSP
     YIQKHCLVDW YSSGGDSLGP TQQAVIQAVP QEGADIITGE GDYKFFSTPS ARVFEMYNSA
     SGTDVLSSTF SDTRLLDNGT EQYAAMASKD ADGNLYLALV NSKLDGKGIV DIKVDGVDLS
     GKTLEIQYIS GDTFYAENTI DNPDNVDVIR TTETVAENSE TARVVVEPHS FTIVKVVNAL
     VEEPDTPDVT ELKNKVEEAL PMVDMEEYTA ESREVLKTAI DEAQAIIAKA EAGEEITQTQ
     VDEALKAIES AVNSLELVKP DFVLGDADGS GSMTIDDASY IQQYLVKAIS ADKFVFEAAD
     TNKDGKITVY DATKIQLAIA SNEDL
//
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