ID A0A1G1WDP2_9BACT Unreviewed; 804 AA.
AC A0A1G1WDP2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 22-FEB-2023, entry version 16.
DE RecName: Full=Dockerin domain-containing protein {ECO:0000259|PROSITE:PS51766};
GN ORFNames=A2Z24_00440 {ECO:0000313|EMBL:OGY25816.1};
OS Candidatus Woykebacteria bacterium RBG_16_44_10.
OC Bacteria; Candidatus Woykebacteria.
OX NCBI_TaxID=1802597 {ECO:0000313|EMBL:OGY25816.1, ECO:0000313|Proteomes:UP000177588};
RN [1] {ECO:0000313|EMBL:OGY25816.1, ECO:0000313|Proteomes:UP000177588}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGY25816.1}.
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DR EMBL; MHCT01000020; OGY25816.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G1WDP2; -.
DR STRING; 1802597.A2Z24_00440; -.
DR Proteomes; UP000177588; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR018905; A-galactase_NEW3.
DR InterPro; IPR002105; Dockerin_1_rpt.
DR InterPro; IPR016134; Dockerin_dom.
DR InterPro; IPR036439; Dockerin_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR41775:SF1; PEPTIDASE_M6 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR41775; SECRETED PROTEIN-RELATED; 1.
DR Pfam; PF00404; Dockerin_1; 1.
DR Pfam; PF10633; NPCBM_assoc; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF63446; Type I dockerin domain; 1.
DR PROSITE; PS51766; DOCKERIN; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..42
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 750..804
FT /note="Dockerin"
FT /evidence="ECO:0000259|PROSITE:PS51766"
SQ SEQUENCE 804 AA; 85979 MW; 3815F1824A8F9C71 CRC64;
MKPADLLKQY REHINPPYSH RDIISVFGTL FLLLAIPLTT IFTTQGGERV GGSQLAVKAQ
TVSELDAVRN ESFKLLKLND QLVKAIPGQK GKILEEMASV ANSRKARMES LLEKNPKEVL
KASFPKEIVA SFPAEIQKNL EQPVTVSGDL EVLATDDFAK KQSKTQYFLN SDKERFSLYP
TKKLAVAKSG TKVEISGIKI DNKIIFEGTP SQDFKVLGTL TDTLGEQKTV VILVNFQNDT
SQPFTTATAQ DVTFTGTDSV SSYYLDASYN KTWLTGDAYG WYTMAINKTC DYGDIEAAAI
DAADPFVNFQ NYSRIILAFP GSSCGWAGLG TIGKWAVSTD DGVVQSSISW IIASYFGLFV
VGHEFGHNLG VYHANALDCG SVTLGDSCTD VEYGDIYDIM GGYNPGHHNA AHKQALNWFE
PSNVVTATDS TVYWLEPLET ATSGPKVIKV PRNANQAFYV EYRQAIGKDA IFSGDSDLLD
GVLIHLVTTN FEEEETWLLD ASPNDAGWHG PAFTVDHFYL YDPVTNITIT PSLEMGGLMY
VEIDLGDTVC ERANPLVTID PTSVLKAPGE TATFSVSVTN NDTSPCGSSA FTITRAVPDG
WSASLAASEL TISPGATSST TLSVTSSVAA PEGFYDITVT AANKTFPVYN SSDTTSYEVD
TQAPATVDIK ADSSDGPITI AYNTATTLSW SSSNATSCSA SGVWSGTKAT SGSQSSGSLT
VSSTFTLTCS GLGGSASDSV TVNVSDQGAP LGKLGDLNGD GLVNIRDASI LVSRWNSADA
TADLNHDGMV NIRDASILVS RWGS
//