ID A0A1T2X1E5_9BACL Unreviewed; 1505 AA.
AC A0A1T2X1E5;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Dockerin domain-containing protein {ECO:0000259|PROSITE:PS51766};
GN ORFNames=BVG16_26835 {ECO:0000313|EMBL:OPA73711.1};
OS Paenibacillus selenitireducens.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1324314 {ECO:0000313|EMBL:OPA73711.1, ECO:0000313|Proteomes:UP000190188};
RN [1] {ECO:0000313|EMBL:OPA73711.1, ECO:0000313|Proteomes:UP000190188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ES3-24 {ECO:0000313|EMBL:OPA73711.1,
RC ECO:0000313|Proteomes:UP000190188};
RA Xu D., Yao R., Zheng S.;
RT "Genome analysis of Paenibacillus selenitrireducens ES3-24.";
RL Submitted (JAN-2017) 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:OPA73711.1}.
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DR EMBL; MSZX01000014; OPA73711.1; -; Genomic_DNA.
DR STRING; 1324314.BVG16_26835; -.
DR OrthoDB; 1095434at2; -.
DR Proteomes; UP000190188; Unassembled WGS sequence.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0033926; F:glycopeptide alpha-N-acetylgalactosaminidase activity; IEA:InterPro.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:InterPro.
DR CDD; cd14254; Dockerin_II; 1.
DR CDD; cd14244; GH_101_like; 1.
DR CDD; cd08547; Type_II_cohesin; 1.
DR Gene3D; 2.60.120.870; -; 1.
DR Gene3D; 2.60.40.1080; -; 1.
DR Gene3D; 2.60.40.680; -; 1.
DR Gene3D; 2.70.98.10; -; 1.
DR Gene3D; 1.10.1330.10; Dockerin domain; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR003343; Big_2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
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; IPR025706; Endoa_GalNAc.
DR InterPro; IPR040633; Gal_mutarotas_3.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR014718; GH-type_carb-bd.
DR InterPro; IPR049314; GH101_dom-5.
DR InterPro; IPR040502; GH101_dom-6.
DR InterPro; IPR035364; Glyco_hyd_101_beta.
DR InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR Pfam; PF02368; Big_2; 1.
DR Pfam; PF00404; Dockerin_1; 1.
DR Pfam; PF18080; Gal_mutarotas_3; 1.
DR Pfam; PF17974; GalBD_like; 1.
DR Pfam; PF21466; GH101_dom-5; 1.
DR Pfam; PF17451; Glyco_hyd_101C; 1.
DR Pfam; PF12905; Glyco_hydro_101; 1.
DR SMART; SM00635; BID_2; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 1.
DR SUPFAM; SSF63446; Type I dockerin domain; 1.
DR PROSITE; PS51766; DOCKERIN; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000190188};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1505
FT /note="Dockerin domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039551987"
FT DOMAIN 1442..1505
FT /note="Dockerin"
FT /evidence="ECO:0000259|PROSITE:PS51766"
SQ SEQUENCE 1505 AA; 164037 MW; 348CA436A480F0BD CRC64;
MKKNYVKQTS VALALFMSMQ MGVPAALVYA DGNTGNNVTA LSQDVLNQAA AALASYSRDF
NDGDISGWNA VKGTTTFSAD NGTLKAVTTG AVVFVDQKSP VVKNGDYEIK MRFKDVPSRF
GLVIRYVDTN NYAVIQFDNG TWGWDYMKNG TETYGNIETL TNPSFEANKE YSFKLSYFDD
SVKLTLDDNV ILNTTLPSIP MSAGKIGVRS WFANKTINID DVKVNERTVA DDHARPITLV
DTLTSNLLTA EIDQEFPRVK KYVWTGTGAE MLGQILGPNE VKINGNSYYP LANKYEKHPA
SATKGETSTY TLQIPELNVV LDVELELKDN VLNFRVTRIA ENGTAKVNTV EFPSHDLATV
LSSQPKAQQT SSQITGAWNI VNDEYVDLKS GATDGGGSRT YAFLNSDTLA ATIVNNVING
NDKVRVKTVT GTDSVKKASL WNGAWTYRGS TNPNIPHEEL PWAKIILTPD ANNDGQVDWQ
DGAIAYRSQA EAPYKSELIK DNISYISMNI GSTTSTPFLR AFDNAKKISN LTDGFGQIIL
FKGYQAEGHD DSHPDYGGHI GIRQGGVKDF NYVLSEGKKY NIKGGVHINA TEYMLDANET
KMDNMIQPLS KGWGWLDQAY YVDQKKDVES GELKRRLDML KADTGDNLSF VYVDVYTGSG
WNAKKLSEYV KDNGWMLGTE FAGPLNEQVS WVHWGTDPGY PNQGNSSKII RFLRNDTLDG
FLSDPLLKGN KQVGIGYWQE NPVFYDLKQT SKAFFVQNLP TKYMQYHQIL KMTNDRVDFT
DNVSVARQSD GKIHLSKDGK DIAIMTDSSN ISDGTVFIPW DPEKEDKIYH WNPAGGTTTW
DVPTSWSGLQ HAQLYKLTDL GRELIGSVPI NNGKITIMAI KDVGYVLYKG EAPAALDNDW
GAGGPAKDVG FDSQGFSTWQ KSSTSGSTDH IKIVKNNNAD DKLQVTGPGD ATVQQVITGL
TPGKTYSASV WVNITGERRT SISVKQGDKE VSNYALHTKL PFYAQQHKYL KTNFERIKVN
FDATSDTATV ALQTEPGTQT VQFDDVRVWE NPTKTDPGTS AFYEDFENVD EGWGPFVYSK
VGSVRTHLAE KTPNQPQTFV IDGQFSLKTN EDGMGEWLRT LPQTLRLKQD NKYHLTMDVK
AEVKDAYTVA VRVNDNGTVR DLAKATLNAG SSKVDLTFNT ENAKDAYLAI IKNADASTVL
IVDNIRVTDE GAMNAVPVTG VQLNKAEATL RIGETVELEA NIQPEQATKK DVTWASSNES
IATVAIVNGK AIITAKKAGT ADITVTTVDG NFKASAKITV QEGPAAPATS LAAPSSVLSG
SSFQVQLGVQ GVTEHVYAQD IAVDYDVNTL EFVEAKSLIS GVSIVETKKT PAGKLRLIIA
SEGEGHAVTG STNVIELTFR AKEVTQPANG TISVTQAILS NAQGVESTVG NSAANVAVTI
EDPTPTGDLN GDGKISIGDL ALAAANYGAT KASPNWDKVK MGDMDRNGVI DILDLAAIAQ
RIIGN
//
