ID A0A1R1DGX8_9BACL Unreviewed; 1522 AA.
AC A0A1R1DGX8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Dockerin domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=BK133_01210 {ECO:0000313|EMBL:OMF38847.1};
OS Paenibacillus sp. FSL H8-0548.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1920422 {ECO:0000313|EMBL:OMF38847.1, ECO:0000313|Proteomes:UP000187405};
RN [1] {ECO:0000313|EMBL:OMF38847.1, ECO:0000313|Proteomes:UP000187405}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL H8-0548 {ECO:0000313|EMBL:OMF38847.1,
RC ECO:0000313|Proteomes:UP000187405};
RA Beno S.M.;
RT "Paenibacillus species isolates.";
RL Submitted (NOV-2016) 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:OMF38847.1}.
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DR EMBL; MRTK01000001; OMF38847.1; -; Genomic_DNA.
DR RefSeq; WP_076334523.1; NZ_MRTK01000001.1.
DR STRING; 1920422.BK133_01210; -.
DR OrthoDB; 9757939at2; -.
DR Proteomes; UP000187405; Unassembled WGS sequence.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
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; cd14254; Dockerin_II; 1.
DR CDD; cd08547; Type_II_cohesin; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.60.40.680; -; 1.
DR Gene3D; 1.20.1270.90; AF1782-like; 1.
DR Gene3D; 1.10.1330.10; Dockerin domain; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR046780; aBig_2.
DR InterPro; IPR012878; Beta-AFase-like_GH127_cat.
DR InterPro; IPR049046; Beta-AFase-like_GH127_middle.
DR InterPro; IPR025883; Cadherin-like_b_sandwich.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR002102; Cohesin_dom.
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; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR046544; GH146_SB_dom.
DR PANTHER; PTHR31151; PROLINE-TRNA LIGASE (DUF1680); 1.
DR PANTHER; PTHR31151:SF0; PROLINE-TRNA LIGASE (DUF1680); 1.
DR Pfam; PF20578; aBig_2; 1.
DR Pfam; PF12733; Cadherin-like; 1.
DR Pfam; PF00963; Cohesin; 1.
DR Pfam; PF00404; Dockerin_1; 1.
DR Pfam; PF20620; DUF6805; 1.
DR Pfam; PF20736; Glyco_hydro127M; 1.
DR Pfam; PF07944; Glyco_hydro_127; 1.
DR Pfam; PF13385; Laminin_G_3; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR SUPFAM; SSF63446; Type I dockerin domain; 1.
DR PROSITE; PS51766; DOCKERIN; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000187405};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1522
FT /note="Dockerin domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039473177"
FT DOMAIN 1459..1522
FT /note="Dockerin"
FT /evidence="ECO:0000259|PROSITE:PS51766"
FT DOMAIN 1496..1522
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
SQ SEQUENCE 1522 AA; 167030 MW; 6793A3BF18179FF7 CRC64;
MKYQRKLGIW ALTVVMLSSN LLAGQTLFAA NVNSNTLALL DASKVLSLKF EDNVQDSSAK
GNNGTISGVN YSYVPDVDGG KALKLSGSTF VDLGKSGTLQ PADLTVSFWI KPNETMTGEQ
MLMWNKTSYY SDGWYLTSES DSKPLAISLG SSEANRQPYK VNITGSRNNF FPIDAWTHVA
ITYNNLTKAV KIYRNGILQT ITIENPTGVS GADGVIKSDD TTSKSLGYNG PQYNGAYAKY
SLDDYFVYST AASYEAIVAL YEDKSGTSFD YELVARSDAE AIVLPEKASS DIALPLIGKS
ESTISWVSSN VDVIDLLGGV QRPAAGESDA SVILTANVSF GSKSVTRDFI VIVPAMKSSS
DSLEAVPMAD VTLTDSYYAN AFKKEVDYLL SLEADRLLSA FRTTSGLNPK AAVYDGWENT
EIRGHTLGHY LSAISTAYVN ATGADKARLK ERMDYIIDEL AACQDANGNG YISAFPTSFL
DKVENGQAVW VPWYTIHKIL AGLVSAAEFG DNPKALQIAE KFGEYIYNRT ATWNEAMKSR
VLSVEYGGMN DSLYDLYSLT DNNHFLKAAE KFDEISLFNS LYNNVDILNG KHANTTIPKV
IGALKRYTVL DESEIEEYYL QVAENFWEMV VKHHSYVTGG NSENEHFGHS DVLEAELTNV
NDETCNVYNM LKLTRELYKI TKDKKYADFY ENAFTNSIIS SQNPETGMTM YFQPMDTGYF
KVFSSAFFHF WCCTGTGMEN FAKLNDSIYF TSKDSVYVNQ YLSSIVKLSD KNLVITQQSQ
LPNTGIGDAA TGIVAFTINT TGPTNTTLRF RIPDWAKTTP RVKLNGAVSQ DYAIEGGYLV
FTKNWTDGTT ITLDFPMEVI GFDLPDAKNT VAFKYGPIVL SAGLGTKDMQ TQTHGVNVLK
PNKDTSAKNF ITILGHDIEL WKENVAQNLV KTDGKLEFTL KGTDADDGIL TFSPHFARYE
DRYGIYFDLI TADSLSYQQS LLAEKEAGRA EAASVSFVIV ANDQYELAAN RQTNQSTVGI
YNGKSYRDAL ANGSFSYDME VTPGVANYLF STYYSGDAGR KFDIFIDDTK LVSESIENRI
PGNFYNQTRK ITQQLVESSR TKTVQESDKY GNPVQRTVHY VTVKFASSGG LVGGLFDIFR
VITDYKTNPS LKSLTFTEGN LSQEFDPEVT EYTLTVPTAT ESITMNAQPM DEFGLVYYGE
ILINDKVTRN ISLTGDSTEI VLTAKAEDHT TSKQYAIHIV KSDEAASNPL TISGAASVVS
NQIFDVMVSL NMETADVFAK DLTFSYDPSK VEFVSAEALK PDFIIVDQSE TLGKVRLLTV
DLHPEKNTES PFSVLKLQFK AKEISEAQSS SITMSDIVFA NGSGMESAIS NPNPYLFEII
AGITKDALND AVGAAQSLYD AAVEGTHTGQ YPAGSKASLF AAIQDAKEVL NDSTASQAQI
NQAAERISTA VQLFRSLVNT QVLGDLNGDN VVRVGDLAIL ASHYGMTSSD PEWNKFNSAD
FNKDGKIDIE DIAAIARLIL GE
//
