ID A0A1F8DUB7_9BACT Unreviewed; 1378 AA.
AC A0A1F8DUB7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=LamG-like jellyroll fold domain-containing protein {ECO:0000259|SMART:SM00560};
GN ORFNames=A2935_00105 {ECO:0000313|EMBL:OGM92174.1};
OS Candidatus Wolfebacteria bacterium RIFCSPLOWO2_01_FULL_47_17b.
OC Bacteria; Candidatus Wolfebacteria.
OX NCBI_TaxID=1802558 {ECO:0000313|EMBL:OGM92174.1, ECO:0000313|Proteomes:UP000177011};
RN [1] {ECO:0000313|EMBL:OGM92174.1, ECO:0000313|Proteomes:UP000177011}
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:OGM92174.1}.
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DR EMBL; MGIS01000023; OGM92174.1; -; Genomic_DNA.
DR Proteomes; UP000177011; 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; cd00229; SGNH_hydrolase; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 1.10.1330.10; Dockerin domain; 1.
DR Gene3D; 3.40.50.1110; SGNH hydrolase; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR002105; Dockerin_1_rpt.
DR InterPro; IPR036439; Dockerin_dom_sf.
DR InterPro; IPR018765; DUF2341.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR006558; LamG-like.
DR InterPro; IPR041286; MBG_2.
DR InterPro; IPR043772; MBG_3.
DR InterPro; IPR013830; SGNH_hydro.
DR InterPro; IPR036514; SGNH_hydro_sf.
DR InterPro; IPR041248; YDG.
DR PANTHER; PTHR30383; THIOESTERASE 1/PROTEASE 1/LYSOPHOSPHOLIPASE L1; 1.
DR PANTHER; PTHR30383:SF5; THIOESTERASE 1_PROTEASE 1_LYSOPHOSPHOLIPASE L1; 1.
DR Pfam; PF00404; Dockerin_1; 1.
DR Pfam; PF10102; DUF2341; 1.
DR Pfam; PF13385; Laminin_G_3; 1.
DR Pfam; PF13472; Lipase_GDSL_2; 1.
DR Pfam; PF18676; MBG_2; 1.
DR Pfam; PF18887; MBG_3; 2.
DR Pfam; PF18657; YDG; 1.
DR SMART; SM00560; LamGL; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF52266; SGNH hydrolase; 1.
DR SUPFAM; SSF63446; Type I dockerin domain; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius}; Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 581..722
FT /note="LamG-like jellyroll fold"
FT /evidence="ECO:0000259|SMART:SM00560"
FT REGION 375..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..403
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1378 AA; 146497 MW; F648186FC0839AC1 CRC64;
MKKREYYYLI PVCVLLFAGI YVWFGHADEN ISHNIKAAEA VFEYSVTDPG VEPYISFEGP
ANNWEEIPYG TSTAMKANGL PTGTKNIEQS VRGYFTYAGG GTISMEVLLN GAAFVATIDG
EDGSVVTAPS GGGYGWVEVA NGISAEPHEI VIKVVDWKDD ENSTWEIAKL RVENGELDAS
SPIASRPLLL AYGDSITCCH FDDITLGFPH KAARQLGYAV SNQGVGGSHV AEVWVYPGSS
DERLAALASV SPQPDVVLVM YGTNDVGESG ESLEEFAAAD LHMAQSIRDI FPDARLVRIS
IPPRLTNGEL DTETARPYNE KIQENIAAVT GDPWEYLDIE NISGGVTFDS AYSGSDVHPD
SNAHTRIADA IVDFLSEGNP SPSPEPSPTP QAPPTPTPTS SPSPNPDSDE WWNESWQNRV
KIVFDTTQTA PTEDLVNFPY FVRASGEFGS DIRFLDSDNQ TLLPYEIETQ TNTETLAWIK
APQIDHNSTA DHIWMYYGNS DAADAQQPAA VWNENYLGVW HMSQDPSATM EDSTDNGMDA
LSGGAMASGQ QIDGVLGGSI DFDGVDDVLQ TQNTSALDAS HQITLETWVR LQNWPDDASV
FMWRDNTAVG SKRIFQLYQG FGGGGNIRWY LRDAGDIDHI LVSDEEISLG SWYQIAAVYD
GDAMKFYING SKDQNEVVES FAIQTGNVRL ALGAASDENN GGFYANAALD ESRISNIARS
AEWIAFEYCN MAGECQSYEA PENNPSESVP ADPVLSLENE YKTYNGSPQS AEVISSTPGT
VSDVTYSGSL TIPTDAGVYA ITADFIPDDL ANYNSLDDAP VGSFEIKKAD ADIAINPYSL
VYDGSSHTAA GTVHGAFGED LSADLDLSGT THTNAGTYSD TWRFMGGANY SDDDGVISNV
IDKAGATIAV EGYNGVYDGT PHGTTGAATG IAEESLAGFD PGDSFTDVPG GTAHWTFIDI
TGNYHNASGN ENIVISPKNL GVTVTGGNKI YDGTTSATVL LGSEDILAGD DVDVISGSPS
FGDPEVGANK NVNVPDISIA GADANNYNLL VPPTSTTANI SPQAAAIALQ GELHATYDGN
EHTVSAATNP EGLEFVILYD GLTTPPVNVG EYKVSALITD VNYAGSNTAT LYVNKAEITV
TADEKSKMYG ESPDPELSYS ITSEGGLMGD DVLFGSLVRE TGEHAGAYDI TQGTLDNLNY
DIDFIGSIFT ITKADQTVDF NPLEDRVYGD PDFELHADAS SGLPVVYSVG DGSICELVGE
GGSSIVHILG AGACTIIASQ EGDDDYKNAE SVSRTFAVVA DTGPSQSTGG GGGSIGGGSN
AITALPGDLN KDGTVDKYDF ALLMAQWGSA GSNGSDINND LTVDKYDFAL FMSYWAQN
//
