ID   R6G0X8_9CLOT            Unreviewed;       933 AA.
AC   R6G0X8;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=Endo-1 3(4)-beta-glucanase {ECO:0000313|EMBL:CDB15189.1};
GN   ORFNames=BN542_00032 {ECO:0000313|EMBL:CDB15189.1};
OS   Clostridium sp. CAG:221.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1262780 {ECO:0000313|EMBL:CDB15189.1, ECO:0000313|Proteomes:UP000018176};
RN   [1] {ECO:0000313|EMBL:CDB15189.1, ECO:0000313|Proteomes:UP000018176}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:221 {ECO:0000313|Proteomes:UP000018176};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family.
CC       {ECO:0000256|ARBA:ARBA00006865}.
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:CDB15189.1}.
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DR   EMBL; CBDC010000050; CDB15189.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6G0X8; -.
DR   Proteomes; UP000018176; 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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd08023; GH16_laminarinase_like; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 1.20.1270.90; AF1782-like; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 3.
DR   InterPro; IPR003305; CenC_carb-bd.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR000757; GH16.
DR   PANTHER; PTHR10963:SF55; GH16 DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR10963; GLYCOSYL HYDROLASE-RELATED; 1.
DR   Pfam; PF02018; CBM_4_9; 2.
DR   Pfam; PF00722; Glyco_hydro_16; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 3.
DR   PROSITE; PS51762; GH16_2; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius}; Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..933
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004406622"
FT   TRANSMEM        907..926
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          33..288
FT                   /note="GH16"
FT                   /evidence="ECO:0000259|PROSITE:PS51762"
FT   REGION          851..898
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        863..898
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   933 AA;  105959 MW;  5D8567A1A5EDCA19 CRC64;
     MKKKFCNVLV GTLVTSMMSN MVTISNAYAD DNIDFMKETS EDWKLVWEDN FDGDSLNMEN
     WNYETHEPGW VNNELQEYTD STDNIYVKDG ELVLKAIKDE TEDGVKYTSG KVTTQNKRDY
     KYGRFEARLK VPEGKGLWPA FWMMPTDENL YGSWPRCGEI DIMEVLGHEP EKAYGTIHYG
     NPHREQQGTY ILDGTTFADD YHVFSVEWEP SEMRFYIDGN LYHTVNDWYT KQEGDDEKTY
     PAPFDQPFYL QFNLAVGGNW PGNPDETTDF ENAELKVDYV KVYQLDNYDE NVTKPEKEPV
     DLRDPDATGN YINNGDFSVN EDLTDNEGWI KLTTLGGRGE SIIENNKIIL TTEEVGSENH
     SLQLVQPQLP LKQYGEYRLT FDARADEDRT MIVNVTSPDR GYVRQFEDTV VNLTNELQSY
     SYDFIMKDID EANGRVEFNY GNQGSLANIE ISNVRLEKIG QHEAEDNNKK TVLPDGNYVY
     NGTFDVGQDR MKYWDIESTI DNVSIGVPNI NNSRELKVDV KENPASLSDV IVKQTDLAIA
     KNKEYTLSFD AYGEEDKTIK AQINDESFEA NITTEKNNFK YKFKTGEVLN NSNLELLLGA
     SGVTYIDNVR IEETGLITNG DFGNGFAKWE LFADSSVSSK VSSSIDNSTG DPSARIDIQD
     TGDADWKIQL KQSNVKLEKG KKYILSLDAK SSIDRSIMFT IQRDGSSDND WRPYSPNEIV
     ELKGEYNKYQ VIFEMTEESD KNSIFSIAMG AVNGTQITDE HSINIDNVKL EEYIPLVTEN
     LFNTIKNAKV IVYSDEFDEI VEEDREKLIA ALNEAEEVYE NAVSENPTVT QEIIDNAEQN
     LKNIMDNLRK EEQKEPGQDD NNQDENNKPG NNKPGDNKPG NNKPGAGNKN ESINKNNKPL
     VNTGSEAYII ILVSALVMVA VGVKIIKRKK SIN
//