ID   C6LEK9_9FIRM            Unreviewed;      1225 AA.
AC   C6LEK9;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   SubName: Full=Glycosyl hydrolase family 3 N-terminal domain protein {ECO:0000313|EMBL:EET60992.1};
GN   ORFNames=BRYFOR_07059 {ECO:0000313|EMBL:EET60992.1};
OS   Marvinbryantia formatexigens DSM 14469.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Marvinbryantia.
OX   NCBI_TaxID=478749 {ECO:0000313|EMBL:EET60992.1, ECO:0000313|Proteomes:UP000005561};
RN   [1] {ECO:0000313|EMBL:EET60992.1, ECO:0000313|Proteomes:UP000005561}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14469 {ECO:0000313|EMBL:EET60992.1,
RC   ECO:0000313|Proteomes:UP000005561};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC       {ECO:0000256|ARBA:ARBA00005336}.
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:EET60992.1}.
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DR   EMBL; ACCL02000008; EET60992.1; -; Genomic_DNA.
DR   AlphaFoldDB; C6LEK9; -.
DR   STRING; 168384.SAMN05660368_00331; -.
DR   eggNOG; COG1472; Bacteria.
DR   OrthoDB; 98455at2; -.
DR   Proteomes; UP000005561; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR   Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR026891; Fn3-like.
DR   InterPro; IPR002772; Glyco_hydro_3_C.
DR   InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR   InterPro; IPR001764; Glyco_hydro_3_N.
DR   InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR42715:SF10; BETA-GLUCOSIDASE F-RELATED; 1.
DR   Pfam; PF14310; Fn3-like; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   Pfam; PF01915; Glyco_hydro_3_C; 1.
DR   SMART; SM01217; Fn3_like; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EET60992.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005561};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..1225
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002968393"
FT   DOMAIN          403..482
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   1225 AA;  132766 MW;  10F88B2A67AA612D CRC64;
     MKKMRKQISV LAAAVMMTNP VAVMAETVVP EGNTYGFAGT GGRYYTDYAT LEDEQLAARE
     LAIEAAAEGF TLLKNENNAL PLKKGGYVSL FGMHSVNLVA STVGSAAGST GANGLEESTL
     QMAMEQAGFK VNPKLVDLYT KHEALGTTDN ELPMEYYSNA TVSTYNGYGD AAILVFSRTG
     SEGIDKVASN VAGHSDPADH EMMLDDNEKA LVKHVKENYP DKPIIVLINS SNILQIPELA
     APKAESEYGV DAIFWVGNTG NNAIEAIGQL LNGDVNPSGH TVEVWEKDFT KGPTWTNFGQ
     QTQNGTDAYL YTEDGNATIY ANIEYREGIY LGYKYYETAY DDAAEEEKDA AYENVLYPFG
     YGLSYTTFDW ELVENEESTI SDAWQKMAMQ VKVTNTGDTA GKDVVQIYAN PPYTPGGIEK
     ASANLVGFAK TDLLQPGESQ TVTIEWVAQD MASFDWNDAN ANDFAGYELE AGSYEITARR
     NSHDVVLEKT YTVDEGILCT NDYTTGNEIT PLFVDDWTTV NDSLLDHTIS RATGMVQPEV
     SSVEDRTIDS DYLEMIDNQY TYRSYMDQGY EDWYVDEGGI PSTWTQATAR GEEDKAEITI
     QDMTGIDFTL DVEDGAVVQG DDEGSQKWEA FMNQFTWEEL TDMVRNGGGV VSLPFAGIEG
     AGADETPLQL AGGTMWACPP ILAASFNVEL AERVGVMMGN EALFKGCSYW QGNAMNIHRS
     PLSGRNVEYY SQDGMHGGAF AAAVAKGVTS KGVTCEIKHM MLNDQESYRD LNGGVFTWAT
     EQVIREIYAR PFEAALKEGN ATGVMGSFNR LGNINSQLNP AVKALVRDEW DNRAIFETDA
     WQGTYCPIDL MVRQGNNQIL GSGSTLPVVD LEVGTWSAED NCVLVSDGGE GTFASQTHYA
     AVRKSAQEML WNYSNGNAIR NGYTTLDDAV MIFDAHVGQS LAINFEGVDF TEVSLAEGAE
     LPAGFTLEGG VITADGSQDI SEFTVGVVLT GIDGYITMEA NVDVKVIDPI HVSSTELKTG
     EAADITIDAP SYPYQALVTM FGTYVNGITD NDGNGVPSAE GELFGNPVTI PGTGDAVSGD
     FNIINWYWVD AAQPYGQTGY DTVGHIPATN SQSTDTRMIE LEDIAAGNYY KAFEYGYTVS
     DEDIAKLAEY GLTLEKVMTD SGYSYDVNTG LKISGTPAQA GTVEFGVTLN LPLARGFGSA
     FPNNVKVCSP AYVQIPTTVT LTIAE
//