ID C6LJM4_9FIRM Unreviewed; 1005 AA.
AC C6LJM4;
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:EET59147.1};
GN ORFNames=BRYFOR_08861 {ECO:0000313|EMBL:EET59147.1};
OS Marvinbryantia formatexigens DSM 14469.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Marvinbryantia.
OX NCBI_TaxID=478749 {ECO:0000313|EMBL:EET59147.1, ECO:0000313|Proteomes:UP000005561};
RN [1] {ECO:0000313|EMBL:EET59147.1, ECO:0000313|Proteomes:UP000005561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14469 {ECO:0000313|EMBL:EET59147.1,
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:EET59147.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ACCL02000021; EET59147.1; -; Genomic_DNA.
DR RefSeq; WP_006863624.1; NZ_CP102268.1.
DR AlphaFoldDB; C6LJM4; -.
DR STRING; 168384.SAMN05660368_01956; -.
DR eggNOG; COG1472; Bacteria.
DR OrthoDB; 98455at2; -.
DR Proteomes; UP000005561; 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 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 PRINTS; PR00133; GLHYDRLASE3.
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:EET59147.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000005561};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 31..52
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 64..86
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 971..996
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 479..557
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 1005 AA; 109299 MW; F434CD0829FE699A CRC64;
MVNLLANLLG PIFGSLGVSE ADLLAYLTQL QGYVYFILAA LVVLIVVLIL ASKAKKGFKH
VIRWEAVMAF FAALLITVNV ICYGPMYTNV SGFLNASKAD LSEETIAQSK DIIKRIGEEG
TVLLKNNGLL PLSSDVNALN VFGWDSTNPL FGGTGSGSSD ASTAVGILQS LQDAGYATNE
TLTKLYTDYR TERPTIAMSS QDWTLPEPTV DAYTDDIMTE AKEFSDTAVI VIGRSGGEGA
DLPMDMNAII HGTYNPGLEV SVAPANWCYM NAYYTNNGSY DDFEPGESYL ELSVTEEQLV
EKVCSEFDNV IVIINANNTM ELGWVDEYEQ IGAVLLAPGA GNTGFAALGE IINGSVNPSG
KTTDTFVKDL METPYINNIG NMPYNNVEDL KQQIAAADAS YEGNIAFANY VEGIYVGYKF
YETAAEEGFL KYEDYVQYPF GYGLSFTTFE KTIENFADNG DSISFDVVVT NTGDVAGKDV
AEIYFTPPYT NGGIEKASVN LVQFEKTGVL EPGASETLSF EIAKEDLASY DSEGIKIQGG
GYILEEGDYV ISVRSDSHTV DAEETFTVDA DIDYSTEGRA GDAVAATNQF EDYSRGDFVQ
LSRADKFANY DEACGPLKDE QFVMSDETRA AVEEYAFGTY DGTKYNNDED VMPTLGADNG
LTLFDLKGAP YDDAKWEQLL DQLTFDDMSM MINVGGWQTV AIDSVGKVAT SDCDGPAGLS
NFITGSYGTA YPSEVLLAQT WNKQLAYEVG QAMGQEYADA NNYGWYGPAM NTHRSAFAGR
NFEYYSEDGV LAGYLAANQV NGAAEKGVYA YIKHFAVNDQ ETNRCSFLLT YASEQAIREI
YLKPFEICVK GFTGNSQACM SSFNWIGTIP SCGNPYLLNN VLRGEWGFEG MVITDYDGSY
GYMISDHCVR SGNDLMLGFA SAASNQFTDQ SATATLAMRQ ACKNIMYTIV NSGYYAGDTN
PVGGMTNMDK LFVMVDVIGG VIIVGIAVLV LVRYLLKKKK KASVE
//