ID C6LMH9_9FIRM Unreviewed; 1031 AA.
AC C6LMH9;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Glycosyl hydrolase family 3 N-terminal domain protein {ECO:0000313|EMBL:EET58176.1};
GN ORFNames=BRYFOR_09880 {ECO:0000313|EMBL:EET58176.1};
OS Marvinbryantia formatexigens DSM 14469.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Marvinbryantia.
OX NCBI_TaxID=478749 {ECO:0000313|EMBL:EET58176.1, ECO:0000313|Proteomes:UP000005561};
RN [1] {ECO:0000313|EMBL:EET58176.1, ECO:0000313|Proteomes:UP000005561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14469 {ECO:0000313|EMBL:EET58176.1,
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, ECO:0000256|RuleBase:RU361161}.
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:EET58176.1}.
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DR EMBL; ACCL02000044; EET58176.1; -; Genomic_DNA.
DR AlphaFoldDB; C6LMH9; -.
DR STRING; 168384.SAMN05660368_04215; -.
DR eggNOG; COG1472; Bacteria.
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; IPR019800; Glyco_hydro_3_AS.
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.
DR PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361161};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
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 76..96
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 989..1009
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 512..586
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 1031 AA; 114233 MW; FCA67681DE1670C8 CRC64;
MYRKNRRTKK VCRFFYQFYP VQNQIYQKNF PVFFCGIVLS QDMKTQRKRM EEKSMGNVEV
AYEDVISVIQ LVRNHIIVIA AALVVMIAVM IFARKFKKPA KGFIRWQSLI AFVIVTALTV
NNMLSGALYN TINVVLADKG ELSQENADSS RQIIEEITNE GIVMTKNEDS FLPIAPEKIN
VFGWASTNPI YGGTGSGTVD ASTAVGILEG LENAGFETNK ELSDMYVEYR ADRPLISIND
GQDWTLPEVP VAQYSEEMIE NAKAFSDTAV IVIARTGGEG ADLPHDMGSV MDGSTLEIGT
KYVRGTYTNN GDYDDFEDGQ SYLELSRTEA DLVEMVCSEF DNVIVVYNGA NALELGWTED
YEQIKSVLLC AGAGATGFNA LGNIISGEVN PSGKTADTWV KDLHQTPYIN NIGHFAYTNT
QEVSDAALAA WERADGIVSF VNYTEGIYTG YRFYETAAEE ELIDYDELVM YPFGYGLSYT
TFEQEMGELE VTDDTISVDV TVTNTGSMAG KEVAELYYNP PYTNGGIEKS SVNLAAFDKT
DLLEPGQSQT LTLAFNIEDM ASYDTYGNGA WVLEEGTYEI SLRSDSHTVI DTKEYELADE
IVYNESNPHA GDVTAAANKL DFAEGNVTYL SRADGFANYE DAVKGPESYE LDGEVKGNGT
WNPEDYNNPE DVMPVTGADN GLELYDLRGA AYDDPRWEEL LDEVTVDEMV ELIAYGGHQT
ASVESVNKLR TLDTDGPAGL NSRTINAFGT GYCSEILIAQ TWNEDLAAKA GEGICREFTD
FHIVGWYAPS MNLHRSAFGG RNFEYYSEDS LLSSRMALAE VTAAVEQGVY PYIKHLVMNE
QETNRNALLC TWFTEQSARE LYLKPFEYCV KNTPSGKLAV MSSYNFLGTE WAGGCSALLK
DILREEWGFE GMVISDYFGN YGYMDADRAV RGGTDMMLGT SGNEAIMTDL SATSVIAMRE
ATKNIFYVVV NSNAYEEYVP GAIPSWMQIV YIVDAILAAL LILAEVFLIR GYLKKKKSVI
TIESATAEKK K
//
