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Database: UniProt
Entry: C6LLI8_9FIRM
LinkDB: C6LLI8_9FIRM
Original site: C6LLI8_9FIRM 
ID   C6LLI8_9FIRM            Unreviewed;       988 AA.
AC   C6LLI8;
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 C-terminal domain protein {ECO:0000313|EMBL:EET58528.1};
GN   ORFNames=BRYFOR_09536 {ECO:0000313|EMBL:EET58528.1};
OS   Marvinbryantia formatexigens DSM 14469.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Marvinbryantia.
OX   NCBI_TaxID=478749 {ECO:0000313|EMBL:EET58528.1, ECO:0000313|Proteomes:UP000005561};
RN   [1] {ECO:0000313|EMBL:EET58528.1, ECO:0000313|Proteomes:UP000005561}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14469 {ECO:0000313|EMBL:EET58528.1,
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:EET58528.1}.
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DR   EMBL; ACCL02000030; EET58528.1; -; Genomic_DNA.
DR   RefSeq; WP_006864289.1; NZ_CP102268.1.
DR   AlphaFoldDB; C6LLI8; -.
DR   STRING; 168384.SAMN05660368_03940; -.
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   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:EET58528.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005561};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           34..988
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002966442"
FT   DOMAIN          415..498
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
FT   REGION          129..152
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   988 AA;  106414 MW;  F75F857859368D21 CRC64;
     MRKHNAVKRI SSMAFAAAMV MSVVNPATIY VQAAPTADEC YAEGYDVNVQ LEAEGAVLLK
     NDDNCLPLAE GTKVTMLGAM SYNYVEGGTG SAGGQDDENT VMMNDAFIEA GLDVNEEAWS
     WLEEQCGGYR NNGDSNPGAS AGEDSGDDIF GTGGAGGGDW TSYTTVHEFS SDVYESGKDV
     LTADGYTDYA VVTFSRSGAE GASPSMDYDG DGSTLTGSTY LELTQEEKDL LAFCKENYTH
     TIVLINSATA MELGFVDSEE YNVDACLWIG HPGEAGVVGV GTILTGRTNP SGRLVDTYAY
     DMTTNPTYYN TDDNRYANAD NQTFYQYEEG IYVGYRYYET ADSVGYFDSE EFSSIEFKNG
     TATGYEEVVQ YPFGYGLSYT EFTEEITASD VSLEAHGTNS VTVTVTNTGD VAGKDVVELY
     MEAPYQSDTD NFGIKGVGLE KAKVVLVGFG KTSTLEPGAS EEVTIEFDTD DLASFDNFGQ
     GCYVLEKGDY KFNVQKDAHQ WGEEGSENAA SDSEAVTLET SIIYDESGDV ADAEYAGARD
     SDVTVAKNAM DDVTAGDGNM LEGYLSRNDI AGGMATIMEH TSNEEPNEML ADGIAEALAV
     KGTDSVEYTF ETYLKGEKTT VTETIYANGN NMMPFAETTP DGEDAAAVED PLWDQTYYVV
     EGETTESGLP VVVEEEPTEG SYHKLTVDDM ANVPIDTEEG LAIWDMLASE TSMDEAIELQ
     GNSGWKVPAV SSVGKSEEIA VDGPGEPGNG QYSGGTWFTC AVTIAATWNK DLAYAEGVAY
     GNQCVLYGIG NAYAPAMNLH RSPFGGRNFE YYSEDGLLSG QIGGNAVSGI MSTGTNVFIK
     HCALNDGDTN RGGNTTWANE QAIRELYMVP YEISIKEYGA DGVMGSLNRI GMSWFHYGMY
     KTMMRDEWGW HGMLITDGDG GTGDVYNTPQ AMLCIEGSML SISNYINASA TVDAYGDPTE
     SVYARYMLHN IMRDALYQYC GSSDAAAE
//
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