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Database: UniProt
Entry: D1PQW1_9FIRM
LinkDB: D1PQW1_9FIRM
Original site: D1PQW1_9FIRM 
ID   D1PQW1_9FIRM            Unreviewed;       809 AA.
AC   D1PQW1;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   SubName: Full=Glycosyl hydrolase family 3 N-terminal domain protein {ECO:0000313|EMBL:EFB74976.1};
GN   ORFNames=SUBVAR_06788 {ECO:0000313|EMBL:EFB74976.1};
OS   Subdoligranulum variabile DSM 15176.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Subdoligranulum.
OX   NCBI_TaxID=411471 {ECO:0000313|EMBL:EFB74976.1, ECO:0000313|Proteomes:UP000003438};
RN   [1] {ECO:0000313|EMBL:EFB74976.1, ECO:0000313|Proteomes:UP000003438}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15176 {ECO:0000313|EMBL:EFB74976.1,
RC   ECO:0000313|Proteomes:UP000003438};
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 (DEC-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:EFB74976.1}.
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DR   EMBL; ACBY02000052; EFB74976.1; -; Genomic_DNA.
DR   RefSeq; WP_007048139.1; NZ_GG704770.1.
DR   AlphaFoldDB; D1PQW1; -.
DR   STRING; 411471.SUBVAR_06788; -.
DR   CAZy; GH3; Glycoside Hydrolase Family 3.
DR   GeneID; 78307375; -.
DR   eggNOG; COG1472; Bacteria.
DR   HOGENOM; CLU_004542_4_1_9; -.
DR   OrthoDB; 98455at2; -.
DR   Proteomes; UP000003438; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
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   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023001};
KW   Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
KW   Glycosidase {ECO:0000256|RuleBase:RU361161};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023001};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003438}.
FT   DOMAIN          573..643
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   809 AA;  88698 MW;  CD207A105E3BDF5E CRC64;
     MNQSILSTLT LEEKCALLSG KGEWETWDLP RAGVPSLVCS DGPHGIRRQA GAGDHLGLNP
     SLPATCFPTA ATVAGSWDPD LGEEIGQALG EEAAAQGVNI VLGPGLNIKR SPLCGRNFEY
     FSEDPYLAGK LAAGYIRGIQ SQGVYACPKH FAVNSQELRR MAMNAVVDER TLREIYLTGF
     EIAVREGGPG AIMTSYNQVN GTYANENPHL LQDILRGEWG YDGLVITDWG GSNDHVEGVR
     NGSDLEMPNP GMDSARQLVE AVRSGRLPES AVDACAARLV RATLALHETR DRPRSFDKEA
     HHTLARRAAS ESAVLLKNED DLLPLKPGTR VALIGDFAFT PRYQGAGSSM VNATRVDTME
     ALLPDSGLDW LGTARGYTRD GTPDPEREKN ALDLARAADV VIYCFGLDER SESEGIDRSH
     MRLPGHQIAL LEALARVNPH IVGVLSAGAA VEMPWLSCCQ ALLHGYLYGQ AGAGAMLDIL
     TGAVNPSGRL AESYPLHYED TPAYRYYPSE QRNAEYREGP YVGYRYYATA RVPVLFPFGY
     GLSYTSFAYR DLVVDEDGVT LTVENTGLRD GAEVVQLYIG KQDARVFRPV RELKGFQKVF
     LKAGERQRVH IAFDDKTFRY WNTAANRWAV EGGVYRVEVG ASSTDIRLTG TVEKEATTDQ
     LPCEGKALPH YRSGDIRQVP DEEFEALLGT PIPDGRWSGA LTANDAICQM YYARSSLARL
     VCRILTRKKQ RSEAAGTPDL NILFIYNMPF RAIAKMTGGA VSSEMVDGLV LMVNGHFWKG
     LTRTVRGFFR NRAKNEAYVA MLSADCKEE
//
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