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Database: UniProt
Entry: A0A140DRC4_9FIRM
LinkDB: A0A140DRC4_9FIRM
Original site: A0A140DRC4_9FIRM 
ID   A0A140DRC4_9FIRM        Unreviewed;       473 AA.
AC   A0A140DRC4;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=NodB homology domain-containing protein {ECO:0000259|PROSITE:PS51677};
GN   ORFNames=AALO17_00670 {ECO:0000313|EMBL:AMK53201.1};
OS   Faecalibaculum rodentium.
OC   Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC   Erysipelotrichaceae; Faecalibaculum.
OX   NCBI_TaxID=1702221 {ECO:0000313|EMBL:AMK53201.1, ECO:0000313|Proteomes:UP000069771};
RN   [1] {ECO:0000313|EMBL:AMK53201.1, ECO:0000313|Proteomes:UP000069771}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Alo17 {ECO:0000313|EMBL:AMK53201.1,
RC   ECO:0000313|Proteomes:UP000069771};
RX   PubMed=26877770; DOI=10.1186/s13099-016-0087-3;
RA   Lim S., Chang D.H., Ahn S., Kim B.C.;
RT   "Whole genome sequencing of "Faecalibaculum rodentium" ALO17, isolated from
RT   C57BL/6J laboratory mouse feces.";
RL   Gut Pathog. 8:3-3(2016).
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DR   EMBL; CP011391; AMK53201.1; -; Genomic_DNA.
DR   RefSeq; WP_067554038.1; NZ_CP011391.1.
DR   AlphaFoldDB; A0A140DRC4; -.
DR   STRING; 1702221.AALO17_00670; -.
DR   GeneID; 78476989; -.
DR   KEGG; fro:AALO17_00670; -.
DR   PATRIC; fig|1702221.3.peg.64; -.
DR   OrthoDB; 9806342at2; -.
DR   Proteomes; UP000069771; Chromosome.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd10944; CE4_SmPgdA_like; 1.
DR   Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   InterPro; IPR032179; Cry22Aa_Ig-like.
DR   InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR   InterPro; IPR022038; Ig-like_bact.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR002509; NODB_dom.
DR   PANTHER; PTHR10587; GLYCOSYL TRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR10587:SF125; POLYSACCHARIDE DEACETYLASE YHEN-RELATED; 1.
DR   Pfam; PF16403; Bact_surface_Ig-like; 1.
DR   Pfam; PF07523; Big_3; 1.
DR   Pfam; PF01522; Polysacc_deac_1; 1.
DR   SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR   PROSITE; PS51677; NODB; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000069771}.
FT   DOMAIN          267..458
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|PROSITE:PS51677"
SQ   SEQUENCE   473 AA;  52438 MW;  1EFA2EC7BB786839 CRC64;
     MAAKRKKGRR RRIRWSRFLV LGACAALVLG LFTSICLLIS PLHLKAGEVT TEYKHKYDPE
     SNIRVAFLGS PADVKIEGTV DTNQVGDYPL TYTYKGHEAK AVVHVTDTTA PTLEVRDYMA
     DMTQDVKPED MVTSAKDAGE VTVAFAPDTE DLTPKGKHRV TIVATDEFGN KTERQATLDR
     VEDTTKPQLK SDNKTLKVKQ GTAFELSGIT ATDDMDPEPA ITWDEDSIDM TKAGDYEVTV
     VATDRSGNKS ELKQKVTVEK NPEYGNKVVF LTFDDGPSEN TGKILKILEK YDAKATFFVT
     GNGQADNHFI KEAYDQGNAI GLHTYTHDYS YVYSSVDNYF QDLQQISDMV KDITGEAPKV
     IRFPGGSSNT VSANYTEGIM SRLVDLVHEK GYEYFDWNVS SGDAGGNDIP VDTIVQGATA
     CEEQYCTILF HDTMAKNTTV EALPEIIRHY KERGYVFLPL TRDSVAAHHG VNN
//
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