ID   R6V571_9FIRM            Unreviewed;       264 AA.
AC   R6V571;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=NodB homology domain-containing protein {ECO:0000259|PROSITE:PS51677};
GN   ORFNames=BN746_01656 {ECO:0000313|EMBL:CDC87301.1};
OS   Erysipelotrichaceae bacterium CAG:64.
OC   Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC   Erysipelotrichaceae.
OX   NCBI_TaxID=1262981 {ECO:0000313|EMBL:CDC87301.1, ECO:0000313|Proteomes:UP000018179};
RN   [1] {ECO:0000313|EMBL:CDC87301.1, ECO:0000313|Proteomes:UP000018179}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:64 {ECO:0000313|Proteomes:UP000018179};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the polysaccharide deacetylase family.
CC       {ECO:0000256|ARBA:ARBA00010973}.
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:CDC87301.1}.
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DR   EMBL; CBGA010000210; CDC87301.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6V571; -.
DR   Proteomes; UP000018179; Unassembled WGS sequence.
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; cd10966; CE4_yadE_5s; 1.
DR   Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR   InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR   InterPro; IPR002509; NODB_dom.
DR   PANTHER; PTHR34216; -; 1.
DR   PANTHER; PTHR34216:SF3; POLY-BETA-1,6-N-ACETYL-D-GLUCOSAMINE N-DEACETYLASE; 1.
DR   Pfam; PF01522; Polysacc_deac_1; 1.
DR   SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR   PROSITE; PS51677; NODB; 1.
PE   3: Inferred from homology;
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          96..264
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|PROSITE:PS51677"
SQ   SEQUENCE   264 AA;  30700 MW;  B42FD007ACA21B3F CRC64;
     MRQRKLTVIL LCILLLLYAG NALVQAFNRE DGIPIIGYHH VVPDADKQAF FPNNMWVISL
     SDFERQMQLL KEEGYHSVTL EDVYAWKMGK KDLDEKSIAI TFDDGFYSTT KFAQPVLKRY
     GFTGSVFVIG SVIDEQHGPY DPKLRQHASH ADMQDERVLQ YFSHSYDLHH KNADGFRIDQ
     LNDEQLQRDT EQAAKQGSIT YYAYPYGKYN KRIQKILNDN GTRLAFGYNE NRKAKRSDDS
     YALPRFNVNA YTRLDVFRAM LESR
//