ID K4LJY1_9FIRM Unreviewed; 479 AA.
AC K4LJY1;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Transcriptional regulatory protein {ECO:0000313|EMBL:AFV06958.1};
GN ORFNames=DCF50_p2955 {ECO:0000313|EMBL:AFV06958.1};
OS Dehalobacter sp. CF.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Dehalobacter.
OX NCBI_TaxID=1131462 {ECO:0000313|EMBL:AFV06958.1, ECO:0000313|Proteomes:UP000000482};
RN [1] {ECO:0000313|EMBL:AFV06958.1, ECO:0000313|Proteomes:UP000000482}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF {ECO:0000313|EMBL:AFV06958.1};
RX PubMed=23284863; DOI=10.1371/journal.pone.0052038;
RA Tang S., Gong Y., Edwards E.A.;
RT "Semi-automatic in silico gap closure enabled de novo assembly of two
RT dehalobacter genomes from metagenomic data.";
RL PLoS ONE 7:E52038-E52038(2012).
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. Anaerobic
CC sulfatase-maturating enzyme family. {ECO:0000256|ARBA:ARBA00023601}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003870; AFV06958.1; -; Genomic_DNA.
DR RefSeq; WP_015044986.1; NC_018867.1.
DR AlphaFoldDB; K4LJY1; -.
DR STRING; 1131462.DCF50_p2955; -.
DR KEGG; dec:DCF50_p2955; -.
DR PATRIC; fig|1131462.4.peg.2986; -.
DR eggNOG; COG0641; Bacteria.
DR HOGENOM; CLU_009273_3_3_9; -.
DR Proteomes; UP000000482; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd01335; Radical_SAM; 1.
DR CDD; cd21124; SPASM_CteB-like; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR023885; 4Fe4S-binding_SPASM_dom.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000385; MoaA_NifB_PqqE_Fe-S-bd_CS.
DR InterPro; IPR007197; rSAM.
DR InterPro; IPR024025; SCIFF_rSAM_maturase.
DR InterPro; IPR047602; SPASM_CteB-like.
DR InterPro; IPR023867; Sulphatase_maturase_rSAM.
DR NCBIfam; TIGR04085; rSAM_more_4Fe4S; 1.
DR NCBIfam; TIGR03974; rSAM_six_Cys; 1.
DR PANTHER; PTHR43273; ANAEROBIC SULFATASE-MATURATING ENZYME HOMOLOG ASLB-RELATED; 1.
DR PANTHER; PTHR43273:SF8; RADICAL SAM PROTEIN-RELATED; 1.
DR Pfam; PF13353; Fer4_12; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR Pfam; PF13186; SPASM; 1.
DR SFLD; SFLDG01383; cyclic_pyranopterin_phosphate; 1.
DR SFLD; SFLDG01384; thioether_bond_formation_requi; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS01305; MOAA_NIFB_PQQE; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000000482};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 104..310
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 479 AA; 54497 MW; C427A676AE0F4B56 CRC64;
MKLTNYNIAK NVHVYTQGKL QIAYDVNSGS LHVIDDKTYA FIQELITYQQ KNSLEDSEEM
LDSCGYNLSS EEKQEILVEL KVLQDQKLLF SCEPEETVLP FSDRPVIKAM CLHVAHDCNL
RCKYCFAGTG PFGGNRELMN VKTGKKALKF LLDHSGDRGH CEVDFFGGEP LMNLPVIREL
IVYGREIAAQ AGKKIKFTLT TNAVLMDEET ARFLEDEGIS VVLSLDGRKE VNDRMRPFLN
GAGSYDRIMP QILKFTEMRP ETSRYAVGNY FYVRGTYTHF NKDFYKDVLH MADSGIRRIS
VEPVVASPQE VYAFREEDLA EIKESYDILG EKVLEYREAG KEFVFFHFNA GLDEGPCLIK
RLSGCGAGHE YVAVSPEGDI YPCHQFVGQE KYKMGSVNDL NCELKEEIVQ SFRQAQVYAK
EECRVCWARF SCSGGCHAAN EAFSGELTKV YPMGCELQKK RLEVAYYLKI MEARQRVLV
//
