Y4379_ANADF
ID Y4379_ANADF Reviewed; 336 AA.
AC A7HIL1;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Probable RNA methyltransferase Anae109_4379;
DE EC=2.1.1.-;
GN OrderedLocusNames=Anae109_4379;
OS Anaeromyxobacter sp. (strain Fw109-5).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter;
OC unclassified Anaeromyxobacter.
OX NCBI_TaxID=404589;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fw109-5;
RX PubMed=25614562; DOI=10.1128/genomea.01449-14;
RA Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Glavina Del Rio T.,
RA Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.C.,
RA Detter J.C., Han C.S., Schmutz J., Larimer F.W., Land M.L., Hauser L.J.,
RA Kyrpides N., Lykidis A., Richardson P., Belieav A., Sanford R.A.,
RA Loeffler F.E., Fields M.W.;
RT "Complete genome sequence of Anaeromyxobacter sp. Fw109-5, an anaerobic,
RT metal-reducing bacterium isolated from a contaminated subsurface
RT environment.";
RL Genome Announc. 3:0-0(2015).
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC cysteines and an exchangeable S-adenosyl-L-methionine. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. RlmN family.
CC {ECO:0000305}.
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DR EMBL; CP000769; ABS28557.1; -; Genomic_DNA.
DR RefSeq; WP_012099202.1; NC_009675.1.
DR AlphaFoldDB; A7HIL1; -.
DR SMR; A7HIL1; -.
DR STRING; 404589.Anae109_4379; -.
DR EnsemblBacteria; ABS28557; ABS28557; Anae109_4379.
DR KEGG; afw:Anae109_4379; -.
DR eggNOG; COG0820; Bacteria.
DR HOGENOM; CLU_029101_2_0_7; -.
DR OMA; QDEHAAC; -.
DR OrthoDB; 1111428at2; -.
DR Proteomes; UP000006382; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR GO; GO:0006364; P:rRNA processing; IEA:InterPro.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR040072; Methyltransferase_A.
DR InterPro; IPR004383; rRNA_lsu_MTrfase_RlmN/Cfr.
DR InterPro; IPR007197; rSAM.
DR PANTHER; PTHR30544; PTHR30544; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR PIRSF; PIRSF006004; CHP00048; 1.
DR SFLD; SFLDF00275; adenosine_C2_methyltransferase; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Cytoplasm; Disulfide bond; Iron; Iron-sulfur; Metal-binding;
KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..336
FT /note="Probable RNA methyltransferase Anae109_4379"
FT /id="PRO_0000350017"
FT DOMAIN 93..322
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT ACT_SITE 86
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT ACT_SITE 328
FT /note="S-methylcysteine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 107
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
FT BINDING 111
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
FT BINDING 114
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
FT BINDING 154..155
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 209..211
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT DISULFID 100..328
FT /note="(transient)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 336 AA; 36414 MW; 7C55057CEB912E40 CRC64;
MLHLLGQDSR ALARKAGISL EDARRITGAV IGRGAPLRSA RNVRRAVLDR VEALATPGEL
RRVACTDAKD GFRRYLLELG DGARVEAVRI PLFDTHHTVC LSSQAGCALG CSFCATGALG
LARSLRAWEI VAQLLHVRAD STRPITGVVF MGQGEPFLNY DAVLEAAYTL CDPAGGRIDG
RRISISTAGV VPMIRRYTAE GHKFRLCVSL NAAIPWKRRA LMPIEEGFPL DELVDAVREH
AAQRGRVTLE YVMIAGVNTG DEDAAALGRL LAGIPVRLNP IAVNDATGRH RPPDEAEWNA
FRDALARELP GQPIVRRYSG GQDEHAACGM LSSRTR
