ID   Y2870_AROAE             Reviewed;         354 AA.
AC   Q5P119;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Probable RNA methyltransferase AZOSEA28700;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=AZOSEA28700; ORFNames=ebA5068;
OS   Aromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC   Rhodocyclaceae; Aromatoleum.
OX   NCBI_TaxID=76114;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EbN1;
RX   PubMed=15551059; DOI=10.1007/s00203-004-0742-9;
RA   Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F.,
RA   Reinhardt R.;
RT   "The genome sequence of an anaerobic aromatic-degrading denitrifying
RT   bacterium, strain EbN1.";
RL   Arch. Microbiol. 183:27-36(2005).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAI08995.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CR555306; CAI08995.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041647372.1; NC_006513.1.
DR   AlphaFoldDB; Q5P119; -.
DR   SMR; Q5P119; -.
DR   STRING; 76114.ebA5068; -.
DR   EnsemblBacteria; CAI08995; CAI08995; ebA5068.
DR   KEGG; eba:ebA5068; -.
DR   eggNOG; COG0820; Bacteria.
DR   HOGENOM; CLU_029101_3_3_4; -.
DR   OMA; KVVFMGM; -.
DR   OrthoDB; 1111428at2; -.
DR   Proteomes; UP000006552; 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   SFLD; SFLDF00275; adenosine_C2_methyltransferase; 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..354
FT                   /note="Probable RNA methyltransferase AZOSEA28700"
FT                   /id="PRO_0000350023"
FT   DOMAIN          91..317
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT   ACT_SITE        88
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        322
FT                   /note="S-methylcysteine intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         105
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000250"
FT   BINDING         109
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000250"
FT   BINDING         112
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000250"
FT   BINDING         150..151
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         180
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         203..205
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         279
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   DISULFID        98..322
FT                   /note="(transient)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   354 AA;  38198 MW;  A5479CCFE110BC72 CRC64;
     MRIDHIRQRL RASGAKPCHE QRVLRAWTHA LPLDRGRCRS EDFFPAPLGA RLPALGAELA
     ALAQVRSEHA GEDGARLLVE LADGQTVESV LLPRDGLCVS TQVGCAVGCA FCMTGRDGLL
     RQLGSAEIVA QVVLARSRRA VRKVVFMGMG EPAHNLDNVL EAIALLGTEG GIGHKNLVFS
     TVGDRRVFER LPQGSVKPAL ALSLHTTRPA LRTKLMPRAP RLDPAELVEL GETYARATGY
     PIQYQWTLLA GVNDDDEELD GIVRLLAGKY AVMNFIPYNS VAGAGFARPS WEHAAAMARY
     LHRRGILTKL RHSAGQDVDG GCGQLRARVI ASGALGQPAE AAPDRVVLVR RGQA