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Y3453_PSEA7
ID   Y3453_PSEA7             Reviewed;         346 AA.
AC   A6V6X8;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Probable RNA methyltransferase PSPA7_3453;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=PSPA7_3453;
OS   Pseudomonas aeruginosa (strain PA7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=381754;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PA7;
RA   Dodson R.J., Harkins D., Paulsen I.T.;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000744; ABR82142.1; -; Genomic_DNA.
DR   RefSeq; WP_012076146.1; NC_009656.1.
DR   AlphaFoldDB; A6V6X8; -.
DR   SMR; A6V6X8; -.
DR   EnsemblBacteria; ABR82142; ABR82142; PSPA7_3453.
DR   KEGG; pap:PSPA7_3453; -.
DR   HOGENOM; CLU_029101_3_3_6; -.
DR   OMA; KVVFMGM; -.
DR   OrthoDB; 1111428at2; -.
DR   Proteomes; UP000001582; 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; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..346
FT                   /note="Probable RNA methyltransferase PSPA7_3453"
FT                   /id="PRO_0000350332"
FT   DOMAIN          94..320
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT   ACT_SITE        91
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        325
FT                   /note="S-methylcysteine intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         108
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         115
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000250"
FT   BINDING         153..154
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         183
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         206..208
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         282
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   DISULFID        101..325
FT                   /note="(transient)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   346 AA;  38215 MW;  62420E2DF08C7E53 CRC64;
     MRSQDLHQRL ADLGAKPLHC GRIVRAWLQG RALDACTARQ RAEDFLPLSV RQGLPRVAEE
     LEGIARLHSE HPASDGSSRL LVELADRQRV ESVLLPRGGL CVSTQVGCAV GCVFCMTGRS
     GLLRQVGSLE MVAQVVLARR RRAVKKVVFM GMGEPAHNLD NVLEAIDLLG TDGGIGHKNL
     VFSTVGDPRV FERLPGQRVK PALALSLHST DAELRRRLLP KAPPLSPEEL VEAGETYARQ
     VDYPIQYQWT LLEGVNDSLE EMDGILRLLK GRFAVMNLIP YNSMDGDAYR RPRGERIVEL
     VRYLHSRGVL TKVRNSAGQD IDGGCGQLRA RAEGAAPQRH IRVRRG
 
 
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