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