ID D7UZ82_LISGR Unreviewed; 318 AA.
AC D7UZ82;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Ribosomal protein L11 methyltransferase {ECO:0000256|HAMAP-Rule:MF_00735};
DE Short=L11 Mtase {ECO:0000256|HAMAP-Rule:MF_00735};
DE EC=2.1.1.- {ECO:0000256|HAMAP-Rule:MF_00735};
GN Name=prmA {ECO:0000256|HAMAP-Rule:MF_00735,
GN ECO:0000313|EMBL:EFI83649.1};
GN ORFNames=HMPREF0556_12334 {ECO:0000313|EMBL:EFI83649.1};
OS Listeria grayi DSM 20601.
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=525367 {ECO:0000313|EMBL:EFI83649.1, ECO:0000313|Proteomes:UP000010119};
RN [1] {ECO:0000313|EMBL:EFI83649.1, ECO:0000313|Proteomes:UP000010119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20601 {ECO:0000313|EMBL:EFI83649.1,
RC ECO:0000313|Proteomes:UP000010119};
RA Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., Hawes A.,
RA Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., Liu X.,
RA Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., Deng J.,
RA Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., Johnson A.,
RA Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., Song B.-B.,
RA Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M.,
RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N.,
RA Okwuonu G., Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W.,
RA Jakkamsetti A., Pham P., Ruth R., San Lucas F., Warren J., Zhang J.,
RA Zhao Z., Zhou C., Zhu D., Lee S., Bess C., Blankenburg K., Forbes L.,
RA Fu Q., Gubbala S., Hirani K., Jayaseelan J.C., Lara F., Munidasa M.,
RA Palculict T., Patil S., Pu L.-L., Saada N., Tang L., Weissenberger G.,
RA Zhu Y., Hemphill L., Shang Y., Youmans B., Ayvaz T., Ross M.,
RA Santibanez J., Aqrawi P., Gross S., Joshi V., Fowler G., Nazareth L.,
RA Reid J., Worley K., Petrosino J., Highlander S., Gibbs R.;
RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Methylates ribosomal protein L11. {ECO:0000256|HAMAP-
CC Rule:MF_00735}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) +
CC N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:54192, Rhea:RHEA-COMP:9752, Rhea:RHEA-
CC COMP:13826, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00735};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00735}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. PrmA family.
CC {ECO:0000256|ARBA:ARBA00009741, ECO:0000256|HAMAP-Rule:MF_00735}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFI83649.1}.
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DR EMBL; ACCR02000005; EFI83649.1; -; Genomic_DNA.
DR AlphaFoldDB; D7UZ82; -.
DR STRING; 525367.HMPREF0556_12334; -.
DR eggNOG; COG2264; Bacteria.
DR HOGENOM; CLU_049382_0_1_9; -.
DR Proteomes; UP000010119; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0042054; F:histone methyltransferase activity; IEA:RHEA.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR HAMAP; MF_00735; Methyltr_PrmA; 1.
DR InterPro; IPR004498; Ribosomal_PrmA_MeTrfase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; TIGR00406; prmA; 1.
DR PANTHER; PTHR43648; ELECTRON TRANSFER FLAVOPROTEIN BETA SUBUNIT LYSINE METHYLTRANSFERASE; 1.
DR PANTHER; PTHR43648:SF1; ELECTRON TRANSFER FLAVOPROTEIN BETA SUBUNIT LYSINE METHYLTRANSFERASE; 1.
DR Pfam; PF06325; PrmA; 1.
DR PIRSF; PIRSF000401; RPL11_MTase; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00735};
KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_00735,
KW ECO:0000313|EMBL:EFI83649.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010119};
KW Ribonucleoprotein {ECO:0000313|EMBL:EFI83649.1};
KW Ribosomal protein {ECO:0000313|EMBL:EFI83649.1};
KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00735};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00735, ECO:0000313|EMBL:EFI83649.1}.
FT BINDING 166
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
FT BINDING 187
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
FT BINDING 209
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
FT BINDING 252
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
SQ SEQUENCE 318 AA; 35057 MW; 664E060D62DCAF34 CRC64;
MRDQSMDWSE VEIHTINEAV EPVANVLTEH GASGVSIEDV ADFFKEREDR FGEIYELARE
DYPEDGVIIK AYFLKTSEFI QQIPALEKAV QHLATFDIPL GDLKFQVNDV SDEEWATAWK
KYYHPVQVTE QITIVPSWES YTPSEHEIII ELDPGLAFGT GTHPTTQLCI RELATQLKGG
ETILDVGTGS GVLSIVSAKL GAETVLATDL DEVAVRAAAE NIALNNTENV VTVKQNDLLK
GIEEEADVIV ANILAEVIVL FPEDVRRLLK PNGLFIASGI IKDKEEFVKE ALVKAGLEII
ATKQQGDWIA IISKQGGN
//
