PRMA_THENE
ID PRMA_THENE Reviewed; 264 AA.
AC O86951;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2003, sequence version 2.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Ribosomal protein L11 methyltransferase {ECO:0000255|HAMAP-Rule:MF_00735};
DE Short=L11 Mtase {ECO:0000255|HAMAP-Rule:MF_00735};
DE EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_00735};
GN Name=prmA {ECO:0000255|HAMAP-Rule:MF_00735};
OS Thermotoga neapolitana.
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=2337;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Z2706-MC24;
RX PubMed=10390868; DOI=10.1016/s0723-2020(99)80063-0;
RA Zverlov V.V., Schwarz W.H.;
RT "Organization of the chromosomal region containing the genes lexA and topA
RT in Thermotoga neapolitana. Primary structure of LexA reveals phylogenetic
RT relevance.";
RL Syst. Appl. Microbiol. 22:174-178(1999).
CC -!- FUNCTION: Methylates ribosomal protein L11. {ECO:0000255|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:0000255|HAMAP-
CC Rule:MF_00735};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00735}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. PrmA family.
CC {ECO:0000255|HAMAP-Rule:MF_00735}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA07516.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ007446; CAA07516.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; O86951; -.
DR SMR; O86951; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008276; F:protein methyltransferase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_00735; Methyltr_PrmA; 1.
DR InterPro; IPR004498; Ribosomal_PrmA_MeTrfase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PIRSF; PIRSF000401; RPL11_MTase; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..264
FT /note="Ribosomal protein L11 methyltransferase"
FT /id="PRO_0000192327"
FT BINDING 116
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00735"
FT BINDING 137
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00735"
FT BINDING 159
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00735"
FT BINDING 200
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00735"
SQ SEQUENCE 264 AA; 30162 MW; 63DF2DF2141CF590 CRC64;
MRFKELVFLL KIDEEELLEK LYEEGFFNFA IEENKEGDRL LRVYLREGET LPSFLSNWKI
LDERLTTPKD WMVELEPFEI VEDVVVDPTE KVTRTDKIVV KLSPGVAFGT GLHPTTQMSV
LFLKKYLKKG DRVVDVGCGT GILAIVAKKL GASYVLAVDV DEQAVEVAKE NVQKNSVDVT
VKRSDLLSEV EGVFDLVVSN ILAEIHLRLL EDVSRVTHEK SILILSGIVD TKEDMVREKA
QKKGWNLLER KQEREWVTLV MKRS
