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PRMA_HAEDU
ID   PRMA_HAEDU              Reviewed;         293 AA.
AC   Q7VPN5;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 96.
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}; OrderedLocusNames=HD_0016;
OS   Haemophilus ducreyi (strain 35000HP / ATCC 700724).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=233412;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=35000HP / ATCC 700724;
RA   Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L.,
RA   Nguyen D., Wang J., Forst C., Hood L.;
RT   "The complete genome sequence of Haemophilus ducreyi.";
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; AE017143; AAP95039.1; -; Genomic_DNA.
DR   RefSeq; WP_010944093.1; NC_002940.2.
DR   AlphaFoldDB; Q7VPN5; -.
DR   SMR; Q7VPN5; -.
DR   STRING; 233412.HD_0016; -.
DR   EnsemblBacteria; AAP95039; AAP95039; HD_0016.
DR   KEGG; hdu:HD_0016; -.
DR   eggNOG; COG2264; Bacteria.
DR   HOGENOM; CLU_049382_4_1_6; -.
DR   OMA; EFFFIFP; -.
DR   Proteomes; UP000001022; Chromosome.
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.
DR   TIGRFAMs; TIGR00406; prmA; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..293
FT                   /note="Ribosomal protein L11 methyltransferase"
FT                   /id="PRO_0000192265"
FT   BINDING         145
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00735"
FT   BINDING         166
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00735"
FT   BINDING         188
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00735"
FT   BINDING         230
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00735"
SQ   SEQUENCE   293 AA;  31961 MW;  37D98197F3010B55 CRC64;
     MAWLQIRLNS TDKYAEQISD FLEEIGAVSV TFMDSQDTPI FEPLPGETRL WGNTDVMGLF
     DAETDMQAVV SALITSGLVT ADFAHKVEQI EDKDWEREWM DNFHPMQFGQ RLWICPSWRE
     VPDEKAVNIM LDPGLAFGTG THPTTALCLQ WLDGLDLTGK TVIDFGCGSG ILAISALKLG
     AKQAIGIDID PQAILASQNN AAANGVADRL QLFLAKDQPQ ALQADVVVAN ILAGPLKELA
     PNIMTLVKPQ GYLGLSGILA TQAQSVCQAY AAVFKLDPVV EKEEWCRITG IKQ
 
 
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