ID   PRMA_HERA2              Reviewed;         321 AA.
AC   A9B5V4;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 70.
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=Haur_3109;
OS   Herpetosiphon aurantiacus (strain ATCC 23779 / DSM 785 / 114-95).
OC   Bacteria; Chloroflexi; Chloroflexia; Herpetosiphonales; Herpetosiphonaceae;
OC   Herpetosiphon.
OX   NCBI_TaxID=316274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23779 / DSM 785 / 114-95;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Bryant D.A., Richardson P.;
RT   "Complete sequence of chromosome of Herpetosiphon aurantiacus ATCC 23779.";
RL   Submitted (OCT-2007) 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; CP000875; ABX05747.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9B5V4; -.
DR   SMR; A9B5V4; -.
DR   STRING; 316274.Haur_3109; -.
DR   EnsemblBacteria; ABX05747; ABX05747; Haur_3109.
DR   KEGG; hau:Haur_3109; -.
DR   eggNOG; COG2264; Bacteria.
DR   HOGENOM; CLU_049382_0_1_0; -.
DR   OMA; EFFFIFP; -.
DR   Proteomes; UP000000787; 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.
PE   3: Inferred from homology;
KW   Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..321
FT                   /note="Ribosomal protein L11 methyltransferase"
FT                   /id="PRO_1000132802"
FT   BINDING         150
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00735"
FT   BINDING         171
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00735"
FT   BINDING         193
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00735"
FT   BINDING         256
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00735"
SQ   SEQUENCE   321 AA;  35192 MW;  187D54F7E33717C0 CRC64;
     MQWLELSVTV DTEAVESVSE LFAQYGYNGG VAVEEAIIPS LDSPEYQIDT NKPVIVRTYL
     LANEQAADAQ TQIERGLWVL GMMRPVGDLQ VKTIAEEDWA NAWKEHYRTR RIGQRFVIVP
     SWLEYEPAEN DVVLNLDPGM AFGTGLHPTT QLCLELMELI EFNNTTVLDL GCGSGILAVG
     AAKLGSQRVL ALDTDPIAVE ATAENARINH AETLVTALEG SLGDAPLEHW LGWEGAQLGT
     PQSYRHHNEF DVILANILAK VHVVLGNDYL AALKPGGVLI TSGIINEREA DVVAAFDAVG
     LEQVERRTQG DWVAFTHRKP V