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Database: UniProt
Entry: A0A0D6AUD1_9CHRO
LinkDB: A0A0D6AUD1_9CHRO
Original site: A0A0D6AUD1_9CHRO 
ID   A0A0D6AUD1_9CHRO        Unreviewed;       304 AA.
AC   A0A0D6AUD1;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 38.
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   ORFNames=GM3709_3111 {ECO:0000313|EMBL:BAQ66346.1};
OS   Geminocystis sp. NIES-3709.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Chroococcales; Geminocystaceae; Geminocystis.
OX   NCBI_TaxID=1617448 {ECO:0000313|EMBL:BAQ66346.1, ECO:0000313|Proteomes:UP000064126};
RN   [1] {ECO:0000313|EMBL:BAQ66346.1, ECO:0000313|Proteomes:UP000064126}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-3709 {ECO:0000313|EMBL:BAQ66346.1,
RC   ECO:0000313|Proteomes:UP000064126};
RA   Hirose Y.;
RT   "Geminocystis sp. NIES-3709 complete genome sequence.";
RL   Submitted (MAR-2015) 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}.
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DR   EMBL; AP014821; BAQ66346.1; -; Genomic_DNA.
DR   RefSeq; WP_066120816.1; NZ_AP014821.1.
DR   AlphaFoldDB; A0A0D6AUD1; -.
DR   STRING; 1617448.GM3709_3111; -.
DR   KEGG; gen:GM3709_3111; -.
DR   PATRIC; fig|1617448.3.peg.3151; -.
DR   OrthoDB; 9785995at2; -.
DR   Proteomes; UP000064126; Chromosome.
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:BAQ66346.1};
KW   Ribonucleoprotein {ECO:0000313|EMBL:BAQ66346.1};
KW   Ribosomal protein {ECO:0000313|EMBL:BAQ66346.1};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00735};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00735, ECO:0000313|EMBL:BAQ66346.1}.
FT   BINDING         139
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
FT   BINDING         163
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
FT   BINDING         185
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
FT   BINDING         230
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
SQ   SEQUENCE   304 AA;  34276 MW;  9A4FB11950046DB4 CRC64;
     MMTPWWEIKI NHIPELEDTI FWRLQEFGCQ GTALAKEDDS WFIKAYIPSI TKEVVDLAAL
     SLWLKQDCFL LGYNTPPISW QLINDEDWAS SWKEHWQPMD IGDRFTIYPA WIEPPTESNR
     IIIRLDPGSA FGTGVHATTQ LCLESLEMRL DELETPVTIA DIGCGSGILS IGAKLLGAKQ
     VYATDIDPLA IKATKENSEL NHVEGIEIFQ GSIDQLMLIP GLKFDGIVCN ILAEVIKTMI
     PDMCKIIKPD GWITLSGILV DQSLEIANLL EKDGWTIASL WKRGEWSCLN ARRLSTIKSN
     EWNS
//
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