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Database: UniProt
Entry: G4F2A0_9GAMM
LinkDB: G4F2A0_9GAMM
Original site: G4F2A0_9GAMM 
ID   G4F2A0_9GAMM            Unreviewed;       304 AA.
AC   G4F2A0;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 44.
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=HAL1_02480 {ECO:0000313|EMBL:EHA17175.1};
OS   Halomonas sp. HAL1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=550984 {ECO:0000313|EMBL:EHA17175.1, ECO:0000313|Proteomes:UP000005692};
RN   [1] {ECO:0000313|EMBL:EHA17175.1, ECO:0000313|Proteomes:UP000005692}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=strain {ECO:0000313|Proteomes:UP000005692};
RX   PubMed=22156396; DOI=10.1128/JB.06359-11;
RA   Lin Y., Fan H., Hao X., Johnstone L., Hu Y., Wei G., Alwathnani H.A.,
RA   Wang G., Rensing C.;
RT   "Draft Genome Sequence of Halomonas sp. Strain HAL1, a Moderately
RT   Halophilic Arsenite-Oxidizing Bacterium Isolated from Gold-Mine Soil.";
RL   J. Bacteriol. 194:199-200(2012).
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:EHA17175.1}.
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DR   EMBL; AGIB01000014; EHA17175.1; -; Genomic_DNA.
DR   RefSeq; WP_008956428.1; NZ_CP130610.1.
DR   AlphaFoldDB; G4F2A0; -.
DR   PATRIC; fig|550984.5.peg.489; -.
DR   Proteomes; UP000005692; 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:EHA17175.1};
KW   Ribonucleoprotein {ECO:0000313|EMBL:EHA17175.1};
KW   Ribosomal protein {ECO:0000313|EMBL:EHA17175.1};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00735};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00735, ECO:0000313|EMBL:EHA17175.1}.
FT   BINDING         149
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
FT   BINDING         174
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
FT   BINDING         196
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
FT   BINDING         239
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
SQ   SEQUENCE   304 AA;  33209 MW;  D72337EF64262958 CRC64;
     MPWLQLKAHV APEQAEFLEE LLLDEGATAI GLQDAHDDPV FEPERGTTPL WEDTILTGLY
     DDLEGVESML ERIEAAWSEQ MPEEPCPTIV YELLADRDWE REWMDDFTPL QMGQRLWIVP
     SWHEPPHADA VNLILDPGLA FGTGTHPTTA LCLEWLDELA VAGHLAQQTV LDVGCGSGIL
     AIAALKLGAS HADATDIDPQ ALQASRDNAE RNGIAEPDLT LYYPEQLSDG GDYPVVTANI
     LAGPLVELAP MIAGHVTPSG RIALSGILAN QANEVYEAYA AQGIAMEEPV IREGWVRLNG
     QRPR
//
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