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Database: UniProt
Entry: A0A1B8PNA7_MORNO
LinkDB: A0A1B8PNA7_MORNO
Original site: A0A1B8PNA7_MORNO 
ID   A0A1B8PNA7_MORNO        Unreviewed;       308 AA.
AC   A0A1B8PNA7;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 34.
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=A9Z60_00755 {ECO:0000313|EMBL:OBX52542.1};
OS   Moraxella nonliquefaciens.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Moraxella.
OX   NCBI_TaxID=478 {ECO:0000313|EMBL:OBX52542.1, ECO:0000313|Proteomes:UP000092671};
RN   [1] {ECO:0000313|EMBL:OBX52542.1, ECO:0000313|Proteomes:UP000092671}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 60284 {ECO:0000313|EMBL:OBX52542.1,
RC   ECO:0000313|Proteomes:UP000092671};
RA   Salva-Serra F., Engstrom-Jakobsson H., Thorell K., Gonzales-Siles L.,
RA   Karlsson R., Boulund F., Engstrand L., Kristiansson E., Moore E.;
RT   "Draft genome of Moraxella nonliquefaciens CCUG 60284.";
RL   Submitted (JUN-2016) 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}.
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:OBX52542.1}.
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DR   EMBL; LZDN01000001; OBX52542.1; -; Genomic_DNA.
DR   RefSeq; WP_066891511.1; NZ_LZDN01000001.1.
DR   AlphaFoldDB; A0A1B8PNA7; -.
DR   OrthoDB; 9785995at2; -.
DR   Proteomes; UP000092671; 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:OBX52542.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092671};
KW   Ribonucleoprotein {ECO:0000313|EMBL:OBX52542.1};
KW   Ribosomal protein {ECO:0000313|EMBL:OBX52542.1};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00735};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00735, ECO:0000313|EMBL:OBX52542.1}.
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         170
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
FT   BINDING         192
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   308 AA;  34630 MW;  BE4C3A5A871325AF CRC64;
     MAWQQIHLQL TKEQVELAEA LFYEAQAVSI LLEDAGDEPL FEPMPGEEPL WGDVVLTAIF
     DTNTDDRWDD TNFESLAHDI AAQVGASRVW LSVLDDKDWT CEWMIHYKPI QCAGNLWIVP
     KWLDAPNPNA INLILDPGLA FGTGYHATTR LCLDWLAGQD LTDKIIIDYG CGSGILGVGA
     LLLGAKQVLA VDIDPQALLA THQNAKLNGV EDKMLIFLPE EFKTHQKMHN ILADTITANI
     LAKPLIHFAP FFTTLLKNKG SIVLSGLIEN QVDDVMMAYQ PYFDLDMPYH YENSEDRHWY
     RLSAIKHS
//
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