GenomeNet

Database: UniProt
Entry: A0A136WIS1_9FIRM
LinkDB: A0A136WIS1_9FIRM
Original site: A0A136WIS1_9FIRM 
ID   A0A136WIS1_9FIRM        Unreviewed;       325 AA.
AC   A0A136WIS1;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
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   ECO:0000313|EMBL:KXL54442.1};
GN   ORFNames=CLNEO_05480 {ECO:0000313|EMBL:KXL54442.1};
OS   Anaerotignum neopropionicum.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Anaerotignum.
OX   NCBI_TaxID=36847 {ECO:0000313|EMBL:KXL54442.1, ECO:0000313|Proteomes:UP000070539};
RN   [1] {ECO:0000313|EMBL:KXL54442.1, ECO:0000313|Proteomes:UP000070539}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM-3847 {ECO:0000313|EMBL:KXL54442.1,
RC   ECO:0000313|Proteomes:UP000070539};
RA   Poehlein A., Beck M.H., Bengelsdorf F.R., Daniel R., Duerre P.;
RT   "Genome sequence of Clostridium neopropionicum X4, DSM-3847.";
RL   Submitted (JAN-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:KXL54442.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LRVM01000001; KXL54442.1; -; Genomic_DNA.
DR   RefSeq; WP_066084028.1; NZ_LRVM01000001.1.
DR   AlphaFoldDB; A0A136WIS1; -.
DR   STRING; 36847.CLNEO_05480; -.
DR   PATRIC; fig|36847.3.peg.679; -.
DR   OrthoDB; 9785995at2; -.
DR   Proteomes; UP000070539; 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:KXL54442.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070539};
KW   Ribonucleoprotein {ECO:0000313|EMBL:KXL54442.1};
KW   Ribosomal protein {ECO:0000313|EMBL:KXL54442.1};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00735};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00735, ECO:0000313|EMBL:KXL54442.1}.
FT   BINDING         166
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
FT   BINDING         187
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
FT   BINDING         209
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
FT   BINDING         260
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
SQ   SEQUENCE   325 AA;  36547 MW;  6060906E7718BFD3 CRC64;
     MEWIEVFVAV SQTGLEPVAG LLYECGLTGL MISDEADFQE FLDSPNRDWD YIADELVEEK
     QKLETGITFF LRDNLYGREQ LAQIKSALAV IKEQEKELDL GTLEMTMKNV QEEDWANNWK
     KYFKPFPVGE KIMIKPSWEE LTEPTDKVVL KIDPGHIFGT GTHETTQLCM ELIETYLKKD
     DMVLDIGCGS GILSIASLLL EAKEADAVDI DPNAMEIAYE NSDRNDIPRE KYHVCAGNIL
     EDEALHEKYS GKKYDMVEAN IVADVIIALT KKVPDYIKDG GIFLCSGIII ERKEDVLGAL
     DAGGYSVLEV KEKKGWVAIA ARYEG
//
DBGET integrated database retrieval system