RSMJ_NEIGO
ID RSMJ_NEIGO Reviewed; 250 AA.
AC P72077;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Ribosomal RNA small subunit methyltransferase J {ECO:0000255|HAMAP-Rule:MF_01523};
DE EC=2.1.1.242 {ECO:0000255|HAMAP-Rule:MF_01523};
DE AltName: Full=16S rRNA m2G1516 methyltransferase {ECO:0000255|HAMAP-Rule:MF_01523};
DE AltName: Full=rRNA (guanine-N(2)-)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01523};
GN Name=rsmJ {ECO:0000255|HAMAP-Rule:MF_01523};
OS Neisseria gonorrhoeae.
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=485;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MS11;
RX PubMed=9767087; DOI=10.1016/s0378-1119(98)00424-7;
RA Carrick C.S., Fyfe J.A.M., Davies J.K.;
RT "Neisseria gonorrhoeae contains multiple copies of a gene that may encode a
RT site-specific recombinase and is associated with DNA rearrangements.";
RL Gene 220:21-29(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RG Northeast structural genomics consortium (NESG);
RT "Crystal structure of the SAM-dependent methyltransferase NGO1261 from
RT Neisseria gonorrhoeae.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: Specifically methylates the guanosine in position 1516 of 16S
CC rRNA. {ECO:0000255|HAMAP-Rule:MF_01523}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(1516) in 16S rRNA + S-adenosyl-L-methionine = H(+) +
CC N(2)-methylguanosine(1516) in 16S rRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:43220, Rhea:RHEA-COMP:10412, Rhea:RHEA-COMP:10413,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74269, ChEBI:CHEBI:74481; EC=2.1.1.242;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01523};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01523}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RsmJ family.
CC {ECO:0000255|HAMAP-Rule:MF_01523}.
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; U65994; AAC82508.1; -; Genomic_DNA.
DR RefSeq; WP_003689730.1; NZ_WHPL01000001.1.
DR PDB; 2R6Z; X-ray; 1.80 A; A/B=1-250.
DR PDBsum; 2R6Z; -.
DR AlphaFoldDB; P72077; -.
DR SMR; P72077; -.
DR EvolutionaryTrace; P72077; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008990; F:rRNA (guanine-N2-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_01523; 16SrRNA_methyltr_J; 1.
DR InterPro; IPR007536; 16SrRNA_methylTrfase_J.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR36112; PTHR36112; 1.
DR Pfam; PF04445; SAM_MT; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Methyltransferase; rRNA processing;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..250
FT /note="Ribosomal RNA small subunit methyltransferase J"
FT /id="PRO_0000212077"
FT BINDING 96..97
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01523"
FT BINDING 168
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01523"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:2R6Z"
FT HELIX 12..18
FT /evidence="ECO:0007829|PDB:2R6Z"
FT STRAND 24..28
FT /evidence="ECO:0007829|PDB:2R6Z"
FT STRAND 31..39
FT /evidence="ECO:0007829|PDB:2R6Z"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:2R6Z"
FT HELIX 61..67
FT /evidence="ECO:0007829|PDB:2R6Z"
FT HELIX 74..78
FT /evidence="ECO:0007829|PDB:2R6Z"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:2R6Z"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:2R6Z"
FT HELIX 96..103
FT /evidence="ECO:0007829|PDB:2R6Z"
FT STRAND 108..112
FT /evidence="ECO:0007829|PDB:2R6Z"
FT HELIX 115..130
FT /evidence="ECO:0007829|PDB:2R6Z"
FT HELIX 132..138
FT /evidence="ECO:0007829|PDB:2R6Z"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:2R6Z"
FT HELIX 148..159
FT /evidence="ECO:0007829|PDB:2R6Z"
FT STRAND 163..167
FT /evidence="ECO:0007829|PDB:2R6Z"
FT HELIX 185..191
FT /evidence="ECO:0007829|PDB:2R6Z"
FT HELIX 193..207
FT /evidence="ECO:0007829|PDB:2R6Z"
FT STRAND 209..217
FT /evidence="ECO:0007829|PDB:2R6Z"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:2R6Z"
FT STRAND 229..233
FT /evidence="ECO:0007829|PDB:2R6Z"
FT STRAND 235..242
FT /evidence="ECO:0007829|PDB:2R6Z"
SQ SEQUENCE 250 AA; 27316 MW; FC749D6B91985763 CRC64;
MTDILIDDTA TEAVRTLIRA FPLVPVSQPP EQGSYLLAEH DTVSLRLVGE KSNVIVDFTS
GAAQYRRTKG GGELIAKAVN HTAHPTVWDA TAGLGRDSFV LASLGLTVTA FEQHPAVACL
LSDGIRRALL NPETQDTAAR INLHFGNAAE QMPALVKTQG KPDIVYLDPM YPERRKSAAV
KKEMAYFHRL VGEAQDEVVL LHTARQTAKK RVVVKRPRLG EHLAGQAPAY QYTGKSTRFD
VYLPYGADKG
