RSMH_THET8
ID RSMH_THET8 Reviewed; 285 AA.
AC Q5SJD8;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Ribosomal RNA small subunit methyltransferase H {ECO:0000255|HAMAP-Rule:MF_01007};
DE EC=2.1.1.199 {ECO:0000255|HAMAP-Rule:MF_01007};
DE AltName: Full=16S rRNA m(4)C1402 methyltransferase {ECO:0000255|HAMAP-Rule:MF_01007};
DE AltName: Full=rRNA (cytosine-N(4)-)-methyltransferase RsmH {ECO:0000255|HAMAP-Rule:MF_01007};
GN Name=rsmH {ECO:0000255|HAMAP-Rule:MF_01007}; Synonyms=mraW;
GN OrderedLocusNames=TTHA1076;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH
RP S-ADENOSYL-L-METHIONINE.
RA Kishishita S., Murayama K., Shirouzu M., Yokoyama S.;
RT "Crystal structure of a predicted S-adenosylmethionine-dependent
RT methyltransferase TT1512 from Thermus thermophilus HB8 at 2.0 Ang.
RT resolution.";
RL Submitted (NOV-2004) to the PDB data bank.
CC -!- FUNCTION: Specifically methylates the N4 position of cytidine in
CC position 1402 (C1402) of 16S rRNA. {ECO:0000255|HAMAP-Rule:MF_01007}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = H(+) +
CC N(4)-methylcytidine(1402) in 16S rRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42928, Rhea:RHEA-COMP:10286, Rhea:RHEA-COMP:10287,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74506, ChEBI:CHEBI:82748; EC=2.1.1.199;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01007};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01007}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RsmH family.
CC {ECO:0000255|HAMAP-Rule:MF_01007}.
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; AP008226; BAD70899.1; -; Genomic_DNA.
DR RefSeq; WP_011228422.1; NC_006461.1.
DR RefSeq; YP_144342.1; NC_006461.1.
DR PDB; 1WG8; X-ray; 2.00 A; A/B=1-285.
DR PDBsum; 1WG8; -.
DR AlphaFoldDB; Q5SJD8; -.
DR SMR; Q5SJD8; -.
DR STRING; 300852.55772458; -.
DR EnsemblBacteria; BAD70899; BAD70899; BAD70899.
DR GeneID; 3168225; -.
DR KEGG; ttj:TTHA1076; -.
DR PATRIC; fig|300852.9.peg.1056; -.
DR eggNOG; COG0275; Bacteria.
DR HOGENOM; CLU_038422_2_0_0; -.
DR OMA; NPAKRTF; -.
DR PhylomeDB; Q5SJD8; -.
DR EvolutionaryTrace; Q5SJD8; -.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0071424; F:rRNA (cytosine-N4-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0070475; P:rRNA base methylation; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.150.170; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_01007; 16SrRNA_methyltr_H; 1.
DR InterPro; IPR002903; RsmH.
DR InterPro; IPR023397; SAM-dep_MeTrfase_MraW_recog.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR11265; PTHR11265; 1.
DR Pfam; PF01795; Methyltransf_5; 1.
DR PIRSF; PIRSF004486; MraW; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF81799; SSF81799; 1.
DR TIGRFAMs; TIGR00006; TIGR00006; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Methyltransferase; Reference proteome;
KW rRNA processing; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..285
FT /note="Ribosomal RNA small subunit methyltransferase H"
FT /id="PRO_0000108734"
FT REGION 259..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..285
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 34..36
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT BINDING 51
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01007,
FT ECO:0000269|Ref.2"
FT BINDING 75
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01007,
FT ECO:0000269|Ref.2"
FT BINDING 96
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01007,
FT ECO:0000269|Ref.2"
FT BINDING 103
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01007,
FT ECO:0000269|Ref.2"
FT HELIX 11..18
FT /evidence="ECO:0007829|PDB:1WG8"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:1WG8"
FT HELIX 35..42
FT /evidence="ECO:0007829|PDB:1WG8"
FT STRAND 46..52
FT /evidence="ECO:0007829|PDB:1WG8"
FT HELIX 54..62
FT /evidence="ECO:0007829|PDB:1WG8"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:1WG8"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:1WG8"
FT HELIX 78..84
FT /evidence="ECO:0007829|PDB:1WG8"
FT STRAND 90..96
FT /evidence="ECO:0007829|PDB:1WG8"
FT HELIX 101..105
FT /evidence="ECO:0007829|PDB:1WG8"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:1WG8"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:1WG8"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:1WG8"
FT HELIX 130..136
FT /evidence="ECO:0007829|PDB:1WG8"
FT HELIX 139..150
FT /evidence="ECO:0007829|PDB:1WG8"
FT HELIX 155..168
FT /evidence="ECO:0007829|PDB:1WG8"
FT HELIX 174..185
FT /evidence="ECO:0007829|PDB:1WG8"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:1WG8"
FT HELIX 195..205
FT /evidence="ECO:0007829|PDB:1WG8"
FT HELIX 208..222
FT /evidence="ECO:0007829|PDB:1WG8"
FT STRAND 223..233
FT /evidence="ECO:0007829|PDB:1WG8"
FT HELIX 236..249
FT /evidence="ECO:0007829|PDB:1WG8"
FT STRAND 251..254
FT /evidence="ECO:0007829|PDB:1WG8"
FT HELIX 263..268
FT /evidence="ECO:0007829|PDB:1WG8"
FT HELIX 270..274
FT /evidence="ECO:0007829|PDB:1WG8"
FT STRAND 276..281
FT /evidence="ECO:0007829|PDB:1WG8"
SQ SEQUENCE 285 AA; 31171 MW; E1EE6E83A286ABB7 CRC64;
MRPMTHVPVL YQEALDLLAV RPGGVYVDAT LGGAGHARGI LERGGRVIGL DQDPEAVARA
KGLHLPGLTV VQGNFRHLKR HLAALGVERV DGILADLGVS SFHLDDPSRG FSYQKEGPLD
MRMGLEGPTA KEVVNRLPLE ALARLLRELG EEPQAYRIAR AIVAAREKAP IETTTQLAEI
VRKAVGFRRA GHPARKTFQA LRIYVNDELN ALKEFLEQAA EVLAPGGRLV VIAFHSLEDR
VVKRFLRESG LKVLTKKPLV PSEKEAAQNP RARSAKLRAA EKEAP
