RSMH_THEMA
ID RSMH_THEMA Reviewed; 299 AA.
AC Q9WZX6;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 141.
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=TM_0872;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEXES WITH
RP S-ADENOSYL-L-METHIONINE AND S-ADENOSYL-L-HOMOCYSTEINE.
RX PubMed=12824489; DOI=10.1110/ps.0302403;
RA Miller D.J., Ouellette N., Evdokimova E., Savchenko A., Edwards A.,
RA Anderson W.F.;
RT "Crystal complexes of a predicted S-adenosylmethionine-dependent
RT methyltransferase reveal a typical AdoMet binding domain and a substrate
RT recognition domain.";
RL Protein Sci. 12:1432-1442(2003).
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}.
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DR EMBL; AE000512; AAD35954.1; -; Genomic_DNA.
DR PIR; C72323; C72323.
DR RefSeq; NP_228681.1; NC_000853.1.
DR RefSeq; WP_004080729.1; NZ_CP011107.1.
DR PDB; 1M6Y; X-ray; 1.90 A; A/B=1-299.
DR PDB; 1N2X; X-ray; 1.90 A; A/B=1-299.
DR PDBsum; 1M6Y; -.
DR PDBsum; 1N2X; -.
DR AlphaFoldDB; Q9WZX6; -.
DR SMR; Q9WZX6; -.
DR STRING; 243274.THEMA_00275; -.
DR DrugBank; DB01752; S-adenosyl-L-homocysteine.
DR EnsemblBacteria; AAD35954; AAD35954; TM_0872.
DR KEGG; tma:TM0872; -.
DR eggNOG; COG0275; Bacteria.
DR InParanoid; Q9WZX6; -.
DR OMA; NPAKRTF; -.
DR OrthoDB; 1272633at2; -.
DR EvolutionaryTrace; Q9WZX6; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0071424; F:rRNA (cytosine-N4-)-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0070475; P:rRNA base methylation; IBA:GO_Central.
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..299
FT /note="Ribosomal RNA small subunit methyltransferase H"
FT /id="PRO_0000108732"
FT REGION 269..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 36..38
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:12824489"
FT BINDING 55
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:12824489"
FT BINDING 82
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:12824489"
FT BINDING 103
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:12824489"
FT BINDING 110
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:12824489"
FT HELIX 13..20
FT /evidence="ECO:0007829|PDB:1M6Y"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:1M6Y"
FT HELIX 37..45
FT /evidence="ECO:0007829|PDB:1M6Y"
FT STRAND 50..56
FT /evidence="ECO:0007829|PDB:1M6Y"
FT HELIX 58..67
FT /evidence="ECO:0007829|PDB:1M6Y"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:1M6Y"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:1M6Y"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:1M6Y"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:1M6Y"
FT HELIX 85..91
FT /evidence="ECO:0007829|PDB:1M6Y"
FT STRAND 97..103
FT /evidence="ECO:0007829|PDB:1M6Y"
FT HELIX 108..112
FT /evidence="ECO:0007829|PDB:1M6Y"
FT STRAND 118..122
FT /evidence="ECO:0007829|PDB:1M6Y"
FT HELIX 138..144
FT /evidence="ECO:0007829|PDB:1M6Y"
FT HELIX 147..156
FT /evidence="ECO:0007829|PDB:1M6Y"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:1M6Y"
FT HELIX 164..173
FT /evidence="ECO:0007829|PDB:1M6Y"
FT HELIX 180..190
FT /evidence="ECO:0007829|PDB:1M6Y"
FT HELIX 193..198
FT /evidence="ECO:0007829|PDB:1M6Y"
FT HELIX 205..216
FT /evidence="ECO:0007829|PDB:1M6Y"
FT HELIX 218..228
FT /evidence="ECO:0007829|PDB:1M6Y"
FT HELIX 229..232
FT /evidence="ECO:0007829|PDB:1M6Y"
FT STRAND 233..245
FT /evidence="ECO:0007829|PDB:1M6Y"
FT HELIX 246..258
FT /evidence="ECO:0007829|PDB:1M6Y"
FT STRAND 260..265
FT /evidence="ECO:0007829|PDB:1M6Y"
FT HELIX 274..279
FT /evidence="ECO:0007829|PDB:1M6Y"
FT HELIX 281..283
FT /evidence="ECO:0007829|PDB:1M6Y"
FT STRAND 287..293
FT /evidence="ECO:0007829|PDB:1M6Y"
SQ SEQUENCE 299 AA; 34893 MW; 790BBC2F3BB271F7 CRC64;
MRKYSQRHIP VMVREVIEFL KPEDEKIILD CTVGEGGHSR AILEHCPGCR IIGIDVDSEV
LRIAEEKLKE FSDRVSLFKV SYREADFLLK TLGIEKVDGI LMDLGVSTYQ LKGENRGFTF
EREEPLDMRM DLESEVTAQK VLNELPEEEL ARIIFEYGEE KRFARRIARK IVENRPLNTT
LDLVKAVREA LPSYEIRRRK RHFATKTFQA IRIYVNRELE NLKEFLKKAE DLLNPGGRIV
VISFHSLEDR IVKETFRNSK KLRILTEKPV RPSEEEIREN PRARSGRLRA AERIEEGGD
