ID D1Y635_9BACT Unreviewed; 313 AA.
AC D1Y635;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE RecName: Full=Ribosomal RNA small subunit methyltransferase H {ECO:0000256|HAMAP-Rule:MF_01007};
DE EC=2.1.1.199 {ECO:0000256|HAMAP-Rule:MF_01007};
DE AltName: Full=16S rRNA m(4)C1402 methyltransferase {ECO:0000256|HAMAP-Rule:MF_01007};
DE AltName: Full=rRNA (cytosine-N(4)-)-methyltransferase RsmH {ECO:0000256|HAMAP-Rule:MF_01007};
GN Name=mraW {ECO:0000313|EMBL:EFB90229.1};
GN Synonyms=rsmH {ECO:0000256|HAMAP-Rule:MF_01007};
GN ORFNames=HMPREF7215_2701 {ECO:0000313|EMBL:EFB90229.1};
OS Pyramidobacter piscolens W5455.
OC Bacteria; Synergistota; Synergistia; Synergistales;
OC Dethiosulfovibrionaceae; Pyramidobacter.
OX NCBI_TaxID=352165 {ECO:0000313|EMBL:EFB90229.1, ECO:0000313|Proteomes:UP000006462};
RN [1] {ECO:0000313|EMBL:EFB90229.1, ECO:0000313|Proteomes:UP000006462}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W5455 {ECO:0000313|EMBL:EFB90229.1,
RC ECO:0000313|Proteomes:UP000006462};
RA Shrivastava S., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Strausberg R.L., Nelson K.E.;
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Specifically methylates the N4 position of cytidine in
CC position 1402 (C1402) of 16S rRNA. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01007};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01007}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RsmH family.
CC {ECO:0000256|ARBA:ARBA00010396, ECO:0000256|HAMAP-Rule:MF_01007}.
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:EFB90229.1}.
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DR EMBL; ADFP01000090; EFB90229.1; -; Genomic_DNA.
DR RefSeq; WP_009165316.1; NZ_ADFP01000090.1.
DR AlphaFoldDB; D1Y635; -.
DR STRING; 352165.HMPREF7215_2701; -.
DR eggNOG; COG0275; Bacteria.
DR Proteomes; UP000006462; Unassembled WGS sequence.
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; Putative methyltransferase TM0872, insert domain; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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 NCBIfam; TIGR00006; 16S rRNA (cytosine(1402)-N(4))-methyltransferase RsmH; 1.
DR PANTHER; PTHR11265:SF0; 12S RRNA N4-METHYLCYTIDINE METHYLTRANSFERASE; 1.
DR PANTHER; PTHR11265; S-ADENOSYL-METHYLTRANSFERASE MRAW; 1.
DR Pfam; PF01795; Methyltransf_5; 1.
DR PIRSF; PIRSF004486; MraW; 1.
DR SUPFAM; SSF81799; Putative methyltransferase TM0872, insert domain; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01007};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_01007};
KW rRNA processing {ECO:0000256|ARBA:ARBA00022552, ECO:0000256|HAMAP-
KW Rule:MF_01007};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_01007};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01007}.
FT REGION 267..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..288
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 33..35
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01007"
FT BINDING 52
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01007"
FT BINDING 79
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01007"
FT BINDING 100
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01007"
FT BINDING 107
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01007"
SQ SEQUENCE 313 AA; 35214 MW; E8EA6BEB69E375D1 CRC64;
MEFEHVPVLL AKVVESMDLK ADALIVDGTL GLGGYSEAFL KRSPRWRVVG IDRDERARNI
ACQRLAPFGE RFLALDGDFR NIGGLCASVG IRAVDCVVLD LGVSNMQLAD GRRGFSFRED
GPLDMRMNPA EGTRSASELV NELPRESLAD IFRKYGEERF AWSIAGEIVK ERLKRPITST
AELVEVIRRG IPAPVMRKMN GHPARKVFQA LRVAVNDELG ALEQGLDEAF SLLAEEGRLL
VVTYHSLEDR IVKRRFREWN EEGKGVLEPR KGQVPDDEEV ERNPKSRSAR LRGFLKKNVP
NKAEGRIGPW RRV
//
