ID A0A0S4LD43_9BACT Unreviewed; 310 AA.
AC A0A0S4LD43;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
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:CUS34777.1};
GN Synonyms=rsmH {ECO:0000256|HAMAP-Rule:MF_01007};
GN ORFNames=COMA2_190009 {ECO:0000313|EMBL:CUS34777.1};
OS Candidatus Nitrospira nitrificans.
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Nitrospira.
OX NCBI_TaxID=1742973 {ECO:0000313|EMBL:CUS34777.1, ECO:0000313|Proteomes:UP000198736};
RN [1] {ECO:0000313|Proteomes:UP000198736}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Luecker S., Luecker S.;
RL Submitted (OCT-2015) 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}.
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DR EMBL; CZPZ01000011; CUS34777.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S4LD43; -.
DR STRING; 1742973.COMA2_190009; -.
DR OrthoDB; 9806637at2; -.
DR Proteomes; UP000198736; 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 CDD; cd02440; AdoMet_MTases; 1.
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}; Reference proteome {ECO:0000313|Proteomes:UP000198736};
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 285..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 39..41
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01007"
FT BINDING 59
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01007"
FT BINDING 86
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"
FT BINDING 114
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01007"
SQ SEQUENCE 310 AA; 34358 MW; 481F674222A35754 CRC64;
MGESIVDENL HISVLGREVC SWLISERPTT IVDCTVGYGG HAEILLTSSP VGTRVIGLDR
DSQAIEFSQR RLSRFGDRIV LRQGNYRDLK SHLAEAGIAK VDGVLFDFGV SSPQLDDPSR
GFSFQREGPL DMRMDQTVGK TAADLVNRSP EDELADIIFQ YGEERYARRI ARAIVQERQR
HPVETTGVLA SVITRSVPAS YRHGRIHCAT RTFQALRIVV NQELDFLESS LRDATEVLAV
GGKVCAIAFH SLEDRIVKHT FRSLAQGPEA TLSILTKKPV LPSRAECGAN PRSRSAKLRV
AERQPRMGPL
//