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RSMH_NOSP7
ID   RSMH_NOSP7              Reviewed;         298 AA.
AC   B2J183;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 75.
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=Npun_R4969;
OS   Nostoc punctiforme (strain ATCC 29133 / PCC 73102).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=63737;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29133 / PCC 73102;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Meeks J.C., Elhai J.,
RA   Campbell E.L., Thiel T., Longmire J., Potts M., Atlas R.;
RT   "Complete sequence of chromosome of Nostoc punctiforme ATCC 29133.";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001037; ACC83314.1; -; Genomic_DNA.
DR   RefSeq; WP_012411269.1; NC_010628.1.
DR   AlphaFoldDB; B2J183; -.
DR   SMR; B2J183; -.
DR   STRING; 63737.Npun_R4969; -.
DR   EnsemblBacteria; ACC83314; ACC83314; Npun_R4969.
DR   KEGG; npu:Npun_R4969; -.
DR   eggNOG; COG0275; Bacteria.
DR   HOGENOM; CLU_038422_3_0_3; -.
DR   OMA; NPAKRTF; -.
DR   OrthoDB; 1272633at2; -.
DR   PhylomeDB; B2J183; -.
DR   Proteomes; UP000001191; 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   3: Inferred from homology;
KW   Cytoplasm; Methyltransferase; Reference proteome; rRNA processing;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..298
FT                   /note="Ribosomal RNA small subunit methyltransferase H"
FT                   /id="PRO_0000387012"
FT   BINDING         46..48
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01007"
FT   BINDING         65
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01007"
FT   BINDING         92
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01007"
FT   BINDING         108
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01007"
FT   BINDING         115
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01007"
SQ   SEQUENCE   298 AA;  33299 MW;  7967FB198C44AEE6 CRC64;
     MKSDLETPLN LEELAFSHIS VLGREVIEGL AVRPGGHYLD VTVGGGGHSR LILEAAADVR
     VTAVDQDEDA LVAANKNLAE YSDRIQFIYS NFADYEFPPN TFDGILADLG VSSYHLDQAE
     RGFSFRQAAN LDMRMDRGRS LTAADVINNW DEAELADIFF KYGEERLSRR IARRIVERRP
     LHTTTELADA IASSVPPKYR YGRIHPATRV FQALRIVVND ELKSLETFLD KAPNALVPGG
     RIAIISFHSL EDRPVKHGLR NSPLLKVLTK KPIIAQEEEI SNNPRSRSAK LRIAEKLV
 
 
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