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Database: UniProt
Entry: A0A0C9N860_SPHPI
LinkDB: A0A0C9N860_SPHPI
Original site: A0A0C9N860_SPHPI 
ID   A0A0C9N860_SPHPI        Unreviewed;       326 AA.
AC   A0A0C9N860;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
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=rsmH {ECO:0000256|HAMAP-Rule:MF_01007,
GN   ECO:0000313|EMBL:GAN12282.1};
GN   ORFNames=SP6_07_00680 {ECO:0000313|EMBL:GAN12282.1};
OS   Sphingomonas paucimobilis NBRC 13935.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1219050 {ECO:0000313|EMBL:GAN12282.1, ECO:0000313|Proteomes:UP000032025};
RN   [1] {ECO:0000313|EMBL:GAN12282.1, ECO:0000313|Proteomes:UP000032025}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 13935 {ECO:0000313|EMBL:GAN12282.1,
RC   ECO:0000313|Proteomes:UP000032025};
RA   Hosoyama A., Hashimoto M., Hosoyama Y., Noguchi M., Uohara A., Ohji S.,
RA   Katano-Makiyama Y., Ichikawa N., Kimura A., Yamazoe A., Fujita N.;
RT   "Whole genome shotgun sequence of Sphingomonas paucimobilis NBRC 13935.";
RL   Submitted (AUG-2014) 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:GAN12282.1}.
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DR   EMBL; BBJS01000007; GAN12282.1; -; Genomic_DNA.
DR   RefSeq; WP_007405422.1; NZ_BBJS01000007.1.
DR   AlphaFoldDB; A0A0C9N860; -.
DR   GeneID; 78526545; -.
DR   Proteomes; UP000032025; 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};
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          306..326
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         38..40
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01007"
FT   BINDING         55
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01007"
FT   BINDING         81
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01007"
FT   BINDING         98
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01007"
FT   BINDING         105
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01007"
SQ   SEQUENCE   326 AA;  34790 MW;  C36D9CF1E036D3C0 CRC64;
     MSPAVNDAPH IPVLLDEVLD ALAILPGETH VDGTFGAGGY TRAMLGRGAK VIAFDRDPDA
     IANGQALIQA EPGLALVHRE FSGLDQALEA QVDGVVLDIG VSSMQLDQAE RGFSFQGDGP
     LDMRMAQAGE SAADFLNTAD EAAIADVLYH YGEEPRSRRV AQAIVAARPL MRTGELAAVV
     RRALGYRPHD KKDPATRTFQ AIRIHVNREL EELAEGLAAA ERALKPGGRL AIVTFHSLED
     RMVKRFFRER AGQLPGGSRH LPQQVAAQAP SFTAVGKAVR AGAAELARNP RARSATLRFA
     TRTESPAWSA GQGWAPGGEL TQELGV
//
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