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Database: UniProt
Entry: A0A1B8J9X6_9HELI
LinkDB: A0A1B8J9X6_9HELI
Original site: A0A1B8J9X6_9HELI 
ID   A0A1B8J9X6_9HELI        Unreviewed;       330 AA.
AC   A0A1B8J9X6;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
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   ORFNames=BA723_04330 {ECO:0000313|EMBL:OBV29731.1}, BKN38_06455
GN   {ECO:0000313|EMBL:OHU82845.1};
OS   Helicobacter sp. CLO-3.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=211 {ECO:0000313|EMBL:OBV29731.1, ECO:0000313|Proteomes:UP000092701};
RN   [1] {ECO:0000313|EMBL:OBV29731.1, ECO:0000313|Proteomes:UP000092701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HMC1 {ECO:0000313|EMBL:OBV29731.1,
RC   ECO:0000313|Proteomes:UP000092701};
RA   Greninger A.L., Bateman A., Jerome K., Fang F.;
RT   "Genome sequence of Helicobacter sp. CLO-3.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:OHU82845.1, ECO:0000313|Proteomes:UP000179541}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLO-3 {ECO:0000313|EMBL:OHU82845.1,
RC   ECO:0000313|Proteomes:UP000179541};
RA   Greninger A.L., Bateman A.C., Fang F., Jerome K.;
RT   "Genome sequence of Helicobacter sp. CLO-3 Fennel-37 strain.";
RL   Submitted (OCT-2016) 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:OBV29731.1}.
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DR   EMBL; MAMQ01000046; OBV29731.1; -; Genomic_DNA.
DR   EMBL; MLQN01000020; OHU82845.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B8J9X6; -.
DR   STRING; 211.BKN38_06455; -.
DR   OrthoDB; 9806637at2; -.
DR   Proteomes; UP000092701; Unassembled WGS sequence.
DR   Proteomes; UP000179541; 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}; Reference proteome {ECO:0000313|Proteomes:UP000092701};
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   BINDING         46..48
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01007"
FT   BINDING         65
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01007"
FT   BINDING         92
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01007"
FT   BINDING         116
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01007"
FT   BINDING         123
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01007"
SQ   SEQUENCE   330 AA;  36668 MW;  47241C04E9DEB482 CRC64;
     MQSELIAQDK PATQGEPPAQ NELFAQNKPL AQKPQKLFID CTLGLGGHSG ALLKAHSDIA
     LIGIDQDEFA LNIARENLAL YASRARFIHA NFAQGLVQAL EIAQNERLKI AGVLADIGVS
     SLQLDDASRG FGFSSERLDM RMDTRASRTA SDILRDYSEF ELAGIFRDYG EIKEHKKMAR
     LTKEYMQTHK GGFSSAREFS DFLAKHFKSS RIHPATLAFQ ALRIEVNDEL GVLKSLLDTL
     ESTYKSHPNL LSGAIVAIIS FHSLEDRIIK ERFKEWSRAC ICPASAYRCE CGGDNAKGAM
     LTKKPIIASE AEIRKNPRAR SAKLRAFRLK
//
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