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RLMH_ALCBS
ID   RLMH_ALCBS              Reviewed;         160 AA.
AC   Q0VN46;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Ribosomal RNA large subunit methyltransferase H {ECO:0000255|HAMAP-Rule:MF_00658};
DE            EC=2.1.1.177 {ECO:0000255|HAMAP-Rule:MF_00658};
DE   AltName: Full=23S rRNA (pseudouridine1915-N3)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_00658};
DE   AltName: Full=23S rRNA m3Psi1915 methyltransferase {ECO:0000255|HAMAP-Rule:MF_00658};
DE   AltName: Full=rRNA (pseudouridine-N3-)-methyltransferase RlmH {ECO:0000255|HAMAP-Rule:MF_00658};
GN   Name=rlmH {ECO:0000255|HAMAP-Rule:MF_00658}; OrderedLocusNames=ABO_1954;
OS   Alcanivorax borkumensis (strain ATCC 700651 / DSM 11573 / NCIMB 13689 /
OS   SK2).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700651 / DSM 11573 / NCIMB 13689 / SK2;
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., Brecht M.,
RA   Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., Gertler C.,
RA   Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., Lang S., Linke B.,
RA   McHardy A.C., Meyer F., Nechitaylo T., Puehler A., Regenhardt D., Rupp O.,
RA   Sabirova J.S., Selbitschka W., Yakimov M.M., Timmis K.N., Vorhoelter F.-J.,
RA   Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine bacterium
RT   Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(2006).
CC   -!- FUNCTION: Specifically methylates the pseudouridine at position 1915
CC       (m3Psi1915) in 23S rRNA. {ECO:0000255|HAMAP-Rule:MF_00658}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=pseudouridine(1915) in 23S rRNA + S-adenosyl-L-methionine =
CC         H(+) + N(3)-methylpseudouridine(1915) in 23S rRNA + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:42752, Rhea:RHEA-COMP:10221, Rhea:RHEA-
CC         COMP:10222, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:65314, ChEBI:CHEBI:74486; EC=2.1.1.177;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00658};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00658}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00658}.
CC   -!- SIMILARITY: Belongs to the RNA methyltransferase RlmH family.
CC       {ECO:0000255|HAMAP-Rule:MF_00658}.
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DR   EMBL; AM286690; CAL17402.1; -; Genomic_DNA.
DR   RefSeq; WP_011589233.1; NC_008260.1.
DR   AlphaFoldDB; Q0VN46; -.
DR   SMR; Q0VN46; -.
DR   STRING; 393595.ABO_1954; -.
DR   EnsemblBacteria; CAL17402; CAL17402; ABO_1954.
DR   KEGG; abo:ABO_1954; -.
DR   eggNOG; COG1576; Bacteria.
DR   HOGENOM; CLU_100552_1_0_6; -.
DR   OMA; ARADQRW; -.
DR   OrthoDB; 1783583at2; -.
DR   Proteomes; UP000008871; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0070038; F:rRNA (pseudouridine-N3-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd18081; RlmH-like; 1.
DR   Gene3D; 3.40.1280.10; -; 1.
DR   HAMAP; MF_00658; 23SrRNA_methyltr_H; 1.
DR   InterPro; IPR029028; Alpha/beta_knot_MTases.
DR   InterPro; IPR003742; RlmH-like.
DR   InterPro; IPR029026; tRNA_m1G_MTases_N.
DR   PANTHER; PTHR33603; PTHR33603; 1.
DR   Pfam; PF02590; SPOUT_MTase; 1.
DR   PIRSF; PIRSF004505; MT_bac; 1.
DR   SUPFAM; SSF75217; SSF75217; 1.
DR   TIGRFAMs; TIGR00246; tRNA_RlmH_YbeA; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Methyltransferase; Reference proteome; rRNA processing;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..160
FT                   /note="Ribosomal RNA large subunit methyltransferase H"
FT                   /id="PRO_0000260533"
FT   BINDING         78
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00658"
FT   BINDING         109
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00658"
FT   BINDING         128..133
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00658"
SQ   SEQUENCE   160 AA;  17757 MW;  4AA821100FC471E5 CRC64;
     MHLVLLAIGT RMPAWVTEGF NEYQKRMPPD MRLTLEEIPM PKRGKGDAGS QIRAEADALR
     KRLETIVKKS PGAKTVALEV NGRALDTHAL SRKLGELKDV GQDLVLLVGG PDGLCPELSA
     SAHERWSLSN LTLPHPLVRV LLAEQLYRGW TLLTGHPYHR
 
 
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