位置:首页 > 蛋白库 > RLMH_PORG3
RLMH_PORG3
ID   RLMH_PORG3              Reviewed;         157 AA.
AC   B2RH13;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 68.
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=PGN_0139;
OS   Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM
OS   12257 / NCTC 11834 / 2561).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=431947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561;
RX   PubMed=18524787; DOI=10.1093/dnares/dsn013;
RA   Naito M., Hirakawa H., Yamashita A., Ohara N., Shoji M., Yukitake H.,
RA   Nakayama K., Toh H., Yoshimura F., Kuhara S., Hattori M., Hayashi T.,
RA   Nakayama K.;
RT   "Determination of the genome sequence of Porphyromonas gingivalis strain
RT   ATCC 33277 and genomic comparison with strain W83 revealed extensive genome
RT   rearrangements in P. gingivalis.";
RL   DNA Res. 15:215-225(2008).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP009380; BAG32658.1; -; Genomic_DNA.
DR   RefSeq; WP_012457274.1; NZ_CP025930.1.
DR   AlphaFoldDB; B2RH13; -.
DR   SMR; B2RH13; -.
DR   STRING; 431947.PGN_0139; -.
DR   EnsemblBacteria; BAG32658; BAG32658; PGN_0139.
DR   GeneID; 29255391; -.
DR   KEGG; pgn:PGN_0139; -.
DR   eggNOG; COG1576; Bacteria.
DR   HOGENOM; CLU_100552_2_0_10; -.
DR   OMA; NEPYHHQ; -.
DR   BioCyc; PGIN431947:G1G2V-158-MON; -.
DR   Proteomes; UP000008842; 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.
PE   3: Inferred from homology;
KW   Cytoplasm; Methyltransferase; rRNA processing; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..157
FT                   /note="Ribosomal RNA large subunit methyltransferase H"
FT                   /id="PRO_0000366636"
FT   BINDING         73
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00658"
FT   BINDING         105
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00658"
FT   BINDING         124..129
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00658"
SQ   SEQUENCE   157 AA;  18091 MW;  747FC283222D7C70 CRC64;
     MKIVLLVVGK TDSKLMAQAT EEYIRRLSHY VSFEVEVIPD VRLGSKLSSE QQKDAEGREI
     LARLRPSDST VLLDERGREY SSMEFSAFLQ KKMLTGTRRM VFVIGGPYGF SPAVQEAVAD
     RISLSRMTFS HQMIRLFFTE QVYRAMTILN HEPYHHE
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024