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RLMH_STAAU
ID   RLMH_STAAU              Reviewed;         159 AA.
AC   P0C1V0; P0A0N8; Q9WVW7;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 83.
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};
OS   Staphylococcus aureus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=HUC19;
RX   PubMed=10858352; DOI=10.1128/aac.44.7.1906-1910.2000;
RA   Oliveira D.C., Wu S.W., de Lencastre H.;
RT   "Genetic organization of the downstream region of the mecA element in
RT   methicillin-resistant Staphylococcus aureus isolates carrying different
RT   polymorphisms of this region.";
RL   Antimicrob. Agents Chemother. 44:1906-1910(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=85/2082, 85/3907,
RC   ATCC 25923 / DSM 1104 / JCM 2413 / NBRC 14462 / NCIMB 12702 / NCTC 12981 /
RC   Seattle 1945, and NCTC 10442;
RX   PubMed=11302791; DOI=10.1128/aac.45.5.1323-1336.2001;
RA   Ito T., Katayama Y., Asada K., Mori N., Tsutsumimoto K.;
RT   "Structural comparison of three types of staphylococcal cassette chromosome
RT   mec integrated in the chromosome in methicillin-resistant Staphylococcus
RT   aureus.";
RL   Antimicrob. Agents Chemother. 45:1323-1336(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CA05(JCSC1968), and JCSC1978(8/6-3P);
RX   PubMed=11897611; DOI=10.1128/aac.46.4.1147-1152.2002;
RA   Ma X.X., Ito T., Tiensasitorn C., Jamklang M., Chongtrakool P.,
RA   Boyle-Vavra S., Daum R.S., Hiramatsu K.;
RT   "Novel type of staphylococcal cassette chromosome mec identified in
RT   community-acquired methicillin-resistant Staphylococcus aureus strains.";
RL   Antimicrob. Agents Chemother. 46:1147-1152(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MR108;
RX   PubMed=12654286; DOI=10.1016/s1368-7646(03)00003-7;
RA   Ito T., Okuma K., Ma X.X., Yuzawa H., Hiramatsu K.;
RT   "Insights on antibiotic resistance of Staphylococcus aureus from its whole
RT   genome: genomic island SCC.";
RL   Drug Resist. Updat. 6:41-52(2003).
RN   [5] {ECO:0007744|PDB:1VH0}
RP   X-RAY CRYSTALLOGRAPHY (2.31 ANGSTROMS) OF 2-159.
RX   PubMed=16021622; DOI=10.1002/prot.20541;
RA   Badger J., Sauder J.M., Adams J.M., Antonysamy S., Bain K., Bergseid M.G.,
RA   Buchanan S.G., Buchanan M.D., Batiyenko Y., Christopher J.A., Emtage S.,
RA   Eroshkina A., Feil I., Furlong E.B., Gajiwala K.S., Gao X., He D.,
RA   Hendle J., Huber A., Hoda K., Kearins P., Kissinger C., Laubert B.,
RA   Lewis H.A., Lin J., Loomis K., Lorimer D., Louie G., Maletic M.,
RA   Marsh C.D., Miller I., Molinari J., Muller-Dieckmann H.J., Newman J.M.,
RA   Noland B.W., Pagarigan B., Park F., Peat T.S., Post K.W., Radojicic S.,
RA   Ramos A., Romero R., Rutter M.E., Sanderson W.E., Schwinn K.D., Tresser J.,
RA   Winhoven J., Wright T.A., Wu L., Xu J., Harris T.J.R.;
RT   "Structural analysis of a set of proteins resulting from a bacterial
RT   genomics project.";
RL   Proteins 60:787-796(2005).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.31 ANGSTROMS) OF 2-159.
RX   PubMed=16460560; DOI=10.1186/1471-2105-7-53;
RA   von Grotthuss M., Plewczynski D., Ginalski K., Rychlewski L.,
RA   Shakhnovich E.I.;
RT   "PDB-UF: database of predicted enzymatic functions for unannotated protein
RT   structures from structural genomics.";
RL   BMC Bioinformatics 7:53-53(2006).
RN   [7] {ECO:0007744|PDB:4FAK}
RP   X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH
RP   S-ADENOSYL-L-METHIONINE, FUNCTION AS A METHYLTRANSFERASE, SUBUNIT, AND
RP   MUTAGENESIS OF GLU-77.
RX   PubMed=23150671; DOI=10.1074/jbc.m112.385138;
RA   Boundy S., Safo M.K., Wang L., Musayev F.N., O'Farrell H.C., Rife J.P.,
RA   Archer G.L.;
RT   "Characterization of the Staphylococcus aureus rRNA methyltransferase
RT   encoded by orfX, the gene containing the staphylococcal chromosome cassette
RT   mec (SCCmec) insertion site.";
RL   J. Biol. Chem. 288:132-140(2013).
CC   -!- FUNCTION: Specifically methylates the pseudouridine at position 1915
CC       (m3Psi1915) in 23S rRNA (By similarity). Specific for fully assembled
CC       70S ribosomes (PubMed:23150671). {ECO:0000255|HAMAP-Rule:MF_00658,
CC       ECO:0000269|PubMed:23150671}.
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       ECO:0000269|PubMed:23150671}.
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; AF181950; AAF85653.1; -; Genomic_DNA.
DR   EMBL; D86934; BAA82243.1; -; Genomic_DNA.
DR   EMBL; AB033763; BAA86653.1; -; Genomic_DNA.
DR   EMBL; AB037671; BAB47681.1; -; Genomic_DNA.
DR   EMBL; AB038513; BAC53844.1; -; Genomic_DNA.
DR   EMBL; AB047089; BAC57492.1; -; Genomic_DNA.
DR   EMBL; AB047239; BAB47141.1; -; Genomic_DNA.
DR   EMBL; AB063172; BAB72121.1; -; Genomic_DNA.
DR   EMBL; AB063173; BAB72138.1; -; Genomic_DNA.
DR   EMBL; AB096217; BAC67575.1; -; Genomic_DNA.
DR   RefSeq; WP_000704775.1; NZ_WYDB01000001.1.
DR   PDB; 1VH0; X-ray; 2.31 A; A/B/C/D/E/F=2-159.
DR   PDB; 4FAK; X-ray; 1.70 A; A=1-159.
DR   PDBsum; 1VH0; -.
DR   PDBsum; 4FAK; -.
DR   AlphaFoldDB; P0C1V0; -.
DR   SMR; P0C1V0; -.
DR   GeneID; 66838363; -.
DR   OMA; NEPYHHQ; -.
DR   EvolutionaryTrace; P0C1V0; -.
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   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Methyltransferase; rRNA processing;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..159
FT                   /note="Ribosomal RNA large subunit methyltransferase H"
FT                   /id="PRO_0000198181"
FT   BINDING         76
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00658,
FT                   ECO:0000269|PubMed:23150671, ECO:0007744|PDB:4FAK"
FT   BINDING         108
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00658,
FT                   ECO:0000269|PubMed:23150671, ECO:0007744|PDB:4FAK"
FT   BINDING         127..132
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00658,
FT                   ECO:0000269|PubMed:23150671, ECO:0007744|PDB:4FAK"
FT   MUTAGEN         77
FT                   /note="E->A: 30% decrease in methyltransferase activity."
FT                   /evidence="ECO:0000269|PubMed:23150671"
FT   STRAND          2..9
FT                   /evidence="ECO:0007829|PDB:4FAK"
FT   HELIX           14..27
FT                   /evidence="ECO:0007829|PDB:4FAK"
FT   TURN            28..30
FT                   /evidence="ECO:0007829|PDB:4FAK"
FT   STRAND          32..38
FT                   /evidence="ECO:0007829|PDB:4FAK"
FT   HELIX           49..65
FT                   /evidence="ECO:0007829|PDB:4FAK"
FT   STRAND          71..76
FT                   /evidence="ECO:0007829|PDB:4FAK"
FT   STRAND          80..82
FT                   /evidence="ECO:0007829|PDB:4FAK"
FT   HELIX           85..97
FT                   /evidence="ECO:0007829|PDB:4FAK"
FT   STRAND          102..107
FT                   /evidence="ECO:0007829|PDB:4FAK"
FT   HELIX           115..120
FT                   /evidence="ECO:0007829|PDB:4FAK"
FT   STRAND          122..127
FT                   /evidence="ECO:0007829|PDB:4FAK"
FT   HELIX           134..153
FT                   /evidence="ECO:0007829|PDB:4FAK"
SQ   SEQUENCE   159 AA;  18306 MW;  8B38405E61012716 CRC64;
     MKITILAVGK LKEKYWKQAI AEYEKRLGPY TKIDIIEVPD EKAPENMSDK EIEQVKEKEG
     QRILAKIKPQ STVITLEIQG KMLSSEGLAQ ELNQRMTQGQ SDFVFVIGGS NGLHKDVLQR
     SNYALSFSKM TFPHQMMRVV LIEQVYRAFK IMRGEAYHK
 
 
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