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RLMG_ECOLI
ID   RLMG_ECOLI              Reviewed;         378 AA.
AC   P42596; Q2M9C2;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   03-AUG-2022, entry version 149.
DE   RecName: Full=Ribosomal RNA large subunit methyltransferase G;
DE            EC=2.1.1.174 {ECO:0000269|PubMed:17010380};
DE   AltName: Full=23S rRNA m2G1835 methyltransferase;
DE   AltName: Full=rRNA (guanine-N(2)-)-methyltransferase RlmG;
GN   Name=rlmG; Synonyms=ygjO; OrderedLocusNames=b3084, JW5513;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [3]
RP   FUNCTION AS RRNA METHYLTRANSFERASE, AND CATALYTIC ACTIVITY.
RX   PubMed=17010380; DOI=10.1016/j.jmb.2006.09.008;
RA   Sergiev P.V., Lesnyak D.V., Bogdanov A.A., Dontsova O.A.;
RT   "Identification of Escherichia coli m2G methyltransferases: II. The ygjO
RT   gene encodes a methyltransferase specific for G1835 of the 23 S rRNA.";
RL   J. Mol. Biol. 364:26-31(2006).
CC   -!- FUNCTION: Specifically methylates the guanine in position 1835
CC       (m2G1835) of 23S rRNA. {ECO:0000269|PubMed:17010380}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=guanosine(1835) in 23S rRNA + S-adenosyl-L-methionine = H(+) +
CC         N(2)-methylguanosine(1835) in 23S rRNA + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:42744, Rhea:RHEA-COMP:10217, Rhea:RHEA-COMP:10218,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74269, ChEBI:CHEBI:74481; EC=2.1.1.174;
CC         Evidence={ECO:0000269|PubMed:17010380};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42745;
CC         Evidence={ECO:0000269|PubMed:17010380};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. RlmG family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA57885.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; U18997; AAA57885.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U00096; AAC76119.2; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77134.1; -; Genomic_DNA.
DR   PIR; A65097; A65097.
DR   RefSeq; NP_417555.4; NC_000913.3.
DR   RefSeq; WP_000018695.1; NZ_LN832404.1.
DR   PDB; 4DCM; X-ray; 2.30 A; A=9-373.
DR   PDBsum; 4DCM; -.
DR   AlphaFoldDB; P42596; -.
DR   SMR; P42596; -.
DR   BioGRID; 4260876; 40.
DR   BioGRID; 851905; 1.
DR   IntAct; P42596; 1.
DR   STRING; 511145.b3084; -.
DR   jPOST; P42596; -.
DR   PaxDb; P42596; -.
DR   PRIDE; P42596; -.
DR   EnsemblBacteria; AAC76119; AAC76119; b3084.
DR   EnsemblBacteria; BAE77134; BAE77134; BAE77134.
DR   GeneID; 947589; -.
DR   KEGG; ecj:JW5513; -.
DR   KEGG; eco:b3084; -.
DR   PATRIC; fig|511145.12.peg.3179; -.
DR   EchoBASE; EB2585; -.
DR   eggNOG; COG2813; Bacteria.
DR   HOGENOM; CLU_040288_4_0_6; -.
DR   InParanoid; P42596; -.
DR   OMA; DFLAWRM; -.
DR   PhylomeDB; P42596; -.
DR   BioCyc; EcoCyc:G7603-MON; -.
DR   BioCyc; MetaCyc:G7603-MON; -.
DR   BRENDA; 2.1.1.174; 2026.
DR   PRO; PR:P42596; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0052916; F:23S rRNA (guanine(1835)-N(2))-methyltransferase activity; IDA:EcoCyc.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0070475; P:rRNA base methylation; IMP:EcoCyc.
DR   Gene3D; 3.40.50.150; -; 2.
DR   HAMAP; MF_01859; 23SrRNA_methyltr_G; 1.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR017237; rRNA_m2G-MeTrfase_RsmD.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR007848; Small_mtfrase_dom.
DR   PANTHER; PTHR47816:SF5; PTHR47816:SF5; 1.
DR   Pfam; PF05175; MTS; 1.
DR   PIRSF; PIRSF037565; RRNA_m2G_Mtase_RsmD_prd; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Methyltransferase; Reference proteome;
KW   rRNA processing; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..378
FT                   /note="Ribosomal RNA large subunit methyltransferase G"
FT                   /id="PRO_0000097492"
FT   HELIX           30..37
FT                   /evidence="ECO:0007829|PDB:4DCM"
FT   TURN            38..41
FT                   /evidence="ECO:0007829|PDB:4DCM"
FT   STRAND          48..51
FT                   /evidence="ECO:0007829|PDB:4DCM"
FT   STRAND          54..56
FT                   /evidence="ECO:0007829|PDB:4DCM"
FT   HELIX           57..61
FT                   /evidence="ECO:0007829|PDB:4DCM"
FT   HELIX           63..65
FT                   /evidence="ECO:0007829|PDB:4DCM"
FT   STRAND          68..72
FT                   /evidence="ECO:0007829|PDB:4DCM"
FT   HELIX           74..86
FT                   /evidence="ECO:0007829|PDB:4DCM"
FT   HELIX           91..93
FT                   /evidence="ECO:0007829|PDB:4DCM"
FT   STRAND          94..98
FT                   /evidence="ECO:0007829|PDB:4DCM"
FT   STRAND          108..113
FT                   /evidence="ECO:0007829|PDB:4DCM"
FT   HELIX           118..129
FT                   /evidence="ECO:0007829|PDB:4DCM"
FT   STRAND          136..143
FT                   /evidence="ECO:0007829|PDB:4DCM"
FT   HELIX           144..146
FT                   /evidence="ECO:0007829|PDB:4DCM"
FT   HELIX           149..158
FT                   /evidence="ECO:0007829|PDB:4DCM"
FT   STRAND          162..164
FT                   /evidence="ECO:0007829|PDB:4DCM"
FT   STRAND          171..176
FT                   /evidence="ECO:0007829|PDB:4DCM"
FT   STRAND          190..194
FT                   /evidence="ECO:0007829|PDB:4DCM"
FT   TURN            195..198
FT                   /evidence="ECO:0007829|PDB:4DCM"
FT   STRAND          199..203
FT                   /evidence="ECO:0007829|PDB:4DCM"
FT   HELIX           215..222
FT                   /evidence="ECO:0007829|PDB:4DCM"
FT   STRAND          230..236
FT                   /evidence="ECO:0007829|PDB:4DCM"
FT   HELIX           241..249
FT                   /evidence="ECO:0007829|PDB:4DCM"
FT   STRAND          254..260
FT                   /evidence="ECO:0007829|PDB:4DCM"
FT   HELIX           262..275
FT                   /evidence="ECO:0007829|PDB:4DCM"
FT   HELIX           277..282
FT                   /evidence="ECO:0007829|PDB:4DCM"
FT   STRAND          283..287
FT                   /evidence="ECO:0007829|PDB:4DCM"
FT   TURN            290..293
FT                   /evidence="ECO:0007829|PDB:4DCM"
FT   STRAND          299..304
FT                   /evidence="ECO:0007829|PDB:4DCM"
FT   HELIX           318..329
FT                   /evidence="ECO:0007829|PDB:4DCM"
FT   STRAND          330..341
FT                   /evidence="ECO:0007829|PDB:4DCM"
FT   HELIX           346..354
FT                   /evidence="ECO:0007829|PDB:4DCM"
FT   STRAND          358..362
FT                   /evidence="ECO:0007829|PDB:4DCM"
FT   STRAND          364..372
FT                   /evidence="ECO:0007829|PDB:4DCM"
SQ   SEQUENCE   378 AA;  42331 MW;  0496E8BBD36FFB2C CRC64;
     MSHLDNGFRS LTLQRFPATD DVNPLQAWEA ADEYLLQQLD DTEIRGPVLI LNDAFGALSC
     ALAEHKPYSI GDSYISELAT RENLRLNGID ESSVKFLDST ADYPQQPGVV LIKVPKTLAL
     LEQQLRALRK VVTSDTRIIA GAKARDIHTS TLELFEKVLG PTTTTLAWKK ARLINCTFNE
     PQLADAPQTV SWKLEGTDWT IHNHANVFSR TGLDIGARFF MQHLPENLEG EIVDLGCGNG
     VIGLTLLDKN PQAKVVFVDE SPMAVASSRL NVETNMPEAL DRCEFMINNA LSGVEPFRFN
     AVLCNPPFHQ QHALTDNVAW EMFHHARRCL KINGELYIVA NRHLDYFHKL KKIFGNCTTI
     ATNNKFVVLK AVKLGRRR
 
 
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