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RLMI_ECOLI
ID   RLMI_ECOLI              Reviewed;         396 AA.
AC   P75876; Q9R7Q2;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 2.
DT   03-AUG-2022, entry version 153.
DE   RecName: Full=Ribosomal RNA large subunit methyltransferase I;
DE            EC=2.1.1.191;
DE   AltName: Full=23S rRNA m5C1962 methyltransferase;
DE   AltName: Full=rRNA (cytosine-C(5)-)-methyltransferase RlmI;
GN   Name=rlmI; Synonyms=yccW; OrderedLocusNames=b0967, JW5898;
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 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA   Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA   Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA   Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA   Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA   Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA   Horiuchi T.;
RT   "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 12.7-28.0 min region on the linkage map.";
RL   DNA Res. 3:137-155(1996).
RN   [2]
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   [3]
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   [4]
RP   FUNCTION AS A METHYLTRANSFERASE, AND CATALYTIC ACTIVITY.
RC   STRAIN=K12;
RX   PubMed=18786544; DOI=10.1016/j.jmb.2008.08.061;
RA   Purta E., O'Connor M., Bujnicki J.M., Douthwaite S.;
RT   "YccW is the m5C methyltransferase specific for 23S rRNA nucleotide 1962.";
RL   J. Mol. Biol. 383:641-651(2008).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND SUBUNIT.
RX   PubMed=18789337; DOI=10.1016/j.jmb.2008.08.062;
RA   Sunita S., Tkaczuk K.L., Purta E., Kasprzak J.M., Douthwaite S.,
RA   Bujnicki J.M., Sivaraman J.;
RT   "Crystal structure of the Escherichia coli 23S rRNA:m5C methyltransferase
RT   RlmI (YccW) reveals evolutionary links between RNA modification enzymes.";
RL   J. Mol. Biol. 383:652-666(2008).
CC   -!- FUNCTION: Specifically methylates the cytosine at position 1962
CC       (m5C1962) of 23S rRNA. Methylation occurs before assembly of 23S rRNA
CC       into 50S subunits. {ECO:0000269|PubMed:18786544}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cytidine(1962) in 23S rRNA + S-adenosyl-L-methionine = 5-
CC         methylcytidine(1962) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:42912, Rhea:RHEA-COMP:10382, Rhea:RHEA-COMP:10386,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74483, ChEBI:CHEBI:82748; EC=2.1.1.191;
CC         Evidence={ECO:0000269|PubMed:18786544};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18789337}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. RlmI family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA35732.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; U00096; AAC74053.2; -; Genomic_DNA.
DR   EMBL; AP009048; BAA35732.2; ALT_INIT; Genomic_DNA.
DR   PIR; F64837; F64837.
DR   RefSeq; NP_415487.4; NC_000913.3.
DR   RefSeq; WP_000116297.1; NZ_SSZK01000002.1.
DR   PDB; 3C0K; X-ray; 2.00 A; A/B=1-396.
DR   PDBsum; 3C0K; -.
DR   AlphaFoldDB; P75876; -.
DR   SMR; P75876; -.
DR   BioGRID; 4259463; 53.
DR   DIP; DIP-11501N; -.
DR   IntAct; P75876; 12.
DR   STRING; 511145.b0967; -.
DR   jPOST; P75876; -.
DR   PaxDb; P75876; -.
DR   PRIDE; P75876; -.
DR   EnsemblBacteria; AAC74053; AAC74053; b0967.
DR   EnsemblBacteria; BAA35732; BAA35732; BAA35732.
DR   GeneID; 946691; -.
DR   KEGG; ecj:JW5898; -.
DR   KEGG; eco:b0967; -.
DR   PATRIC; fig|511145.12.peg.1002; -.
DR   EchoBASE; EB3489; -.
DR   eggNOG; COG1092; Bacteria.
DR   HOGENOM; CLU_014042_0_0_6; -.
DR   InParanoid; P75876; -.
DR   OMA; VMDVFDY; -.
DR   PhylomeDB; P75876; -.
DR   BioCyc; EcoCyc:G6501-MON; -.
DR   BioCyc; MetaCyc:G6501-MON; -.
DR   BRENDA; 2.1.1.191; 2026.
DR   EvolutionaryTrace; P75876; -.
DR   PRO; PR:P75876; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IC:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0016434; F:rRNA (cytosine) methyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0009383; F:rRNA (cytosine-C5-)-methyltransferase activity; IDA:EcoCyc.
DR   GO; GO:0070475; P:rRNA base methylation; IMP:EcoCyc.
DR   GO; GO:0031167; P:rRNA methylation; IDA:UniProtKB.
DR   GO; GO:0044010; P:single-species biofilm formation; IMP:EcoCyc.
DR   Gene3D; 2.30.130.10; -; 1.
DR   Gene3D; 3.40.50.150; -; 1.
DR   HAMAP; MF_01857; 23SrRNA_methyltr_I; 1.
DR   InterPro; IPR002478; PUA.
DR   InterPro; IPR015947; PUA-like_sf.
DR   InterPro; IPR036974; PUA_sf.
DR   InterPro; IPR041532; RlmI_PUA-like.
DR   InterPro; IPR023542; rRNA_lsu_MeTfrase_I.
DR   InterPro; IPR019614; SAM-dep_methyl-trfase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF10672; Methyltrans_SAM; 1.
DR   Pfam; PF17785; PUA_3; 1.
DR   SMART; SM00359; PUA; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   SUPFAM; SSF88697; SSF88697; 1.
DR   PROSITE; PS50890; PUA; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Methyltransferase; Reference proteome;
KW   RNA-binding; rRNA processing; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..396
FT                   /note="Ribosomal RNA large subunit methyltransferase I"
FT                   /id="PRO_0000213169"
FT   DOMAIN          2..81
FT                   /note="PUA"
FT   STRAND          4..7
FT                   /evidence="ECO:0007829|PDB:3C0K"
FT   HELIX           13..16
FT                   /evidence="ECO:0007829|PDB:3C0K"
FT   STRAND          20..23
FT                   /evidence="ECO:0007829|PDB:3C0K"
FT   HELIX           24..26
FT                   /evidence="ECO:0007829|PDB:3C0K"
FT   STRAND          27..32
FT                   /evidence="ECO:0007829|PDB:3C0K"
FT   STRAND          39..43
FT                   /evidence="ECO:0007829|PDB:3C0K"
FT   STRAND          49..55
FT                   /evidence="ECO:0007829|PDB:3C0K"
FT   STRAND          59..68
FT                   /evidence="ECO:0007829|PDB:3C0K"
FT   HELIX           76..97
FT                   /evidence="ECO:0007829|PDB:3C0K"
FT   STRAND          100..106
FT                   /evidence="ECO:0007829|PDB:3C0K"
FT   HELIX           107..110
FT                   /evidence="ECO:0007829|PDB:3C0K"
FT   STRAND          115..120
FT                   /evidence="ECO:0007829|PDB:3C0K"
FT   STRAND          123..128
FT                   /evidence="ECO:0007829|PDB:3C0K"
FT   HELIX           131..135
FT                   /evidence="ECO:0007829|PDB:3C0K"
FT   HELIX           137..147
FT                   /evidence="ECO:0007829|PDB:3C0K"
FT   STRAND          151..157
FT                   /evidence="ECO:0007829|PDB:3C0K"
FT   HELIX           161..164
FT                   /evidence="ECO:0007829|PDB:3C0K"
FT   STRAND          170..176
FT                   /evidence="ECO:0007829|PDB:3C0K"
FT   STRAND          181..187
FT                   /evidence="ECO:0007829|PDB:3C0K"
FT   STRAND          190..194
FT                   /evidence="ECO:0007829|PDB:3C0K"
FT   TURN            196..198
FT                   /evidence="ECO:0007829|PDB:3C0K"
FT   HELIX           206..208
FT                   /evidence="ECO:0007829|PDB:3C0K"
FT   HELIX           209..218
FT                   /evidence="ECO:0007829|PDB:3C0K"
FT   STRAND          223..228
FT                   /evidence="ECO:0007829|PDB:3C0K"
FT   HELIX           234..240
FT                   /evidence="ECO:0007829|PDB:3C0K"
FT   STRAND          244..251
FT                   /evidence="ECO:0007829|PDB:3C0K"
FT   HELIX           253..265
FT                   /evidence="ECO:0007829|PDB:3C0K"
FT   HELIX           270..272
FT                   /evidence="ECO:0007829|PDB:3C0K"
FT   STRAND          273..278
FT                   /evidence="ECO:0007829|PDB:3C0K"
FT   HELIX           280..289
FT                   /evidence="ECO:0007829|PDB:3C0K"
FT   STRAND          294..299
FT                   /evidence="ECO:0007829|PDB:3C0K"
FT   TURN            304..306
FT                   /evidence="ECO:0007829|PDB:3C0K"
FT   STRAND          308..312
FT                   /evidence="ECO:0007829|PDB:3C0K"
FT   HELIX           317..327
FT                   /evidence="ECO:0007829|PDB:3C0K"
FT   STRAND          329..339
FT                   /evidence="ECO:0007829|PDB:3C0K"
FT   HELIX           346..360
FT                   /evidence="ECO:0007829|PDB:3C0K"
FT   STRAND          364..371
FT                   /evidence="ECO:0007829|PDB:3C0K"
FT   HELIX           383..385
FT                   /evidence="ECO:0007829|PDB:3C0K"
FT   STRAND          389..395
FT                   /evidence="ECO:0007829|PDB:3C0K"
SQ   SEQUENCE   396 AA;  44357 MW;  09C5ECEB62733D8B CRC64;
     MSVRLVLAKG REKSLLRRHP WVFSGAVARM EGKASLGETI DIVDHQGKWL ARGAYSPASQ
     IRARVWTFDP SESIDIAFFS RRLQQAQKWR DWLAQKDGLD SYRLIAGESD GLPGITIDRF
     GNFLVLQLLS AGAEYQRAAL ISALQTLYPE CSIYDRSDVA VRKKEGMELT QGPVTGELPP
     ALLPIEEHGM KLLVDIQHGH KTGYYLDQRD SRLATRRYVE NKRVLNCFSY TGGFAVSALM
     GGCSQVVSVD TSQEALDIAR QNVELNKLDL SKAEFVRDDV FKLLRTYRDR GEKFDVIVMD
     PPKFVENKSQ LMGACRGYKD INMLAIQLLN EGGILLTFSC SGLMTSDLFQ KIIADAAIDA
     GRDVQFIEQF RQAADHPVIA TYPEGLYLKG FACRVM
 
 
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