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RSMJ_SHIFL
ID   RSMJ_SHIFL              Reviewed;         250 AA.
AC   Q7UAV7; Q83J64;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Ribosomal RNA small subunit methyltransferase J {ECO:0000255|HAMAP-Rule:MF_01523};
DE            EC=2.1.1.242 {ECO:0000255|HAMAP-Rule:MF_01523};
DE   AltName: Full=16S rRNA m2G1516 methyltransferase {ECO:0000255|HAMAP-Rule:MF_01523};
DE   AltName: Full=rRNA (guanine-N(2)-)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01523};
GN   Name=rsmJ {ECO:0000255|HAMAP-Rule:MF_01523}; Synonyms=yhiQ;
GN   OrderedLocusNames=SF3528, S4240;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH
RP   S-ADENOSYL-L-HOMOCYSTEINE.
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RG   Northeast structural genomics consortium (NESG);
RT   "Crystal structure of UPF0341 protein (YhiQ) from Shigella flexneri in
RT   complex with S-adenosyl homocysteine, northeast structural genomics target
RT   sfr275.";
RL   Submitted (FEB-2009) to the PDB data bank.
CC   -!- FUNCTION: Specifically methylates the guanosine in position 1516 of 16S
CC       rRNA. {ECO:0000255|HAMAP-Rule:MF_01523}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=guanosine(1516) in 16S rRNA + S-adenosyl-L-methionine = H(+) +
CC         N(2)-methylguanosine(1516) in 16S rRNA + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:43220, Rhea:RHEA-COMP:10412, Rhea:RHEA-COMP:10413,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74269, ChEBI:CHEBI:74481; EC=2.1.1.242;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01523};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01523}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. RsmJ family.
CC       {ECO:0000255|HAMAP-Rule:MF_01523}.
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DR   EMBL; AE005674; AAN44984.2; -; Genomic_DNA.
DR   EMBL; AE014073; AAP19202.1; -; Genomic_DNA.
DR   RefSeq; NP_709277.2; NC_004337.2.
DR   RefSeq; WP_000686608.1; NZ_WPGN01000102.1.
DR   PDB; 2OYR; X-ray; 2.00 A; A=1-250.
DR   PDBsum; 2OYR; -.
DR   AlphaFoldDB; Q7UAV7; -.
DR   SMR; Q7UAV7; -.
DR   STRING; 198214.SF3528; -.
DR   DNASU; 1080448; -.
DR   EnsemblBacteria; AAN44984; AAN44984; SF3528.
DR   EnsemblBacteria; AAP19202; AAP19202; S4240.
DR   GeneID; 1026390; -.
DR   GeneID; 58391087; -.
DR   KEGG; sfl:SF3528; -.
DR   KEGG; sfx:S4240; -.
DR   PATRIC; fig|198214.7.peg.4153; -.
DR   HOGENOM; CLU_076324_0_0_6; -.
DR   OMA; SRYDIYP; -.
DR   OrthoDB; 1696461at2; -.
DR   EvolutionaryTrace; Q7UAV7; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008990; F:rRNA (guanine-N2-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.150; -; 1.
DR   HAMAP; MF_01523; 16SrRNA_methyltr_J; 1.
DR   InterPro; IPR007536; 16SrRNA_methylTrfase_J.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR36112; PTHR36112; 1.
DR   Pfam; PF04445; SAM_MT; 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..250
FT                   /note="Ribosomal RNA small subunit methyltransferase J"
FT                   /id="PRO_0000212093"
FT   BINDING         101..102
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000305|Ref.3"
FT   BINDING         117..118
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000305|Ref.3"
FT   BINDING         153..154
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000305|Ref.3"
FT   BINDING         171
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000305|Ref.3"
FT   STRAND          2..7
FT                   /evidence="ECO:0007829|PDB:2OYR"
FT   HELIX           15..23
FT                   /evidence="ECO:0007829|PDB:2OYR"
FT   STRAND          32..37
FT                   /evidence="ECO:0007829|PDB:2OYR"
FT   STRAND          42..46
FT                   /evidence="ECO:0007829|PDB:2OYR"
FT   HELIX           50..52
FT                   /evidence="ECO:0007829|PDB:2OYR"
FT   STRAND          59..61
FT                   /evidence="ECO:0007829|PDB:2OYR"
FT   HELIX           62..70
FT                   /evidence="ECO:0007829|PDB:2OYR"
FT   HELIX           73..75
FT                   /evidence="ECO:0007829|PDB:2OYR"
FT   HELIX           77..81
FT                   /evidence="ECO:0007829|PDB:2OYR"
FT   STRAND          92..94
FT                   /evidence="ECO:0007829|PDB:2OYR"
FT   HELIX           101..109
FT                   /evidence="ECO:0007829|PDB:2OYR"
FT   STRAND          113..117
FT                   /evidence="ECO:0007829|PDB:2OYR"
FT   HELIX           120..135
FT                   /evidence="ECO:0007829|PDB:2OYR"
FT   TURN            137..139
FT                   /evidence="ECO:0007829|PDB:2OYR"
FT   HELIX           140..146
FT                   /evidence="ECO:0007829|PDB:2OYR"
FT   STRAND          147..152
FT                   /evidence="ECO:0007829|PDB:2OYR"
FT   HELIX           154..157
FT                   /evidence="ECO:0007829|PDB:2OYR"
FT   STRAND          166..170
FT                   /evidence="ECO:0007829|PDB:2OYR"
FT   HELIX           185..193
FT                   /evidence="ECO:0007829|PDB:2OYR"
FT   HELIX           200..203
FT                   /evidence="ECO:0007829|PDB:2OYR"
FT   HELIX           204..210
FT                   /evidence="ECO:0007829|PDB:2OYR"
FT   STRAND          212..220
FT                   /evidence="ECO:0007829|PDB:2OYR"
FT   HELIX           226..228
FT                   /evidence="ECO:0007829|PDB:2OYR"
FT   STRAND          232..236
FT                   /evidence="ECO:0007829|PDB:2OYR"
FT   STRAND          238..246
FT                   /evidence="ECO:0007829|PDB:2OYR"
SQ   SEQUENCE   250 AA;  26919 MW;  7826E98CBAC1C978 CRC64;
     MKICLIDETG AGDGALSVLA ARWGLEHDED NLMALVLTPE HLELRKRDEP KLGGIFVDFV
     GGAMAHRRKF GGGRGEAVAK AVGIKGDYLP DVVDATAGLG RDAFVLASVG CRVRMLERNP
     VVAALLDDGL ARGYADAEIG GWLQERLQLI HASSLTALTD ITPRPQVVYL DPMFPHKQKS
     ALVKKEMRVF QSLVGPDLDA DGLLEPARLL ATKRVVVKRP DYAPPLANVA TPNAVVTKGH
     RFDIYAGTPV
 
 
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