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Database: UniProt
Entry: Q0T5N9
LinkDB: Q0T5N9
Original site: Q0T5N9 
ID   MNMA_SHIF8              Reviewed;         368 AA.
AC   Q0T5N9;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   19-FEB-2014, entry version 58.
DE   RecName: Full=tRNA-specific 2-thiouridylase MnmA;
DE            EC=2.8.1.-;
GN   Name=mnmA; OrderedLocusNames=SFV_1168;
OS   Shigella flexneri serotype 5b (strain 8401).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=373384;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8401;
RX   PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA   Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z.,
RA   Peng J., Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y.,
RA   Jin Q.;
RT   "Complete genome sequence of Shigella flexneri 5b and comparison with
RT   Shigella flexneri 2a.";
RL   BMC Genomics 7:173-173(2006).
CC   -!- FUNCTION: Catalyzes the 2-thiolation of uridine at the wobble
CC       position (U34) of tRNA(Lys), tRNA(Glu) and tRNA(Gln), leading to
CC       the formation of s(2)U34, the first step of tRNA-mnm(5)s(2)U34
CC       synthesis. Sulfur is provided by IscS, via a sulfur-relay system.
CC       Binds ATP and its substrate tRNAs (By similarity).
CC   -!- SUBUNIT: Interacts with TusE (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the MnmA/TRMU family.
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DR   EMBL; CP000266; ABF03376.1; -; Genomic_DNA.
DR   RefSeq; YP_688681.1; NC_008258.1.
DR   ProteinModelPortal; Q0T5N9; -.
DR   SMR; Q0T5N9; 4-368.
DR   STRING; 373384.SFV_1168; -.
DR   EnsemblBacteria; ABF03376; ABF03376; SFV_1168.
DR   GeneID; 4209110; -.
DR   KEGG; sfv:SFV_1168; -.
DR   PATRIC; 18725638; VBIShiFle33408_1343.
DR   eggNOG; COG0482; -.
DR   HOGENOM; HOG000218046; -.
DR   KO; K00566; -.
DR   OMA; HFLEEYK; -.
DR   OrthoDB; EOG6RZB5H; -.
DR   ProtClustDB; PRK00143; -.
DR   BioCyc; SFLE373384:GHZM-1167-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016783; F:sulfurtransferase activity; IEA:InterPro.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006400; P:tRNA modification; IEA:UniProtKB-HAMAP.
DR   Gene3D; 2.30.30.280; -; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_00144; tRNA_thiouridyl_MnmA; 1.
DR   InterPro; IPR023382; Adenine_a_hdrlase_dom.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR004506; tRNA-specific_2-thiouridylase.
DR   PANTHER; PTHR11933; PTHR11933; 1.
DR   Pfam; PF03054; tRNA_Me_trans; 1.
DR   TIGRFAMs; TIGR00420; trmU; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Cytoplasm; Disulfide bond;
KW   Nucleotide-binding; RNA-binding; Transferase; tRNA processing;
KW   tRNA-binding.
FT   CHAIN         1    368       tRNA-specific 2-thiouridylase MnmA.
FT                                /FTId=PRO_0000349799.
FT   NP_BIND      11     18       ATP (By similarity).
FT   REGION       97     99       Interaction with target base in tRNA (By
FT                                similarity).
FT   REGION      149    151       Interaction with tRNA (By similarity).
FT   REGION      311    312       Interaction with tRNA (By similarity).
FT   ACT_SITE    102    102       Nucleophile (By similarity).
FT   ACT_SITE    199    199       Cysteine persulfide intermediate (By
FT                                similarity).
FT   BINDING      37     37       ATP; via amide nitrogen and carbonyl
FT                                oxygen (By similarity).
FT   BINDING     127    127       ATP; via amide nitrogen (By similarity).
FT   SITE        128    128       Interaction with tRNA (By similarity).
FT   SITE        344    344       Interaction with tRNA (By similarity).
FT   DISULFID    102    199       Alternate (By similarity).
SQ   SEQUENCE   368 AA;  40958 MW;  F41C92676D080D6E CRC64;
     MSETAKKVIV GMSGGVDSSV SAWLLQQQGY QVEGLFMKNW EEDDGEEYCT AAADLADAQA
     VCDKLGIELH TVNFAAEYWD NVFELFLAEY KAGRTPNPDI LCNKEIKFKA FLEFAAEDLG
     ADYIATGHYV RRADVDGKSR LLRGLDSNKD QSYFLYTLSH EQIAQSLFPV GELEKPQVRK
     IAEDLGLVTA KKKDSTGICF IGERKFREFL GRYLPAQPGK IITVDGDEIG EHQGLMYHTL
     GQRKGLGIGG TKEGTEEPWY VVDKDVENNI LVVAQGHEHP RLMSVGLIAQ QLHWVDREPF
     TGTMRCTVKT RYRQTDIPCT VKALDDDRIK VIFDEPVAAV TPGQSAVFYN GEVCLGGGII
     EQRLPLPV
//
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