(data stored in ACNUC9435 zone)

HOGENOM: ECOK1_1_PE1012

ID   ECOK1_1_PE1012                       STANDARD;      PRT;   383 AA.
AC   ECOK1_1_PE1012; A1AA27;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=tRNA-specific 2-thiouridylase mnmA; EC=2.8.1 -;
DE   (ECOK1_1.PE1012).
GN   Name=mnmA; OrderedLocusNames=Ecok1_10230; ORFNames=APECO1_215;
OS   ESCHERICHIA COLI APEC O1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=405955;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ECOK1_1.PE1012.
CC       Escherichia coli APEC O1, complete genome.
CC       chromosome, complete sequence.
CC   -!- ANNOTATIONS ORIGIN:MNMA_ECOK1
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.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABJ00517.1; Type=Erroneous initiation;
CC   -!- GENE_FAMILY: HOG000218046 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; A1AA27; -.
DR   EMBL; CP000468; ABJ00517.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_852231.1; NC_008563.1.
DR   ProteinModelPortal; A1AA27; -.
DR   SMR; A1AA27; 4-368.
DR   STRING; A1AA27; -.
DR   EnsemblBacteria; EBESCT00000036777; EBESCP00000035294; EBESCG00000035827.
DR   GeneID; 4492303; -.
DR   GenomeReviews; CP000468_GR; Ecok1_10230.
DR   KEGG; ecv:APECO1_215; -.
DR   eggNOG; COG0482; -.
DR   GeneTree; EBGT00050000010099; -.
DR   ProtClustDB; PRK00143; -.
DR   BioCyc; ECOL405955:APECO1_215-MON; -.
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:0008033; P:tRNA processing; IEA:UniProtKB-KW.
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   Gene3D; G3DSA:2.30.30.280; G3DSA:2.30.30.280; 1.
DR   Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
DR   PANTHER; PTHR11933; TrmU_mtfrase; 1.
DR   Pfam; PF03054; tRNA_Me_trans; 1.
DR   TIGRFAMs; TIGR00420; TrmU; 1.
DR   HOGENOMDNA; ECOK1_1.PE1012; -.
KW   ATP-binding; Complete proteome; Cytoplasm; Disulfide bond;
KW   Nucleotide-binding; RNA-binding; Transferase; tRNA processing;
KW   tRNA-binding.
SQ   SEQUENCE   383 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MIEYAALKFN VVSDPMSETA KKVIVGMSGG VDSSVSAWLL QQQGYQVEGL FMKNWEEDDG
     EEYCTAAADL ADAQAVCDKL GIELHTVNFA AEYWDNVFEL FLAEYKAGRT PNPDILCNKE
     IKFKAFLEFA AEDLGADYIA TGHYVRRADV DGKSRLLRGL DSNKDQSYFL YTLSHEQIAQ
     SLFPVGELEK PQVRKIAEDL GLVTAKKKDS TGICFIGERK FREFLGRYLP AQPGKIITVD
     GDEIGEHQGL MYHTLGQRKG LGIGGTKDGT EEPWYVVDKD VENNILIVAQ GHEHPRLMSV
     GLIAQQLHWV DREPFTGTMR CTVKTRYRQT DIPCTVKALD ADRIEVIFDE PVAAVTPGQS
     AVFYNGEVCL GGGIIEQRLP LPV
//

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