(data stored in SCRATCH3701 zone)

SWISSPROT: TSAE_RICTY

ID   TSAE_RICTY              Reviewed;         144 AA.
AC   Q68XZ1;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   11-DEC-2019, entry version 70.
DE   RecName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein TsaE;
DE   AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaE;
GN   Name=tsaE; OrderedLocusNames=RT0012;
OS   Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=257363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-144 / Wilmington;
RX   PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA   McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA   McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA   Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA   Yu X.-J., Walker D.H., Weinstock G.M.;
RT   "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT   of other Rickettsiae.";
RL   J. Bacteriol. 186:5842-5855(2004).
CC   -!- FUNCTION: Required for the formation of a threonylcarbamoyl group on
CC       adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning
CC       with adenine. Is involved in the transfer of the threonylcarbamoyl
CC       moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37,
CC       together with TsaD and TsaB. TsaE seems to play an indirect role in the
CC       t(6)A biosynthesis pathway, possibly in regulating the core enzymatic
CC       function of TsaD (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TsaE family. {ECO:0000305}.
DR   EMBL; AE017197; AAU03501.1; -; Genomic_DNA.
DR   RefSeq; WP_011190488.1; NC_006142.1.
DR   SMR; Q68XZ1; -.
DR   STRING; 257363.RT0012; -.
DR   EnsemblBacteria; AAU03501; AAU03501; RT0012.
DR   KEGG; rty:RT0012; -.
DR   eggNOG; ENOG4108E87; Bacteria.
DR   eggNOG; COG0802; LUCA.
DR   HOGENOM; HOG000052239; -.
DR   KO; K06925; -.
DR   OMA; FTDDAIC; -.
DR   OrthoDB; 1827295at2; -.
DR   BioCyc; RTYP257363:G1G0L-12-MONOMER; -.
DR   Proteomes; UP000000604; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IEA:InterPro.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR003442; T6A_TsaE.
DR   Pfam; PF02367; TsaE; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00150; T6A_YjeE; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q68XZ1.
DR   SWISS-2DPAGE; Q68XZ1.
KW   ATP-binding; Cytoplasm; Magnesium; Metal-binding; Nucleotide-binding;
KW   tRNA processing.
FT   CHAIN           1..144
FT                   /note="tRNA threonylcarbamoyladenosine biosynthesis protein
FT                   TsaE"
FT                   /id="PRO_0000281043"
FT   NP_BIND         34..39
FT                   /note="ATP"
FT                   /evidence="ECO:0000250"
FT   METAL           38
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000250"
FT   METAL           104
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000250"
FT   BINDING         7
FT                   /note="ATP"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   144 AA;  16854 MW;  BE7A8DEBCBD0B3C4 CRC64;
     MHTLNSEKET KNFAKLFAQN LKPNDIVLLN GDLGAGKTFF CREIIKHFCG KNTNIISPTF
     NLLQIYKTPN FNIYHYDMYR IKSPEEIYEL GFEEALNGNL ILIEWSEIIK HLLTPPLIEV
     NLKILDNNKR LCSIKKENFL FDFL
//

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