ID   TSAC_METJA              Reviewed;         207 AA.
AC   Q60369;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=Putative threonylcarbamoyl-AMP synthase;
DE            Short=TC-AMP synthase;
DE            EC=2.7.7.87;
DE   AltName: Full=L-threonylcarbamoyladenylate synthase;
DE   AltName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein MJ0062;
GN   OrderedLocusNames=MJ0062;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
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. Catalyzes the conversion of L-threonine, HCO(3)(-)/CO(2)
CC       and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate
CC       intermediate, with the release of diphosphate. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + hydrogencarbonate + L-threonine = diphosphate + H2O + L-
CC         threonylcarbamoyladenylate; Xref=Rhea:RHEA:36407, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57926, ChEBI:CHEBI:73682; EC=2.7.7.87;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the SUA5 family. {ECO:0000305}.
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DR   EMBL; L77117; AAB98044.1; -; Genomic_DNA.
DR   PIR; F64307; F64307.
DR   RefSeq; WP_010869554.1; NC_000909.1.
DR   AlphaFoldDB; Q60369; -.
DR   SMR; Q60369; -.
DR   STRING; 243232.MJ_0062; -.
DR   EnsemblBacteria; AAB98044; AAB98044; MJ_0062.
DR   GeneID; 1450901; -.
DR   KEGG; mja:MJ_0062; -.
DR   eggNOG; arCOG01952; Archaea.
DR   HOGENOM; CLU_031397_3_2_2; -.
DR   InParanoid; Q60369; -.
DR   OMA; MLYPTDT; -.
DR   OrthoDB; 52427at2157; -.
DR   PhylomeDB; Q60369; -.
DR   Proteomes; UP000000805; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
DR   GO; GO:0061710; F:L-threonylcarbamoyladenylate synthase; IEA:UniProtKB-EC.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IBA:GO_Central.
DR   GO; GO:0000049; F:tRNA binding; IBA:GO_Central.
DR   GO; GO:0006450; P:regulation of translational fidelity; IBA:GO_Central.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR   InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom.
DR   InterPro; IPR006070; YrdC-like_dom.
DR   Pfam; PF01300; Sua5_yciO_yrdC; 1.
DR   SUPFAM; SSF55821; SSF55821; 1.
DR   TIGRFAMs; TIGR00057; TIGR00057; 1.
DR   PROSITE; PS51163; YRDC; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Nucleotide-binding; Nucleotidyltransferase;
KW   Reference proteome; Transferase; tRNA processing.
FT   CHAIN           1..207
FT                   /note="Putative threonylcarbamoyl-AMP synthase"
FT                   /id="PRO_0000202028"
FT   DOMAIN          15..199
FT                   /note="YrdC-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00518"
SQ   SEQUENCE   207 AA;  23496 MW;  B7EF4298F2432774 CRC64;
     MGLKNKIIKI YELNEEERKK VLEFLKKEIL NGKIVICGTD TLYGISANAL NEKAVRKVYN
     IKRREFNKPL SICVRDKNEI EKYAYVNDLA KKIIDKFLPG PLTIILKKKP GIPDIVAKDY
     IGIRIPDEPI IRELSIVPLT TTSANISGKE SPTTVDEIDK EVLKKVDYVI DIGKCKYSKP
     STIIKIEDDK IISIREGVIP IQKLARC