(data stored in ACNUC7421 zone)

SWISSPROT: Q758Q3_ASHGO

ID   Q758Q3_ASHGO            Unreviewed;       418 AA.
AC   Q758Q3;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 91.
DE   RecName: Full=Threonylcarbamoyl-AMP synthase {ECO:0000256|PIRNR:PIRNR004930};
DE            Short=TC-AMP synthase {ECO:0000256|PIRNR:PIRNR004930};
DE            EC=2.7.7.87 {ECO:0000256|PIRNR:PIRNR004930};
DE   AltName: Full=L-threonylcarbamoyladenylate synthase {ECO:0000256|PIRNR:PIRNR004930};
GN   ORFNames=AGOS_AEL300C {ECO:0000313|EMBL:AAS52384.1};
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811 {ECO:0000313|EMBL:AAS52384.1, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS52384.1, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Pohlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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. {ECO:0000256|PIRNR:PIRNR004930}.
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         Evidence={ECO:0000256|PIRNR:PIRNR004930};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR004930}.
CC   -!- SIMILARITY: Belongs to the SUA5 family.
CC       {ECO:0000256|PIRNR:PIRNR004930}.
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DR   EMBL; AE016818; AAS52384.1; -; Genomic_DNA.
DR   RefSeq; NP_984560.1; NM_209913.1.
DR   STRING; 33169.AAS52384; -.
DR   EnsemblFungi; AAS52384; AAS52384; AGOS_AEL300C.
DR   GeneID; 4620735; -.
DR   KEGG; ago:AGOS_AEL300C; -.
DR   HOGENOM; HOG000076160; -.
DR   InParanoid; Q758Q3; -.
DR   KO; K07566; -.
DR   OMA; RSCPGWE; -.
DR   Proteomes; UP000000591; Chromosome V.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003725; F:double-stranded RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0061710; F:L-threonylcarbamoyladenylate synthase; IEA:UniProtKB-EC.
DR   GO; GO:0061711; F:N(6)-L-threonylcarbamoyladenine synthase activity; IEA:EnsemblFungi.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IBA:GO_Central.
DR   GO; GO:0043047; F:single-stranded telomeric DNA binding; IEA:EnsemblFungi.
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:0000723; P:telomere maintenance; IEA:EnsemblFungi.
DR   GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IEA:EnsemblFungi.
DR   Gene3D; 3.40.50.11030; -; 1.
DR   InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom.
DR   InterPro; IPR005145; SUA5.
DR   InterPro; IPR038385; Sua5/YwlC_C.
DR   InterPro; IPR010923; T(6)A37_SUA5.
DR   InterPro; IPR006070; YrdC-like_dom.
DR   Pfam; PF03481; SUA5; 1.
DR   Pfam; PF01300; Sua5_yciO_yrdC; 1.
DR   PIRSF; PIRSF004930; Tln_factor_SUA5; 1.
DR   SUPFAM; SSF55821; SSF55821; 1.
DR   TIGRFAMs; TIGR00057; TIGR00057; 1.
DR   PROSITE; PS51163; YRDC; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q758Q3.
DR   SWISS-2DPAGE; Q758Q3.
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR004930, ECO:0000256|PIRSR:PIRSR004930-
KW   1}; Cytoplasm {ECO:0000256|PIRNR:PIRNR004930};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR004930,
KW   ECO:0000256|PIRSR:PIRSR004930-1};
KW   Nucleotidyltransferase {ECO:0000256|PIRNR:PIRNR004930};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591};
KW   Transferase {ECO:0000256|PIRNR:PIRNR004930};
KW   tRNA processing {ECO:0000256|PIRNR:PIRNR004930}.
FT   DOMAIN          52..251
FT                   /note="YrdC-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51163"
FT   BINDING         75
FT                   /note="L-threonine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004930-1"
FT   BINDING         98
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004930-1"
FT   BINDING         102
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004930-1"
FT   BINDING         107
FT                   /note="L-threonine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004930-1"
FT   BINDING         169
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004930-1"
FT   BINDING         173
FT                   /note="L-threonine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004930-1"
FT   BINDING         193
FT                   /note="L-threonine; via carbonyl oxygen"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004930-1"
FT   BINDING         195
FT                   /note="ATP; via amide nitrogen"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004930-1"
FT   BINDING         203
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004930-1"
FT   BINDING         233
FT                   /note="L-threonine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004930-1"
FT   BINDING         247
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004930-1"
FT   BINDING         291
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004930-1"
SQ   SEQUENCE   418 AA;  45932 MW;  F38E88F5B47D3F62 CRC64;
     MQRSFSFLRR SGFHSAMSYN TKVLRVDPSA IHFSATAHID GSLPRISDPE TEKHLLEAAR
     LIRDDGETVA FPTETVYGLG GSSLNDASVR NIYKAKNRPS DNPLISHVSS IAQLNRRIYQ
     QDREGDVLRN IPVVYHELVR QLWPGPLTIL LPINEETALS VLTTAGQPTF AVRIPADPVA
     RALIALSDTP IAAPSANVST RPSPTAAEHV YHDLKGKIPL ILDGGSCRVG VESTVIDGLV
     NPPMLLRPGG FTYEEIIELG GEQWSHCKVE NRMTVGSGEK VRTPGMKYKH YSPRASTVAF
     APINDDLPTS ERMKIVTSEI MKYMTSHGTD KRQKVGLLTS IMFPNNLLES ITDEVDVVVY
     SLGSSGKEVQ SNLFAMLRRL DEEDEVDLIF VEGISDRNEG LAVMNRLRKA AGGNVVSF
//

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