ID   SUA5_SCHPO              Reviewed;         408 AA.
AC   O94530;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 113.
DE   RecName: Full=Threonylcarbamoyl-AMP synthase;
DE            Short=TC-AMP synthase;
DE            EC=2.7.7.87;
DE   AltName: Full=L-threonylcarbamoyladenylate synthase;
DE   AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein sua5;
DE   AltName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein sua5;
GN   Name=sua5; ORFNames=SPCC895.03c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
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. Likely catalyzes the conversion of L-threonine,
CC       HCO(3)(-)/CO(2) and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the
CC       acyladenylate intermediate, with the release of diphosphate. Required
CC       for normal translation, by ensuring translation fidelity at the level
CC       of codon recognition, appropriate translation initiation selection and
CC       maintenance of reading frame. Also involved in telomere replication.
CC       Binds to single-stranded telomeric (ssTG) DNA and positively regulates
CC       telomere length (By similarity). {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:0000269|PubMed:16823372}. Nucleus
CC       {ECO:0000269|PubMed:16823372}. Chromosome, telomere {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SUA5 family. {ECO:0000305}.
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DR   EMBL; CU329672; CAA22839.1; -; Genomic_DNA.
DR   PIR; T41641; T41641.
DR   RefSeq; NP_588044.1; NM_001023036.2.
DR   AlphaFoldDB; O94530; -.
DR   SMR; O94530; -.
DR   BioGRID; 276154; 1.
DR   STRING; 4896.SPCC895.03c.1; -.
DR   MaxQB; O94530; -.
DR   PaxDb; O94530; -.
DR   EnsemblFungi; SPCC895.03c.1; SPCC895.03c.1:pep; SPCC895.03c.
DR   GeneID; 2539596; -.
DR   KEGG; spo:SPCC895.03c; -.
DR   PomBase; SPCC895.03c; sua5.
DR   VEuPathDB; FungiDB:SPCC895.03c; -.
DR   eggNOG; KOG3051; Eukaryota.
DR   HOGENOM; CLU_031397_0_0_1; -.
DR   InParanoid; O94530; -.
DR   OMA; GMLKSHY; -.
DR   PhylomeDB; O94530; -.
DR   PRO; PR:O94530; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA 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:0072670; P:mitochondrial tRNA threonylcarbamoyladenosine modification; TAS:PomBase.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   GO; GO:0006450; P:regulation of translational fidelity; IBA:GO_Central.
DR   Gene3D; 3.40.50.11030; -; 1.
DR   InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom.
DR   InterPro; IPR038385; Sua5/YwlC_C.
DR   InterPro; IPR005145; Sua5_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;
KW   ATP-binding; Chromosome; Cytoplasm; DNA-binding; Nucleotide-binding;
KW   Nucleotidyltransferase; Nucleus; Reference proteome; Telomere; Transferase;
KW   Translation regulation; tRNA processing.
FT   CHAIN           1..408
FT                   /note="Threonylcarbamoyl-AMP synthase"
FT                   /id="PRO_0000315950"
FT   DOMAIN          39..249
FT                   /note="YrdC-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00518"
SQ   SEQUENCE   408 AA;  44773 MW;  37ED575E8915C437 CRC64;
     METKIQTVDT RLISFEKPSN DSEHPFEHTR VSIPPSETRS ALENAANILR NTDYPVAFPT
     ETVYGLGADA RRTEAVLSIY KAKNRPADNP LIVHVASLDQ LRRLLLSAYP KAKSEVKNQA
     HDSEEIIPKV YLPLIKKFWP GPLSILLPVV DEANPPVSPI VTAGQKTFAV RMPQHPVALA
     LISISDSPLA APSANASTRP SPTLAKHVYN DLQGKIPLIL DGGACGVGVE STVVNGLCDP
     PVILRPGGIS LEEIQSSGGA WERTKVFVAK KSDMETDFIP QTPGMKYRHY SPTAKVLLFV
     NYTESDAYGV FEKYLSEQGI TKEKQKIGVL CSKRWNEESF PSHCPFVFLH MGRDGHEITK
     NLFAQLRDLD LQGVDFVLVE GVSEENEGLA IMNRLGKAAS VVFEGPSH