(data stored in ACNUC7421 zone)

SWISSPROT: KAE1_ASPFU

ID   KAE1_ASPFU              Reviewed;         352 AA.
AC   Q4WDE9;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   11-DEC-2019, entry version 103.
DE   RecName: Full=tRNA N6-adenosine threonylcarbamoyltransferase {ECO:0000255|HAMAP-Rule:MF_03180};
DE            EC=2.3.1.234 {ECO:0000255|HAMAP-Rule:MF_03180};
DE   AltName: Full=N6-L-threonylcarbamoyladenine synthase;
DE            Short=t(6)A synthase;
DE   AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein kae1 {ECO:0000255|HAMAP-Rule:MF_03180};
DE   AltName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein kae1 {ECO:0000255|HAMAP-Rule:MF_03180};
GN   Name=kae1; ORFNames=AFUA_6G04510;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
CC   -!- FUNCTION: Component of the EKC/KEOPS complex that is required for the
CC       formation of a threonylcarbamoyl group on adenosine at position 37
CC       (t(6)A37) in tRNAs that read codons beginning with adenine. The complex
CC       is probably involved in the transfer of the threonylcarbamoyl moiety of
CC       threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. Kae1 likely
CC       plays a direct catalytic role in this reaction, but requires other
CC       protein(s) of the complex to fulfill this activity. The EKC/KEOPS
CC       complex also promotes both telomere uncapping and telomere elongation.
CC       The complex is required for efficient recruitment of transcriptional
CC       coactivators. {ECO:0000255|HAMAP-Rule:MF_03180}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine(37) in tRNA + L-threonylcarbamoyladenylate = AMP +
CC         H(+) + N(6)-L-threonylcarbamoyladenosine(37) in tRNA;
CC         Xref=Rhea:RHEA:37059, Rhea:RHEA-COMP:10162, Rhea:RHEA-COMP:10163,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:73682, ChEBI:CHEBI:74411,
CC         ChEBI:CHEBI:74418, ChEBI:CHEBI:456215; EC=2.3.1.234;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03180};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03180};
CC       Note=Binds 1 divalent metal cation per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_03180};
CC   -!- SUBUNIT: Component of the EKC/KEOPS complex composed of at least bud32,
CC       cgi121, gon7, kae1 and pcc1; the whole complex dimerizes.
CC       {ECO:0000255|HAMAP-Rule:MF_03180}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03180}.
CC       Nucleus {ECO:0000255|HAMAP-Rule:MF_03180}.
CC   -!- SIMILARITY: Belongs to the KAE1 / TsaD family. {ECO:0000255|HAMAP-
CC       Rule:MF_03180}.
DR   EMBL; AAHF01000012; EAL85589.1; -; Genomic_DNA.
DR   RefSeq; XP_747627.1; XM_742534.1.
DR   STRING; 746128.CADAFUBP00009116; -.
DR   PRIDE; Q4WDE9; -.
DR   EnsemblFungi; EAL85589; EAL85589; AFUA_6G04510.
DR   GeneID; 3505228; -.
DR   KEGG; afm:AFUA_6G04510; -.
DR   EuPathDB; FungiDB:Afu6g04510; -.
DR   HOGENOM; HOG000109569; -.
DR   InParanoid; Q4WDE9; -.
DR   KO; K01409; -.
DR   OMA; HLEGHIY; -.
DR   OrthoDB; 829465at2759; -.
DR   Proteomes; UP000002530; Chromosome 6.
DR   Proteomes; UP000002530; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000408; C:EKC/KEOPS complex; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0061711; F:N(6)-L-threonylcarbamoyladenine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01446; Kae1; 1.
DR   InterPro; IPR000905; Gcp-like_dom.
DR   InterPro; IPR034680; Kae1/OSGEP.
DR   InterPro; IPR017861; KAE1/TsaD.
DR   PANTHER; PTHR11735; PTHR11735; 1.
DR   PANTHER; PTHR11735:SF14; PTHR11735:SF14; 1.
DR   Pfam; PF00814; Peptidase_M22; 1.
DR   PRINTS; PR00789; OSIALOPTASE.
DR   TIGRFAMs; TIGR00329; gcp_kae1; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q4WDE9.
DR   SWISS-2DPAGE; Q4WDE9.
KW   Activator; Acyltransferase; Cytoplasm; Metal-binding; Nucleus;
KW   Reference proteome; Transcription; Transcription regulation; Transferase;
KW   tRNA processing.
FT   CHAIN           1..352
FT                   /note="tRNA N6-adenosine threonylcarbamoyltransferase"
FT                   /id="PRO_0000278926"
FT   REGION          135..139
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT   METAL           114
FT                   /note="Divalent metal cation"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT   METAL           118
FT                   /note="Divalent metal cation"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT   METAL           135
FT                   /note="Divalent metal cation"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT   METAL           311
FT                   /note="Divalent metal cation"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT   BINDING         167
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT   BINDING         182
FT                   /note="Substrate; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT   BINDING         186
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT   BINDING         283
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
SQ   SEQUENCE   352 AA;  38273 MW;  1390A3CFF83C43A6 CRC64;
     MIAIGLEGSA NKLGVGIMLH PEDGSTPRVL ANIRHTYVSP PGEGFLPKDT ARHHRSWVVK
     LVKRALREAR ISVRDVDCIC FTKGPGMGAP LQSVAVAARM LSLLWGKELV GVNHCVGHIE
     MGRLITGSTN PVVLYVSGGN TQVIAYSSQR YRIFGETLDI AVGNCLDRFA RTLHISNDPA
     PGYNIEQLAK KGKQLVDLPY TVKGMDCSFS GILAAIDGLA ASYGLNGEEK EEEGAGDDSK
     PTRADLCFSL QETVFSMLVE ITERAMAHVG SKEVLIVGGV GCNERLQEMM GIMARDRGGS
     VHATDERFCI DNGIMIAQAG LLAYKTGFRT PLKESTCTQR FRTDDVFVKW RD
//

If you have problems or comments...

PBIL Back to PBIL home page