(data stored in ACNUC7421 zone)

SWISSPROT: KAE1_ASHGO

ID   KAE1_ASHGO              Reviewed;         385 AA.
AC   Q758R9;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 108.
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 {ECO:0000255|HAMAP-Rule:MF_03180}; OrderedLocusNames=AEL316W;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
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., Poehlmann 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]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
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: 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; AE016818; AAS52368.1; -; Genomic_DNA.
DR   RefSeq; NP_984544.1; NM_209897.1.
DR   STRING; 33169.AAS52368; -.
DR   EnsemblFungi; AAS52368; AAS52368; AGOS_AEL316W.
DR   GeneID; 4620716; -.
DR   KEGG; ago:AGOS_AEL316W; -.
DR   HOGENOM; HOG000109569; -.
DR   InParanoid; Q758R9; -.
DR   KO; K01409; -.
DR   OMA; HLEGHIY; -.
DR   Proteomes; UP000000591; Chromosome V.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000408; C:EKC/KEOPS complex; IBA:GO_Central.
DR   GO; GO:0000790; C:nuclear chromatin; IEA:EnsemblFungi.
DR   GO; GO:0031490; F:chromatin DNA binding; IEA:EnsemblFungi.
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:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
DR   GO; GO:0000722; P:telomere maintenance via recombination; IEA:EnsemblFungi.
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   InterPro; IPR017860; Peptidase_M22_CS.
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.
DR   PROSITE; PS01016; GLYCOPROTEASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q758R9.
DR   SWISS-2DPAGE; Q758R9.
KW   Activator; Acyltransferase; Cytoplasm; Metal-binding; Nucleus;
KW   Reference proteome; Transcription; Transcription regulation; Transferase;
KW   tRNA processing.
FT   CHAIN           1..385
FT                   /note="tRNA N6-adenosine threonylcarbamoyltransferase"
FT                   /id="PRO_0000278924"
FT   REGION          161..165
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT   METAL           140
FT                   /note="Divalent metal cation"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT   METAL           144
FT                   /note="Divalent metal cation"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT   METAL           161
FT                   /note="Divalent metal cation"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT   METAL           343
FT                   /note="Divalent metal cation"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT   BINDING         193
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT   BINDING         208
FT                   /note="Substrate; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT   BINDING         212
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT   BINDING         314
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
SQ   SEQUENCE   385 AA;  43035 MW;  25BFF5263FBB0AD4 CRC64;
     MVNLNKVQPR SGGDHYLALG IEGSANKLGV GILKHPMLSQ HKQGSLSHDC QAEILSNIRD
     TYITPPGEGF LPRDTARHHR NWVVRLVRRA LVEAGIEDPR LLDVICFTKG PGMGAPLHSV
     VVAARTMSML WDVPLVAVNH CIGHIEMGRE ITKAENPVVL YVSGGNTQVI AYSENRYRIF
     GETLDIAIGN CLDRFARTLK IPNDPSPGYN IEQLAKQCKN KDRLVELPYT VKGMDLSMSG
     ILAHIDSLAK DLFRRNTKNY KLFDRETGKQ LVTVEDLCYS LQEHLFAMLV EITERAMAHV
     NSNQVLIVGG VGCNVRLQQM MASMCQSRAD GQVHATDERF CIDNGVMIAQ AGLLQYRMGD
     IVKDFSETVV TQRFRTDEVY VSWRD
//

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