KAE1B_METM5
ID KAE1B_METM5 Reviewed; 545 AA.
AC A4FZ86;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Probable bifunctional tRNA threonylcarbamoyladenosine biosynthesis protein {ECO:0000255|HAMAP-Rule:MF_01447};
DE Includes:
DE RecName: Full=tRNA N6-adenosine threonylcarbamoyltransferase {ECO:0000255|HAMAP-Rule:MF_01447};
DE EC=2.3.1.234 {ECO:0000255|HAMAP-Rule:MF_01447};
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_01447};
DE AltName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein Kae1 {ECO:0000255|HAMAP-Rule:MF_01447};
DE Includes:
DE RecName: Full=Serine/threonine-protein kinase Bud32 {ECO:0000255|HAMAP-Rule:MF_01447};
DE EC=2.7.11.1 {ECO:0000255|HAMAP-Rule:MF_01447};
GN OrderedLocusNames=MmarC5_1222;
OS Methanococcus maripaludis (strain C5 / ATCC BAA-1333).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=402880;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C5 / ATCC BAA-1333;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C.,
RA Detter J.C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT "Complete sequence of chromosome of Methanococcus maripaludis C5.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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. Is a component of the KEOPS complex that is probably
CC involved in the transfer of the threonylcarbamoyl moiety of
CC threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. The Kae1 domain
CC likely plays a direct catalytic role in this reaction. The Bud32 domain
CC probably displays kinase activity that regulates Kae1 function.
CC {ECO:0000255|HAMAP-Rule:MF_01447}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01447};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000255|HAMAP-Rule:MF_01447};
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_01447};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01447};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01447};
CC -!- SUBUNIT: Component of the KEOPS complex that consists of Kae1, Bud32,
CC Cgi121 and Pcc1; the whole complex dimerizes. {ECO:0000255|HAMAP-
CC Rule:MF_01447}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01447}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the KAE1 / TsaD
CC family. {ECO:0000255|HAMAP-Rule:MF_01447}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the protein kinase
CC superfamily. Tyr protein kinase family. BUD32 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01447}.
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DR EMBL; CP000609; ABO35520.1; -; Genomic_DNA.
DR RefSeq; WP_011868973.1; NC_009135.1.
DR AlphaFoldDB; A4FZ86; -.
DR SMR; A4FZ86; -.
DR STRING; 402880.MmarC5_1222; -.
DR EnsemblBacteria; ABO35520; ABO35520; MmarC5_1222.
DR GeneID; 4929014; -.
DR KEGG; mmq:MmarC5_1222; -.
DR eggNOG; arCOG01183; Archaea.
DR eggNOG; arCOG01185; Archaea.
DR HOGENOM; CLU_023208_2_2_2; -.
DR OMA; GETMDTG; -.
DR OrthoDB; 9881at2157; -.
DR Proteomes; UP000000253; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000408; C:EKC/KEOPS complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0061711; F:N(6)-L-threonylcarbamoyladenine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01446; Kae1; 1.
DR HAMAP; MF_01447; Kae1_Bud32_arch; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR022495; Bud32.
DR InterPro; IPR000905; Gcp-like_dom.
DR InterPro; IPR017861; KAE1/TsaD.
DR InterPro; IPR022449; Kae1_arc.
DR InterPro; IPR034680; Kae1_archaea_euk.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR009220; tRNA_threonyl_synthase/kinase.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR PANTHER; PTHR11735; PTHR11735; 1.
DR PANTHER; PTHR11735:SF14; PTHR11735:SF14; 1.
DR Pfam; PF00814; TsaD; 1.
DR PIRSF; PIRSF036401; Gcp_STYKS; 1.
DR PRINTS; PR00789; OSIALOPTASE.
DR SUPFAM; SSF53067; SSF53067; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR TIGRFAMs; TIGR03724; arch_bud32; 1.
DR TIGRFAMs; TIGR03722; arch_KAE1; 1.
DR TIGRFAMs; TIGR00329; gcp_kae1; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 3: Inferred from homology;
KW Acyltransferase; ATP-binding; Cytoplasm; Iron; Kinase; Metal-binding;
KW Multifunctional enzyme; Nucleotide-binding;
KW Serine/threonine-protein kinase; Transferase; tRNA processing.
FT CHAIN 1..545
FT /note="Probable bifunctional tRNA
FT threonylcarbamoyladenosine biosynthesis protein"
FT /id="PRO_1000024464"
FT DOMAIN 344..545
FT /note="Protein kinase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
FT REGION 1..329
FT /note="Kae1"
FT ACT_SITE 463
FT /note="Proton acceptor; for kinase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
FT BINDING 112
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
FT BINDING 116
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
FT BINDING 133..137
FT /ligand="L-threonylcarbamoyladenylate"
FT /ligand_id="ChEBI:CHEBI:73682"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
FT BINDING 133
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
FT BINDING 165
FT /ligand="L-threonylcarbamoyladenylate"
FT /ligand_id="ChEBI:CHEBI:73682"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
FT BINDING 178
FT /ligand="L-threonylcarbamoyladenylate"
FT /ligand_id="ChEBI:CHEBI:73682"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
FT BINDING 182
FT /ligand="L-threonylcarbamoyladenylate"
FT /ligand_id="ChEBI:CHEBI:73682"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
FT BINDING 262
FT /ligand="L-threonylcarbamoyladenylate"
FT /ligand_id="ChEBI:CHEBI:73682"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
FT BINDING 290
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
FT BINDING 350..358
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
FT BINDING 371
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
SQ SEQUENCE 545 AA; 61127 MW; 3D463ED2C3DBC145 CRC64;
MDTSKDLICI GFEGTAEKTG VGIITSNGEV LFNKTIIYTP PVQGIHPREA ADHHAETFVK
LLKEALTVVP IEKIDLVSFS LGPGLGPSLR VTATTARALS LSINKPIIGV NHCISHVEIG
KLKTDALDPL TLYVSGGNTQ VLAYTGKKYR VIGETLDIAI GNCLDQFARH CNMPHPGGVY
VEKYAKNGNK FIKLPYTVKG MDISLSGLLT AAMKKYDSKE RIEDVCYSLQ ENSFSMLTEI
TERALAHTNK AEVMLVGGVA ANNRLKEMLD IMCIEQNVDF YVPEREFCGD NGAMIAWLGI
LQYLNGKRMD LNDTKPISNY RSDMVEVNWI SENEFNNENI KSRIIPEHLI GKGAEADISK
GIYLEFESIT KERVKKGYRI LELDELIRLR RTVKEARFLA SIKELGIYAP SIFDIDKENK
KITMSYIHGK IAKEKIEEGN LNFCEDLGKI IGKMHSGGIV HNDLTTSNFI VSDNTFVIDF
GLGKYSDLVE DKAIDLIVLK KSIMSIHYDK FDSVWNKIIE GYKTYEMFES VLECMKEVEK
RARYL
