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Probable bifunctional tRNA threonylcarbamoyladenosine biosynthesis protein [Includes: tRNA N6-adenosine threonylcarbamoyltransferase (EC 2.3.1.234) (t(6)A37 threonylcarbamoyladenosine biosynthesis protein Kae1) (tRNA threonylcarbamoyladenosine biosynthesis protein Kae1); Serine/threonine-protein kinase Bud32 (EC 2.7.11.1)]

 A0A090I8T6_METFO        Unreviewed;       547 AA.
A0A090I8T6;
26-NOV-2014, integrated into UniProtKB/TrEMBL.
26-NOV-2014, sequence version 1.
20-DEC-2017, entry version 24.
RecName: Full=Probable bifunctional tRNA threonylcarbamoyladenosine biosynthesis protein {ECO:0000256|HAMAP-Rule:MF_01447};
Includes:
RecName: Full=tRNA N6-adenosine threonylcarbamoyltransferase {ECO:0000256|HAMAP-Rule:MF_01447};
EC=2.3.1.234 {ECO:0000256|HAMAP-Rule:MF_01447};
AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein Kae1 {ECO:0000256|HAMAP-Rule:MF_01447};
AltName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein Kae1 {ECO:0000256|HAMAP-Rule:MF_01447};
Includes:
RecName: Full=Serine/threonine-protein kinase Bud32 {ECO:0000256|HAMAP-Rule:MF_01447};
EC=2.7.11.1 {ECO:0000256|HAMAP-Rule:MF_01447};
ORFNames=DSM1535_1331 {ECO:0000313|EMBL:CEA13667.1};
Methanobacterium formicicum.
Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales;
Methanobacteriaceae; Methanobacterium.
NCBI_TaxID=2162 {ECO:0000313|EMBL:CEA13667.1, ECO:0000313|Proteomes:UP000032423};
[1] {ECO:0000313|Proteomes:UP000032423}
NUCLEOTIDE SEQUENCE.
STRAIN=DSM 1535 {ECO:0000313|Proteomes:UP000032423};
PubMed=25270020; DOI=10.1016/j.jbiotec.2014.09.018;
Maus I., Stantscheff R., Wibberg D., Stolze Y., Winkler A., Puhler A.,
Konig H., Schluter A.;
"Complete genome sequence of the methanogenic neotype strain
Methanobacterium formicicum MF.";
J. Biotechnol. 192:40-41(2014).
-!- FUNCTION: Required for the formation of a threonylcarbamoyl group
on adenosine at position 37 (t(6)A37) in tRNAs that read codons
beginning with adenine. Is a component of the KEOPS complex that
is probably involved in the transfer of the threonylcarbamoyl
moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37.
The Kae1 domain likely plays a direct catalytic role in this
reaction. The Bud32 domain probably displays kinase activity that
regulates Kae1 function. {ECO:0000256|HAMAP-Rule:MF_01447}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000256|HAMAP-Rule:MF_01447}.
-!- CATALYTIC ACTIVITY: L-threonylcarbamoyladenylate + adenine(37) in
tRNA = AMP + N(6)-L-threonylcarbamoyladenine(37) in tRNA.
{ECO:0000256|HAMAP-Rule:MF_01447, ECO:0000256|SAAS:SAAS00346554}.
-!- COFACTOR:
Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
Evidence={ECO:0000256|HAMAP-Rule:MF_01447};
Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000256|HAMAP-
Rule:MF_01447};
-!- SUBUNIT: Component of the KEOPS complex that consists of Kae1,
Bud32, Cgi121 and Pcc1; the whole complex dimerizes.
{ECO:0000256|HAMAP-Rule:MF_01447}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01447,
ECO:0000256|SAAS:SAAS00346542}.
-!- SIMILARITY: In the C-terminal section; belongs to the protein
kinase superfamily. Tyr protein kinase family. BUD32 subfamily.
{ECO:0000256|HAMAP-Rule:MF_01447}.
-!- SIMILARITY: In the N-terminal section; belongs to the KAE1 / TsaD
family. {ECO:0000256|HAMAP-Rule:MF_01447}.
-----------------------------------------------------------------------
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EMBL; LN515531; CEA13667.1; -; Genomic_DNA.
EnsemblBacteria; CEA13667; CEA13667; DSM1535_1331.
KEGG; mfi:DSM1535_1331; -.
PATRIC; fig|2162.9.peg.1364; -.
KO; K15904; -.
Proteomes; UP000032423; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0000408; C:EKC/KEOPS complex; IEA:InterPro.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
GO; GO:0061711; F:N(6)-L-threonylcarbamoyladenine synthase; IEA:UniProtKB-EC.
GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:UniProtKB-UniRule.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IEA:UniProtKB-UniRule.
HAMAP; MF_01446; Kae1; 1.
HAMAP; MF_01447; Kae1_Bud32_arch; 1.
InterPro; IPR022495; Bud32.
InterPro; IPR000905; Gcp-like_dom.
InterPro; IPR034680; Kae1/OSGEP.
InterPro; IPR017861; KAE1/TsaD.
InterPro; IPR022449; Kae1_arc.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR017860; Peptidase_M22_CS.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR009220; tRNA_threonyl_synthase/kinase.
InterPro; IPR008266; Tyr_kinase_AS.
PANTHER; PTHR11735; PTHR11735; 1.
PANTHER; PTHR11735:SF14; PTHR11735:SF14; 1.
Pfam; PF00814; Peptidase_M22; 1.
Pfam; PF00069; Pkinase; 1.
PIRSF; PIRSF036401; Gcp_STYKS; 1.
PRINTS; PR00789; OSIALOPTASE.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
TIGRFAMs; TIGR03724; arch_bud32; 1.
TIGRFAMs; TIGR03722; arch_KAE1; 1.
TIGRFAMs; TIGR00329; gcp_kae1; 1.
PROSITE; PS01016; GLYCOPROTEASE; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
3: Inferred from homology;
Acyltransferase {ECO:0000256|HAMAP-Rule:MF_01447,
ECO:0000256|SAAS:SAAS00424711};
ATP-binding {ECO:0000256|HAMAP-Rule:MF_01447};
Complete proteome {ECO:0000313|Proteomes:UP000032423};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01447,
ECO:0000256|SAAS:SAAS00424712};
Iron {ECO:0000256|HAMAP-Rule:MF_01447, ECO:0000256|SAAS:SAAS00424714};
Kinase {ECO:0000256|HAMAP-Rule:MF_01447};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_01447,
ECO:0000256|SAAS:SAAS00424706};
Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01447};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01447};
Serine/threonine-protein kinase {ECO:0000256|HAMAP-Rule:MF_01447};
Transferase {ECO:0000256|HAMAP-Rule:MF_01447,
ECO:0000256|SAAS:SAAS00424711};
tRNA processing {ECO:0000256|HAMAP-Rule:MF_01447,
ECO:0000256|SAAS:SAAS00424702}.
DOMAIN 336 547 Protein kinase.
{ECO:0000259|PROSITE:PS50011}.
NP_BIND 342 350 ATP. {ECO:0000256|HAMAP-Rule:MF_01447}.
REGION 1 327 Kae1. {ECO:0000256|HAMAP-Rule:MF_01447}.
REGION 131 135 Threonylcarbamoyl-AMP binding.
{ECO:0000256|HAMAP-Rule:MF_01447}.
ACT_SITE 462 462 Proton acceptor; for kinase activity.
{ECO:0000256|HAMAP-Rule:MF_01447}.
METAL 110 110 Iron. {ECO:0000256|HAMAP-Rule:MF_01447}.
METAL 114 114 Iron. {ECO:0000256|HAMAP-Rule:MF_01447}.
METAL 131 131 Iron. {ECO:0000256|HAMAP-Rule:MF_01447}.
METAL 288 288 Iron. {ECO:0000256|HAMAP-Rule:MF_01447}.
BINDING 163 163 Threonylcarbamoyl-AMP.
{ECO:0000256|HAMAP-Rule:MF_01447}.
BINDING 176 176 Threonylcarbamoyl-AMP; via amide
nitrogen. {ECO:0000256|HAMAP-
Rule:MF_01447}.
BINDING 180 180 Threonylcarbamoyl-AMP.
{ECO:0000256|HAMAP-Rule:MF_01447}.
BINDING 260 260 Threonylcarbamoyl-AMP.
{ECO:0000256|HAMAP-Rule:MF_01447}.
BINDING 363 363 ATP. {ECO:0000256|HAMAP-Rule:MF_01447}.
SEQUENCE 547 AA; 60309 MW; 0775497A1B0B2146 CRC64;
MYVICIGLEG TAEKTGVGIV DSDGHILALQ GRALLPEKGG IHPREAAQHH AENLVPLIKK
SLDEANLSLE DLDMVAFARG PGLGPALRTV ATAARSLALS LDVPIVGVNH CIGHIEIGRL
TTGCQDPLTL YVSGGNTQVT AFDAGRYQIF GETLDIAIGN CLDQFARTVG LGHPGGPRVE
ELALASDNYL KLPYTVKGMD LSFSGLLTAA IRKYESGAAL EDVCHSLQET AFAMLVEVTE
RALAHSKKSE VLLVGGVAAN QRLREMLEVM AQEHYAEFFM PEMKYCGDNG AMNAWLGLLM
YQNSKKMDIC DTRVKQRFRT DQVDVPWREK SPLKLKLPSE LLAKGAEANI YPDHYLGEEV
LVKKRVVKSY RIKEIDDYLR KKRTKNEAKL MAEAKRCGVV TPLVYDVDLK EYSITMEKVQ
GLEVKKIFSS EDPLDLNQIR SISRTIGENV ARLHDCGLIH GDLTTSNLIL GEDGKSVVFI
DFGLGKVSDL VEDKGVDLLV FKKAINGIHH DISQECFDHI LKGYEGARDY REVVAKIEEI
EGRGRYT


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