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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)]

 I3R619_HALMT            Unreviewed;       552 AA.
I3R619;
05-SEP-2012, integrated into UniProtKB/TrEMBL.
05-SEP-2012, sequence version 1.
10-OCT-2018, entry version 51.
RecName: Full=Probable bifunctional tRNA threonylcarbamoyladenosine biosynthesis protein {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};
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=tRNA threonylcarbamoyladenosine biosynthesis protein Kae1 {ECO:0000256|HAMAP-Rule:MF_01447};
AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein Kae1 {ECO:0000256|HAMAP-Rule:MF_01447};
Name=gcp {ECO:0000313|EMBL:AFK19679.1};
OrderedLocusNames=HFX_1986 {ECO:0000313|EMBL:AFK19679.1};
ORFNames=BM92_10670 {ECO:0000313|EMBL:AHZ23068.1},
C439_11713 {ECO:0000313|EMBL:EMA00001.1};
Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC
14739 / NCIMB 2177 / R-4) (Halobacterium mediterranei).
Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria;
Haloferacales; Haloferacaceae; Haloferax.
NCBI_TaxID=523841 {ECO:0000313|EMBL:AFK19679.1, ECO:0000313|Proteomes:UP000006469};
[1] {ECO:0000313|EMBL:AFK19679.1}
NUCLEOTIDE SEQUENCE.
STRAIN=CGMCC 1.2087 {ECO:0000313|EMBL:AFK19679.1};
PubMed=22247127; DOI=10.1128/AEM.07114-11;
Cai S., Cai L., Liu H., Liu X., Han J., Zhou J., Xiang H.;
"Identification of the haloarchaeal phasin (PhaP) that functions in
polyhydroxyalkanoate accumulation and granule formation in Haloferax
mediterranei.";
Appl. Environ. Microbiol. 78:1946-1952(2012).
[2] {ECO:0000313|EMBL:AFK19679.1, ECO:0000313|Proteomes:UP000006469}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 /
R-4 {ECO:0000313|Proteomes:UP000006469}, and
CGMCC 1.2087 {ECO:0000313|EMBL:AFK19679.1};
PubMed=22843593; DOI=10.1128/JB.00880-12;
Han J., Zhang F., Hou J., Liu X., Li M., Liu H., Cai L., Zhang B.,
Chen Y., Zhou J., Hu S., Xiang H.;
"Complete genome sequence of the metabolically versatile halophilic
archaeon Haloferax mediterranei, a poly(3-hydroxybutyrate-co-3-
hydroxyvalerate) producer.";
J. Bacteriol. 194:4463-4464(2012).
[3] {ECO:0000313|Proteomes:UP000011603}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 /
R-4 {ECO:0000313|Proteomes:UP000011603};
Becker E.A., Seitzer P., Tritt A., Larsen D., Yao A., Wu D.,
Darling A., Eisen J.A., Facciotti M.T.;
Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
[4] {ECO:0000313|EMBL:EMA00001.1}
NUCLEOTIDE SEQUENCE.
STRAIN=ATCC 33500 {ECO:0000313|EMBL:EMA00001.1};
PubMed=25393412;
Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I.,
Wu D., Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
"Phylogenetically driven sequencing of extremely halophilic archaea
reveals strategies for static and dynamic osmo-response.";
PLoS Genet. 10:E1004784-E1004784(2014).
[5] {ECO:0000313|EMBL:AHZ23068.1, ECO:0000313|Proteomes:UP000027075}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 33500 {ECO:0000313|EMBL:AHZ23068.1}, and
ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4
{ECO:0000313|Proteomes:UP000027075};
Bautista V.;
"Transcriptional profiles of Haloferax mediterranei on the basis of
nitrogen availability.";
Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
[6] {ECO:0000313|EMBL:AFK19679.1}
NUCLEOTIDE SEQUENCE.
STRAIN=CGMCC 1.2087;
Wang L., Yang H., Xiang H.;
Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
-!- 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}.
-!- 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}.
-!- 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}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01447}.
-----------------------------------------------------------------------
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EMBL; CP001868; AFK19679.1; -; Genomic_DNA.
EMBL; CP007551; AHZ23068.1; -; Genomic_DNA.
EMBL; AOLO01000009; EMA00001.1; -; Genomic_DNA.
RefSeq; WP_004059325.1; NZ_CP007551.1.
EnsemblBacteria; AFK19679; AFK19679; HFX_1986.
EnsemblBacteria; AHZ23068; AHZ23068; BM92_10670.
EnsemblBacteria; EMA00001; EMA00001; C439_11713.
GeneID; 13028147; -.
KEGG; hme:HFX_1986; -.
PATRIC; fig|523841.21.peg.2368; -.
KO; K15904; -.
OMA; GETMDTG; -.
OrthoDB; POG093Z05SV; -.
BioCyc; HMED523841:G1HBL-2743-MONOMER; -.
Proteomes; UP000006469; Chromosome.
Proteomes; UP000011603; Unassembled WGS sequence.
Proteomes; UP000027075; 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 activity; 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; IPR011009; Kinase-like_dom_sf.
InterPro; IPR017860; Peptidase_M22_CS.
InterPro; IPR009220; tRNA_threonyl_synthase/kinase.
PANTHER; PTHR11735; PTHR11735; 1.
PANTHER; PTHR11735:SF14; PTHR11735:SF14; 1.
Pfam; PF00814; Peptidase_M22; 1.
PIRSF; PIRSF036401; Gcp_STYKS; 1.
PRINTS; PR00789; OSIALOPTASE.
SUPFAM; SSF56112; SSF56112; 1.
TIGRFAMs; TIGR03724; arch_bud32; 1.
TIGRFAMs; TIGR00329; gcp_kae1; 1.
PROSITE; PS01016; GLYCOPROTEASE; 1.
3: Inferred from homology;
Acyltransferase {ECO:0000256|HAMAP-Rule:MF_01447};
ATP-binding {ECO:0000256|HAMAP-Rule:MF_01447};
Complete proteome {ECO:0000313|Proteomes:UP000006469};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01447};
Hydrolase {ECO:0000313|EMBL:AFK19679.1};
Iron {ECO:0000256|HAMAP-Rule:MF_01447};
Kinase {ECO:0000256|HAMAP-Rule:MF_01447, ECO:0000313|EMBL:AHZ23068.1};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_01447};
Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01447};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01447};
Reference proteome {ECO:0000313|Proteomes:UP000006469};
Serine/threonine-protein kinase {ECO:0000256|HAMAP-Rule:MF_01447,
ECO:0000313|EMBL:AHZ23068.1};
Transferase {ECO:0000256|HAMAP-Rule:MF_01447,
ECO:0000313|EMBL:AHZ23068.1};
tRNA processing {ECO:0000256|HAMAP-Rule:MF_01447}.
DOMAIN 42 311 Peptidase_M22.
{ECO:0000259|Pfam:PF00814}.
NP_BIND 360 368 ATP. {ECO:0000256|HAMAP-Rule:MF_01447}.
REGION 1 344 Kae1. {ECO:0000256|HAMAP-Rule:MF_01447}.
REGION 149 153 Threonylcarbamoyl-AMP binding.
{ECO:0000256|HAMAP-Rule:MF_01447}.
ACT_SITE 466 466 Proton acceptor; for kinase activity.
{ECO:0000256|HAMAP-Rule:MF_01447}.
METAL 128 128 Iron. {ECO:0000256|HAMAP-Rule:MF_01447}.
METAL 132 132 Iron. {ECO:0000256|HAMAP-Rule:MF_01447}.
METAL 305 305 Iron. {ECO:0000256|HAMAP-Rule:MF_01447}.
BINDING 181 181 Threonylcarbamoyl-AMP.
{ECO:0000256|HAMAP-Rule:MF_01447}.
BINDING 194 194 Threonylcarbamoyl-AMP; via amide
nitrogen. {ECO:0000256|HAMAP-
Rule:MF_01447}.
BINDING 198 198 Threonylcarbamoyl-AMP.
{ECO:0000256|HAMAP-Rule:MF_01447}.
BINDING 277 277 Threonylcarbamoyl-AMP.
{ECO:0000256|HAMAP-Rule:MF_01447}.
BINDING 377 377 ATP. {ECO:0000256|HAMAP-Rule:MF_01447}.
SEQUENCE 552 AA; 59480 MW; 9EF76014DBA33D8B CRC64;
MRILGIEGTA WAASAAVFET DDPDALSTET YRTPDPSADH VFIESNPYQP ESGGIHPREA
AEHMGNAIPE VVDTALAHAA DRHDGDGPIV DGVAFSRGPG LGPCLRIVGT AARAVAQTLG
VPLLGVNHMV AHLEIGRYQS GFESPVCLNA SGANAHLLGY HNGRYRVLGE TMDTGVGNSI
DKFTRHVGWT HPGGPKVEQA AKDGSYVDLP YVVKGMDFSF SGIMSAAKQE ADAGTPVEDI
CVGLQETIFA MLTEVAERAL SLTGTDELVL GGGVGQNARL REMLAEMCEQ RGAKFHAPEP
RFLRDNAGMI AVLGARMLNS GDALSVEESS VDPNFRPDQV AVTWRGADES VARAYTDDGA
IRGAEATVDI GTDEVVKRRV PKTYRHPELD DRLRRERTKA EARLTSDARR AGVRTPIVRD
VDPIEAVITF QKVGDADLAE RLSPEAARTV GEYLAKLHRV GIVHGDPTTR NVRVESGTHG
TSRVFLIDFG LGFHTDHVED HAMDLHVFAQ SVEGTADDAE PLLDALEAGY ESIGSDEVIT
RLREVESRGR YR


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