ID H1L1H7_9EURY Unreviewed; 534 AA.
AC H1L1H7;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Probable bifunctional tRNA threonylcarbamoyladenosine biosynthesis protein {ECO:0000256|HAMAP-Rule:MF_01447};
DE Includes:
DE RecName: Full=tRNA N6-adenosine threonylcarbamoyltransferase {ECO:0000256|HAMAP-Rule:MF_01447};
DE EC=2.3.1.234 {ECO:0000256|HAMAP-Rule:MF_01447};
DE AltName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein Kae1 {ECO:0000256|HAMAP-Rule:MF_01447};
DE AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein Kae1 {ECO:0000256|HAMAP-Rule:MF_01447};
DE Includes:
DE RecName: Full=Serine/threonine-protein kinase Bud32 {ECO:0000256|HAMAP-Rule:MF_01447};
DE EC=2.7.11.1 {ECO:0000256|HAMAP-Rule:MF_01447};
GN ORFNames=MetfoDRAFT_1901 {ECO:0000313|EMBL:EHP83714.1};
OS Methanotorris formicicus Mc-S-70.
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanotorris.
OX NCBI_TaxID=647171 {ECO:0000313|EMBL:EHP83714.1, ECO:0000313|Proteomes:UP000003706};
RN [1] {ECO:0000313|EMBL:EHP83714.1, ECO:0000313|Proteomes:UP000003706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mc-S-70 {ECO:0000313|EMBL:EHP83714.1,
RC ECO:0000313|Proteomes:UP000003706};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Land M.L., Hauser L., Sieprawska-Lupa M., Takai K., Miyazaki J.,
RA Whitman W., Woyke T.J.;
RT "The draft genome of Methanotorris formicicus Mc-S-70.";
RL Submitted (SEP-2011) 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:0000256|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:0000256|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:0000256|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:0000256|ARBA:ARBA00001866, ECO:0000256|HAMAP-
CC Rule:MF_01447};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01447};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000256|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:0000256|HAMAP-
CC Rule:MF_01447}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|HAMAP-Rule:MF_01447}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the KAE1 / TsaD
CC family. {ECO:0000256|HAMAP-Rule:MF_01447}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHP83714.1}.
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DR EMBL; AGJL01000078; EHP83714.1; -; Genomic_DNA.
DR RefSeq; WP_007045320.1; NZ_AGJL01000078.1.
DR AlphaFoldDB; H1L1H7; -.
DR STRING; 647171.MetfoDRAFT_1901; -.
DR PATRIC; fig|647171.4.peg.1834; -.
DR OrthoDB; 6818at2157; -.
DR Proteomes; UP000003706; Unassembled WGS sequence.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IEA:UniProtKB-UniRule.
DR CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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; IPR034680; Kae1_archaea_euk.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017860; Peptidase_M22_CS.
DR InterPro; IPR009220; tRNA_threonyl_synthase/kinase.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR NCBIfam; TIGR03724; arch_bud32; 1.
DR NCBIfam; TIGR03722; arch_KAE1; 1.
DR NCBIfam; TIGR00329; gcp_kae1; 1.
DR PANTHER; PTHR11735; TRNA N6-ADENOSINE THREONYLCARBAMOYLTRANSFERASE; 1.
DR PANTHER; PTHR11735:SF14; TRNA N6-ADENOSINE THREONYLCARBAMOYLTRANSFERASE; 1.
DR Pfam; PF01163; RIO1; 1.
DR Pfam; PF00814; TsaD; 1.
DR PIRSF; PIRSF036401; Gcp_STYKS; 1.
DR PRINTS; PR00789; OSIALOPTASE.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS01016; GLYCOPROTEASE; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315, ECO:0000256|HAMAP-
KW Rule:MF_01447};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01447};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01447};
KW Hydrolase {ECO:0000313|EMBL:EHP83714.1};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01447};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_01447};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01447};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP-
KW Rule:MF_01447};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01447}; Protease {ECO:0000313|EMBL:EHP83714.1};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|HAMAP-Rule:MF_01447};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01447};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_01447}.
FT DOMAIN 32..291
FT /note="Gcp-like"
FT /evidence="ECO:0000259|Pfam:PF00814"
FT REGION 1..323
FT /note="Kae1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01447"
FT ACT_SITE 452
FT /note="Proton acceptor; for kinase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01447"
FT BINDING 106
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01447"
FT BINDING 110
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01447"
FT BINDING 127..131
FT /ligand="L-threonylcarbamoyladenylate"
FT /ligand_id="ChEBI:CHEBI:73682"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01447"
FT BINDING 127
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01447"
FT BINDING 159
FT /ligand="L-threonylcarbamoyladenylate"
FT /ligand_id="ChEBI:CHEBI:73682"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01447"
FT BINDING 172
FT /ligand="L-threonylcarbamoyladenylate"
FT /ligand_id="ChEBI:CHEBI:73682"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01447"
FT BINDING 176
FT /ligand="L-threonylcarbamoyladenylate"
FT /ligand_id="ChEBI:CHEBI:73682"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01447"
FT BINDING 256
FT /ligand="L-threonylcarbamoyladenylate"
FT /ligand_id="ChEBI:CHEBI:73682"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01447"
FT BINDING 284
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01447"
FT BINDING 339..347
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01447"
FT BINDING 360
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01447"
SQ SEQUENCE 534 AA; 60293 MW; 9238DA6D5B941DD5 CRC64;
MICIGLEGTA EKTGVGVVTS DGEVLFNKTT IYLPPKQGIH PREAADHHAE VFPKLIKEAF
EVVDKDEIDL IAFSQGPGLG PCLRVTATAA RTLSLALKKP IIGVNHCVSH IEIGKLTTDA
EDPLTLYVSG GNTQVIAYVS NKYRVFGETL DIAIGNCLDQ FARFCNLPHP GGPYVEKLAE
KGEKLIDLPY TVKGMDISFS GLLTSAMRSY ESGERLEDVC FSLQEVAFSM LTEITERALA
HTNKPEVMLV GGVAVNNRLR EMLKIMSEEQ NVDFYVPEKQ FCGDNGAMIA WLGILQYING
KRMALEETRI IPNYRTDMVE VNWIKEMPKK KRKIPPHLIG KGAEADIKKD IYLDWDVVVK
ERIKKSYRNN ELDRLIRTRR TTREGRFLAL IKNFGIPAPY VFDVDRDKGI IVMSYIHGKL
AKDAIEDGNL DCCYDIGEII GKLHENNIIH NDLTTSNFIV GNKTYIIDFG LGKFSDLIED
KAVDLIVLKK AILTTHYNKF KEVWEKIIEG YKTYKQWEDI INYMGEVEKR ARYL
//
