PSTK_METJA
ID PSTK_METJA Reviewed; 248 AA.
AC Q58933;
DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=L-seryl-tRNA(Sec) kinase;
DE EC=2.7.1.164;
DE AltName: Full=O-phosphoseryl-tRNA(Sec) kinase;
DE Short=PSTK;
GN Name=pstK; OrderedLocusNames=MJ1538;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP FUNCTION.
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=16201757; DOI=10.1021/bi051110r;
RA Kaiser J.T., Gromadski K., Rother M., Engelhardt H., Rodnina M.V.,
RA Wahl M.C.;
RT "Structural and functional investigation of a putative archaeal
RT selenocysteine synthase.";
RL Biochemistry 44:13315-13327(2005).
CC -!- FUNCTION: Specifically phosphorylates seryl-tRNA(Sec) to O-
CC phosphoseryl-tRNA(Sec), an activated intermediate for selenocysteine
CC biosynthesis. {ECO:0000269|PubMed:16201757}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-tRNA(Sec) = ADP + O-phospho-L-seryl-tRNA(Sec);
CC Xref=Rhea:RHEA:25037, Rhea:RHEA-COMP:9742, Rhea:RHEA-COMP:9947,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:78533, ChEBI:CHEBI:78551,
CC ChEBI:CHEBI:456216; EC=2.7.1.164;
CC -!- PATHWAY: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec)
CC biosynthesis; selenocysteinyl-tRNA(Sec) from L-seryl-tRNA(Sec)
CC (archaeal/eukaryal route): step 1/2.
CC -!- SIMILARITY: Belongs to the L-seryl-tRNA(Sec) kinase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB99557.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L77117; AAB99557.1; ALT_INIT; Genomic_DNA.
DR PIR; A64492; A64492.
DR RefSeq; WP_064496861.1; NC_000909.1.
DR PDB; 3A4L; X-ray; 1.80 A; A/B=1-248.
DR PDB; 3A4M; X-ray; 1.79 A; A/B=1-248.
DR PDB; 3A4N; X-ray; 2.50 A; A/B=1-248.
DR PDB; 3ADB; X-ray; 2.80 A; A/B=1-248.
DR PDB; 3ADC; X-ray; 2.90 A; A/B=1-248.
DR PDB; 3ADD; X-ray; 2.40 A; A/B=1-248.
DR PDB; 3AM1; X-ray; 2.40 A; A=1-248.
DR PDBsum; 3A4L; -.
DR PDBsum; 3A4M; -.
DR PDBsum; 3A4N; -.
DR PDBsum; 3ADB; -.
DR PDBsum; 3ADC; -.
DR PDBsum; 3ADD; -.
DR PDBsum; 3AM1; -.
DR AlphaFoldDB; Q58933; -.
DR SMR; Q58933; -.
DR DIP; DIP-48971N; -.
DR STRING; 243232.MJ_1538; -.
DR PRIDE; Q58933; -.
DR EnsemblBacteria; AAB99557; AAB99557; MJ_1538.
DR GeneID; 1452446; -.
DR KEGG; mja:MJ_1538; -.
DR eggNOG; arCOG01041; Archaea.
DR HOGENOM; CLU_1100964_0_0_2; -.
DR InParanoid; Q58933; -.
DR OMA; RESFPVW; -.
DR OrthoDB; 67618at2157; -.
DR PhylomeDB; Q58933; -.
DR BioCyc; MetaCyc:MON-14956; -.
DR BRENDA; 2.7.1.164; 3260.
DR UniPathway; UPA00906; UER00897.
DR EvolutionaryTrace; Q58933; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0043915; F:L-seryl-tRNA(Sec) kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0097056; P:selenocysteinyl-tRNA(Sec) biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR013641; KTI12/PSTK.
DR InterPro; IPR020024; L-seryl-tRNA_Sec_kinase_arc.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF08433; KTI12; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR03574; selen_PSTK; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..248
FT /note="L-seryl-tRNA(Sec) kinase"
FT /id="PRO_0000107396"
FT BINDING 7..14
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT STRAND 1..6
FT /evidence="ECO:0007829|PDB:3A4M"
FT HELIX 13..26
FT /evidence="ECO:0007829|PDB:3A4M"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:3A4M"
FT HELIX 37..40
FT /evidence="ECO:0007829|PDB:3A4M"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:3A4M"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:3A4M"
FT HELIX 51..66
FT /evidence="ECO:0007829|PDB:3A4M"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:3A4M"
FT HELIX 80..92
FT /evidence="ECO:0007829|PDB:3A4M"
FT STRAND 96..103
FT /evidence="ECO:0007829|PDB:3A4M"
FT HELIX 106..115
FT /evidence="ECO:0007829|PDB:3A4M"
FT HELIX 122..131
FT /evidence="ECO:0007829|PDB:3A4M"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:3A4M"
FT STRAND 145..149
FT /evidence="ECO:0007829|PDB:3A4M"
FT HELIX 156..167
FT /evidence="ECO:0007829|PDB:3A4M"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:3ADD"
FT HELIX 186..205
FT /evidence="ECO:0007829|PDB:3A4M"
FT HELIX 209..227
FT /evidence="ECO:0007829|PDB:3A4M"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:3ADC"
FT HELIX 234..247
FT /evidence="ECO:0007829|PDB:3A4M"
SQ SEQUENCE 248 AA; 29467 MW; 815EF9A453BEA450 CRC64;
MLIILTGLPG VGKSTFSKNL AKILSKNNID VIVLGSDLIR ESFPVWKEKY EEFIKKSTYR
LIDSALKNYW VIVDDTNYYN SMRRDLINIA KKYNKNYAII YLKASLDVLI RRNIERGEKI
PNEVIKKMYE KFDEPGKKYK WDEPFLIIDT TKDIDFNEIA KKLIEKSKEI PKFYVLEENK
NKNNNISDKI DKETRKIVSE YIKSKKLDKD KIKEVVELRK EFLKKIKKME EVDADRVLKE
FKDLLNSY
