ID   PSTK_METKA              Reviewed;         255 AA.
AC   Q8TUS5;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=MK1679;
OS   Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC   Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae;
OC   Methanopyrus.
OX   NCBI_TaxID=190192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX   PubMed=11930014; DOI=10.1073/pnas.032671499;
RA   Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA   Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA   Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA   Koonin E.V., Kozyavkin S.A.;
RT   "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT   monophyly of archaeal methanogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
CC   -!- FUNCTION: Specifically phosphorylates seryl-tRNA(Sec) to O-
CC       phosphoseryl-tRNA(Sec), an activated intermediate for selenocysteine
CC       biosynthesis. {ECO:0000250}.
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE009439; AAM02892.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8TUS5; -.
DR   SMR; Q8TUS5; -.
DR   STRING; 190192.MK1679; -.
DR   EnsemblBacteria; AAM02892; AAM02892; MK1679.
DR   KEGG; mka:MK1679; -.
DR   HOGENOM; CLU_1100964_0_0_2; -.
DR   OMA; RESFPVW; -.
DR   UniPathway; UPA00906; UER00897.
DR   Proteomes; UP000001826; 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   3: Inferred from homology;
KW   ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN           1..255
FT                   /note="L-seryl-tRNA(Sec) kinase"
FT                   /id="PRO_0000285593"
FT   BINDING         8..15
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   255 AA;  29790 MW;  DC44E95EDF2A58B2 CRC64;
     MRLLILTGPP GSGKTCFARE LARELRQEGW RVAHVEADAL RGFLWDEFDP KLEQVARELF
     LKSVETCLDA ELDLVIADDT NYYSSMRREL ALLALERKVP WGIVYLRTGL DTCLRRNRER
     GEPIPEEVVR RIYDRFEPPE PDRWWERATL VLDDSRVSEE VLEFVESGLR VEKPKKRRRR
     TDPSSVNEVD VRTRQVMGEL MRRLSETGAA TQELGRKLSE LRREIVSSVE DPEKAVREFR
     RRAEEVIREC LHGDG