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PSTK_METMP
ID   PSTK_METMP              Reviewed;         255 AA.
AC   Q6LX62;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=MMP1490;
OS   Methanococcus maripaludis (strain S2 / LL).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=267377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S2 / LL;
RX   PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA   Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA   Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA   Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA   Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA   Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA   Olson M.V., Leigh J.A.;
RT   "Complete genome sequence of the genetically tractable hydrogenotrophic
RT   methanogen Methanococcus maripaludis.";
RL   J. Bacteriol. 186:6956-6969(2004).
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}.
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DR   EMBL; BX950229; CAF31046.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6LX62; -.
DR   SMR; Q6LX62; -.
DR   STRING; 267377.MMP1490; -.
DR   EnsemblBacteria; CAF31046; CAF31046; MMP1490.
DR   KEGG; mmp:MMP1490; -.
DR   PATRIC; fig|267377.15.peg.1527; -.
DR   eggNOG; arCOG01041; Archaea.
DR   HOGENOM; CLU_1100964_0_0_2; -.
DR   OMA; RESFPVW; -.
DR   UniPathway; UPA00906; UER00897.
DR   Proteomes; UP000000590; 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_0000285592"
FT   BINDING         7..14
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   255 AA;  29776 MW;  6E59548199C8B62F CRC64;
     MLIILTGLPS VGKSTFSKAF SKKMAEKNID NIILGTDLIR ESFPVWKESY EEFIRDSNNY
     LIKEALENKF SVIVDDTNYY NSKRRDLMNI AKECDTNYVT IYLKAPLNLL LKRNIERGQK
     IPNEVIKNMY EKFDTPGTKY AWDLPDITVD TTEKIDYNEI LNEILEINEN KNLKIEEDKI
     PKSEPVESDL VKIDSLTRNI VGNLIKTGKI DKKDIKLLSE IRKSFLKDCK KIESEKLDFE
     KIEKDFLDYL NKNLK
 
 
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