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ATP + L-seryl-tRNASec
ADP + O-phospho-L-seryl-tRNASec
ATP + L-seryl-tRNASec
O-phospho-L-seryl-tRNASec + ADP
ATP + seryl-tRNASec
ADP + O-phospho-L-seryl-tRNASec
CTP + L-seryl-tRNASec
CDP + O-phospho-L-seryl-tRNASec
dATP + L-seryl-tRNASec
dADP + O-phospho-L-seryl-tRNASec
GTP + L-seryl-tRNASec
GDP + O-phospho-L-seryl-tRNASec
phosphorylation at about 40% the activity of ATP
-
-
?
ITP + L-seryl-tRNASec
IDP + O-phospho-L-seryl-tRNASec
phosphorylation at about 85% the activity of ATP
-
-
?
L-threonyl-tRNASec + ATP
O-phospho-L-threonyl-tRNASec + ADP
UTP + L-seryl-tRNASec
UDP + O-phospho-L-seryl-tRNASec
phosphorylation at about 40% the activity of ATP
-
-
?
additional information
?
-
ATP + L-seryl-tRNASec
ADP + O-phospho-L-seryl-tRNASec
-
-
-
-
?
ATP + L-seryl-tRNASec
ADP + O-phospho-L-seryl-tRNASec
-
-
-
-
?
ATP + L-seryl-tRNASec
ADP + O-phospho-L-seryl-tRNASec
-
-
-
?
ATP + L-seryl-tRNASec
ADP + O-phospho-L-seryl-tRNASec
-
-
-
-
?
ATP + L-seryl-tRNASec
ADP + O-phospho-L-seryl-tRNASec
-
-
-
?
ATP + L-seryl-tRNASec
ADP + O-phospho-L-seryl-tRNASec
L-phosphoseryl-tRNA is the crucial precursor for L-selenocysteinyl-tRNA formation in archaea and eukarya. Selenocysteine formation is achieved by a two-step process: O-phosphoseryl-tRNASec kinase (PSTK) phosphorylates the endogenous Ser-tRNASec to O-phosphoseryl-tRNASec, and then this misacylated amino acid-tRNA species is converted to L-selenocysteinyl-tRNASec by Sep-tRNA:Sec-tRNA synthase (SepSecS)
-
-
?
ATP + L-seryl-tRNASec
ADP + O-phospho-L-seryl-tRNASec
the enzyme does not recognize free Ser as a substrate for phosphate transfer. Ser attached to tRNASec is its obligate substrate. Neither tRNASer nor L-seryl-tRNASer is a substrate for phosphorylation
-
-
?
ATP + L-seryl-tRNASec
ADP + O-phospho-L-seryl-tRNASec
-
-
-
?
ATP + L-seryl-tRNASec
ADP + O-phospho-L-seryl-tRNASec
L-phosphoseryl-tRNA is the crucial precursor for L-selenocysteinyl-tRNA formation in archaea and eukarya. Selenocysteine formation is achieved by a two-step process: O-phosphoseryl-tRNASec kinase (PSTK) phosphorylates the endogenous Ser-tRNASec to O-phosphoseryl-tRNASec, and then this misacylated amino acid-tRNA species is converted to L-selenocysteinyl-tRNASec by Sep-tRNA:Sec-tRNA synthase (SepSecS)
-
-
?
ATP + L-seryl-tRNASec
ADP + O-phospho-L-seryl-tRNASec
-
-
-
?
ATP + L-seryl-tRNASec
ADP + O-phospho-L-seryl-tRNASec
the enzyme does not recognize free Ser as a substrate for phosphate transfer. Ser attached to tRNASec is its obligate substrate. Neither tRNASer nor L-seryl-tRNASer is a substrate for phosphorylation
-
-
?
ATP + L-seryl-tRNASec
ADP + O-phospho-L-seryl-tRNASec
Pstk is a limiting factor for hepatic selenoprotein biosynthesis, and its mRNA expression is most strongly affected during the lipopolysaccharide (LPS)-induced acute-phase response
-
-
?
ATP + L-seryl-tRNASec
ADP + O-phospho-L-seryl-tRNASec
about 30% of O-phospho-L-seryltRNA[Ser]Sec is converted to L-seryl-tRNA[Ser]Sec and ATP during the course of the reaction. The kinase is specific for the two major isoforms of O-phospho-L-seryl-tRNA[Ser]Sec. Seryl-tRNA1Ser does not serve as a substrate for PSTK
-
-
r
ATP + L-seryl-tRNASec
ADP + O-phospho-L-seryl-tRNASec
-
-
-
-
?
ATP + L-seryl-tRNASec
ADP + O-phospho-L-seryl-tRNASec
-
null mutants of PSTK abolish selenoprotein synthesis, demonstrating the essentiality of the enzyme for the formation of L-selenocysteinyl-tRNASec. Growth of the knockout strain is not impaired. Thus, unlike mammals, trypanosomes do not require selenoproteins for viability
-
-
?
ATP + L-seryl-tRNASec
ADP + O-phospho-L-seryl-tRNASec
-
-
-
?
ATP + L-seryl-tRNASec
ADP + O-phospho-L-seryl-tRNASec
-
-
-
?
ATP + L-seryl-tRNASec
O-phospho-L-seryl-tRNASec + ADP
PSTK distinguishes tRNASec from tRNASer. Unlike eukaryotic PSTK, the archaeal enzyme recognizes the acceptor stem rather than the length and secondary structure of the D-stem. The seryl moiety of L-seryl-tRNASec is not required for enzyme recognition, as PSTK efficiently phosphorylates L-threonyl-tRNASec
-
-
?
ATP + L-seryl-tRNASec
O-phospho-L-seryl-tRNASec + ADP
PSTK distinguishes tRNASec from tRNASer. Unlike eukaryotic PSTK, the archaeal enzyme recognizes the acceptor stem rather than the length and secondary structure of the D-stem. The seryl moiety of L-seryl-tRNASec is not required for enzyme recognition, as PSTK efficiently phosphorylates L-threonyl-tRNASec
-
-
?
ATP + seryl-tRNASec
ADP + O-phospho-L-seryl-tRNASec
L-phosphoseryl-tRNA is the crucial precursor for L-selenocysteinyl-tRNA formation in archaea and eukarya. Selenocysteine formation is achieved by a two-step process: O-phosphoseryl-tRNASec kinase (PSTK) phosphorylates the endogenous Ser-tRNASec to O-phosphoseryl-tRNASec, and then this misacylated amino acid-tRNA species is converted to L-selenocysteinyl-tRNASec by Sep-tRNA:Sec-tRNA synthase (SepSecS)
-
-
?
ATP + seryl-tRNASec
ADP + O-phospho-L-seryl-tRNASec
L-phosphoseryl-tRNA is the crucial precursor for L-selenocysteinyl-tRNA formation in archaea and eukarya. Selenocysteine formation is achieved by a two-step process: O-phosphoseryl-tRNASec kinase (PSTK) phosphorylates the endogenous Ser-tRNASec to O-phosphoseryl-tRNASec, and then this misacylated amino acid-tRNA species is converted to L-selenocysteinyl-tRNASec by Sep-tRNA:Sec-tRNA synthase (SepSecS)
-
-
?
CTP + L-seryl-tRNASec
CDP + O-phospho-L-seryl-tRNASec
phosphorylation at about 60% the activity of ATP
-
-
?
CTP + L-seryl-tRNASec
CDP + O-phospho-L-seryl-tRNASec
phosphorylation at about 60% the activity of ATP
-
-
?
dATP + L-seryl-tRNASec
dADP + O-phospho-L-seryl-tRNASec
phosphorylation at about 65% the activity of ATP
-
-
?
dATP + L-seryl-tRNASec
dADP + O-phospho-L-seryl-tRNASec
phosphorylation at about 65% the activity of ATP
-
-
?
L-threonyl-tRNASec + ATP
O-phospho-L-threonyl-tRNASec + ADP
-
-
-
?
L-threonyl-tRNASec + ATP
O-phospho-L-threonyl-tRNASec + ADP
-
-
-
?
additional information
?
-
no phosphorylation activity with 5'-adenylyl (beta,gamma-methylene)diphosphonate, very low phosphorylation activity with alpha,beta-methyleneadenosine 5'-triphosphate
-
-
?
additional information
?
-
-
no phosphorylation activity with 5'-adenylyl (beta,gamma-methylene)diphosphonate, very low phosphorylation activity with alpha,beta-methyleneadenosine 5'-triphosphate
-
-
?
additional information
?
-
no phosphorylation activity with 5'-adenylyl (beta,gamma-methylene)diphosphonate, very low phosphorylation activity with alpha,beta-methyleneadenosine 5'-triphosphate
-
-
?
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ATP + L-seryl-tRNASec
ADP + O-phospho-L-seryl-tRNASec
ATP + seryl-tRNASec
ADP + O-phospho-L-seryl-tRNASec
ATP + L-seryl-tRNASec
ADP + O-phospho-L-seryl-tRNASec
-
-
-
-
?
ATP + L-seryl-tRNASec
ADP + O-phospho-L-seryl-tRNASec
-
-
-
-
?
ATP + L-seryl-tRNASec
ADP + O-phospho-L-seryl-tRNASec
-
-
-
?
ATP + L-seryl-tRNASec
ADP + O-phospho-L-seryl-tRNASec
-
-
-
-
?
ATP + L-seryl-tRNASec
ADP + O-phospho-L-seryl-tRNASec
-
-
-
?
ATP + L-seryl-tRNASec
ADP + O-phospho-L-seryl-tRNASec
-
-
-
?
ATP + L-seryl-tRNASec
ADP + O-phospho-L-seryl-tRNASec
Pstk is a limiting factor for hepatic selenoprotein biosynthesis, and its mRNA expression is most strongly affected during the lipopolysaccharide (LPS)-induced acute-phase response
-
-
?
ATP + L-seryl-tRNASec
ADP + O-phospho-L-seryl-tRNASec
-
null mutants of PSTK abolish selenoprotein synthesis, demonstrating the essentiality of the enzyme for the formation of L-selenocysteinyl-tRNASec. Growth of the knockout strain is not impaired. Thus, unlike mammals, trypanosomes do not require selenoproteins for viability
-
-
?
ATP + L-seryl-tRNASec
ADP + O-phospho-L-seryl-tRNASec
-
-
-
?
ATP + L-seryl-tRNASec
ADP + O-phospho-L-seryl-tRNASec
-
-
-
?
ATP + seryl-tRNASec
ADP + O-phospho-L-seryl-tRNASec
L-phosphoseryl-tRNA is the crucial precursor for L-selenocysteinyl-tRNA formation in archaea and eukarya. Selenocysteine formation is achieved by a two-step process: O-phosphoseryl-tRNASec kinase (PSTK) phosphorylates the endogenous Ser-tRNASec to O-phosphoseryl-tRNASec, and then this misacylated amino acid-tRNA species is converted to L-selenocysteinyl-tRNASec by Sep-tRNA:Sec-tRNA synthase (SepSecS)
-
-
?
ATP + seryl-tRNASec
ADP + O-phospho-L-seryl-tRNASec
L-phosphoseryl-tRNA is the crucial precursor for L-selenocysteinyl-tRNA formation in archaea and eukarya. Selenocysteine formation is achieved by a two-step process: O-phosphoseryl-tRNASec kinase (PSTK) phosphorylates the endogenous Ser-tRNASec to O-phosphoseryl-tRNASec, and then this misacylated amino acid-tRNA species is converted to L-selenocysteinyl-tRNASec by Sep-tRNA:Sec-tRNA synthase (SepSecS)
-
-
?
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malfunction
knockdown of TbPSTK impairs selenoprotein synthesis in the parasite procyclic form (PCF). TbPSTK and TbSEPSECS double-knockout cell lines demonstrate that Trypanosoma brucei parasite procyclic form does not depend on selenoproteins
malfunction
-
knockdown of TbPSTK impairs selenoprotein synthesis in the parasite procyclic form (PCF). TbPSTK and TbSEPSECS double-knockout cell lines demonstrate that Trypanosoma brucei parasite procyclic form does not depend on selenoproteins
-
metabolism
the enzyme is involved in the selenocysteine incorporation pathway in this primitive eukaryote
metabolism
-
the synthesis of selenocysteine, the 21st amino acid, occurs on its transfer RNA, tRNASec. tRNASec is initially aminoacylated with serine by seryl-tRNA synthetase and the resulting seryl moiety is converted to phosphoserine by O-phosphoseryl-tRNA kinase (PSTK) in eukaryotes. The selenium donor, selenophosphate is synthesized from selenide and ATP by selenophosphate synthetase. Selenocysteinyl-tRNA synthase (Sep-SecS) then uses the O-phosphoseryl-tRNASec and selenophosphate to form Sec-tRNASec in eukaryotes. Leishmania SepSecS enzyme is active and able to complement the DELTAselA deletion in Escherichia coli JS1 strain only in the presence of archaeal PSTK, indicating the conserved nature of the PSTK-SepSecS pathway, selenocysteinyl-tRNA synthase is dependent on the action of PSTK enzyme in the Sec insertion pathway
metabolism
selenocysteine biosynthesis and incorporation into selenoproteins require an intricate molecular machinery that is present, but not ubiquitous, in all domains of life. In eukaryotes it begins with tRNA[Ser]Sec acylation with L-serine by the seryl-tRNA synthetase (SerRS) followed by its conversion to Sec-tRNA[Ser]Sec, sequentially catalyzed by phosphoseryl-tRNASec kinase (PSTK) and Sec-tRNA[Ser]Sec synthase (SEPSECS). Selenophosphate synthetase (SEPHS) is a key enzyme in the Sec pathway, being responsible for catalyzing the formation of the active selenium donor for this reaction, selenophosphate, from selenide and ATP. Enzyme phosphoseryl-tRNASec kinase (PSTK) forms a stable complex with the Sec-tRNASec synthase (SEPSECS)
metabolism
-
the enzyme is involved in the selenocysteine incorporation pathway in this primitive eukaryote
-
metabolism
-
the synthesis of selenocysteine, the 21st amino acid, occurs on its transfer RNA, tRNASec. tRNASec is initially aminoacylated with serine by seryl-tRNA synthetase and the resulting seryl moiety is converted to phosphoserine by O-phosphoseryl-tRNA kinase (PSTK) in eukaryotes. The selenium donor, selenophosphate is synthesized from selenide and ATP by selenophosphate synthetase. Selenocysteinyl-tRNA synthase (Sep-SecS) then uses the O-phosphoseryl-tRNASec and selenophosphate to form Sec-tRNASec in eukaryotes. Leishmania SepSecS enzyme is active and able to complement the DELTAselA deletion in Escherichia coli JS1 strain only in the presence of archaeal PSTK, indicating the conserved nature of the PSTK-SepSecS pathway, selenocysteinyl-tRNA synthase is dependent on the action of PSTK enzyme in the Sec insertion pathway
-
metabolism
-
selenocysteine biosynthesis and incorporation into selenoproteins require an intricate molecular machinery that is present, but not ubiquitous, in all domains of life. In eukaryotes it begins with tRNA[Ser]Sec acylation with L-serine by the seryl-tRNA synthetase (SerRS) followed by its conversion to Sec-tRNA[Ser]Sec, sequentially catalyzed by phosphoseryl-tRNASec kinase (PSTK) and Sec-tRNA[Ser]Sec synthase (SEPSECS). Selenophosphate synthetase (SEPHS) is a key enzyme in the Sec pathway, being responsible for catalyzing the formation of the active selenium donor for this reaction, selenophosphate, from selenide and ATP. Enzyme phosphoseryl-tRNASec kinase (PSTK) forms a stable complex with the Sec-tRNASec synthase (SEPSECS)
-
physiological function
the enzyme is involved in the biosynthesis of selenocysteine
physiological function
-
the enzyme is essential in the selenocysteine insertion
physiological function
-
the enzyme is involved in the biosynthesis of selenocysteine
-
physiological function
-
the enzyme is essential in the selenocysteine insertion
-
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PSTK_HUMAN
348
0
39527
Swiss-Prot
other Location (Reliability: 3)
PSTK_METJA
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
248
0
29467
Swiss-Prot
-
PSTK_METKA
Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)
255
0
29790
Swiss-Prot
-
PSTK_METMP
Methanococcus maripaludis (strain S2 / LL)
255
0
29776
Swiss-Prot
-
PSTK_MOUSE
359
0
40763
Swiss-Prot
Mitochondrion (Reliability: 5)
A0A8B6EWS6_MYTGA
344
0
39024
TrEMBL
other Location (Reliability: 2)
A0A5E4HF10_9ARCH
288
0
33547
TrEMBL
-
A0A401HQK0_9EURY
256
0
30574
TrEMBL
-
I2CRI4_NANGC
Nannochloropsis gaditana (strain CCMP526)
338
0
38401
TrEMBL
Secretory Pathway (Reliability: 5)
A0A113QNR3_PLABE
540
0
65699
TrEMBL
other Location (Reliability: 3)
A0A5E4LRV1_9ARCH
162
0
18378
TrEMBL
-
A0A8J7S1L6_METVO
271
0
31932
TrEMBL
-
B2GUE1_XENTR
374
0
42183
TrEMBL
Mitochondrion (Reliability: 3)
A0A1Q9NL27_THOAA
Thorarchaeota archaeon (strain AB_25)
249
0
28793
TrEMBL
-
A0A7J9SC54_METMI
255
0
29760
TrEMBL
-
A0A150J3M2_9EURY
164
0
18971
TrEMBL
-
A0A7J9P458_METMI
255
0
29612
TrEMBL
-
A0A6J8F0S9_MYTCO
311
0
35192
TrEMBL
other Location (Reliability: 3)
A0A1G4GRF0_PLAVI
575
0
67554
TrEMBL
other Location (Reliability: 3)
A0A7J9NFY9_METMI
257
0
30210
TrEMBL
-
A0A150JG54_9EURY
164
0
19050
TrEMBL
-
A0A7J9PFK0_METMI
257
0
29823
TrEMBL
-
A0A812CY58_SEPPH
290
0
33354
TrEMBL
other Location (Reliability: 1)
Q8I2A3_PLAF7
535
0
65607
TrEMBL
other Location (Reliability: 3)
A0A832T4X8_9EURY
248
0
29467
TrEMBL
-
A0A060RMT0_PLARE
541
0
66466
TrEMBL
other Location (Reliability: 3)
A0A653HND1_9APIC
538
0
65667
TrEMBL
other Location (Reliability: 3)
A0A6J8F3N9_MYTCO
328
0
37593
TrEMBL
other Location (Reliability: 3)
A0A7J9NS51_METMI
255
0
29814
TrEMBL
-
A0A7R8D6V8_LEPSM
142
0
16076
TrEMBL
other Location (Reliability: 2)
A0A1D3LAU9_PLACH
540
0
64397
TrEMBL
other Location (Reliability: 4)
A0A8D6SY69_9EURY
250
0
29739
TrEMBL
-
A0A5B9DD47_9ARCH
295
0
34495
TrEMBL
-
A0A7J9NZ39_METMI
257
0
29923
TrEMBL
-
A0A7J9NQL8_METMI
255
0
29823
TrEMBL
-
A0A833E461_9EURY
257
0
31085
TrEMBL
-
A0A832ZYL8_9EURY
251
0
29910
TrEMBL
-
A0A1A7W2Z0_PLAKH
535
0
64116
TrEMBL
other Location (Reliability: 2)
A0A1J1GLT9_PLAGA
507
0
63071
TrEMBL
other Location (Reliability: 3)
A0A1V6INE5_9EURY
164
0
19050
TrEMBL
-
A0A6J8F3T5_MYTCO
344
0
39386
TrEMBL
other Location (Reliability: 3)
A0A679KT63_PLAKH
535
0
64116
TrEMBL
other Location (Reliability: 2)
A0A1Z5JEZ8_FISSO
336
0
38662
TrEMBL
other Location (Reliability: 2)
A0A150J0A4_9EURY
164
0
18795
TrEMBL
-
A0A1C6X1V3_PLACH
540
0
64381
TrEMBL
other Location (Reliability: 4)
A0A078K5T6_PLAYE
572
0
68354
TrEMBL
other Location (Reliability: 4)
A0A7J9P9G5_METMI
257
0
29973
TrEMBL
-
A0A8D6PVD9_9EURY
254
0
30098
TrEMBL
-
A0A1G4H6Y2_PLAVI
575
0
67524
TrEMBL
other Location (Reliability: 3)
A0A1D3LEB4_PLACH
540
0
64498
TrEMBL
other Location (Reliability: 4)
A0A7J4EXH5_9EURY
257
0
31085
TrEMBL
-
A0A061ICD5_CRIGR
358
0
40702
TrEMBL
other Location (Reliability: 4)
A0A061IEX8_CRIGR
346
0
39127
TrEMBL
other Location (Reliability: 4)
A0A8B6EY34_MYTGA
352
0
39753
TrEMBL
other Location (Reliability: 2)
A0A7J9PRC1_METMI
257
0
29883
TrEMBL
-
A0A7J9S5M1_METMI
257
0
29977
TrEMBL
-
A0A7J9RYE8_METMI
255
0
29710
TrEMBL
-
A0A150IWP6_9EURY
164
0
19011
TrEMBL
-
A0A832TC21_9EURY
255
0
29790
TrEMBL
-
A0A832Z7D6_9EURY
257
0
31051
TrEMBL
-
A0A1Z5KNE8_FISSO
336
0
38716
TrEMBL
other Location (Reliability: 1)
A0A1C6X7T0_PLACH
540
0
64469
TrEMBL
other Location (Reliability: 4)
D2V263_NAEGR
284
0
33243
TrEMBL
-
Q38A45_TRYB2
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
360
0
40101
TrEMBL
-
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D146A
mutant is active in vivo
D41A
strongly reduced activity
G14W
strongly reduced activity
K142A
mutant is active in vivo
K142A/Y143A
mutant shows severely reduced activity with the Methanopyrus kandleri tRNASec substrate
K30A
mutant is defective in phosphorylation activity
N161A
mutant is defective in phosphorylation activity
R116A
mutant enzyme is 23.5fold less active than wild-type enzyme
R120A
strongly reduced activity
T19W
mutant enzyme is 2.8fold less active than wild-type enzyme
W145A
mutant is active in vivo
D146A
-
mutant is active in vivo
-
G14W
-
strongly reduced activity
-
K142A
-
mutant is active in vivo
-
K17A
-
strongly reduced activity
-
K30A
-
mutant is defective in phosphorylation activity
-
R116A
-
mutant enzyme is 23.5fold less active than wild-type enzyme
-
T19W
-
mutant enzyme is 2.8fold less active than wild-type enzyme
-
K17A
strongly reduced activity
K17A
mutation abolishes catalytic activity and and inhibits tRNASec recognition
S18A
strongly reduced activity
S18A
mutation abolishes catalytic activity and and inhibits tRNASec recognition
S18A
-
mutation abolishes catalytic activity and and inhibits tRNASec recognition
-
S18A
-
strongly reduced activity
-
additional information
truncation of the C-termional domain. Deletions of up to 98 amino acids, PSTK1-153, still show activity, albeit at a much reduced level of about 6% of the initial velocity of the intact enzyme. In vivo, PSTK1-153 is still able compensate for the Escherichia coli selA deletion. Truncation PSTK1-192 lacks the entire CTD domain and exhibits 40% residual activity. PSTK1-215 and PSTK1-240 mutants lack the terminal two and one helices of the helix bundle, respectively. PSTK1-215 mutant shows remarkably reduced activity
additional information
-
truncation of the C-termional domain. Deletions of up to 98 amino acids, PSTK1-153, still show activity, albeit at a much reduced level of about 6% of the initial velocity of the intact enzyme. In vivo, PSTK1-153 is still able compensate for the Escherichia coli selA deletion. Truncation PSTK1-192 lacks the entire CTD domain and exhibits 40% residual activity. PSTK1-215 and PSTK1-240 mutants lack the terminal two and one helices of the helix bundle, respectively. PSTK1-215 mutant shows remarkably reduced activity
additional information
-
truncation of the C-termional domain. Deletions of up to 98 amino acids, PSTK1-153, still show activity, albeit at a much reduced level of about 6% of the initial velocity of the intact enzyme. In vivo, PSTK1-153 is still able compensate for the Escherichia coli selA deletion. Truncation PSTK1-192 lacks the entire CTD domain and exhibits 40% residual activity. PSTK1-215 and PSTK1-240 mutants lack the terminal two and one helices of the helix bundle, respectively. PSTK1-215 mutant shows remarkably reduced activity
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Kaiser, J.T.; Gromadski, K.; Rother, M.; Engelhardt, H.; Rodnina, M.V.; Wahl, M.C.
Structural and functional investigation of a putative archaeal selenocysteine synthase
Biochemistry
44
13315-13327
2005
Methanocaldococcus jannaschii (Q58933), Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661 (Q58933)
brenda
Renko, K.; Hofmann, P.J.; Stoedter, M.; Hollenbach, B.; Behrends. T.; Khrle, J.; Schweizer, U.; Schomburg, L.
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Mus musculus (Q8BP74)
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Sherrer, R.L.; O'Donoghue, P.; Sll D.
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Methanocaldococcus jannaschii (Q58933), Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661 (Q58933)
brenda
Sherrer, R.L.; Ho, J.M.; Sll, D.
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Methanocaldococcus jannaschii (Q58933), Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661 (Q58933)
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Carlson, B.A.; Xu, X.M.; Kryukov, G.V.; Rao, M.; Berry, M.J.; Gladyshev, V.N.; Hatfield, D.L.
Identification and characterization of posphoseryl-tRNA[Ser]Sec kinase
Proc. Natl. Acad. Sci. USA
101
12848-12853
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Mus musculus (Q8BP74), Mus musculus
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Yuan, J.; Palioura, S.; Salazar, J.C.; Su, D.; O'Donoghue, P.; Hohn, M.J.; Cardoso, A.M.; Whitman, W.B.; Sll, D.
RNA-dependent conversion of phosphoserine forms selenocysteine in eukaryotes and archaea
Proc. Natl. Acad. Sci. USA
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2006
Methanocaldococcus jannaschii (Q58933), Methanocaldococcus jannaschii DSM 2661 (Q58933)
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Aeby, E.; Palioura, S.; Pusnik, M.; Marazzi, J.; Lieberman, A.; Ullu, E.; Sll, D.; Schneider, A.
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Proc. Natl. Acad. Sci. USA
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5088-5092
2009
Trypanosoma brucei
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Chiba, S.; Itoh, Y.; Sekine, S.; Yokoyama, S.
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Mol. Cell
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Methanocaldococcus jannaschii (Q58933), Methanocaldococcus jannaschii DSM 2661 (Q58933)
brenda
Sherrer, R.L.; Araiso, Y.; Aldag, C.; Ishitani, R.; Ho, J.M.; Soell, D.; Nureki, O.
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Nucleic Acids Res.
39
1034-1041
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Methanocaldococcus jannaschii (Q58933), Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661 (Q58933)
brenda
Araiso, Y.; Sherrer, R.L.; Ishitani, R.; Ho, J.M.; Sll, D.; Nureki, O.
Structure of a tRNA-dependent kinase essential for selenocysteine decoding
Proc. Natl. Acad. Sci. USA
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16215-16220
2009
Methanocaldococcus jannaschii (Q58933), Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661 (Q58933)
brenda
Manhas, R.; Gowri, V.S.; Madhubala, R.
Leishmania donovani encodes a functional selenocysteinyl-tRNA synthase
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291
1203-1220
2016
Leishmania donovani
brenda
da Silva, M.T.; Caldas, V.E.; Costa, F.C.; Silvestre, D.A.; Thiemann, O.H.
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87-90
2013
Naegleria gruberi (D2V263), Naegleria gruberi ATCC 30224 (D2V263)
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da Silva, M.; E. Silva, I.; Faim, L.; Bellini, N.; Pereira, M.; Lima, A.; de Jesus, T.; Costa, F.; Watanabe, T.; Pereira, H.; Valentini, S.; Zanelli, C.; Borges, J.; Dias, M.; da Cunha, J.; Mittra, B.; Andrews, N.; Thiemann, O.
Trypanosomatid selenophosphate synthetase structure, function and interaction with selenocysteine lyase
PLoS Negl. Trop. Dis.
14
1-31
2020
Trypanosoma brucei brucei (Q38A45), Trypanosoma brucei brucei 927/4 GUTat10.1 (Q38A45)
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