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Conserved domains on  [gi|224465209|ref|NP_699167|]
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L-seryl-tRNA(Sec) kinase isoform 2 [Homo sapiens]

Protein Classification

nucleoside/nucleotide kinase family protein( domain architecture ID 106737)

nucleoside/nucleotide kinase family protein may catalyze the reversible phosphate group transfer from nucleoside triphosphates to nucleosides/nucleotides, nucleoside monophosphates, or sugars

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NK super family cl17190
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ...
 20-301 0e+00

Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of enzymes that share structural similarity and are functionally related to the catalysis of the reversible phosphate group transfer from nucleoside triphosphates to nucleosides/nucleotides, nucleoside monophosphates, or sugars. Members of this family play a wide variety of essential roles in nucleotide metabolism, the biosynthesis of coenzymes and aromatic compounds, as well as the metabolism of sugar and sulfate.


The actual alignment was detected with superfamily member TIGR03575:

Pssm-ID: 450170 [Multi-domain]  Cd Length: 340  Bit Score: 510.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465209   20 LCVLCGLPAAGKSTFARALAHRLQQEQGWAIGVVAYDDVMPDAFLAGARARPAPSQWKLLRQELLKYLEYFLMAVINGCQ 99
Cdd:TIGR03575   1 LCVLCGLPAAGKSTLARSLSATLRRERGWAVAVITYDDIIPEAAFELDQSRPLPSQWKQFRQELLKYLEHFLVAVINGSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465209  100 MSVPPNRTEAMWEDFITCLKDQDL-IFSAAFEAQSCYLLTKTAVSRPLFLVLDDNFYYQSMRYEVYQLARKYSLGFCQLF 178
Cdd:TIGR03575  81 LSAPPGKTEGMWEDFVDCLKEQGLiISSGASEAQGCHSLTKPAVSRPLCLVLDDNFYYQSMRYEVYQLARKYSLGFCQLF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465209  179 LDCPLETCLQRNGQRPQALPPETIHLMGRKLEKPNPEKNAWEHNSLTIPSPACASEASLEVTDLLLTALENPVKYAEDNM 258
Cdd:TIGR03575 161 LDCPVESCLLRNKQRPVPLPDETIQLMGRKIEKPNPEKNAWEHNSLVIQSSACISEDSLEVTDLLNTALENPIKCVEENL 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 224465209  259 EQKDTDRIICSTNILHKTDQTLRRIVSQTMKEAKGNQEAFSEM 301
Cdd:TIGR03575 241 EQKETDRIICSTNILHQADQTLRRIISQTMREAKDEQASAYNL 283
 
Name Accession Description Interval E-value
selen_PSTK_euk TIGR03575
L-seryl-tRNA(Sec) kinase, eukaryotic; Members of this protein are L-seryl-tRNA(Sec) kinase. ...
 20-301 0e+00

L-seryl-tRNA(Sec) kinase, eukaryotic; Members of this protein are L-seryl-tRNA(Sec) kinase. This enzyme is part of a two-step pathway in Eukaryota and Archaea for performing selenocysteine biosynthesis by changing serine misacylated on selenocysteine-tRNA to selenocysteine. This enzyme performs the first step, phosphorylation of the OH group of the serine side chain. This family represents eukaryotic proteins with this activity.


Pssm-ID: 188340 [Multi-domain]  Cd Length: 340  Bit Score: 510.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465209   20 LCVLCGLPAAGKSTFARALAHRLQQEQGWAIGVVAYDDVMPDAFLAGARARPAPSQWKLLRQELLKYLEYFLMAVINGCQ 99
Cdd:TIGR03575   1 LCVLCGLPAAGKSTLARSLSATLRRERGWAVAVITYDDIIPEAAFELDQSRPLPSQWKQFRQELLKYLEHFLVAVINGSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465209  100 MSVPPNRTEAMWEDFITCLKDQDL-IFSAAFEAQSCYLLTKTAVSRPLFLVLDDNFYYQSMRYEVYQLARKYSLGFCQLF 178
Cdd:TIGR03575  81 LSAPPGKTEGMWEDFVDCLKEQGLiISSGASEAQGCHSLTKPAVSRPLCLVLDDNFYYQSMRYEVYQLARKYSLGFCQLF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465209  179 LDCPLETCLQRNGQRPQALPPETIHLMGRKLEKPNPEKNAWEHNSLTIPSPACASEASLEVTDLLLTALENPVKYAEDNM 258
Cdd:TIGR03575 161 LDCPVESCLLRNKQRPVPLPDETIQLMGRKIEKPNPEKNAWEHNSLVIQSSACISEDSLEVTDLLNTALENPIKCVEENL 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 224465209  259 EQKDTDRIICSTNILHKTDQTLRRIVSQTMKEAKGNQEAFSEM 301
Cdd:TIGR03575 241 EQKETDRIICSTNILHQADQTLRRIISQTMREAKDEQASAYNL 283
KTI12 pfam08433
Chromatin associated protein KTI12; This is a family of chromatin associated proteins which ...
 20-302 9.47e-20

Chromatin associated protein KTI12; This is a family of chromatin associated proteins which interact with the Elongator complex, a component of the elongating form of RNA polymerase II. The Elongator complex has histone acetyltransferase activity.


Pssm-ID: 400643  Cd Length: 269  Bit Score: 87.35  E-value: 9.47e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465209   20 LCVLCGLPAAGKSTFARALAHRLQQEQgwaIGVVAYDDvmpdaflagararpapsqwkllrqELLkyleyflmavinGCQ 99
Cdd:pfam08433   1 LVLLTGLPSSGKSTRAKQLAKYLEESN---YDVIVISD------------------------ESL------------GIE 41

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465209  100 MSvpPNRTEAMwEDFItclkdQDLIFSAAfeaqscylltKTAVSRPLFLVLDDNFYYQSMRYEVYQLARKYSLGFCQLFL 179
Cdd:pfam08433  42 KD--DYKDSAK-EKFL-----RGSLRSAV----------KRDLSKNTIVIVDSLNYIKGFRYELYCIAKAARTTYCVIHC 103

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465209  180 DCPLETCLQRNGQRPQ--ALPPETIHLMGRKLEKPNPeKNAWEHNSLTIPSPacasEASLEVTDLLLTALEN-PVKYAED 256
Cdd:pfam08433 104 KAPLDLCRKWNEERGQksRYPDELLDALIQRYEEPNS-KNRWDSPLFTVLSD----DETLPLDEIWKALIEKqPLPPNQA 178

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 224465209  257 NMEQKDTdriicSTNILHKTDQTLRRIVSQTMKEAKGNQeAFSEMT 302
Cdd:pfam08433 179 TQLKPLS-----ETNFLQELDKETQDIVSEILKAQQSAV-AIGLVT 218
Kti12 COG4088
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) ...
 20-219 6.41e-16

tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) [Translation, ribosomal structure and biogenesis, Defense mechanisms];


Pssm-ID: 443264 [Multi-domain]  Cd Length: 179  Bit Score: 74.76  E-value: 6.41e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465209  20 LCVLCGLPAAGKSTFARALAHRLQQEqGWAIGVVAYDDVmpdaflagararpapsqWKLLRQEllkyleyflmavingcq 99
Cdd:COG4088    6 LLILTGPPGSGKTTFAKALAQRLYAE-GIAVALLHSDDF-----------------RRFLVNE----------------- 50

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465209 100 mSVPPNRTEAMWEDFITCLKDQdlifsaafeaqscylltktAVSRPLFLVLDDNFYYQSMRYEVYQLAR-KYSLGFcqLF 178
Cdd:COG4088   51 -SFPKETYEEVVEDVRTTTADN-------------------ALDNGYSVIVDGTFYYRSWQRDFRNLAKhKAPIHI--IY 108

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 224465209 179 LDCPLETCLQRNGQRPQALPPETIHLMGRKLEKPNPEKNAW 219
Cdd:COG4088  109 LKAPLETALRRNRERGEPIPERVIARMYRKFDKPGTKDRPD 149
PRK09270 PRK09270
nucleoside triphosphate hydrolase domain-containing protein; Reviewed
 15-70 2.15e-04

nucleoside triphosphate hydrolase domain-containing protein; Reviewed


Pssm-ID: 236442  Cd Length: 229  Bit Score: 42.23  E-value: 2.15e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 224465209  15 PRKRGLCVLCGLPAAGKSTFARALAHRLQQEQGWAIGVVAYDDV-MPDAFLA--GARAR 70
Cdd:PRK09270  30 PQRRTIVGIAGPPGAGKSTLAEFLEALLQQDGELPAIQVPMDGFhLDNAVLDahGLRPR 88
APSK cd02027
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ...
 23-45 7.65e-04

Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5'-phosphosulfate to form 3'-phosphoadenosine 5'-phosphosulfate (PAPS). The end-product PAPS is a biologically "activated" sulfate form important for the assimilation of inorganic sulfate.


Pssm-ID: 238985 [Multi-domain]  Cd Length: 149  Bit Score: 39.38  E-value: 7.65e-04
                         10        20
                 ....*....|....*....|...
gi 224465209  23 LCGLPAAGKSTFARALAHRLQQE 45
Cdd:cd02027    4 LTGLSGSGKSTIARALEEKLFQR 26
 
Name Accession Description Interval E-value
selen_PSTK_euk TIGR03575
L-seryl-tRNA(Sec) kinase, eukaryotic; Members of this protein are L-seryl-tRNA(Sec) kinase. ...
 20-301 0e+00

L-seryl-tRNA(Sec) kinase, eukaryotic; Members of this protein are L-seryl-tRNA(Sec) kinase. This enzyme is part of a two-step pathway in Eukaryota and Archaea for performing selenocysteine biosynthesis by changing serine misacylated on selenocysteine-tRNA to selenocysteine. This enzyme performs the first step, phosphorylation of the OH group of the serine side chain. This family represents eukaryotic proteins with this activity.


Pssm-ID: 188340 [Multi-domain]  Cd Length: 340  Bit Score: 510.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465209   20 LCVLCGLPAAGKSTFARALAHRLQQEQGWAIGVVAYDDVMPDAFLAGARARPAPSQWKLLRQELLKYLEYFLMAVINGCQ 99
Cdd:TIGR03575   1 LCVLCGLPAAGKSTLARSLSATLRRERGWAVAVITYDDIIPEAAFELDQSRPLPSQWKQFRQELLKYLEHFLVAVINGSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465209  100 MSVPPNRTEAMWEDFITCLKDQDL-IFSAAFEAQSCYLLTKTAVSRPLFLVLDDNFYYQSMRYEVYQLARKYSLGFCQLF 178
Cdd:TIGR03575  81 LSAPPGKTEGMWEDFVDCLKEQGLiISSGASEAQGCHSLTKPAVSRPLCLVLDDNFYYQSMRYEVYQLARKYSLGFCQLF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465209  179 LDCPLETCLQRNGQRPQALPPETIHLMGRKLEKPNPEKNAWEHNSLTIPSPACASEASLEVTDLLLTALENPVKYAEDNM 258
Cdd:TIGR03575 161 LDCPVESCLLRNKQRPVPLPDETIQLMGRKIEKPNPEKNAWEHNSLVIQSSACISEDSLEVTDLLNTALENPIKCVEENL 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 224465209  259 EQKDTDRIICSTNILHKTDQTLRRIVSQTMKEAKGNQEAFSEM 301
Cdd:TIGR03575 241 EQKETDRIICSTNILHQADQTLRRIISQTMREAKDEQASAYNL 283
KTI12 pfam08433
Chromatin associated protein KTI12; This is a family of chromatin associated proteins which ...
 20-302 9.47e-20

Chromatin associated protein KTI12; This is a family of chromatin associated proteins which interact with the Elongator complex, a component of the elongating form of RNA polymerase II. The Elongator complex has histone acetyltransferase activity.


Pssm-ID: 400643  Cd Length: 269  Bit Score: 87.35  E-value: 9.47e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465209   20 LCVLCGLPAAGKSTFARALAHRLQQEQgwaIGVVAYDDvmpdaflagararpapsqwkllrqELLkyleyflmavinGCQ 99
Cdd:pfam08433   1 LVLLTGLPSSGKSTRAKQLAKYLEESN---YDVIVISD------------------------ESL------------GIE 41

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465209  100 MSvpPNRTEAMwEDFItclkdQDLIFSAAfeaqscylltKTAVSRPLFLVLDDNFYYQSMRYEVYQLARKYSLGFCQLFL 179
Cdd:pfam08433  42 KD--DYKDSAK-EKFL-----RGSLRSAV----------KRDLSKNTIVIVDSLNYIKGFRYELYCIAKAARTTYCVIHC 103

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465209  180 DCPLETCLQRNGQRPQ--ALPPETIHLMGRKLEKPNPeKNAWEHNSLTIPSPacasEASLEVTDLLLTALEN-PVKYAED 256
Cdd:pfam08433 104 KAPLDLCRKWNEERGQksRYPDELLDALIQRYEEPNS-KNRWDSPLFTVLSD----DETLPLDEIWKALIEKqPLPPNQA 178

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 224465209  257 NMEQKDTdriicSTNILHKTDQTLRRIVSQTMKEAKGNQeAFSEMT 302
Cdd:pfam08433 179 TQLKPLS-----ETNFLQELDKETQDIVSEILKAQQSAV-AIGLVT 218
Kti12 COG4088
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) ...
 20-219 6.41e-16

tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) [Translation, ribosomal structure and biogenesis, Defense mechanisms];


Pssm-ID: 443264 [Multi-domain]  Cd Length: 179  Bit Score: 74.76  E-value: 6.41e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465209  20 LCVLCGLPAAGKSTFARALAHRLQQEqGWAIGVVAYDDVmpdaflagararpapsqWKLLRQEllkyleyflmavingcq 99
Cdd:COG4088    6 LLILTGPPGSGKTTFAKALAQRLYAE-GIAVALLHSDDF-----------------RRFLVNE----------------- 50

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465209 100 mSVPPNRTEAMWEDFITCLKDQdlifsaafeaqscylltktAVSRPLFLVLDDNFYYQSMRYEVYQLAR-KYSLGFcqLF 178
Cdd:COG4088   51 -SFPKETYEEVVEDVRTTTADN-------------------ALDNGYSVIVDGTFYYRSWQRDFRNLAKhKAPIHI--IY 108

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 224465209 179 LDCPLETCLQRNGQRPQALPPETIHLMGRKLEKPNPEKNAW 219
Cdd:COG4088  109 LKAPLETALRRNRERGEPIPERVIARMYRKFDKPGTKDRPD 149
COG4639 COG4639
Predicted kinase [General function prediction only];
22-212 5.51e-15

Predicted kinase [General function prediction only];


Pssm-ID: 443677 [Multi-domain]  Cd Length: 145  Bit Score: 71.01  E-value: 5.51e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465209  22 VLCGLPAAGKSTFARALAHRLQqeqgwaigVVAYDDvmpdaflagararpapsqwklLRQELlkyleyflmavingcqms 101
Cdd:COG4639    6 VLIGLPGSGKSTFARRLFAPTE--------VVSSDD---------------------IRALL------------------ 38

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465209 102 vppnrteAMWEdfiTCLKDQDLIFSAAFEAqscyllTKTAVSRPLFLVLDDNFYYQSMRYEVYQLARKYSLGFCQLFLDC 181
Cdd:COG4639   39 -------GGDE---NDQSAWGDVFQLAHEI------ARARLRAGRLTVVDATNLQREARRRLLALARAYGALVVAVVLDV 102

                        170       180       190
                 ....*....|....*....|....*....|.
gi 224465209 182 PLETCLQRNGQRPQALPPETIHLMGRKLEKP 212
Cdd:COG4639  103 PLEVCLARNAARDRQVPEEVIRRMLRRLRRP 133
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
22-193 2.81e-08

Predicted kinase, contains AAA domain [General function prediction only];


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 52.61  E-value: 2.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465209  22 VLCGLPAAGKSTFARALAHRLQqeqgwAIgVVAYDDVMpdAFLAGARARPA---PSQWKLLRQELLKYLEYFLMAvinGC 98
Cdd:COG0645    3 LVCGLPGSGKSTLARALAERLG-----AV-RLRSDVVR--KRLFGAGLAPLersPEATARTYARLLALARELLAA---GR 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465209  99 qmSVppnrteamwedfitclkdqdlifsaafeaqscylltktavsrplflVLDDNFYYQSMRYEVYQLARKYSLGFCQLF 178
Cdd:COG0645   72 --SV----------------------------------------------ILDATFLRRAQREAFRALAEEAGAPFVLIW 103

                        170
                 ....*....|....*
gi 224465209 179 LDCPLETCLQRNGQR 193
Cdd:COG0645  104 LDAPEEVLRERLEAR 118
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
 20-212 4.62e-06

AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the AAA superfamily. Many of the proteins in this family are just short fragments so there is no Walker B motif.


Pssm-ID: 463952 [Multi-domain]  Cd Length: 143  Bit Score: 45.76  E-value: 4.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465209   20 LCVLCGLPAAGKSTFARALAHRLqqeqgwaigvvAYDDVMPDAFLAGARARPAPSQ------WKLLRQELLKYLEYFLma 93
Cdd:pfam13671   1 LILLVGLPGSGKSTLARRLLEEL-----------GAVRLSSDDERKRLFGEGRPSIsyytdaTDRTYERLHELARIAL-- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465209   94 vingcqmsvppnrteamwedfitclkdqdlifsaafeaqscylltktavSRPLFLVLDDNFYYQSMRYEVYQLARKYSLG 173
Cdd:pfam13671  68 -------------------------------------------------RAGRPVILDATNLRRDERARLLALAREYGVP 98

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 224465209  174 FCQLFLDCPLETCLQRNGQR------PQALPPETIHLMGRKLEKP 212
Cdd:pfam13671  99 VRIVVFEAPEEVLRERLAARaraggdPSDVPEEVLDRQKARFEPP 143
PRK09270 PRK09270
nucleoside triphosphate hydrolase domain-containing protein; Reviewed
 15-70 2.15e-04

nucleoside triphosphate hydrolase domain-containing protein; Reviewed


Pssm-ID: 236442  Cd Length: 229  Bit Score: 42.23  E-value: 2.15e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 224465209  15 PRKRGLCVLCGLPAAGKSTFARALAHRLQQEQGWAIGVVAYDDV-MPDAFLA--GARAR 70
Cdd:PRK09270  30 PQRRTIVGIAGPPGAGKSTLAEFLEALLQQDGELPAIQVPMDGFhLDNAVLDahGLRPR 88
CysC COG0529
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ...
 18-45 2.41e-04

Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; Adenylylsulfate kinase or related kinase is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 440295 [Multi-domain]  Cd Length: 189  Bit Score: 41.61  E-value: 2.41e-04
                         10        20
                 ....*....|....*....|....*....
gi 224465209  18 RGLCV-LCGLPAAGKSTFARALAHRLQQE 45
Cdd:COG0529   15 KGFVVwFTGLSGSGKSTLANALERRLFER 43
DO-GTPase1 pfam19975
Double-GTPase 1; GTPase of a GTPase-centric, NTP-dependent ternary systems. The domain belongs ...
 22-47 4.42e-04

Double-GTPase 1; GTPase of a GTPase-centric, NTP-dependent ternary systems. The domain belongs to a previously unrecognized family of the TRAFAC clade with a conserved glutamate in its Walker B motif.


Pssm-ID: 466245  Cd Length: 271  Bit Score: 41.47  E-value: 4.42e-04
                          10        20
                  ....*....|....*....|....*.
gi 224465209   22 VLCGLPAAGKSTFARALAHRLQQEQG 47
Cdd:pfam19975   1 LLIGLPGSGKTTFLAALWHRLREVKG 26
APSK cd02027
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ...
 23-45 7.65e-04

Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5'-phosphosulfate to form 3'-phosphoadenosine 5'-phosphosulfate (PAPS). The end-product PAPS is a biologically "activated" sulfate form important for the assimilation of inorganic sulfate.


Pssm-ID: 238985 [Multi-domain]  Cd Length: 149  Bit Score: 39.38  E-value: 7.65e-04
                         10        20
                 ....*....|....*....|...
gi 224465209  23 LCGLPAAGKSTFARALAHRLQQE 45
Cdd:cd02027    4 LTGLSGSGKSTIARALEEKLFQR 26
AAA_22 pfam13401
AAA domain;
18-95 1.43e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 38.09  E-value: 1.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224465209   18 RGLCVLCGLPAAGKSTFARALAHRLQQEQGWAIGVVAYDDVMPDAFLAG-----ARARPAPSQWKLLRQELLKYL-EYFL 91
Cdd:pfam13401   5 AGILVLTGESGTGKTTLLRRLLEQLPEVRDSVVFVDLPSGTSPKDLLRAllralGLPLSGRLSKEELLAALQQLLlALAV 84


                  ....
gi 224465209   92 MAVI 95
Cdd:pfam13401  85 AVVL 88
AroK COG0703
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the ...
 22-42 1.70e-03

Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 440467 [Multi-domain]  Cd Length: 165  Bit Score: 38.57  E-value: 1.70e-03
                         10        20
                 ....*....|....*....|.
gi 224465209  22 VLCGLPAAGKSTFARALAHRL 42
Cdd:COG0703    2 VLIGMMGAGKSTVGRLLAKRL 22
PRK05537 PRK05537
bifunctional sulfate adenylyltransferase/adenylylsulfate kinase;
15-47 2.05e-03

bifunctional sulfate adenylyltransferase/adenylylsulfate kinase;


Pssm-ID: 180124 [Multi-domain]  Cd Length: 568  Bit Score: 40.04  E-value: 2.05e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 224465209  15 PR-KRGLCV-LCGLPAAGKSTFARALAHRLQQEQG 47
Cdd:PRK05537 387 PRhKQGFTVfFTGLSGAGKSTIAKALMVKLMEMRG 421
SK cd00464
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ...
 22-42 2.59e-03

Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic pathway which converts erythrose-4-phosphate to chorismic acid, found in bacteria, fungi and plants. Chorismic acid is a important intermediate in the synthesis of aromatic compounds, such as aromatic amino acids, p-aminobenzoic acid, folate and ubiquinone. Shikimate kinase catalyses the phosphorylation of the 3-hydroxyl group of shikimic acid using ATP.


Pssm-ID: 238260 [Multi-domain]  Cd Length: 154  Bit Score: 37.92  E-value: 2.59e-03
                         10        20
                 ....*....|....*....|.
gi 224465209  22 VLCGLPAAGKSTFARALAHRL 42
Cdd:cd00464    3 VLIGMMGAGKTTVGRLLAKAL 23
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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