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Conserved domains on  [gi|1391723617|ref|NP_001350460|]
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L-seryl-tRNA(Sec) kinase isoform 1 [Homo sapiens]

Protein Classification

nucleoside/nucleotide kinase family protein; dTMP kinase( domain architecture ID 10022674)

nucleoside/nucleotide kinase family protein may catalyze the reversible phosphate group transfer from nucleoside triphosphates to nucleosides/nucleotides, nucleoside monophosphates, or sugars; dTMP (thymidylate) kinase with a major facilitator superfamily (MFS) transporter domain functions in the phosphorylation of thymidine monophosphate and may also transport across cytoplasmic or internal membranes various substrates including sugar phosphates

Graphical summary

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List of domain hits

 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. ...
 20-357 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: 614.97  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723617  20 LCVLCGLPAAGKSTFARALAHRLQQEQGWAIGVVAYDDVMPDAFLAGARARPAPSQWKLLRQELLKYLEYFLMAVINGCQ 99
Cdd:TIGR03575   1 LCVLCGLPAAGKSTLARSLSATLRRERGWAVAVITYDDIIPEAAFELDQSRPLPSQWKQFRQELLKYLEHFLVAVINGSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723617 100 MSVPPNRTEAMWEDFITCLKDQDL-IFSAAFEAQSCYLLTKTAVSRPLFLVLDDNFYYQSMRYEVYQLARKYSLGFCQLF 178
Cdd:TIGR03575  81 LSAPPGKTEGMWEDFVDCLKEQGLiISSGASEAQGCHSLTKPAVSRPLCLVLDDNFYYQSMRYEVYQLARKYSLGFCQLF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723617 179 LDCPLETCLQRNGQRPQALPPETIHLMGRKLEKPNPEKNAWEHNSLTIPSPACASEASLEVTDLLLTALENPVKYAEDNM 258
Cdd:TIGR03575 161 LDCPVESCLLRNKQRPVPLPDETIQLMGRKIEKPNPEKNAWEHNSLVIQSSACISEDSLEVTDLLNTALENPIKCVEENL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723617 259 EQKDTDRIICSTNILHKTDQTLRRIVSQTMKEAKDEQVLPHNLKLLAEELNKLKAEFLEDLKQGN-KKYLCFQQTIDIPD 337
Cdd:TIGR03575 241 EQKETDRIICSTNILHQADQTLRRIISQTMREAKDEQASAYNLKLLAEELNKLKADFLEDLRQGNcKKYLCFQQTCDLSD 320

                         330       340
                  ....*....|....*....|
gi 1391723617 338 VISFFHYEKDNIVQKYFSKQ 357
Cdd:TIGR03575 321 IISLFHYERDNIVQKYFSKE 340
 
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. ...
 20-357 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: 614.97  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723617  20 LCVLCGLPAAGKSTFARALAHRLQQEQGWAIGVVAYDDVMPDAFLAGARARPAPSQWKLLRQELLKYLEYFLMAVINGCQ 99
Cdd:TIGR03575   1 LCVLCGLPAAGKSTLARSLSATLRRERGWAVAVITYDDIIPEAAFELDQSRPLPSQWKQFRQELLKYLEHFLVAVINGSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723617 100 MSVPPNRTEAMWEDFITCLKDQDL-IFSAAFEAQSCYLLTKTAVSRPLFLVLDDNFYYQSMRYEVYQLARKYSLGFCQLF 178
Cdd:TIGR03575  81 LSAPPGKTEGMWEDFVDCLKEQGLiISSGASEAQGCHSLTKPAVSRPLCLVLDDNFYYQSMRYEVYQLARKYSLGFCQLF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723617 179 LDCPLETCLQRNGQRPQALPPETIHLMGRKLEKPNPEKNAWEHNSLTIPSPACASEASLEVTDLLLTALENPVKYAEDNM 258
Cdd:TIGR03575 161 LDCPVESCLLRNKQRPVPLPDETIQLMGRKIEKPNPEKNAWEHNSLVIQSSACISEDSLEVTDLLNTALENPIKCVEENL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723617 259 EQKDTDRIICSTNILHKTDQTLRRIVSQTMKEAKDEQVLPHNLKLLAEELNKLKAEFLEDLKQGN-KKYLCFQQTIDIPD 337
Cdd:TIGR03575 241 EQKETDRIICSTNILHQADQTLRRIISQTMREAKDEQASAYNLKLLAEELNKLKADFLEDLRQGNcKKYLCFQQTCDLSD 320

                         330       340
                  ....*....|....*....|
gi 1391723617 338 VISFFHYEKDNIVQKYFSKQ 357
Cdd:TIGR03575 321 IISLFHYERDNIVQKYFSKE 340
KTI12 pfam08433
Chromatin associated protein KTI12; This is a family of chromatin associated proteins which ...
 20-342 8.91e-21

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: 90.43  E-value: 8.91e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723617  20 LCVLCGLPAAGKSTFARALAHRLQQEQgwaIGVVAYDDvmpdaflagararpapsqwkllrqELLkyleyflmavinGCQ 99
Cdd:pfam08433   1 LVLLTGLPSSGKSTRAKQLAKYLEESN---YDVIVISD------------------------ESL------------GIE 41

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723617 100 MSvpPNRTEAMwEDFItclkdQDLIFSAAfeaqscylltKTAVSRPLFLVLDDNFYYQSMRYEVYQLARKYSLGFCQLFL 179
Cdd:pfam08433  42 KD--DYKDSAK-EKFL-----RGSLRSAV----------KRDLSKNTIVIVDSLNYIKGFRYELYCIAKAARTTYCVIHC 103

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723617 180 DCPLETCLQRNGQRPQ--ALPPETIHLMGRKLEKPNPeKNAWEHNSLTIPSPacasEASLEVTDLLLTALEN-PVKYAED 256
Cdd:pfam08433 104 KAPLDLCRKWNEERGQksRYPDELLDALIQRYEEPNS-KNRWDSPLFTVLSD----DETLPLDEIWKALIEKqPLPPNQA 178

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723617 257 NMEQKDTdriicSTNILHKTDQTLRRIVSQTMKE--------------AKDEQVLPHNLKLLAeELNKLKAEFLedlkqg 322
Cdd:pfam08433 179 TQLKPLS-----ETNFLQELDKETQDIVSEILKAqqsavaiglvtipgPPEPSALPAAPVTLA-ELQRLRRQFV------ 246

                         330       340
                  ....*....|....*....|
gi 1391723617 323 nkKYLCFQQTIDIPDVISFF 342
Cdd:pfam08433 247 --QMNKKLRPVDLDRIAPLF 264
Kti12 COG4088
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) ...
 20-219 6.99e-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: 6.99e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723617  20 LCVLCGLPAAGKSTFARALAHRLQQEqGWAIGVVAYDDVmpdaflagararpapsqWKLLRQEllkyleyflmavingcq 99
Cdd:COG4088     6 LLILTGPPGSGKTTFAKALAQRLYAE-GIAVALLHSDDF-----------------RRFLVNE----------------- 50

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723617 100 mSVPPNRTEAMWEDFITCLKDQdlifsaafeaqscylltktAVSRPLFLVLDDNFYYQSMRYEVYQLAR-KYSLGFcqLF 178
Cdd:COG4088    51 -SFPKETYEEVVEDVRTTTADN-------------------ALDNGYSVIVDGTFYYRSWQRDFRNLAKhKAPIHI--IY 108

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1391723617 179 LDCPLETCLQRNGQRPQALPPETIHLMGRKLEKPNPEKNAW 219
Cdd:COG4088   109 LKAPLETALRRNRERGEPIPERVIARMYRKFDKPGTKDRPD 149
PRK09270 PRK09270
nucleoside triphosphate hydrolase domain-containing protein; Reviewed
 15-70 1.64e-04

nucleoside triphosphate hydrolase domain-containing protein; Reviewed


Pssm-ID: 236442  Cd Length: 229  Bit Score: 42.61  E-value: 1.64e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1391723617  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 7.94e-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: 7.94e-04
                          10        20
                  ....*....|....*....|...
gi 1391723617  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. ...
 20-357 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: 614.97  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723617  20 LCVLCGLPAAGKSTFARALAHRLQQEQGWAIGVVAYDDVMPDAFLAGARARPAPSQWKLLRQELLKYLEYFLMAVINGCQ 99
Cdd:TIGR03575   1 LCVLCGLPAAGKSTLARSLSATLRRERGWAVAVITYDDIIPEAAFELDQSRPLPSQWKQFRQELLKYLEHFLVAVINGSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723617 100 MSVPPNRTEAMWEDFITCLKDQDL-IFSAAFEAQSCYLLTKTAVSRPLFLVLDDNFYYQSMRYEVYQLARKYSLGFCQLF 178
Cdd:TIGR03575  81 LSAPPGKTEGMWEDFVDCLKEQGLiISSGASEAQGCHSLTKPAVSRPLCLVLDDNFYYQSMRYEVYQLARKYSLGFCQLF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723617 179 LDCPLETCLQRNGQRPQALPPETIHLMGRKLEKPNPEKNAWEHNSLTIPSPACASEASLEVTDLLLTALENPVKYAEDNM 258
Cdd:TIGR03575 161 LDCPVESCLLRNKQRPVPLPDETIQLMGRKIEKPNPEKNAWEHNSLVIQSSACISEDSLEVTDLLNTALENPIKCVEENL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723617 259 EQKDTDRIICSTNILHKTDQTLRRIVSQTMKEAKDEQVLPHNLKLLAEELNKLKAEFLEDLKQGN-KKYLCFQQTIDIPD 337
Cdd:TIGR03575 241 EQKETDRIICSTNILHQADQTLRRIISQTMREAKDEQASAYNLKLLAEELNKLKADFLEDLRQGNcKKYLCFQQTCDLSD 320

                         330       340
                  ....*....|....*....|
gi 1391723617 338 VISFFHYEKDNIVQKYFSKQ 357
Cdd:TIGR03575 321 IISLFHYERDNIVQKYFSKE 340
KTI12 pfam08433
Chromatin associated protein KTI12; This is a family of chromatin associated proteins which ...
 20-342 8.91e-21

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: 90.43  E-value: 8.91e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723617  20 LCVLCGLPAAGKSTFARALAHRLQQEQgwaIGVVAYDDvmpdaflagararpapsqwkllrqELLkyleyflmavinGCQ 99
Cdd:pfam08433   1 LVLLTGLPSSGKSTRAKQLAKYLEESN---YDVIVISD------------------------ESL------------GIE 41

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723617 100 MSvpPNRTEAMwEDFItclkdQDLIFSAAfeaqscylltKTAVSRPLFLVLDDNFYYQSMRYEVYQLARKYSLGFCQLFL 179
Cdd:pfam08433  42 KD--DYKDSAK-EKFL-----RGSLRSAV----------KRDLSKNTIVIVDSLNYIKGFRYELYCIAKAARTTYCVIHC 103

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723617 180 DCPLETCLQRNGQRPQ--ALPPETIHLMGRKLEKPNPeKNAWEHNSLTIPSPacasEASLEVTDLLLTALEN-PVKYAED 256
Cdd:pfam08433 104 KAPLDLCRKWNEERGQksRYPDELLDALIQRYEEPNS-KNRWDSPLFTVLSD----DETLPLDEIWKALIEKqPLPPNQA 178

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723617 257 NMEQKDTdriicSTNILHKTDQTLRRIVSQTMKE--------------AKDEQVLPHNLKLLAeELNKLKAEFLedlkqg 322
Cdd:pfam08433 179 TQLKPLS-----ETNFLQELDKETQDIVSEILKAqqsavaiglvtipgPPEPSALPAAPVTLA-ELQRLRRQFV------ 246

                         330       340
                  ....*....|....*....|
gi 1391723617 323 nkKYLCFQQTIDIPDVISFF 342
Cdd:pfam08433 247 --QMNKKLRPVDLDRIAPLF 264
Kti12 COG4088
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) ...
 20-219 6.99e-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: 6.99e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723617  20 LCVLCGLPAAGKSTFARALAHRLQQEqGWAIGVVAYDDVmpdaflagararpapsqWKLLRQEllkyleyflmavingcq 99
Cdd:COG4088     6 LLILTGPPGSGKTTFAKALAQRLYAE-GIAVALLHSDDF-----------------RRFLVNE----------------- 50

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723617 100 mSVPPNRTEAMWEDFITCLKDQdlifsaafeaqscylltktAVSRPLFLVLDDNFYYQSMRYEVYQLAR-KYSLGFcqLF 178
Cdd:COG4088    51 -SFPKETYEEVVEDVRTTTADN-------------------ALDNGYSVIVDGTFYYRSWQRDFRNLAKhKAPIHI--IY 108

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1391723617 179 LDCPLETCLQRNGQRPQALPPETIHLMGRKLEKPNPEKNAW 219
Cdd:COG4088   109 LKAPLETALRRNRERGEPIPERVIARMYRKFDKPGTKDRPD 149
COG4639 COG4639
Predicted kinase [General function prediction only];
22-212 2.91e-15

Predicted kinase [General function prediction only];


Pssm-ID: 443677 [Multi-domain]  Cd Length: 145  Bit Score: 72.17  E-value: 2.91e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723617  22 VLCGLPAAGKSTFARALAHRLQqeqgwaigVVAYDDvmpdaflagararpapsqwklLRQELlkyleyflmavingcqms 101
Cdd:COG4639     6 VLIGLPGSGKSTFARRLFAPTE--------VVSSDD---------------------IRALL------------------ 38

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723617 102 vppnrteAMWEdfiTCLKDQDLIFSAAFEAqscyllTKTAVSRPLFLVLDDNFYYQSMRYEVYQLARKYSLGFCQLFLDC 181
Cdd:COG4639    39 -------GGDE---NDQSAWGDVFQLAHEI------ARARLRAGRLTVVDATNLQREARRRLLALARAYGALVVAVVLDV 102

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1391723617 182 PLETCLQRNGQRPQALPPETIHLMGRKLEKP 212
Cdd:COG4639   103 PLEVCLARNAARDRQVPEEVIRRMLRRLRRP 133
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
22-193 5.03e-09

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


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 54.92  E-value: 5.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723617  22 VLCGLPAAGKSTFARALAHRLQqeqgwAIgVVAYDDVMpdAFLAGARARPA---PSQWKLLRQELLKYLEYFLMAvinGC 98
Cdd:COG0645     3 LVCGLPGSGKSTLARALAERLG-----AV-RLRSDVVR--KRLFGAGLAPLersPEATARTYARLLALARELLAA---GR 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723617  99 qmSVppnrteamwedfitclkdqdlifsaafeaqscylltktavsrplflVLDDNFYYQSMRYEVYQLARKYSLGFCQLF 178
Cdd:COG0645    72 --SV----------------------------------------------ILDATFLRRAQREAFRALAEEAGAPFVLIW 103

                         170
                  ....*....|....*
gi 1391723617 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 1.19e-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: 47.30  E-value: 1.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723617  20 LCVLCGLPAAGKSTFARALAHRLqqeqgwaigvvAYDDVMPDAFLAGARARPAPSQ------WKLLRQELLKYLEYFLma 93
Cdd:pfam13671   1 LILLVGLPGSGKSTLARRLLEEL-----------GAVRLSSDDERKRLFGEGRPSIsyytdaTDRTYERLHELARIAL-- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723617  94 vingcqmsvppnrteamwedfitclkdqdlifsaafeaqscylltktavSRPLFLVLDDNFYYQSMRYEVYQLARKYSLG 173
Cdd:pfam13671  68 -------------------------------------------------RAGRPVILDATNLRRDERARLLALAREYGVP 98

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1391723617 174 FCQLFLDCPLETCLQRNGQR------PQALPPETIHLMGRKLEKP 212
Cdd:pfam13671  99 VRIVVFEAPEEVLRERLAARaraggdPSDVPEEVLDRQKARFEPP 143
PRK09270 PRK09270
nucleoside triphosphate hydrolase domain-containing protein; Reviewed
 15-70 1.64e-04

nucleoside triphosphate hydrolase domain-containing protein; Reviewed


Pssm-ID: 236442  Cd Length: 229  Bit Score: 42.61  E-value: 1.64e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1391723617  15 PRKRGLCVLCGLPAAGKSTFARALAHRLQQEQGWAIGVVAYDDV-MPDAFLA--GARAR 70
Cdd:PRK09270   30 PQRRTIVGIAGPPGAGKSTLAEFLEALLQQDGELPAIQVPMDGFhLDNAVLDahGLRPR 88
CysC COG0529
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ...
 18-45 2.51e-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: 2.51e-04
                          10        20
                  ....*....|....*....|....*....
gi 1391723617  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 4.62e-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: 4.62e-04
                          10        20
                  ....*....|....*....|....*.
gi 1391723617  22 VLCGLPAAGKSTFARALAHRLQQEQG 47
Cdd:pfam19975   1 LLIGLPGSGKTTFLAALWHRLREVKG 26
APSK cd02027
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ...
 23-45 7.94e-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: 7.94e-04
                          10        20
                  ....*....|....*....|...
gi 1391723617  23 LCGLPAAGKSTFARALAHRLQQE 45
Cdd:cd02027     4 LTGLSGSGKSTIARALEEKLFQR 26
AAA_22 pfam13401
AAA domain;
18-95 1.63e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 38.09  E-value: 1.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723617  18 RGLCVLCGLPAAGKSTFARALAHRLQQEQGWAIGVVAYDDVMPDAFLAG-----ARARPAPSQWKLLRQELLKYL-EYFL 91
Cdd:pfam13401   5 AGILVLTGESGTGKTTLLRRLLEQLPEVRDSVVFVDLPSGTSPKDLLRAllralGLPLSGRLSKEELLAALQQLLlALAV 84


                  ....
gi 1391723617  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 1.77e-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: 1.77e-03
                          10        20
                  ....*....|....*....|.
gi 1391723617  22 VLCGLPAAGKSTFARALAHRL 42
Cdd:COG0703     2 VLIGMMGAGKSTVGRLLAKRL 22
PRK05537 PRK05537
bifunctional sulfate adenylyltransferase/adenylylsulfate kinase;
15-47 2.15e-03

bifunctional sulfate adenylyltransferase/adenylylsulfate kinase;


Pssm-ID: 180124 [Multi-domain]  Cd Length: 568  Bit Score: 40.04  E-value: 2.15e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1391723617  15 PR-KRGLCV-LCGLPAAGKSTFARALAHRLQQEQG 47
Cdd:PRK05537  387 PRhKQGFTVfFTGLSGAGKSTIAKALMVKLMEMRG 421
COG3899 COG3899
Predicted ATPase [General function prediction only];
16-152 2.68e-03

Predicted ATPase [General function prediction only];


Pssm-ID: 443106 [Multi-domain]  Cd Length: 1244  Bit Score: 39.84  E-value: 2.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723617   16 RKRGLCVLCGLPAAGKSTFARALAHRLQQEQGWAIGVVAYDDVMPDAF---------LAGARARPAPSQWKLLRQELLKY 86
Cdd:COG3899    309 GRGELVLVSGEAGIGKSRLVRELARRARARGGRVLRGKCDQLERGVPYaplaqalraLLGQLPEDELAAWRARLLAALGA 388

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1391723617   87 LEYFLMAVINGCQMSVPPNRTEAMwedfitclKDQDLIFsAAFEAqscyLLTKTAVSRPLFLVLDD 152
Cdd:COG3899    389 NGRLLADLLPELELQPAPPELDPE--------EARNRLF-RALLR----LLRALAAERPLVLVLDD 441
SK cd00464
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ...
 22-42 2.68e-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: 2.68e-03
                          10        20
                  ....*....|....*....|.
gi 1391723617  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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