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Conserved domains on  [gi|1034566342|ref|XP_016871130|]
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L-seryl-tRNA(Sec) kinase isoform X1 [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 ...
 20-236 2.04e-144

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: 406.96  E-value: 2.04e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566342  20 LCVLCGLPAAGKSTFARALAHRLQQEQGWAIGVVAYDDVMPDAFLAGARARPAPSQWKLLRQELLKYLEYFLMAVINGCQ 99
Cdd:TIGR03575   1 LCVLCGLPAAGKSTLARSLSATLRRERGWAVAVITYDDIIPEAAFELDQSRPLPSQWKQFRQELLKYLEHFLVAVINGSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566342 100 MSVPPNRTEAMWEDFITCLKDQDL-IFSAAFEAQSCYLLTKTAVSRPLFLVLDDNFYYQSMRYEVYQLARKYSLGFCQLF 178
Cdd:TIGR03575  81 LSAPPGKTEGMWEDFVDCLKEQGLiISSGASEAQGCHSLTKPAVSRPLCLVLDDNFYYQSMRYEVYQLARKYSLGFCQLF 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034566342 179 LDCPLETCLQRNGQRPQALPPETIHLMGRKLEKPNPEKNAWEHNSLTIPSPACASEAR 236
Cdd:TIGR03575 161 LDCPVESCLLRNKQRPVPLPDETIQLMGRKIEKPNPEKNAWEHNSLVIQSSACISEDS 218
 
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. ...
 20-236 2.04e-144

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: 406.96  E-value: 2.04e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566342  20 LCVLCGLPAAGKSTFARALAHRLQQEQGWAIGVVAYDDVMPDAFLAGARARPAPSQWKLLRQELLKYLEYFLMAVINGCQ 99
Cdd:TIGR03575   1 LCVLCGLPAAGKSTLARSLSATLRRERGWAVAVITYDDIIPEAAFELDQSRPLPSQWKQFRQELLKYLEHFLVAVINGSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566342 100 MSVPPNRTEAMWEDFITCLKDQDL-IFSAAFEAQSCYLLTKTAVSRPLFLVLDDNFYYQSMRYEVYQLARKYSLGFCQLF 178
Cdd:TIGR03575  81 LSAPPGKTEGMWEDFVDCLKEQGLiISSGASEAQGCHSLTKPAVSRPLCLVLDDNFYYQSMRYEVYQLARKYSLGFCQLF 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034566342 179 LDCPLETCLQRNGQRPQALPPETIHLMGRKLEKPNPEKNAWEHNSLTIPSPACASEAR 236
Cdd:TIGR03575 161 LDCPVESCLLRNKQRPVPLPDETIQLMGRKIEKPNPEKNAWEHNSLVIQSSACISEDS 218
Kti12 COG4088
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) ...
 20-219 1.36e-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: 1.36e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566342  20 LCVLCGLPAAGKSTFARALAHRLQQEqGWAIGVVAYDDVmpdaflagararpapsqWKLLRQEllkyleyflmavingcq 99
Cdd:COG4088     6 LLILTGPPGSGKTTFAKALAQRLYAE-GIAVALLHSDDF-----------------RRFLVNE----------------- 50

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566342 100 mSVPPNRTEAMWEDFITCLKDQdlifsaafeaqscylltktAVSRPLFLVLDDNFYYQSMRYEVYQLAR-KYSLGFcqLF 178
Cdd:COG4088    51 -SFPKETYEEVVEDVRTTTADN-------------------ALDNGYSVIVDGTFYYRSWQRDFRNLAKhKAPIHI--IY 108

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1034566342 179 LDCPLETCLQRNGQRPQALPPETIHLMGRKLEKPNPEKNAW 219
Cdd:COG4088   109 LKAPLETALRRNRERGEPIPERVIARMYRKFDKPGTKDRPD 149
KTI12 pfam08433
Chromatin associated protein KTI12; This is a family of chromatin associated proteins which ...
 20-229 4.53e-16

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: 75.02  E-value: 4.53e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566342  20 LCVLCGLPAAGKSTFARALAHRLQQEQgwaIGVVAYDDvmpdaflagararpapsqwkllrqELLkyleyflmavinGCQ 99
Cdd:pfam08433   1 LVLLTGLPSSGKSTRAKQLAKYLEESN---YDVIVISD------------------------ESL------------GIE 41

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566342 100 MSvpPNRTEAMwEDFItclkdQDLIFSAAfeaqscylltKTAVSRPLFLVLDDNFYYQSMRYEVYQLARKYSLGFCQLFL 179
Cdd:pfam08433  42 KD--DYKDSAK-EKFL-----RGSLRSAV----------KRDLSKNTIVIVDSLNYIKGFRYELYCIAKAARTTYCVIHC 103

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034566342 180 DCPLETCLQRNGQRPQ--ALPPETIHLMGRKLEKPNPeKNAWEHNSLTIPSP 229
Cdd:pfam08433 104 KAPLDLCRKWNEERGQksRYPDELLDALIQRYEEPNS-KNRWDSPLFTVLSD 154
PRK09270 PRK09270
nucleoside triphosphate hydrolase domain-containing protein; Reviewed
 15-70 1.77e-04

nucleoside triphosphate hydrolase domain-containing protein; Reviewed


Pssm-ID: 236442  Cd Length: 229  Bit Score: 41.46  E-value: 1.77e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034566342  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 4.39e-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: 4.39e-04
                          10        20
                  ....*....|....*....|...
gi 1034566342  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. ...
 20-236 2.04e-144

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: 406.96  E-value: 2.04e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566342  20 LCVLCGLPAAGKSTFARALAHRLQQEQGWAIGVVAYDDVMPDAFLAGARARPAPSQWKLLRQELLKYLEYFLMAVINGCQ 99
Cdd:TIGR03575   1 LCVLCGLPAAGKSTLARSLSATLRRERGWAVAVITYDDIIPEAAFELDQSRPLPSQWKQFRQELLKYLEHFLVAVINGSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566342 100 MSVPPNRTEAMWEDFITCLKDQDL-IFSAAFEAQSCYLLTKTAVSRPLFLVLDDNFYYQSMRYEVYQLARKYSLGFCQLF 178
Cdd:TIGR03575  81 LSAPPGKTEGMWEDFVDCLKEQGLiISSGASEAQGCHSLTKPAVSRPLCLVLDDNFYYQSMRYEVYQLARKYSLGFCQLF 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034566342 179 LDCPLETCLQRNGQRPQALPPETIHLMGRKLEKPNPEKNAWEHNSLTIPSPACASEAR 236
Cdd:TIGR03575 161 LDCPVESCLLRNKQRPVPLPDETIQLMGRKIEKPNPEKNAWEHNSLVIQSSACISEDS 218
Kti12 COG4088
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) ...
 20-219 1.36e-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: 1.36e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566342  20 LCVLCGLPAAGKSTFARALAHRLQQEqGWAIGVVAYDDVmpdaflagararpapsqWKLLRQEllkyleyflmavingcq 99
Cdd:COG4088     6 LLILTGPPGSGKTTFAKALAQRLYAE-GIAVALLHSDDF-----------------RRFLVNE----------------- 50

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566342 100 mSVPPNRTEAMWEDFITCLKDQdlifsaafeaqscylltktAVSRPLFLVLDDNFYYQSMRYEVYQLAR-KYSLGFcqLF 178
Cdd:COG4088    51 -SFPKETYEEVVEDVRTTTADN-------------------ALDNGYSVIVDGTFYYRSWQRDFRNLAKhKAPIHI--IY 108

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1034566342 179 LDCPLETCLQRNGQRPQALPPETIHLMGRKLEKPNPEKNAW 219
Cdd:COG4088   109 LKAPLETALRRNRERGEPIPERVIARMYRKFDKPGTKDRPD 149
KTI12 pfam08433
Chromatin associated protein KTI12; This is a family of chromatin associated proteins which ...
 20-229 4.53e-16

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: 75.02  E-value: 4.53e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566342  20 LCVLCGLPAAGKSTFARALAHRLQQEQgwaIGVVAYDDvmpdaflagararpapsqwkllrqELLkyleyflmavinGCQ 99
Cdd:pfam08433   1 LVLLTGLPSSGKSTRAKQLAKYLEESN---YDVIVISD------------------------ESL------------GIE 41

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566342 100 MSvpPNRTEAMwEDFItclkdQDLIFSAAfeaqscylltKTAVSRPLFLVLDDNFYYQSMRYEVYQLARKYSLGFCQLFL 179
Cdd:pfam08433  42 KD--DYKDSAK-EKFL-----RGSLRSAV----------KRDLSKNTIVIVDSLNYIKGFRYELYCIAKAARTTYCVIHC 103

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034566342 180 DCPLETCLQRNGQRPQ--ALPPETIHLMGRKLEKPNPeKNAWEHNSLTIPSP 229
Cdd:pfam08433 104 KAPLDLCRKWNEERGQksRYPDELLDALIQRYEEPNS-KNRWDSPLFTVLSD 154
COG4639 COG4639
Predicted kinase [General function prediction only];
22-212 1.09e-15

Predicted kinase [General function prediction only];


Pssm-ID: 443677 [Multi-domain]  Cd Length: 145  Bit Score: 71.40  E-value: 1.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566342  22 VLCGLPAAGKSTFARALAHRLQqeqgwaigVVAYDDvmpdaflagararpapsqwklLRQELlkyleyflmavingcqms 101
Cdd:COG4639     6 VLIGLPGSGKSTFARRLFAPTE--------VVSSDD---------------------IRALL------------------ 38

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566342 102 vppnrteAMWEdfiTCLKDQDLIFSAAFEAqscyllTKTAVSRPLFLVLDDNFYYQSMRYEVYQLARKYSLGFCQLFLDC 181
Cdd:COG4639    39 -------GGDE---NDQSAWGDVFQLAHEI------ARARLRAGRLTVVDATNLQREARRRLLALARAYGALVVAVVLDV 102

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1034566342 182 PLETCLQRNGQRPQALPPETIHLMGRKLEKP 212
Cdd:COG4639   103 PLEVCLARNAARDRQVPEEVIRRMLRRLRRP 133
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
22-193 1.34e-08

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


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 52.61  E-value: 1.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566342  22 VLCGLPAAGKSTFARALAHRLQqeqgwAIgVVAYDDVMpdAFLAGARARPA---PSQWKLLRQELLKYLEYFLMAvinGC 98
Cdd:COG0645     3 LVCGLPGSGKSTLARALAERLG-----AV-RLRSDVVR--KRLFGAGLAPLersPEATARTYARLLALARELLAA---GR 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566342  99 qmSVppnrteamwedfitclkdqdlifsaafeaqscylltktavsrplflVLDDNFYYQSMRYEVYQLARKYSLGFCQLF 178
Cdd:COG0645    72 --SV----------------------------------------------ILDATFLRRAQREAFRALAEEAGAPFVLIW 103

                         170
                  ....*....|....*
gi 1034566342 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 2.49e-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: 2.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566342  20 LCVLCGLPAAGKSTFARALAHRLqqeqgwaigvvAYDDVMPDAFLAGARARPAPSQ------WKLLRQELLKYLEYFLma 93
Cdd:pfam13671   1 LILLVGLPGSGKSTLARRLLEEL-----------GAVRLSSDDERKRLFGEGRPSIsyytdaTDRTYERLHELARIAL-- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566342  94 vingcqmsvppnrteamwedfitclkdqdlifsaafeaqscylltktavSRPLFLVLDDNFYYQSMRYEVYQLARKYSLG 173
Cdd:pfam13671  68 -------------------------------------------------RAGRPVILDATNLRRDERARLLALAREYGVP 98

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1034566342 174 FCQLFLDCPLETCLQRNGQR------PQALPPETIHLMGRKLEKP 212
Cdd:pfam13671  99 VRIVVFEAPEEVLRERLAARaraggdPSDVPEEVLDRQKARFEPP 143
CysC COG0529
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ...
 18-45 1.28e-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: 1.28e-04
                          10        20
                  ....*....|....*....|....*....
gi 1034566342  18 RGLCV-LCGLPAAGKSTFARALAHRLQQE 45
Cdd:COG0529    15 KGFVVwFTGLSGSGKSTLANALERRLFER 43
PRK09270 PRK09270
nucleoside triphosphate hydrolase domain-containing protein; Reviewed
 15-70 1.77e-04

nucleoside triphosphate hydrolase domain-containing protein; Reviewed


Pssm-ID: 236442  Cd Length: 229  Bit Score: 41.46  E-value: 1.77e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034566342  15 PRKRGLCVLCGLPAAGKSTFARALAHRLQQEQGWAIGVVAYDDV-MPDAFLA--GARAR 70
Cdd:PRK09270   30 PQRRTIVGIAGPPGAGKSTLAEFLEALLQQDGELPAIQVPMDGFhLDNAVLDahGLRPR 88
DO-GTPase1 pfam19975
Double-GTPase 1; GTPase of a GTPase-centric, NTP-dependent ternary systems. The domain belongs ...
 22-47 2.14e-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: 2.14e-04
                          10        20
                  ....*....|....*....|....*.
gi 1034566342  22 VLCGLPAAGKSTFARALAHRLQQEQG 47
Cdd:pfam19975   1 LLIGLPGSGKTTFLAALWHRLREVKG 26
APSK cd02027
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ...
 23-45 4.39e-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: 4.39e-04
                          10        20
                  ....*....|....*....|...
gi 1034566342  23 LCGLPAAGKSTFARALAHRLQQE 45
Cdd:cd02027     4 LTGLSGSGKSTIARALEEKLFQR 26
AAA_22 pfam13401
AAA domain;
18-95 8.51e-04

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 38.09  E-value: 8.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034566342  18 RGLCVLCGLPAAGKSTFARALAHRLQQEQGWAIGVVAYDDVMPDAFLAG-----ARARPAPSQWKLLRQELLKYL-EYFL 91
Cdd:pfam13401   5 AGILVLTGESGTGKTTLLRRLLEQLPEVRDSVVFVDLPSGTSPKDLLRAllralGLPLSGRLSKEELLAALQQLLlALAV 84


                  ....
gi 1034566342  92 MAVI 95
Cdd:pfam13401  85 AVVL 88
PRK05537 PRK05537
bifunctional sulfate adenylyltransferase/adenylylsulfate kinase;
15-47 9.36e-04

bifunctional sulfate adenylyltransferase/adenylylsulfate kinase;


Pssm-ID: 180124 [Multi-domain]  Cd Length: 568  Bit Score: 40.04  E-value: 9.36e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1034566342  15 PR-KRGLCV-LCGLPAAGKSTFARALAHRLQQEQG 47
Cdd:PRK05537  387 PRhKQGFTVfFTGLSGAGKSTIAKALMVKLMEMRG 421
AroK COG0703
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the ...
 22-42 9.62e-04

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: 9.62e-04
                          10        20
                  ....*....|....*....|.
gi 1034566342  22 VLCGLPAAGKSTFARALAHRL 42
Cdd:COG0703     2 VLIGMMGAGKSTVGRLLAKRL 22
SK cd00464
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ...
 22-42 1.49e-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: 1.49e-03
                          10        20
                  ....*....|....*....|.
gi 1034566342  22 VLCGLPAAGKSTFARALAHRL 42
Cdd:cd00464     3 VLIGMMGAGKTTVGRLLAKAL 23
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 20-63 6.55e-03

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 37.40  E-value: 6.55e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1034566342   20 LCVLCGLPAAGKSTFARALAHRLQQEQGWAIGVVAYDDVMPDAF 63
Cdd:TIGR00956   89 LTVVLGRPGSGCSTLLKTIASNTDGFHIGVEGVITYDGITPEEI 132
aroK PRK00131
shikimate kinase; Reviewed
 15-42 7.34e-03

shikimate kinase; Reviewed


Pssm-ID: 234654 [Multi-domain]  Cd Length: 175  Bit Score: 36.32  E-value: 7.34e-03
                          10        20
                  ....*....|....*....|....*...
gi 1034566342  15 PRKRGLCVLCGLPAAGKSTFARALAHRL 42
Cdd:PRK00131    1 MLKGPNIVLIGFMGAGKSTIGRLLAKRL 28
 
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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