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Conserved domains on  [gi|568975901|ref|XP_006534319|]
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bifunctional coenzyme A synthase isoform X1 [Mus musculus]

Protein Classification

nt_trans and DPCK domain-containing protein( domain architecture ID 10205794)

nt_trans and DPCK domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CoaE COG0237
Dephospho-CoA kinase [Coenzyme transport and metabolism]; Dephospho-CoA kinase is part of the ...
 132-325 2.37e-64

Dephospho-CoA kinase [Coenzyme transport and metabolism]; Dephospho-CoA kinase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


:

Pssm-ID: 440007  Cd Length: 193  Bit Score: 201.83  E-value: 2.37e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975901 132 YVLGLTGISGSGKSSVAQRLKNLGAYIIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGTINRKVLGSRVFGNKKQMK 211
Cdd:COG0237    2 LIIGLTGGIGSGKSTVARMFAELGAPVIDADAIARELVEPGGPALAAIVEAFGEEILDADGSLDRKALAEIVFADPEALK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975901 212 ILTDIVWPVIAKLAREEMdvAVAKGKTLCVIDAAMLLEAGWQSMVHEVWTVVIPETEAVRRIVERDGLSEAAAQSRLQSQ 291
Cdd:COG0237   82 KLEAIVHPLVREEIERRL--AAARGAPYVVLDIPLLFETGLEKLVDRVIVVDAPEEVQIERLMARDGLSEEEAEARIAAQ 159

                        170       180       190
                 ....*....|....*....|....*....|....
gi 568975901 292 MSGQQLVEQSNVVLSTLWESHVTQSQVEKAWNLL 325
Cdd:COG0237  160 MPDEEKRARADFVIDNDGSLEELRAQVDALLEKL 193
nt_trans super family cl00015
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ...
 5-112 7.47e-42

nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily includes the class I amino-acyl tRNA synthetases, pantothenate synthetase (PanC), ATP sulfurylase, and the cytidylyltransferases, all of which have a conserved dinucleotide-binding domain.


The actual alignment was detected with superfamily member cd02164:

Pssm-ID: 469580  Cd Length: 143  Bit Score: 142.42  E-value: 7.47e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975901   5 RKGKLLPELLQPYAERVEHLTEFLVDIKPSLTFELVPLLDPYGPAGSDPTLEFLVVSEETYRGGMAVNRFRLENGKEELA 84
Cdd:cd02164   40 LKNKSLKELIEPYEERIANLHEFLVDLKPTLKYEIVPIDDPYGPTGTDPDLEAIVVSPETYPGALKINRKREENGLSPLE 119

                         90       100
                 ....*....|....*....|....*...
gi 568975901  85 LYQIQLLKDqshnENEEDKVSSSSFRQR 112
Cdd:cd02164  120 IVVVPLVKA----DEDGEKISSTRIRRG 143
 
Name Accession Description Interval E-value
CoaE COG0237
Dephospho-CoA kinase [Coenzyme transport and metabolism]; Dephospho-CoA kinase is part of the ...
 132-325 2.37e-64

Dephospho-CoA kinase [Coenzyme transport and metabolism]; Dephospho-CoA kinase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 440007  Cd Length: 193  Bit Score: 201.83  E-value: 2.37e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975901 132 YVLGLTGISGSGKSSVAQRLKNLGAYIIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGTINRKVLGSRVFGNKKQMK 211
Cdd:COG0237    2 LIIGLTGGIGSGKSTVARMFAELGAPVIDADAIARELVEPGGPALAAIVEAFGEEILDADGSLDRKALAEIVFADPEALK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975901 212 ILTDIVWPVIAKLAREEMdvAVAKGKTLCVIDAAMLLEAGWQSMVHEVWTVVIPETEAVRRIVERDGLSEAAAQSRLQSQ 291
Cdd:COG0237   82 KLEAIVHPLVREEIERRL--AAARGAPYVVLDIPLLFETGLEKLVDRVIVVDAPEEVQIERLMARDGLSEEEAEARIAAQ 159

                        170       180       190
                 ....*....|....*....|....*....|....
gi 568975901 292 MSGQQLVEQSNVVLSTLWESHVTQSQVEKAWNLL 325
Cdd:COG0237  160 MPDEEKRARADFVIDNDGSLEELRAQVDALLEKL 193
DPCK cd02022
Dephospho-coenzyme A kinase (DPCK, EC 2.7.1.24) catalyzes the phosphorylation of ...
 133-309 2.45e-64

Dephospho-coenzyme A kinase (DPCK, EC 2.7.1.24) catalyzes the phosphorylation of dephosphocoenzyme A (dCoA) to yield CoA, which is the final step in CoA biosynthesis.


Pssm-ID: 238980  Cd Length: 179  Bit Score: 201.59  E-value: 2.45e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975901 133 VLGLTGISGSGKSSVAQRLKNLGAYIIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGTINRKVLGSRVFGNKKQMKI 212
Cdd:cd02022    1 IIGLTGGIGSGKSTVAKLLKELGIPVIDADKIAHEVYEPGGPALQAIVEAFGPDILLEDGELDRKKLGEIVFADPEKRKK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975901 213 LTDIVWPVIAKLAREEMdvAVAKGKTLCVIDAAMLLEAGWQSMVHEVWTVVIPETEAVRRIVERDGLSEAAAQSRLQSQM 292
Cdd:cd02022   81 LEAITHPLIRKEIEEQL--AEARKEKVVVLDIPLLFETGLEKLVDRVIVVDAPPEIQIERLMKRDGLSEEEAEARIASQM 158

                        170
                 ....*....|....*..
gi 568975901 293 SGQQLVEQSNVVLSTLW 309
Cdd:cd02022  159 PLEEKRARADFVIDNSG 175
CoaE pfam01121
Dephospho-CoA kinase; This family catalyzes the phosphorylation of the 3'-hydroxyl group of ...
 132-305 2.76e-43

Dephospho-CoA kinase; This family catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form Coenzyme A EC:2.7.1.24. This enzyme uses ATP in its reaction.


Pssm-ID: 426062  Cd Length: 180  Bit Score: 147.47  E-value: 2.76e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975901  132 YVLGLTGISGSGKSSVAQRLKNLGAYIIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGTINRKVLGSRVFGNKKQMK 211
Cdd:pfam01121   1 LIVGLTGGIGSGKSTVANYFRDLGVPIIDADAIARQVVEPGGPALSRIVRHFGPTILDADGQLDRRALRELVFSNPERKK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975901  212 ILTDIVWPVIAKLAREEmdVAVAKGKTLCVIDAAMLLEAGWQSMVHEVWTVVIPETEAVRRIVERDGLSEAAAQSRLQSQ 291
Cdd:pfam01121  81 WLNGILHPLIRREIFKQ--IATLTAAPYVVLDIPLLFESGLHKLCHRVLVVDAPPELQVERLVARDGLSREEAQARIAAQ 158

                         170
                  ....*....|....
gi 568975901  292 MSGQQLVEQSNVVL 305
Cdd:pfam01121 159 ASREERLALADDVL 172
PPAT_CoAS cd02164
phosphopantetheine adenylyltransferase domain of eukaryotic and archaeal bifunctional enzymes; ...
 5-112 7.47e-42

phosphopantetheine adenylyltransferase domain of eukaryotic and archaeal bifunctional enzymes; The PPAT domain of the bifunctional enzyme with PPAT and DPCK functions. The final two steps of the CoA biosynthesis pathway are catalyzed by phosphopantetheine adenylyltransferase (PPAT) and dephospho-CoA (dPCoA) kinase (DPCK). The PPAT reaction involves the reversible adenylation of 4'-phosphopantetheine to form 3'-dPCoA and PPi, and DPCK catalyses phosphorylation of the 3'-hydroxy group of the ribose moiety of dPCoA. In eukaryotes the two enzymes are part of a large multienzyme complex . Studies in Corynebacterium ammoniagenes suggested that separate enzymes were present, and this was confirmed through identification of the bacterial PPAT/CoAD.


Pssm-ID: 173915  Cd Length: 143  Bit Score: 142.42  E-value: 7.47e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975901   5 RKGKLLPELLQPYAERVEHLTEFLVDIKPSLTFELVPLLDPYGPAGSDPTLEFLVVSEETYRGGMAVNRFRLENGKEELA 84
Cdd:cd02164   40 LKNKSLKELIEPYEERIANLHEFLVDLKPTLKYEIVPIDDPYGPTGTDPDLEAIVVSPETYPGALKINRKREENGLSPLE 119

                         90       100
                 ....*....|....*....|....*...
gi 568975901  85 LYQIQLLKDqshnENEEDKVSSSSFRQR 112
Cdd:cd02164  120 IVVVPLVKA----DEDGEKISSTRIRRG 143
TIGR00152 TIGR00152
dephospho-CoA kinase; This model produces scores in the range of 0-25 bits against adenylate, ...
 133-305 1.07e-36

dephospho-CoA kinase; This model produces scores in the range of 0-25 bits against adenylate, guanylate, uridine, and thymidylate kinases. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]


Pssm-ID: 272931  Cd Length: 190  Bit Score: 130.59  E-value: 1.07e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975901  133 VLGLTGISGSGKSSVAQRLKNLGAY-IIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGTINRKVLGSRVFGNKKQMK 211
Cdd:TIGR00152   1 LIALTGGIGSGKSTVLQYLADKYHFpVIDADKIAHQVVEPGQPAYHAIADHFGANILNQDGELDRKALGNYVFNDPEELK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975901  212 ILTDIVWPVIAKLAREEMDVAVAKgKTLCVIDAAMLLEAGWQSMVHEVWTVVIPETEAVRRIVERDGLSEAAAQSRLQSQ 291
Cdd:TIGR00152  81 WLNALTHPLIRQWMKKLIAQFQSK-YALVLLDVPLLFENNLRSLVDYVIVVERSPELQLERLMQRNDLTEEEVKKRLASQ 159

                         170
                  ....*....|....
gi 568975901  292 MSGQQLVEQSNVVL 305
Cdd:TIGR00152 160 MDIEEKLARIDTVI 173
coaE PRK14734
dephospho-CoA kinase; Provisional
 131-329 6.51e-35

dephospho-CoA kinase; Provisional


Pssm-ID: 237808  Cd Length: 200  Bit Score: 126.11  E-value: 6.51e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975901 131 LYVLGLTGISGSGKSSVAQRLKNLGAYIIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGTINRKVLGSRVFGNKKQM 210
Cdd:PRK14734   1 MLRIGLTGGIGSGKSTVADLLSSEGFLIVDADQVARDIVEPGQPALAELAEAFGDDILNPDGTLDRAGLAAKAFASPEQT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975901 211 KILTDIVWPVIAKLAREEMDVAVAKGKTLCVIDAAMLLEAGWQSMVHEVWTVVIPETEAVRRIVERDGLSEAAAQSRLQS 290
Cdd:PRK14734  81 ALLNAITHPRIAEETARRFNEARAQGAKVAVYDMPLLVEKGLDRKMDLVVVVDVDVEERVRRLVEKRGLDEDDARRRIAA 160

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 568975901 291 QMSGQQLVEQSNVVLSTLWESHVTQSQVEKAWNLLQKRL 329
Cdd:PRK14734 161 QIPDDVRLKAADIVVDNNGTREQLLAQVDGLIAEILSRV 199
PLN02388 PLN02388
phosphopantetheine adenylyltransferase
 6-111 1.09e-18

phosphopantetheine adenylyltransferase


Pssm-ID: 215218  Cd Length: 177  Bit Score: 82.31  E-value: 1.09e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975901   6 KGKLLPELLQPYAERVEHLTEFLVDIKPSLTFELVPLLDPYGPAGSDPTLEFLVVSEETYRGGMAVNRFRLENGKEELAL 85
Cdd:PLN02388  61 SKKQFAELIQPIEERMHNVEEYIKSIKPELVVQAEPIIDPYGPSIVDENLEAIVVSKETLPGGLSVNKKRAERGLSQLKI 140

                         90       100
                 ....*....|....*....|....*.
gi 568975901  86 YQIQLLKDQSHNEneedKVSSSSFRQ 111
Cdd:PLN02388 141 EVVDIVPEESTGN----KLSSTTLRR 162
 
Name Accession Description Interval E-value
CoaE COG0237
Dephospho-CoA kinase [Coenzyme transport and metabolism]; Dephospho-CoA kinase is part of the ...
 132-325 2.37e-64

Dephospho-CoA kinase [Coenzyme transport and metabolism]; Dephospho-CoA kinase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 440007  Cd Length: 193  Bit Score: 201.83  E-value: 2.37e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975901 132 YVLGLTGISGSGKSSVAQRLKNLGAYIIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGTINRKVLGSRVFGNKKQMK 211
Cdd:COG0237    2 LIIGLTGGIGSGKSTVARMFAELGAPVIDADAIARELVEPGGPALAAIVEAFGEEILDADGSLDRKALAEIVFADPEALK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975901 212 ILTDIVWPVIAKLAREEMdvAVAKGKTLCVIDAAMLLEAGWQSMVHEVWTVVIPETEAVRRIVERDGLSEAAAQSRLQSQ 291
Cdd:COG0237   82 KLEAIVHPLVREEIERRL--AAARGAPYVVLDIPLLFETGLEKLVDRVIVVDAPEEVQIERLMARDGLSEEEAEARIAAQ 159

                        170       180       190
                 ....*....|....*....|....*....|....
gi 568975901 292 MSGQQLVEQSNVVLSTLWESHVTQSQVEKAWNLL 325
Cdd:COG0237  160 MPDEEKRARADFVIDNDGSLEELRAQVDALLEKL 193
DPCK cd02022
Dephospho-coenzyme A kinase (DPCK, EC 2.7.1.24) catalyzes the phosphorylation of ...
 133-309 2.45e-64

Dephospho-coenzyme A kinase (DPCK, EC 2.7.1.24) catalyzes the phosphorylation of dephosphocoenzyme A (dCoA) to yield CoA, which is the final step in CoA biosynthesis.


Pssm-ID: 238980  Cd Length: 179  Bit Score: 201.59  E-value: 2.45e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975901 133 VLGLTGISGSGKSSVAQRLKNLGAYIIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGTINRKVLGSRVFGNKKQMKI 212
Cdd:cd02022    1 IIGLTGGIGSGKSTVAKLLKELGIPVIDADKIAHEVYEPGGPALQAIVEAFGPDILLEDGELDRKKLGEIVFADPEKRKK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975901 213 LTDIVWPVIAKLAREEMdvAVAKGKTLCVIDAAMLLEAGWQSMVHEVWTVVIPETEAVRRIVERDGLSEAAAQSRLQSQM 292
Cdd:cd02022   81 LEAITHPLIRKEIEEQL--AEARKEKVVVLDIPLLFETGLEKLVDRVIVVDAPPEIQIERLMKRDGLSEEEAEARIASQM 158

                        170
                 ....*....|....*..
gi 568975901 293 SGQQLVEQSNVVLSTLW 309
Cdd:cd02022  159 PLEEKRARADFVIDNSG 175
CoaE pfam01121
Dephospho-CoA kinase; This family catalyzes the phosphorylation of the 3'-hydroxyl group of ...
 132-305 2.76e-43

Dephospho-CoA kinase; This family catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form Coenzyme A EC:2.7.1.24. This enzyme uses ATP in its reaction.


Pssm-ID: 426062  Cd Length: 180  Bit Score: 147.47  E-value: 2.76e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975901  132 YVLGLTGISGSGKSSVAQRLKNLGAYIIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGTINRKVLGSRVFGNKKQMK 211
Cdd:pfam01121   1 LIVGLTGGIGSGKSTVANYFRDLGVPIIDADAIARQVVEPGGPALSRIVRHFGPTILDADGQLDRRALRELVFSNPERKK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975901  212 ILTDIVWPVIAKLAREEmdVAVAKGKTLCVIDAAMLLEAGWQSMVHEVWTVVIPETEAVRRIVERDGLSEAAAQSRLQSQ 291
Cdd:pfam01121  81 WLNGILHPLIRREIFKQ--IATLTAAPYVVLDIPLLFESGLHKLCHRVLVVDAPPELQVERLVARDGLSREEAQARIAAQ 158

                         170
                  ....*....|....
gi 568975901  292 MSGQQLVEQSNVVL 305
Cdd:pfam01121 159 ASREERLALADDVL 172
PPAT_CoAS cd02164
phosphopantetheine adenylyltransferase domain of eukaryotic and archaeal bifunctional enzymes; ...
 5-112 7.47e-42

phosphopantetheine adenylyltransferase domain of eukaryotic and archaeal bifunctional enzymes; The PPAT domain of the bifunctional enzyme with PPAT and DPCK functions. The final two steps of the CoA biosynthesis pathway are catalyzed by phosphopantetheine adenylyltransferase (PPAT) and dephospho-CoA (dPCoA) kinase (DPCK). The PPAT reaction involves the reversible adenylation of 4'-phosphopantetheine to form 3'-dPCoA and PPi, and DPCK catalyses phosphorylation of the 3'-hydroxy group of the ribose moiety of dPCoA. In eukaryotes the two enzymes are part of a large multienzyme complex . Studies in Corynebacterium ammoniagenes suggested that separate enzymes were present, and this was confirmed through identification of the bacterial PPAT/CoAD.


Pssm-ID: 173915  Cd Length: 143  Bit Score: 142.42  E-value: 7.47e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975901   5 RKGKLLPELLQPYAERVEHLTEFLVDIKPSLTFELVPLLDPYGPAGSDPTLEFLVVSEETYRGGMAVNRFRLENGKEELA 84
Cdd:cd02164   40 LKNKSLKELIEPYEERIANLHEFLVDLKPTLKYEIVPIDDPYGPTGTDPDLEAIVVSPETYPGALKINRKREENGLSPLE 119

                         90       100
                 ....*....|....*....|....*...
gi 568975901  85 LYQIQLLKDqshnENEEDKVSSSSFRQR 112
Cdd:cd02164  120 IVVVPLVKA----DEDGEKISSTRIRRG 143
TIGR00152 TIGR00152
dephospho-CoA kinase; This model produces scores in the range of 0-25 bits against adenylate, ...
 133-305 1.07e-36

dephospho-CoA kinase; This model produces scores in the range of 0-25 bits against adenylate, guanylate, uridine, and thymidylate kinases. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]


Pssm-ID: 272931  Cd Length: 190  Bit Score: 130.59  E-value: 1.07e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975901  133 VLGLTGISGSGKSSVAQRLKNLGAY-IIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGTINRKVLGSRVFGNKKQMK 211
Cdd:TIGR00152   1 LIALTGGIGSGKSTVLQYLADKYHFpVIDADKIAHQVVEPGQPAYHAIADHFGANILNQDGELDRKALGNYVFNDPEELK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975901  212 ILTDIVWPVIAKLAREEMDVAVAKgKTLCVIDAAMLLEAGWQSMVHEVWTVVIPETEAVRRIVERDGLSEAAAQSRLQSQ 291
Cdd:TIGR00152  81 WLNALTHPLIRQWMKKLIAQFQSK-YALVLLDVPLLFENNLRSLVDYVIVVERSPELQLERLMQRNDLTEEEVKKRLASQ 159

                         170
                  ....*....|....
gi 568975901  292 MSGQQLVEQSNVVL 305
Cdd:TIGR00152 160 MDIEEKLARIDTVI 173
coaE PRK14734
dephospho-CoA kinase; Provisional
 131-329 6.51e-35

dephospho-CoA kinase; Provisional


Pssm-ID: 237808  Cd Length: 200  Bit Score: 126.11  E-value: 6.51e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975901 131 LYVLGLTGISGSGKSSVAQRLKNLGAYIIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGTINRKVLGSRVFGNKKQM 210
Cdd:PRK14734   1 MLRIGLTGGIGSGKSTVADLLSSEGFLIVDADQVARDIVEPGQPALAELAEAFGDDILNPDGTLDRAGLAAKAFASPEQT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975901 211 KILTDIVWPVIAKLAREEMDVAVAKGKTLCVIDAAMLLEAGWQSMVHEVWTVVIPETEAVRRIVERDGLSEAAAQSRLQS 290
Cdd:PRK14734  81 ALLNAITHPRIAEETARRFNEARAQGAKVAVYDMPLLVEKGLDRKMDLVVVVDVDVEERVRRLVEKRGLDEDDARRRIAA 160

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 568975901 291 QMSGQQLVEQSNVVLSTLWESHVTQSQVEKAWNLLQKRL 329
Cdd:PRK14734 161 QIPDDVRLKAADIVVDNNGTREQLLAQVDGLIAEILSRV 199
coaE PRK03333
dephospho-CoA kinase/protein folding accessory domain-containing protein; Provisional
 134-323 3.05e-33

dephospho-CoA kinase/protein folding accessory domain-containing protein; Provisional


Pssm-ID: 179560 [Multi-domain]  Cd Length: 395  Bit Score: 126.66  E-value: 3.05e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975901 134 LGLTGISGSGKSSVAQRLKNLGAYIIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGTINRKVLGSRVFGNKKQMKIL 213
Cdd:PRK03333   4 IGLTGGIGAGKSTVAARLAELGAVVVDADVLAREVVEPGTEGLAALVAAFGDDILLADGALDRPALAAKAFADDEARAVL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975901 214 TDIVWPVIAklAREEMDVAVAKGKTLCVIDAAMLLEAGWQSMVHEVWTVVIPETEAVRRIVERDGLSEAAAQSRLQSQMS 293
Cdd:PRK03333  84 NGIVHPLVG--ARRAELIAAAPEDAVVVEDIPLLVESGMAPLFHLVVVVDADVEVRVRRLVEQRGMAEADARARIAAQAS 161

                        170       180       190
                 ....*....|....*....|....*....|
gi 568975901 294 GQQLVEQSNVVLSTLWESHVTQSQVEKAWN 323
Cdd:PRK03333 162 DEQRRAVADVWLDNSGTPDELVEAVRALWA 191
PLN02422 PLN02422
dephospho-CoA kinase
 133-320 2.81e-25

dephospho-CoA kinase


Pssm-ID: 215232  Cd Length: 232  Bit Score: 101.75  E-value: 2.81e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975901 133 VLGLTGISGSGKSSVAQRLKNLGAYIIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGTINRKVLGSRVFGNKKQMKI 212
Cdd:PLN02422   3 VVGLTGGIASGKSTVSNLFKSSGIPVVDADKVARDVLKKGSGGWKRVVAAFGEDILLPDGEVDREKLGQIVFSDPSKRQL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975901 213 LTDIVWPVIAKLAREEMDVAVAKGKTLCVIDAAMLLEAG---WQSMVHEVWtvVIPETEaVRRIVERDGLSEAAAQSRLQ 289
Cdd:PLN02422  83 LNRLLAPYISSGIFWEILKLWLKGCKVIVLDIPLLFETKmdkWTKPVVVVW--VDPETQ-LERLMARDGLSEEQARNRIN 159

                        170       180       190
                 ....*....|....*....|....*....|.
gi 568975901 290 SQMSGQQLVEQSNVVLSTLWESHVTQSQVEK 320
Cdd:PLN02422 160 AQMPLDWKRSKADIVIDNSGSLEDLKQQFQK 190
PLN02388 PLN02388
phosphopantetheine adenylyltransferase
 6-111 1.09e-18

phosphopantetheine adenylyltransferase


Pssm-ID: 215218  Cd Length: 177  Bit Score: 82.31  E-value: 1.09e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975901   6 KGKLLPELLQPYAERVEHLTEFLVDIKPSLTFELVPLLDPYGPAGSDPTLEFLVVSEETYRGGMAVNRFRLENGKEELAL 85
Cdd:PLN02388  61 SKKQFAELIQPIEERMHNVEEYIKSIKPELVVQAEPIIDPYGPSIVDENLEAIVVSKETLPGGLSVNKKRAERGLSQLKI 140

                         90       100
                 ....*....|....*....|....*.
gi 568975901  86 YQIQLLKDQSHNEneedKVSSSSFRQ 111
Cdd:PLN02388 141 EVVDIVPEESTGN----KLSSTTLRR 162
PRK00777 PRK00777
pantetheine-phosphate adenylyltransferase;
16-121 2.89e-17

pantetheine-phosphate adenylyltransferase;


Pssm-ID: 234834  Cd Length: 153  Bit Score: 77.57  E-value: 2.89e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975901  16 PYAERVEHLTEFLVDIKPSLTFELVPLLDPYGPAGSDPtLEFLVVSEETYRGGMAVNRFRLENGKEELALYQIQLLKDqs 95
Cdd:PRK00777  51 PYEVRLKNLKKFLKAVEYDREYEIVKIDDPYGPALEDD-FDAIVVSPETYPGALKINEIRRERGLKPLEIVVIDFVLA-- 127

                         90       100       110
                 ....*....|....*....|....*....|.
gi 568975901  96 hneneEDKVSSSSFRQR-----ILGNLLQPP 121
Cdd:PRK00777 128 -----EDGKPISSTRIRrgeidEHGNLIKER 153
PTZ00451 PTZ00451
dephospho-CoA kinase; Provisional
 133-293 1.92e-08

dephospho-CoA kinase; Provisional


Pssm-ID: 185630  Cd Length: 244  Bit Score: 54.50  E-value: 1.92e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975901 133 VLGLTGISGSGKSSVAQRLKN-LGAYIIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGTINRKVLGSRVFGNKKQMK 211
Cdd:PTZ00451   3 LIGLTGGIACGKSTVSRILREeHHIEVIDADLVVRELQAPNMACTRKIAARWPLCVHPETGELNRAELGKIIFSDAQARR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975901 212 ILTDIVWPVIAKLAREEMDVA---------VAKGKTLCVIDAAMLLEAG-WQSMVHEVWTVVIPETEAVRRIVERDGLSE 281
Cdd:PTZ00451  83 ALGRIMNPPIFRAILKRIAAAwwedlwrsgAGSSPLIVVLDAPTLFETKtFTYFVSASVVVSCSEERQIERLRKRNGFSK 162

                        170
                 ....*....|..
gi 568975901 282 AAAQSRLQSQMS 293
Cdd:PTZ00451 163 EEALQRIGSQMP 174
PRK01170 PRK01170
bifunctional pantetheine-phosphate adenylyltransferase/NTP phosphatase;
5-88 4.30e-06

bifunctional pantetheine-phosphate adenylyltransferase/NTP phosphatase;


Pssm-ID: 234912 [Multi-domain]  Cd Length: 322  Bit Score: 47.89  E-value: 4.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975901   5 RKGKLLPellQPYAERVEHLTEFLvdIKPSLTFELVPLLDPYGPAGSDPTLEFLVVSEETYRGGMAVNRFRLENGKEELA 84
Cdd:PRK01170  41 RKNKVYP---IPYEDRKRKLENFI--KKFTNKFRIRPIDDRYGNTLYEEDYEIIVVSPETYQRALKINEIRIKNGLPPLK 115


                 ....
gi 568975901  85 LYQI 88
Cdd:PRK01170 116 IVRV 119
COG4639 COG4639
Predicted kinase [General function prediction only];
136-277 2.18e-04

Predicted kinase [General function prediction only];


Pssm-ID: 443677 [Multi-domain]  Cd Length: 145  Bit Score: 40.97  E-value: 2.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975901 136 LTGISGSGKSSVAQRLkNLGAYIIDSDHLghRAyapggpayqpvveafgtdILHKDGTINRkvlgsrvfgnkkqmkiltd 215
Cdd:COG4639    7 LIGLPGSGKSTFARRL-FAPTEVVSSDDI--RA------------------LLGGDENDQS------------------- 46

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568975901 216 iVWPVIAKLAREEMDVAVAKGKTLcVIDA--------AMLLEAGWQsmvHEVWTVVI----PETEAVRRIVERD 277
Cdd:COG4639   47 -AWGDVFQLAHEIARARLRAGRLT-VVDAtnlqrearRRLLALARA---YGALVVAVvldvPLEVCLARNAARD 115
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
 138-276 4.61e-04

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: 39.99  E-value: 4.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975901  138 GISGSGKSSVAQRL-KNLGAYIIDSD--HLGHRAYAPGGPAYQPvveafgtdilhkdgtinrkvlgsrvfgnkkqmkILT 214
Cdd:pfam13671   6 GLPGSGKSTLARRLlEELGAVRLSSDdeRKRLFGEGRPSISYYT---------------------------------DAT 52

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568975901  215 DIVWPVIAKLAREemdvaVAKGKTLCVIDAAMLLEAGWQSMV-----HEVWTVVI----PETEAVRRIVER 276
Cdd:pfam13671  53 DRTYERLHELARI-----ALRAGRPVILDATNLRRDERARLLalareYGVPVRIVvfeaPEEVLRERLAAR 118
CysC COG0529
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ...
 133-162 5.49e-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: 40.46  E-value: 5.49e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 568975901 133 VLGLTGISGSGKSSVA----QRLKNLG--AYIIDSD 162
Cdd:COG0529   18 VVWFTGLSGSGKSTLAnaleRRLFERGrhVYLLDGD 53
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 133-166 7.18e-04

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 41.45  E-value: 7.18e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 568975901 133 VLGLTGISGSGKSSVA----QRLKNLG--AYIIDSDHLGH 166
Cdd:PRK05506 462 TVWFTGLSGSGKSTIAnlveRRLHALGrhTYLLDGDNVRH 501
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
131-182 7.35e-04

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


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 39.51  E-value: 7.35e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568975901 131 LYVLGltGISGSGKSSVAQRL-KNLGAYIIDSDHLGHRAYAPGGPAYQPVVEA 182
Cdd:COG0645    1 LILVC--GLPGSGKSTLARALaERLGAVRLRSDVVRKRLFGAGLAPLERSPEA 51
GntK cd02021
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ...
 131-168 4.28e-03

Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting product gluconate-6-phoshate is an important precursor of gluconate metabolism. GntK acts as a dimmer composed of two identical subunits.


Pssm-ID: 238979 [Multi-domain]  Cd Length: 150  Bit Score: 37.23  E-value: 4.28e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 568975901 131 LYVLglTGISGSGKSSVAQRL-KNLGAYIIDSDHLGHRA 168
Cdd:cd02021    1 IIVV--MGVSGSGKSTVGKALaERLGAPFIDGDDLHPPA 37
PRK03846 PRK03846
adenylylsulfate kinase; Provisional
 132-166 5.81e-03

adenylylsulfate kinase; Provisional


Pssm-ID: 179661  Cd Length: 198  Bit Score: 37.23  E-value: 5.81e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 568975901 132 YVLGLTGISGSGKSSVA----QRLKNLG--AYIIDSDHLGH 166
Cdd:PRK03846  25 VVLWFTGLSGSGKSTVAgaleEALHELGvsTYLLDGDNVRH 65
SK cd00464
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ...
 136-164 7.36e-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: 36.38  E-value: 7.36e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 568975901 136 LTGISGSGKSSVAQRL-KNLGAYIIDSDHL 164
Cdd:cd00464    4 LIGMMGAGKTTVGRLLaKALGLPFVDLDEL 33
 
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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