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Conserved domains on  [gi|564333470|ref|XP_006231340|]
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pantothenate kinase 1 isoform X3 [Rattus norvegicus]

Protein Classification

type II pantothenate kinase( domain architecture ID 10508179)

type II pantothenate kinase catalyzes the formation of (R)-4'-phosphopantothenate from (R)-pantothenate in coenzyme A biosynthesis

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ASKHA_NBD_PanK-II_Pank1 cd24135
nucleotide-binding domain (NBD) of pantothenate kinase 1 (Pank1) from type II pantothenate ...
1-349 0e+00

nucleotide-binding domain (NBD) of pantothenate kinase 1 (Pank1) from type II pantothenate kinase (PanK-II) subfamily; PanK (EC 2.7.1.33), also called pantothenic acid kinase, is the first enzyme in the Coenzyme A (CoA) biosynthetic pathway. It catalyzes the phosphorylation of pantothenate (vitamin B5) to form 4'-phosphopantothenate at the expense of a molecule of adenosine triphosphate (ATP), which is the rate-limiting step in CoA biosynthesis. It cannot utilize a phosphoryl donor other than ATP. Three distinct types of PanK have been identified, PanK-I, PanK-II and PanK-III. Eukaryotic PanK-II enzymes often occur as different isoforms, such as PanK1, PanK2, PanK3 and PanK4. The model corresponds to PanK1.


:

Pssm-ID: 466985 [Multi-domain]  Cd Length: 352  Bit Score: 718.70  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470   1 MDIGGTLVKLVYFEPKDITAEEEQEEVENLKSIRKYLTSNTAYGKTGIRDVHLELKNLTMCGRKGNLHFIRFPTCAMHMF 80
Cdd:cd24135    4 MDIGGTLVKLVYFEPKDITAEEEQEEVENLKSIRKYLTSNTAYGKTGIRDVHLELKNLTMCGRKGNLHFIRFPSCAMHRF 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470  81 IQMGSEKNFSSLHTTLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSVGFNGKPECYYFENPTNPELCQKK 160
Cdd:cd24135   84 IQMGSEKNFSSLHTTLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSVGFNGQPECYYFENPTDPEQCQKK 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470 161 PYCLDNPYPMLLVNMGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALDMAAKGDSTNVDKLVKDIYG 240
Cdd:cd24135  164 PYCLDNPYPMLLVNIGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALEMAAKGDSTNVDKLVKDIYG 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470 241 GDYERFGLQGSAVASSFGNMMSKEKRESISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINMVSMKLLA 320
Cdd:cd24135  244 GDYERFGLQGSAVASSFGHMMSKEKRDSISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINMVSMKLLA 323
                        330       340
                 ....*....|....*....|....*....
gi 564333470 321 YAMDFWSKGQLKALFLEHEGYFGAVGALL 349
Cdd:cd24135  324 YAMDFWSKGQLKALFLEHEGYFGAVGALL 352
 
Name Accession Description Interval E-value
ASKHA_NBD_PanK-II_Pank1 cd24135
nucleotide-binding domain (NBD) of pantothenate kinase 1 (Pank1) from type II pantothenate ...
1-349 0e+00

nucleotide-binding domain (NBD) of pantothenate kinase 1 (Pank1) from type II pantothenate kinase (PanK-II) subfamily; PanK (EC 2.7.1.33), also called pantothenic acid kinase, is the first enzyme in the Coenzyme A (CoA) biosynthetic pathway. It catalyzes the phosphorylation of pantothenate (vitamin B5) to form 4'-phosphopantothenate at the expense of a molecule of adenosine triphosphate (ATP), which is the rate-limiting step in CoA biosynthesis. It cannot utilize a phosphoryl donor other than ATP. Three distinct types of PanK have been identified, PanK-I, PanK-II and PanK-III. Eukaryotic PanK-II enzymes often occur as different isoforms, such as PanK1, PanK2, PanK3 and PanK4. The model corresponds to PanK1.


Pssm-ID: 466985 [Multi-domain]  Cd Length: 352  Bit Score: 718.70  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470   1 MDIGGTLVKLVYFEPKDITAEEEQEEVENLKSIRKYLTSNTAYGKTGIRDVHLELKNLTMCGRKGNLHFIRFPTCAMHMF 80
Cdd:cd24135    4 MDIGGTLVKLVYFEPKDITAEEEQEEVENLKSIRKYLTSNTAYGKTGIRDVHLELKNLTMCGRKGNLHFIRFPSCAMHRF 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470  81 IQMGSEKNFSSLHTTLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSVGFNGKPECYYFENPTNPELCQKK 160
Cdd:cd24135   84 IQMGSEKNFSSLHTTLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSVGFNGQPECYYFENPTDPEQCQKK 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470 161 PYCLDNPYPMLLVNMGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALDMAAKGDSTNVDKLVKDIYG 240
Cdd:cd24135  164 PYCLDNPYPMLLVNIGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALEMAAKGDSTNVDKLVKDIYG 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470 241 GDYERFGLQGSAVASSFGNMMSKEKRESISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINMVSMKLLA 320
Cdd:cd24135  244 GDYERFGLQGSAVASSFGHMMSKEKRDSISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINMVSMKLLA 323
                        330       340
                 ....*....|....*....|....*....
gi 564333470 321 YAMDFWSKGQLKALFLEHEGYFGAVGALL 349
Cdd:cd24135  324 YAMDFWSKGQLKALFLEHEGYFGAVGALL 352
Fumble pfam03630
Fumble; Fumble is required for cell division in Drosophila. Mutants lacking fumble exhibit ...
1-347 3.59e-161

Fumble; Fumble is required for cell division in Drosophila. Mutants lacking fumble exhibit abnormalities in bipolar spindle organization, chromosome segregation, and contractile ring formation. Analyses have demonstrated that encodes three protein isoforms, all of which contain a domain with high similarity to the pantothenate kinases of A. nidulans and mouse. A role of fumble in membrane synthesis has been proposed.


Pssm-ID: 460995 [Multi-domain]  Cd Length: 311  Bit Score: 453.49  E-value: 3.59e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470    1 MDIGGTLVKLVYFEPKDITAEEEQeevenlksirkyltsntaygktgirdvhlelknltmcgrkGNLHFIRFPTCAMHMF 80
Cdd:pfam03630   3 IDIGGTLAKLVYFSPVPDSPKELG----------------------------------------GRLHFIKFETTKIEDC 42
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470   81 IQMGSEKNFSSLHT----TLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSvgfNGKPECYYFENPTNPEL 156
Cdd:pfam03630  43 LEFIKSLGLNSKGTdrglTVKATGGGAYKFYDLFKEKLGVKVDKEDEMECLIKGLNFLLT---NIPDEVFTYSDSPEYFF 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470  157 CQKKPyclDNPYPMLLVNMGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALDMAAKGDSTNVDKLVK 236
Cdd:pfam03630 120 QTVDN---NSIYPYLLVNIGSGVSILKVEGPDKFERVGGTSLGGGTFWGLCSLLTGAKSFDEMLELAEKGDNRNVDMLVG 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470  237 DIYGGDYERFGLQGSAVASSFGNMMSKEKRESISK----EDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRIN 312
Cdd:pfam03630 197 DIYGGDYEKIGLKSDTIASSFGKVFRKKFRESASNdaspEDIARSLLYMISNNIGQIAYLNAKLHGLKRIYFGGNFIRGH 276
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 564333470  313 MVSMKLLAYAMDFWSKGQLKALFLEHEGYFGAVGA 347
Cdd:pfam03630 277 PITMKTLSYAINFWSKGELKALFLRHEGYLGALGA 311
panK_eukar TIGR00555
pantothenate kinase, eukaryotic/staphyloccocal type; This model describes a eukaryotic form of ...
1-350 3.24e-137

pantothenate kinase, eukaryotic/staphyloccocal type; This model describes a eukaryotic form of pantothenate kinase, characterized from the fungus Aspergillus nidulans and with similar forms known in several other eukaryotes. It also includes forms from several Gram-positive bacteria suggested to have originated from the eukaryotic form by lateral transfer. It differs in a number of biochemical properties (such as inhibition by acetyl-CoA) from most bacterial CoaA and lacks sequence similarity. This enzyme is the key regulatory step in the biosynthesis of coenzyme A (CoA). [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]


Pssm-ID: 273135 [Multi-domain]  Cd Length: 296  Bit Score: 392.15  E-value: 3.24e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470    1 MDIGGTLVKLVYFEPKditaeeeqeevenlkSIRKYLTSNTaygktgirdvhlelknltmcgrkGNLH-FIRFPTCAMHM 79
Cdd:TIGR00555   5 IDIGGTLIKVVYEEKK---------------GRRKFKTFET-----------------------TNIDkFIEWLKNQIHR 46
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470   80 FiqmgseknfsSLHTTLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSVGFNGKPECYYFEnptnpelCQK 159
Cdd:TIGR00555  47 H----------SRITTLCATGGGAFKFAELIYESAGIQLHKFDEFDALIQGLNYLLKEEPKEKFTYYDFE-------CQK 109
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470  160 KPYCLDNPYPMLLVNMGSGVSILAVYSkDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALDMAAKGDSTNVDKLVKDIY 239
Cdd:TIGR00555 110 KPIDLDDIYPYLLVNIGTGTSILYVDG-DNYERVGGTSLGGGTFLGLGKLLTGIQTFDELLEMAQHGDRTNVDLLVGDIY 188
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470  240 GGDYERFGLQGSAVASSFGNMMSKEKRESISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINMVSMKLL 319
Cdd:TIGR00555 189 GGDYSESGLDGSLTASSFGKVLSKHLDQSFSPEDIAASLLGLIGNNIGQIAYLCALRYNIDRIVFIGSFLRNNQLLMKVL 268
                         330       340       350
                  ....*....|....*....|....*....|.
gi 564333470  320 AYAMDFWSKgqlKALFLEHEGYFGAVGALLE 350
Cdd:TIGR00555 269 SYATNFWSK---KALFLEHEGYSGAIGALLS 296
PLN02920 PLN02920
pantothenate kinase 1
1-349 1.43e-64

pantothenate kinase 1


Pssm-ID: 215498 [Multi-domain]  Cd Length: 398  Bit Score: 210.08  E-value: 1.43e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470   1 MDIGGTLVKLVYFEPKDitaeeeqeevENLKSIRKYLTSNTAYGKTGIRDVHLELKNLTMCgrkgnLHFIRFPTCAMHMF 80
Cdd:PLN02920  23 LDIGGSLIKLVYFSRNS----------GDSEDPRNDSSVKSDGVNGRLHFAKFETRKINDC-----LEFISSNKLHHGGF 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470  81 IQM---GSEKNFsslhttLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGllyvdsVGFNGKP---ECYYFENPtnp 154
Cdd:PLN02920  88 QHHenpTHDKNF------IKATGGGAYKFADLFKEKLGISLDKEDEMDCLVTG------ANFLLKAvhhEAFTYLDG--- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470 155 elcQKKPYCLDNP--YPMLLVNMGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALDMAAKGDSTNVD 232
Cdd:PLN02920 153 ---QKEFVQIDHNdlYPYLLVNIGSGVSMIKVDGDGKFERVSGTSVGGGTFWGLGKLLTKCKSFDELLELSHQGNNRVID 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470 233 KLVKDIYGG-DYERFGLQGSAVASSFGNMMSKEKR-ESISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLR 310
Cdd:PLN02920 230 MLVGDIYGGmDYSKIGLSSTTIASSFGKAISDNKElEDYKPEDVARSLLRMISNNIGQISYLNALRFGLKRIFFGGFFIR 309
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 564333470 311 INMVSMKLLAYAMDFWSKGQLKALFLEHEGYFGAVGALL 349
Cdd:PLN02920 310 GHSYTMDTISVAVHFWSKGEAKAMFLRHEGFLGALGAFM 348
PanK COG5146
Pantothenate kinase [Coenzyme transport and metabolism]; Pantothenate kinase is part of the ...
2-349 4.59e-34

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


Pssm-ID: 444059 [Multi-domain]  Cd Length: 270  Bit Score: 126.54  E-value: 4.59e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470   2 DIGGTLVKLVYFEpkditaeeeqeevenlksirkyltsntaygktgirdvhlelknltmcgrKGNLHFIRFPTCAMHMFI 81
Cdd:COG5146    7 DAGGTLTKIAYLE-------------------------------------------------DGERRYKKFPSDEIESVA 37
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470  82 Q-MGSEKNFSslhtTLCATGGGAFKFEEdfrMIADLQLHKLDELDCLIQGllyvdsVGFNGKPECYYFENptnpelcqkk 160
Cdd:COG5146   38 DwLNKFINIE----KIGLTGGRAEVLAE---KLNGDPKQYIVEFDATGKG------VRYLLKEEGHDIDK---------- 94
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470 161 pycldnpypMLLVNMGSGVSIlaVYSKDN-YKRVTGTSLGGGTFLGLCCLLTGCETFEEALDMAAKGDSTNVDKLVKDIY 239
Cdd:COG5146   95 ---------FIITNVGTGTSI--HYMDGDtQERVGGTGVGGGTLMGLSYLLTGISDFEEIVELAKKGDRDGIDLKVKDIY 163
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470 240 GGDYErfGLQGSAVASSFGNMMSKEKrESISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINmvsmKLL 319
Cdd:COG5146  164 EGMEP--PIPGDLTASNFGKVLITLD-ESATKEDILAAIIGLVGETITTLSIQAAEEYDTETIVYIGSTLTNN----PLL 236
                        330       340       350
                 ....*....|....*....|....*....|.
gi 564333470 320 AYAMDFWSKGQ-LKALFLEHEGYFGAVGALL 349
Cdd:COG5146  237 QEVIESYTILRgKKPIFLENGEFSGAIGALL 267
 
Name Accession Description Interval E-value
ASKHA_NBD_PanK-II_Pank1 cd24135
nucleotide-binding domain (NBD) of pantothenate kinase 1 (Pank1) from type II pantothenate ...
1-349 0e+00

nucleotide-binding domain (NBD) of pantothenate kinase 1 (Pank1) from type II pantothenate kinase (PanK-II) subfamily; PanK (EC 2.7.1.33), also called pantothenic acid kinase, is the first enzyme in the Coenzyme A (CoA) biosynthetic pathway. It catalyzes the phosphorylation of pantothenate (vitamin B5) to form 4'-phosphopantothenate at the expense of a molecule of adenosine triphosphate (ATP), which is the rate-limiting step in CoA biosynthesis. It cannot utilize a phosphoryl donor other than ATP. Three distinct types of PanK have been identified, PanK-I, PanK-II and PanK-III. Eukaryotic PanK-II enzymes often occur as different isoforms, such as PanK1, PanK2, PanK3 and PanK4. The model corresponds to PanK1.


Pssm-ID: 466985 [Multi-domain]  Cd Length: 352  Bit Score: 718.70  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470   1 MDIGGTLVKLVYFEPKDITAEEEQEEVENLKSIRKYLTSNTAYGKTGIRDVHLELKNLTMCGRKGNLHFIRFPTCAMHMF 80
Cdd:cd24135    4 MDIGGTLVKLVYFEPKDITAEEEQEEVENLKSIRKYLTSNTAYGKTGIRDVHLELKNLTMCGRKGNLHFIRFPSCAMHRF 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470  81 IQMGSEKNFSSLHTTLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSVGFNGKPECYYFENPTNPELCQKK 160
Cdd:cd24135   84 IQMGSEKNFSSLHTTLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSVGFNGQPECYYFENPTDPEQCQKK 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470 161 PYCLDNPYPMLLVNMGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALDMAAKGDSTNVDKLVKDIYG 240
Cdd:cd24135  164 PYCLDNPYPMLLVNIGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALEMAAKGDSTNVDKLVKDIYG 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470 241 GDYERFGLQGSAVASSFGNMMSKEKRESISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINMVSMKLLA 320
Cdd:cd24135  244 GDYERFGLQGSAVASSFGHMMSKEKRDSISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINMVSMKLLA 323
                        330       340
                 ....*....|....*....|....*....
gi 564333470 321 YAMDFWSKGQLKALFLEHEGYFGAVGALL 349
Cdd:cd24135  324 YAMDFWSKGQLKALFLEHEGYFGAVGALL 352
ASKHA_NBD_PanK-II_Pank2 cd24136
nucleotide-binding domain (NBD) of pantothenate kinase 2 (Pank2) from type II pantothenate ...
1-351 0e+00

nucleotide-binding domain (NBD) of pantothenate kinase 2 (Pank2) from type II pantothenate kinase (PanK-II) subfamily; PanK (EC 2.7.1.33), also called pantothenic acid kinase, is the first enzyme in the Coenzyme A (CoA) biosynthetic pathway. It catalyzes the phosphorylation of pantothenate (vitamin B5) to form 4'-phosphopantothenate at the expense of a molecule of adenosine triphosphate (ATP), which is the rate-limiting step in CoA biosynthesis. It cannot utilize a phosphoryl donor other than ATP. Three distinct types of PanK have been identified, PanK-I, PanK-II and PanK-III. Eukaryotic PanK-II enzymes often occur as different isoforms, such as PanK1, PanK2, PanK3 and PanK4. The model corresponds to PanK2.


Pssm-ID: 466986 [Multi-domain]  Cd Length: 354  Bit Score: 632.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470   1 MDIGGTLVKLVYFEPKDITAEEEQEEVENLKSIRKYLTSNTAYGKTGIRDVHLELKNLTMCGRKGNLHFIRFPTCAMHMF 80
Cdd:cd24136    4 LDIGGTLVKLVYFEPKDITAEEEEEEVENLKSIRKYLTSNVAYGSTGIRDVHLELKDLTLCGRKGNLHFIRFPTHDMPAF 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470  81 IQMGSEKNFSSLHTTLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSVGFNGKPECYYFENPTNPELCQKK 160
Cdd:cd24136   84 IQMGRDKHFSSLHTTLCATGGGAYKFEQDFLTMGDLQLCKLDELDCLIKGVLYIDSVGFNGHSECYYFENPTDSEKCQKL 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470 161 PYCLDNPYPMLLVNMGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALDMAAKGDSTNVDKLVKDIYG 240
Cdd:cd24136  164 PFNLKNPYPLLLVNIGSGVSILAVYSKDNYKRVTGTSLGGGTFFGLCCLLTGCTTFEEALEMASRGDSTKVDKLVRDIYG 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470 241 GDYERFGLQGSAVASSFGNMMSKEKRESISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINMVSMKLLA 320
Cdd:cd24136  244 GDYERFGLPGWAVASSFGNMMSKEKREAVSKEDLARATLITITNNIGSIARMCALNENINRVVFVGNFLRINTISMRLLA 323
                        330       340       350
                 ....*....|....*....|....*....|.
gi 564333470 321 YAMDFWSKGQLKALFLEHEGYFGAVGALLEL 351
Cdd:cd24136  324 YALDYWSKGQLKALFLEHEGYFGAVGALLEL 354
ASKHA_NBD_PanK-II_Pank3 cd24137
nucleotide-binding domain (NBD) of pantothenate kinase 3 (Pank3) from type II pantothenate ...
1-349 0e+00

nucleotide-binding domain (NBD) of pantothenate kinase 3 (Pank3) from type II pantothenate kinase (PanK-II) subfamily; PanK (EC 2.7.1.33), also called pantothenic acid kinase, is the first enzyme in the Coenzyme A (CoA) biosynthetic pathway. It catalyzes the phosphorylation of pantothenate (vitamin B5) to form 4'-phosphopantothenate at the expense of a molecule of adenosine triphosphate (ATP), which is the rate-limiting step in CoA biosynthesis. It cannot utilize a phosphoryl donor other than ATP. Three distinct types of PanK have been identified, PanK-I, PanK-II and PanK-III. Eukaryotic PanK-II enzymes often occur as different isoforms, such as PanK1, PanK2, PanK3 and PanK4. The model corresponds to PanK3.


Pssm-ID: 466987 [Multi-domain]  Cd Length: 353  Bit Score: 563.47  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470   1 MDIGGTLVKLVYFEPKDITAEEEQEEVENLKSIRKYLTSNTAYGKTGIRDVHLELKNLTMCGRKGNLHFIRFPTCAMHMF 80
Cdd:cd24137    4 MDIGGTLVKLSYFEPIDITAEEEQEEVESLKSIRKYLTSNVAYGSTGIRDVHLELKDLTLFGRRGNLHFIRFPTQDLPTF 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470  81 IQMGSEKNFSSLHTTLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSVGFNGKPECYYFENPTNPELCQKK 160
Cdd:cd24137   84 IQMGRDKNFSTLQTVLCATGGGAYKFEKDFRTIGNLHLHKLDELDCLVKGLLYIDSVSFNGQAECYYFANASEPERCQKM 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470 161 PYCLDNPYPMLLVNMGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALDMAAKGDSTNVDKLVKDIYG 240
Cdd:cd24137  164 PFNLDDPYPLLVVNIGSGVSILAVHSKDNYKRVTGTSLGGGTFLGLCSLLTGCESFEEALEMASKGDSTQADKLVRDIYG 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470 241 GDYERFGLQGSAVASSFGNMMSKEKRESISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINMVSMKLLA 320
Cdd:cd24137  244 GDYERFGLPGWAVASSFGNMIYKEKRESVSKEDLARATLVTITNNIGSVARMCAVNEKINRVVFVGNFLRVNTLSMKLLA 323
                        330       340
                 ....*....|....*....|....*....
gi 564333470 321 YAMDFWSKGQLKALFLEHEGYFGAVGALL 349
Cdd:cd24137  324 YALDYWSKGQLKALFLEHEGYFGAVGALL 352
ASKHA_NBD_PanK-II_Pank1-like cd24122
nucleotide-binding domain (NBD) of the pantothenate kinase 1 (Pank1)-like subfamily; PanK (EC ...
1-349 0e+00

nucleotide-binding domain (NBD) of the pantothenate kinase 1 (Pank1)-like subfamily; PanK (EC 2.7.1.33), also called pantothenic acid kinase, is the first enzyme in the Coenzyme A (CoA) biosynthetic pathway. It catalyzes the phosphorylation of pantothenate (vitamin B5) to form 4'-phosphopantothenate at the expense of a molecule of adenosine triphosphate (ATP), which is the rate-limiting step in CoA biosynthesis. It cannot utilize a phosphoryl donor other than ATP. Three distinct types of PanK have been identified, PanK-I, PanK-II and PanK-III. Eukaryotic PanK-II enzymes often occur as different isoforms, such as PanK1, PanK2, PanK3 and PanK4. The Pank1-like subfamily includes PanK1-3.


Pssm-ID: 466972 [Multi-domain]  Cd Length: 303  Bit Score: 559.06  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470   1 MDIGGTLVKLVYFEPKditaeeeqeevenlksirkyltsntaygktgirdvhlelknltmcgrkGNLHFIRFPTCAMHMF 80
Cdd:cd24122    4 LDIGGTLVKLVYFEPT------------------------------------------------GTLHFIRFETSRMEGF 35
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470  81 IQMGSEKNFSSLHTTLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSvgfNGKPECYYFENPTNPELCQK- 159
Cdd:cd24122   36 IQLAREKNLSSLIKTVCATGGGAYKFEKLFREELGLQLHKLDELDCLIRGINFLLR---HVPDECYYFENPSDPELCEKr 112
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470 160 -KPYCLDNPYPMLLVNMGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALDMAAKGDSTNVDKLVKDI 238
Cdd:cd24122  113 vVPFDFSDPYPYLLVNIGSGVSILAVESPDNYERVSGTSLGGGTFLGLCCLLTGCETFEEALELAAKGDSTKVDMLVGDI 192
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470 239 YGGDYERFGLQGSAVASSFGNMMSKEKRESISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINMVSMKL 318
Cdd:cd24122  193 YGGDYEKFGLPGDTVASSFGKMVAKEKRESASKEDLARALLVMITNNIGSIARLCAKNEGIKRVVFVGNFLRHNPIAMRL 272
                        330       340       350
                 ....*....|....*....|....*....|.
gi 564333470 319 LAYAMDFWSKGQLKALFLEHEGYFGAVGALL 349
Cdd:cd24122  273 LAYAMDYWSKGEMKALFLEHEGYFGALGALL 303
ASKHA_NBD_PanK-II cd24016
nucleotide-binding domain (NBD) of type II pantothenate kinase (PanK-II) and similar proteins; ...
1-349 0e+00

nucleotide-binding domain (NBD) of type II pantothenate kinase (PanK-II) and similar proteins; PanK (EC 2.7.1.33), also called pantothenic acid kinase, is the first enzyme in the Coenzyme A (CoA) biosynthetic pathway. It catalyzes the phosphorylation of pantothenate (vitamin B5) to form 4'-phosphopantothenate at the expense of a molecule of adenosine triphosphate (ATP), which is the rate-limiting step in CoA biosynthesis. It cannot utilize a phosphoryl donor other than ATP. Three distinct types of PanK have been identified, PanK-I, PanK-II and PanK-III. Eukaryotic PanK-II enzymes often occur as different isoforms, such as PanK1, PanK2, PanK3 and PanK4. The model corresponds to PanK-II that belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.


Pssm-ID: 466866 [Multi-domain]  Cd Length: 299  Bit Score: 508.35  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470   1 MDIGGTLVKLVYFepkditaeeeqeevenlksirkyltsntaygktgirdvhlelknltmcgrkgnLHFIRFPTCAMHMF 80
Cdd:cd24016    4 IDIGGTLVKLVYF-----------------------------------------------------LHFIRFPTDQVVEF 30
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470  81 IQMGSEKNFSSLHTTLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSVGFNGKPECYYFENPTNPELCQKK 160
Cdd:cd24016   31 IQMGQDKNFSTLITKLCATGGGAGKFEEDFRTIGNLPLQKLDELDCLSQGLLYLDSVQFNGQAECYYFANASEPERCQKM 110
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470 161 PYCLDNPYPMLLVNMGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALDMAAKGDSTNVDKLVKDIYG 240
Cdd:cd24016  111 PFNLHDPYPYLFVNVGSGVSILAVDSKDNYKRVTGTSLGGGTFQGLCYLLTGCTDFEEALEMAQHGDSTTIDKLVRDIYG 190
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470 241 GDYERFGLQGSAVASSFGNMMSKEKRESISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINMVSMKLLA 320
Cdd:cd24016  191 GDYERFGLPGDAVASSFGNMLHKEKRADFSKEDLARATLGTITNNIGSMARMCARNEKIENVVFVGNFLRNNALLMKLLA 270
                        330       340
                 ....*....|....*....|....*....
gi 564333470 321 YAMDFWSKGQLKALFLEHEGYFGAVGALL 349
Cdd:cd24016  271 YATDLWSKGQLKALFVEHEGYFGAVGALL 299
Fumble pfam03630
Fumble; Fumble is required for cell division in Drosophila. Mutants lacking fumble exhibit ...
1-347 3.59e-161

Fumble; Fumble is required for cell division in Drosophila. Mutants lacking fumble exhibit abnormalities in bipolar spindle organization, chromosome segregation, and contractile ring formation. Analyses have demonstrated that encodes three protein isoforms, all of which contain a domain with high similarity to the pantothenate kinases of A. nidulans and mouse. A role of fumble in membrane synthesis has been proposed.


Pssm-ID: 460995 [Multi-domain]  Cd Length: 311  Bit Score: 453.49  E-value: 3.59e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470    1 MDIGGTLVKLVYFEPKDITAEEEQeevenlksirkyltsntaygktgirdvhlelknltmcgrkGNLHFIRFPTCAMHMF 80
Cdd:pfam03630   3 IDIGGTLAKLVYFSPVPDSPKELG----------------------------------------GRLHFIKFETTKIEDC 42
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470   81 IQMGSEKNFSSLHT----TLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSvgfNGKPECYYFENPTNPEL 156
Cdd:pfam03630  43 LEFIKSLGLNSKGTdrglTVKATGGGAYKFYDLFKEKLGVKVDKEDEMECLIKGLNFLLT---NIPDEVFTYSDSPEYFF 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470  157 CQKKPyclDNPYPMLLVNMGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALDMAAKGDSTNVDKLVK 236
Cdd:pfam03630 120 QTVDN---NSIYPYLLVNIGSGVSILKVEGPDKFERVGGTSLGGGTFWGLCSLLTGAKSFDEMLELAEKGDNRNVDMLVG 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470  237 DIYGGDYERFGLQGSAVASSFGNMMSKEKRESISK----EDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRIN 312
Cdd:pfam03630 197 DIYGGDYEKIGLKSDTIASSFGKVFRKKFRESASNdaspEDIARSLLYMISNNIGQIAYLNAKLHGLKRIYFGGNFIRGH 276
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 564333470  313 MVSMKLLAYAMDFWSKGQLKALFLEHEGYFGAVGA 347
Cdd:pfam03630 277 PITMKTLSYAINFWSKGELKALFLRHEGYLGALGA 311
ASKHA_NBD_PanK-II_euk cd24086
nucleotide-binding domain (NBD) of type II pantothenate kinase (PanK-II) and similar proteins ...
1-349 8.18e-138

nucleotide-binding domain (NBD) of type II pantothenate kinase (PanK-II) and similar proteins mainly from eukaryotes; PanK (EC 2.7.1.33), also called pantothenic acid kinase, is the first enzyme in the Coenzyme A (CoA) biosynthetic pathway. It catalyzes the phosphorylation of pantothenate (vitamin B5) to form 4'-phosphopantothenate at the expense of a molecule of adenosine triphosphate (ATP), which is the rate-limiting step in CoA biosynthesis. It cannot utilize a phosphoryl donor other than ATP. Three distinct types of PanK have been identified, PanK-I, PanK-II and PanK-III. The model corresponds to a group of PanK-II that is mainly from eukaryotes. Eukaryotic PanK-II enzymes often occur as different isoforms, such as PanK1, PanK2, PanK3 and PanK4.


Pssm-ID: 466936 [Multi-domain]  Cd Length: 327  Bit Score: 394.73  E-value: 8.18e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470   1 MDIGGTLVKLVYFEPKDITAEEEqeevenlksirkyltsntaygktgirDVHLELKNLTMCGRKGNLHFIRFPTCAMHMF 80
Cdd:cd24086    4 LDIGGTLAKLAYLTPIDIDEAEE--------------------------KESVLLKLLANSGEDGELHFISFPNKDLEEF 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470  81 IQMGSEKNF--SSLHTTLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSVGFngKPECYYFENPTNPELCQ 158
Cdd:cd24086   58 LNFLRDKNFedSSKGKVLYATGGGAYKYAELIEETLGVQLVKVDEMDSLVNGLHFLLSVLS--KDECFPFPNDSGPEFLQ 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470 159 KKPYCLDNPYPMLLVNMGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALDMAAKGDSTNVDKLVKDI 238
Cdd:cd24086  136 KDPQLSDDLFPCLLVNIGSGVSILKVDSDGKYERVSGTSLGGGTFLGLASLLTGTNSFDELLELASRGDRANVDLLVRDI 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470 239 YGGDYERFGLQGSAVASSFGNMMSKEK-RESISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINMVSMK 317
Cdd:cd24086  216 YGGDYPYLGLPGDLLASSFGKLADDEKsREDFSKEDIARSLLRMIVNNIGYLAYLVAKLHNVKRVFFTGNFIRNNELARK 295
                        330       340       350
                 ....*....|....*....|....*....|..
gi 564333470 318 LLAYAMDFWSKGQLKALFLEHEGYFGAVGALL 349
Cdd:cd24086  296 LIAEALNYWSKGSLNALFLRHDGYLGALGALL 327
panK_eukar TIGR00555
pantothenate kinase, eukaryotic/staphyloccocal type; This model describes a eukaryotic form of ...
1-350 3.24e-137

pantothenate kinase, eukaryotic/staphyloccocal type; This model describes a eukaryotic form of pantothenate kinase, characterized from the fungus Aspergillus nidulans and with similar forms known in several other eukaryotes. It also includes forms from several Gram-positive bacteria suggested to have originated from the eukaryotic form by lateral transfer. It differs in a number of biochemical properties (such as inhibition by acetyl-CoA) from most bacterial CoaA and lacks sequence similarity. This enzyme is the key regulatory step in the biosynthesis of coenzyme A (CoA). [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]


Pssm-ID: 273135 [Multi-domain]  Cd Length: 296  Bit Score: 392.15  E-value: 3.24e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470    1 MDIGGTLVKLVYFEPKditaeeeqeevenlkSIRKYLTSNTaygktgirdvhlelknltmcgrkGNLH-FIRFPTCAMHM 79
Cdd:TIGR00555   5 IDIGGTLIKVVYEEKK---------------GRRKFKTFET-----------------------TNIDkFIEWLKNQIHR 46
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470   80 FiqmgseknfsSLHTTLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSVGFNGKPECYYFEnptnpelCQK 159
Cdd:TIGR00555  47 H----------SRITTLCATGGGAFKFAELIYESAGIQLHKFDEFDALIQGLNYLLKEEPKEKFTYYDFE-------CQK 109
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470  160 KPYCLDNPYPMLLVNMGSGVSILAVYSkDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALDMAAKGDSTNVDKLVKDIY 239
Cdd:TIGR00555 110 KPIDLDDIYPYLLVNIGTGTSILYVDG-DNYERVGGTSLGGGTFLGLGKLLTGIQTFDELLEMAQHGDRTNVDLLVGDIY 188
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470  240 GGDYERFGLQGSAVASSFGNMMSKEKRESISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINMVSMKLL 319
Cdd:TIGR00555 189 GGDYSESGLDGSLTASSFGKVLSKHLDQSFSPEDIAASLLGLIGNNIGQIAYLCALRYNIDRIVFIGSFLRNNQLLMKVL 268
                         330       340       350
                  ....*....|....*....|....*....|.
gi 564333470  320 AYAMDFWSKgqlKALFLEHEGYFGAVGALLE 350
Cdd:TIGR00555 269 SYATNFWSK---KALFLEHEGYSGAIGALLS 296
ASKHA_NBD_PanK-II_Pank4 cd24123
nucleotide-binding domain (NBD) of pantothenate kinase 4 (Pank4) from type II pantothenate ...
1-349 1.62e-109

nucleotide-binding domain (NBD) of pantothenate kinase 4 (Pank4) from type II pantothenate kinase (PanK-II) subfamily; PanK (EC 2.7.1.33), also called pantothenic acid kinase, is the first enzyme in the Coenzyme A (CoA) biosynthetic pathway. It catalyzes the phosphorylation of pantothenate (vitamin B5) to form 4'-phosphopantothenate at the expense of a molecule of adenosine triphosphate (ATP), which is the rate-limiting step in CoA biosynthesis. It cannot utilize a phosphoryl donor other than ATP. Three distinct types of PanK have been identified, PanK-I, PanK-II and PanK-III. Eukaryotic PanK-II enzymes often occur as different isoforms, such as PanK1, PanK2, PanK3 and PanK4. The model corresponds to PanK4, which is a putative bifunctional protein with a predicted amino-terminal pantothenate kinase (type II PanK) domain fused to a carboxy-terminal phosphatase domain. PanK4 homologs are found in animals, fungi, and plants. The human PanK4 kinase domain has catalytically-inactivating amino acid substitutions, thus it is characterized as a catalytically inactive pseudoPanK.


Pssm-ID: 466973 [Multi-domain]  Cd Length: 339  Bit Score: 323.36  E-value: 1.62e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470   1 MDIGGTLVKLVYFEPKDitaeeeqeevenlKSIRKYLTSNTAYGKTGIRDVHLELKNLTMCGRkgnLHFIRFPTCAMHMF 80
Cdd:cd24123    4 IDIGGSLAKLVYFSRVS-------------DKAASVSSSSGTSKGPSDEPLYEVSEQPELGGR---LHFVKFETKYIEEC 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470  81 IQMGSEKNFSSLHTTLC-----ATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSvgfNGKPECYYFENPTNPE 155
Cdd:cd24123   68 LDFIKDNLLHSRQGNKRgkvikATGGGAYKYADLIKEKLGVEVDKEDEMECLIKGCNFLLK---NIPDEVFTYDEHAKPE 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470 156 LcqKKPYCLDNPYPMLLVNMGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALDMAAKGDSTNVDKLV 235
Cdd:cd24123  145 V--KFQSDPPDIFPYLLVNIGSGVSILKVDSEDKFERVGGTSLGGGTFWGLGSLLTGAKSFDELLELAEKGDNRNVDMLV 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470 236 KDIYGGDYERFGLQGSAVASSFGNMMSKEK---RESISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRIN 312
Cdd:cd24123  223 GDIYGGDYSKIGLKSDTIASSFGKVARADKdarLEDFSPEDIAKSLLRMISNNIGQIAYLNAKLHGLKRIYFGGFFIRGH 302
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 564333470 313 MVSMKLLAYAMDFWSKGQLKALFLEHEGYFGAVGALL 349
Cdd:cd24123  303 PLTMHTISYAINFWSKGEMQALFLRHEGYLGAIGAFL 339
PLN02920 PLN02920
pantothenate kinase 1
1-349 1.43e-64

pantothenate kinase 1


Pssm-ID: 215498 [Multi-domain]  Cd Length: 398  Bit Score: 210.08  E-value: 1.43e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470   1 MDIGGTLVKLVYFEPKDitaeeeqeevENLKSIRKYLTSNTAYGKTGIRDVHLELKNLTMCgrkgnLHFIRFPTCAMHMF 80
Cdd:PLN02920  23 LDIGGSLIKLVYFSRNS----------GDSEDPRNDSSVKSDGVNGRLHFAKFETRKINDC-----LEFISSNKLHHGGF 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470  81 IQM---GSEKNFsslhttLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGllyvdsVGFNGKP---ECYYFENPtnp 154
Cdd:PLN02920  88 QHHenpTHDKNF------IKATGGGAYKFADLFKEKLGISLDKEDEMDCLVTG------ANFLLKAvhhEAFTYLDG--- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470 155 elcQKKPYCLDNP--YPMLLVNMGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALDMAAKGDSTNVD 232
Cdd:PLN02920 153 ---QKEFVQIDHNdlYPYLLVNIGSGVSMIKVDGDGKFERVSGTSVGGGTFWGLGKLLTKCKSFDELLELSHQGNNRVID 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470 233 KLVKDIYGG-DYERFGLQGSAVASSFGNMMSKEKR-ESISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLR 310
Cdd:PLN02920 230 MLVGDIYGGmDYSKIGLSSTTIASSFGKAISDNKElEDYKPEDVARSLLRMISNNIGQISYLNALRFGLKRIFFGGFFIR 309
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 564333470 311 INMVSMKLLAYAMDFWSKGQLKALFLEHEGYFGAVGALL 349
Cdd:PLN02920 310 GHSYTMDTISVAVHFWSKGEAKAMFLRHEGFLGALGAFM 348
PLN02902 PLN02902
pantothenate kinase
1-349 3.77e-63

pantothenate kinase


Pssm-ID: 215489 [Multi-domain]  Cd Length: 876  Bit Score: 215.91  E-value: 3.77e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470   1 MDIGGTLVKLVYFEPKDitaeeeqeeVENLKSIRKyltsNTAYGKTGIRDVHLelKNLTMCGrkGNLHFIRFPTCAMHMF 80
Cdd:PLN02902  58 LDIGGSLIKLVYFSRHE---------DRSTDDKRK----RTIKERLGITNGNR--RSYPILG--GRLHFVKFETSKINEC 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470  81 IQMGSEKNF-------------SSLHTTLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLlyvdsvgfNGKPECYY 147
Cdd:PLN02902 121 LDFISSKQLhrggihswlskapPNGNGVIKATGGGAYKFADLFKERLGVSLDKEDEMDCLVAGA--------NFLLKAIR 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470 148 FENPTNPElCQKKPYCLD--NPYPMLLVNMGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALDMAAK 225
Cdd:PLN02902 193 HEAFTHME-GEKEFVQIDqnDLFPYLLVNIGSGVSMIKVDGDGKFERVSGTNVGGGTYWGLGRLLTKCKSFDELLELSQR 271
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470 226 GDSTNVDKLVKDIYGG-DYERFGLQGSAVASSFGNMMSKEKR-ESISKEDLARATLVTITNNIGSIARMCALNENIDRVV 303
Cdd:PLN02902 272 GDNSAIDMLVGDIYGGmDYSKIGLSASTIASSFGKVISENKElSDYRPEDISLSLLRMISYNIGQISYLNALRFGLKRIF 351
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 564333470 304 FVGNFLRINMVSMKLLAYAMDFWSKGQLKALFLEHEGYFGAVGALL 349
Cdd:PLN02902 352 FGGFFIRGHAYTMDTISFAVHFWSKGEAQAMFLRHEGFLGALGAFM 397
ASKHA_NBD_PanK-II_bac cd24085
nucleotide-binding domain (NBD) of type II pantothenate kinase (PanK-II) and similar proteins ...
61-349 4.28e-52

nucleotide-binding domain (NBD) of type II pantothenate kinase (PanK-II) and similar proteins mainly from bacteria; PanK (EC 2.7.1.33), also called pantothenic acid kinase, is the first enzyme in the Coenzyme A (CoA) biosynthetic pathway. It catalyzes the phosphorylation of pantothenate (vitamin B5) to form 4'-phosphopantothenate at the expense of a molecule of adenosine triphosphate (ATP), which is the rate-limiting step in CoA biosynthesis. It cannot utilize a phosphoryl donor other than ATP. Three distinct types of PanK have been identified, PanK-I, PanK-II and PanK-III. The model corresponds to a group of PanK-II that is mainly from bacteria.


Pssm-ID: 466935 [Multi-domain]  Cd Length: 262  Bit Score: 173.52  E-value: 4.28e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470  61 CGRKGNLHFIRFPTCAMHM---FIQMGSEKNFSslhtTLCATGGGAFKFEEDfrmIADLQLHKLDELDCLIQGLLYVdsV 137
Cdd:cd24085   16 LENNGELKFKAFDSLKIEAlvkFLNELGINDIE----KIAVTGGGASRLPEN---IDGIPIVKVDEFEAIGRGALYL--L 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470 138 GFNGKPecyyfenptnpelcqkkpycldnpypMLLVNMGSGVSILAVySKDNYKRVTGTSLGGGTFLGLCCLLTGCETFE 217
Cdd:cd24085   87 GEILDD--------------------------ALVVSIGTGTSIVLA-KNGTIRHVGGTGVGGGTLLGLGKLLLGVTDYD 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470 218 EALDMAAKGDSTNVDKLVKDIYGGDYErfGLQGSAVASSFGNMmskEKRESISKEDLARATLVTITNNIGSIARMCALNE 297
Cdd:cd24085  140 EITELARKGDRSNVDLTVGDIYGGGIG--PLPPDLTASNFGKL---ADDNKASREDLAAALINLVGETIGTLAALAARAE 214
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 564333470 298 NIDRVVFVGNFLRiNMVSMKLLAYAMDFwskGQLKALFLEHEGYFGAVGALL 349
Cdd:cd24085  215 GVKDIVLVGSTLR-NPLLKEVLERYTKL---YGVKPIFPENGEFAGAIGALL 262
PTZ00297 PTZ00297
pantothenate kinase; Provisional
1-347 2.85e-36

pantothenate kinase; Provisional


Pssm-ID: 140318 [Multi-domain]  Cd Length: 1452  Bit Score: 139.99  E-value: 2.85e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470    1 MDIGGTLVKLVYFEPKDITAeeeqeevenlksIRKYLT--SNTAYGKTGIRDVHL--------ELKNLTMCGRKGNLHFI 70
Cdd:PTZ00297 1044 IDIGGTFAKIAYVQPPGGFA------------FPTYIVheASSLSEKLGLRTFHFfadaeaaeSELRTRPHSRVGTLRFA 1111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470   71 RFPTCAMHMFIQMGSE----KNFSSLHTT-LCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSVGfngkPEC 145
Cdd:PTZ00297 1112 KIPSKQIPDFADYLAGshaiNYYKPQYRTkVRATGGGAFKYASVAKKVLGINFSVMREMDAVVKGLNLVIRVA----PES 1187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470  146 YYFENPTN----PELCQKKPYCLDNPYPMLLVNMGSGVSILAVYSKD-NYKRVTGTSLGGGTFLGLCCLLTGCETFEEAL 220
Cdd:PTZ00297 1188 IFTVDPSTgvhhPHQLVSPPGDGFSPFPCLLVNIGSGISIIKCLGPDgSHVRVGGSPIGGATFWGLVRTMTNVTSWEEVM 1267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470  221 D---MAAKGDSTNVDKLVKDIYGGDYERFG--LQGSAVASSFGNM----------------------------MSKEKRE 267
Cdd:PTZ00297 1268 EimrLDGPGDNKNVDLLVGDIYGYNAKDLPamLSVDTVASTFGKLgterfyemmrgvstahfsdddaageilsPKALKSP 1347
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470  268 SISKE-------------DLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINMVSMKLLAYAMDFWSKGQLKAL 334
Cdd:PTZ00297 1348 TVISElpvrngtkkasaiDIVRSLLNMISSNVTQLAYLHSRVQGVPNIFFAGGFVRDNPIIWSHISSTMKYWSKGECHAH 1427
                         410
                  ....*....|...
gi 564333470  335 FLEHEGYFGAVGA 347
Cdd:PTZ00297 1428 FLEHDGYLGALGC 1440
PRK13317 PRK13317
pantothenate kinase; Provisional
2-353 1.06e-34

pantothenate kinase; Provisional


Pssm-ID: 237346 [Multi-domain]  Cd Length: 277  Bit Score: 128.53  E-value: 1.06e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470   2 DIGGTLVKLVYFEPKditaeeeqeeveNLKSIRKYLTSNtaygktgIRDVHLELKNLTMCGRkgnlhfirfptcamhmfi 81
Cdd:PRK13317   8 DAGGTLTKIVYLEEK------------KQRTFKTEYSAE-------GKKVIDWLINLQDIEK------------------ 50
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470  82 qmgseknfsslhttLCATGGGAFKFEEdfRMIADLQLHKLDELDCLIQGLLYvdsvgfngkpecyyfenptnpeLCQKKP 161
Cdd:PRK13317  51 --------------ICLTGGKAGYLQQ--LLNYGYPIAEFVEFEATGLGVRY----------------------LLKEEG 92
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470 162 YCLDNpypMLLVNMGSGVSILAVYSKDnYKRVTGTSLGGGTFLGLCCLLTGCETFEEALDMAAKGDSTNVDKLVKDIYGG 241
Cdd:PRK13317  93 HDLND---YIFTNIGTGTSIHYVDGNS-QRRVGGTGIGGGTIQGLSKLLTNISDYEQLIELAKHGDRNNIDLKVGDIYKG 168
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470 242 DYErfGLQGSAVASSFGNMMSKEKRESiSKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNflriNMVSMKLLAY 321
Cdd:PRK13317 169 PLP--PIPGDLTASNFGKVLHHLDSEF-TSSDILAGVIGLVGEVITTLSIQAAREKNIENIVYIGS----TLTNNPLLQE 241
                        330       340       350
                 ....*....|....*....|....*....|...
gi 564333470 322 AMDFWSKGQ-LKALFLEHEGYFGAVGALLELFK 353
Cdd:PRK13317 242 IIESYTKLRnCTPIFLENGGYSGAIGALLLATN 274
PanK COG5146
Pantothenate kinase [Coenzyme transport and metabolism]; Pantothenate kinase is part of the ...
2-349 4.59e-34

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


Pssm-ID: 444059 [Multi-domain]  Cd Length: 270  Bit Score: 126.54  E-value: 4.59e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470   2 DIGGTLVKLVYFEpkditaeeeqeevenlksirkyltsntaygktgirdvhlelknltmcgrKGNLHFIRFPTCAMHMFI 81
Cdd:COG5146    7 DAGGTLTKIAYLE-------------------------------------------------DGERRYKKFPSDEIESVA 37
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470  82 Q-MGSEKNFSslhtTLCATGGGAFKFEEdfrMIADLQLHKLDELDCLIQGllyvdsVGFNGKPECYYFENptnpelcqkk 160
Cdd:COG5146   38 DwLNKFINIE----KIGLTGGRAEVLAE---KLNGDPKQYIVEFDATGKG------VRYLLKEEGHDIDK---------- 94
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470 161 pycldnpypMLLVNMGSGVSIlaVYSKDN-YKRVTGTSLGGGTFLGLCCLLTGCETFEEALDMAAKGDSTNVDKLVKDIY 239
Cdd:COG5146   95 ---------FIITNVGTGTSI--HYMDGDtQERVGGTGVGGGTLMGLSYLLTGISDFEEIVELAKKGDRDGIDLKVKDIY 163
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333470 240 GGDYErfGLQGSAVASSFGNMMSKEKrESISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINmvsmKLL 319
Cdd:COG5146  164 EGMEP--PIPGDLTASNFGKVLITLD-ESATKEDILAAIIGLVGETITTLSIQAAEEYDTETIVYIGSTLTNN----PLL 236
                        330       340       350
                 ....*....|....*....|....*....|.
gi 564333470 320 AYAMDFWSKGQ-LKALFLEHEGYFGAVGALL 349
Cdd:COG5146  237 QEVIESYTILRgKKPIFLENGEFSGAIGALL 267
 
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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