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Conserved domains on  [gi|19484050|gb|AAH23496|]
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Pantothenate kinase 1 [Mus musculus]

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 ...
13-364 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: 729.10  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050  13 WFGMDIGGTLVKLVYFEPKDITAEEEQEEVENLKSIRKYLTSNTAYGKTGIRDVHLELKNLTMCGRKGNLHFIRFPTCAM 92
Cdd:cd24135   1 WFGMDIGGTLVKLVYFEPKDITAEEEQEEVENLKSIRKYLTSNTAYGKTGIRDVHLELKNLTMCGRKGNLHFIRFPSCAM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050  93 HLFIQMGSEKNFSSLHTTLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSVGFNGKPECYYFENPTNPELC 172
Cdd:cd24135  81 HRFIQMGSEKNFSSLHTTLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSVGFNGQPECYYFENPTDPEQC 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050 173 QKKPYCLDNPYPMLLVNMGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALDMAAKGDSTNVDKLVKD 252
Cdd:cd24135 161 QKKPYCLDNPYPMLLVNIGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALEMAAKGDSTNVDKLVKD 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050 253 IYGGDYERFGLQGSAVASSFGNMMSKEKRESISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINMVSMK 332
Cdd:cd24135 241 IYGGDYERFGLQGSAVASSFGHMMSKEKRDSISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINMVSMK 320
                       330       340       350
                ....*....|....*....|....*....|..
gi 19484050 333 LLAYAMDFWSKGQLKALFLEHEGYFGAVGALL 364
Cdd:cd24135 321 LLAYAMDFWSKGQLKALFLEHEGYFGAVGALL 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 ...
13-364 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: 729.10  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050  13 WFGMDIGGTLVKLVYFEPKDITAEEEQEEVENLKSIRKYLTSNTAYGKTGIRDVHLELKNLTMCGRKGNLHFIRFPTCAM 92
Cdd:cd24135   1 WFGMDIGGTLVKLVYFEPKDITAEEEQEEVENLKSIRKYLTSNTAYGKTGIRDVHLELKNLTMCGRKGNLHFIRFPSCAM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050  93 HLFIQMGSEKNFSSLHTTLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSVGFNGKPECYYFENPTNPELC 172
Cdd:cd24135  81 HRFIQMGSEKNFSSLHTTLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSVGFNGQPECYYFENPTDPEQC 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050 173 QKKPYCLDNPYPMLLVNMGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALDMAAKGDSTNVDKLVKD 252
Cdd:cd24135 161 QKKPYCLDNPYPMLLVNIGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALEMAAKGDSTNVDKLVKD 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050 253 IYGGDYERFGLQGSAVASSFGNMMSKEKRESISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINMVSMK 332
Cdd:cd24135 241 IYGGDYERFGLQGSAVASSFGHMMSKEKRDSISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINMVSMK 320
                       330       340       350
                ....*....|....*....|....*....|..
gi 19484050 333 LLAYAMDFWSKGQLKALFLEHEGYFGAVGALL 364
Cdd:cd24135 321 LLAYAMDFWSKGQLKALFLEHEGYFGAVGALL 352
Fumble pfam03630
Fumble; Fumble is required for cell division in Drosophila. Mutants lacking fumble exhibit ...
14-362 2.61e-163

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: 459.27  E-value: 2.61e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050    14 FGMDIGGTLVKLVYFEPKDITAEEEQeevenlksirkyltsntaygktgirdvhlelknltmcgrkGNLHFIRFPTCAMH 93
Cdd:pfam03630   1 FAIDIGGTLAKLVYFSPVPDSPKELG----------------------------------------GRLHFIKFETTKIE 40
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050    94 LFIQMGSEKNFSSLHT----TLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSvgfNGKPECYYFENPTNP 169
Cdd:pfam03630  41 DCLEFIKSLGLNSKGTdrglTVKATGGGAYKFYDLFKEKLGVKVDKEDEMECLIKGLNFLLT---NIPDEVFTYSDSPEY 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050   170 ELCQKKPyclDNPYPMLLVNMGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALDMAAKGDSTNVDKL 249
Cdd:pfam03630 118 FFQTVDN---NSIYPYLLVNIGSGVSILKVEGPDKFERVGGTSLGGGTFWGLCSLLTGAKSFDEMLELAEKGDNRNVDML 194
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050   250 VKDIYGGDYERFGLQGSAVASSFGNMMSKEKRESISK----EDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLR 325
Cdd:pfam03630 195 VGDIYGGDYEKIGLKSDTIASSFGKVFRKKFRESASNdaspEDIARSLLYMISNNIGQIAYLNAKLHGLKRIYFGGNFIR 274
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 19484050   326 INMVSMKLLAYAMDFWSKGQLKALFLEHEGYFGAVGA 362
Cdd:pfam03630 275 GHPITMKTLSYAINFWSKGELKALFLRHEGYLGALGA 311
panK_eukar TIGR00555
pantothenate kinase, eukaryotic/staphyloccocal type; This model describes a eukaryotic form of ...
12-365 8.37e-140

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: 399.47  E-value: 8.37e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050    12 PWFGMDIGGTLVKLVYFEPKditaeeeqeevenlkSIRKYLTSNTaygktgirdvhlelknltmcgrkGNLH-FIRFPTC 90
Cdd:TIGR00555   1 SRIGIDIGGTLIKVVYEEKK---------------GRRKFKTFET-----------------------TNIDkFIEWLKN 42
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050    91 AMHLFiqmgseknfsSLHTTLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSVGFNGKPECYYFEnptnpe 170
Cdd:TIGR00555  43 QIHRH----------SRITTLCATGGGAFKFAELIYESAGIQLHKFDEFDALIQGLNYLLKEEPKEKFTYYDFE------ 106
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050   171 lCQKKPYCLDNPYPMLLVNMGSGVSILAVYSkDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALDMAAKGDSTNVDKLV 250
Cdd:TIGR00555 107 -CQKKPIDLDDIYPYLLVNIGTGTSILYVDG-DNYERVGGTSLGGGTFLGLGKLLTGIQTFDELLEMAQHGDRTNVDLLV 184
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050   251 KDIYGGDYERFGLQGSAVASSFGNMMSKEKRESISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINMVS 330
Cdd:TIGR00555 185 GDIYGGDYSESGLDGSLTASSFGKVLSKHLDQSFSPEDIAASLLGLIGNNIGQIAYLCALRYNIDRIVFIGSFLRNNQLL 264
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 19484050   331 MKLLAYAMDFWSKgqlKALFLEHEGYFGAVGALLE 365
Cdd:TIGR00555 265 MKVLSYATNFWSK---KALFLEHEGYSGAIGALLS 296
PLN02920 PLN02920
pantothenate kinase 1
16-364 1.60e-64

pantothenate kinase 1


Pssm-ID: 215498 [Multi-domain]  Cd Length: 398  Bit Score: 210.47  E-value: 1.60e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050   16 MDIGGTLVKLVYFEPKDitaeeeqeevENLKSIRKYLTSNTAYGKTGIRDVHLELKNLTMCgrkgnLHFIRFPTCAMHLF 95
Cdd:PLN02920  23 LDIGGSLIKLVYFSRNS----------GDSEDPRNDSSVKSDGVNGRLHFAKFETRKINDC-----LEFISSNKLHHGGF 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050   96 IQM---GSEKNFsslhttLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGllyvdsVGFNGKP---ECYYFENPtnp 169
Cdd:PLN02920  88 QHHenpTHDKNF------IKATGGGAYKFADLFKEKLGISLDKEDEMDCLVTG------ANFLLKAvhhEAFTYLDG--- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050  170 elcQKKPYCLDNP--YPMLLVNMGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALDMAAKGDSTNVD 247
Cdd:PLN02920 153 ---QKEFVQIDHNdlYPYLLVNIGSGVSMIKVDGDGKFERVSGTSVGGGTFWGLGKLLTKCKSFDELLELSHQGNNRVID 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050  248 KLVKDIYGG-DYERFGLQGSAVASSFGNMMSKEKR-ESISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLR 325
Cdd:PLN02920 230 MLVGDIYGGmDYSKIGLSSTTIASSFGKAISDNKElEDYKPEDVARSLLRMISNNIGQISYLNALRFGLKRIFFGGFFIR 309
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 19484050  326 INMVSMKLLAYAMDFWSKGQLKALFLEHEGYFGAVGALL 364
Cdd:PLN02920 310 GHSYTMDTISVAVHFWSKGEAKAMFLRHEGFLGALGAFM 348
PanK COG5146
Pantothenate kinase [Coenzyme transport and metabolism]; Pantothenate kinase is part of the ...
15-364 1.76e-35

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: 130.78  E-value: 1.76e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050  15 GMDIGGTLVKLVYFEpkditaeeeqeevenlksirkyltsntaygktgirdvhlelknltmcgrKGNLHFIRFPTCAMHL 94
Cdd:COG5146   5 GIDAGGTLTKIAYLE-------------------------------------------------DGERRYKKFPSDEIES 35
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050  95 FIQ-MGSEKNFSslhtTLCATGGGAFKFEEdfrMIADLQLHKLDELDCLIQGllyvdsVGFNGKPECYYFENptnpelcq 173
Cdd:COG5146  36 VADwLNKFINIE----KIGLTGGRAEVLAE---KLNGDPKQYIVEFDATGKG------VRYLLKEEGHDIDK-------- 94
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050 174 kkpycldnpypMLLVNMGSGVSIlaVYSKDN-YKRVTGTSLGGGTFLGLCCLLTGCETFEEALDMAAKGDSTNVDKLVKD 252
Cdd:COG5146  95 -----------FIITNVGTGTSI--HYMDGDtQERVGGTGVGGGTLMGLSYLLTGISDFEEIVELAKKGDRDGIDLKVKD 161
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050 253 IYGGDYErfGLQGSAVASSFGNMMSKEKrESISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINmvsmK 332
Cdd:COG5146 162 IYEGMEP--PIPGDLTASNFGKVLITLD-ESATKEDILAAIIGLVGETITTLSIQAAEEYDTETIVYIGSTLTNN----P 234
                       330       340       350
                ....*....|....*....|....*....|...
gi 19484050 333 LLAYAMDFWSKGQ-LKALFLEHEGYFGAVGALL 364
Cdd:COG5146 235 LLQEVIESYTILRgKKPIFLENGEFSGAIGALL 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 ...
13-364 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: 729.10  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050  13 WFGMDIGGTLVKLVYFEPKDITAEEEQEEVENLKSIRKYLTSNTAYGKTGIRDVHLELKNLTMCGRKGNLHFIRFPTCAM 92
Cdd:cd24135   1 WFGMDIGGTLVKLVYFEPKDITAEEEQEEVENLKSIRKYLTSNTAYGKTGIRDVHLELKNLTMCGRKGNLHFIRFPSCAM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050  93 HLFIQMGSEKNFSSLHTTLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSVGFNGKPECYYFENPTNPELC 172
Cdd:cd24135  81 HRFIQMGSEKNFSSLHTTLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSVGFNGQPECYYFENPTDPEQC 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050 173 QKKPYCLDNPYPMLLVNMGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALDMAAKGDSTNVDKLVKD 252
Cdd:cd24135 161 QKKPYCLDNPYPMLLVNIGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALEMAAKGDSTNVDKLVKD 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050 253 IYGGDYERFGLQGSAVASSFGNMMSKEKRESISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINMVSMK 332
Cdd:cd24135 241 IYGGDYERFGLQGSAVASSFGHMMSKEKRDSISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINMVSMK 320
                       330       340       350
                ....*....|....*....|....*....|..
gi 19484050 333 LLAYAMDFWSKGQLKALFLEHEGYFGAVGALL 364
Cdd:cd24135 321 LLAYAMDFWSKGQLKALFLEHEGYFGAVGALL 352
ASKHA_NBD_PanK-II_Pank2 cd24136
nucleotide-binding domain (NBD) of pantothenate kinase 2 (Pank2) from type II pantothenate ...
13-366 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: 642.04  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050  13 WFGMDIGGTLVKLVYFEPKDITAEEEQEEVENLKSIRKYLTSNTAYGKTGIRDVHLELKNLTMCGRKGNLHFIRFPTCAM 92
Cdd:cd24136   1 WFGLDIGGTLVKLVYFEPKDITAEEEEEEVENLKSIRKYLTSNVAYGSTGIRDVHLELKDLTLCGRKGNLHFIRFPTHDM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050  93 HLFIQMGSEKNFSSLHTTLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSVGFNGKPECYYFENPTNPELC 172
Cdd:cd24136  81 PAFIQMGRDKHFSSLHTTLCATGGGAYKFEQDFLTMGDLQLCKLDELDCLIKGVLYIDSVGFNGHSECYYFENPTDSEKC 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050 173 QKKPYCLDNPYPMLLVNMGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALDMAAKGDSTNVDKLVKD 252
Cdd:cd24136 161 QKLPFNLKNPYPLLLVNIGSGVSILAVYSKDNYKRVTGTSLGGGTFFGLCCLLTGCTTFEEALEMASRGDSTKVDKLVRD 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050 253 IYGGDYERFGLQGSAVASSFGNMMSKEKRESISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINMVSMK 332
Cdd:cd24136 241 IYGGDYERFGLPGWAVASSFGNMMSKEKREAVSKEDLARATLITITNNIGSIARMCALNENINRVVFVGNFLRINTISMR 320
                       330       340       350
                ....*....|....*....|....*....|....
gi 19484050 333 LLAYAMDFWSKGQLKALFLEHEGYFGAVGALLEL 366
Cdd:cd24136 321 LLAYALDYWSKGQLKALFLEHEGYFGAVGALLEL 354
ASKHA_NBD_PanK-II_Pank3 cd24137
nucleotide-binding domain (NBD) of pantothenate kinase 3 (Pank3) from type II pantothenate ...
13-364 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: 572.72  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050  13 WFGMDIGGTLVKLVYFEPKDITAEEEQEEVENLKSIRKYLTSNTAYGKTGIRDVHLELKNLTMCGRKGNLHFIRFPTCAM 92
Cdd:cd24137   1 WFGMDIGGTLVKLSYFEPIDITAEEEQEEVESLKSIRKYLTSNVAYGSTGIRDVHLELKDLTLFGRRGNLHFIRFPTQDL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050  93 HLFIQMGSEKNFSSLHTTLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSVGFNGKPECYYFENPTNPELC 172
Cdd:cd24137  81 PTFIQMGRDKNFSTLQTVLCATGGGAYKFEKDFRTIGNLHLHKLDELDCLVKGLLYIDSVSFNGQAECYYFANASEPERC 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050 173 QKKPYCLDNPYPMLLVNMGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALDMAAKGDSTNVDKLVKD 252
Cdd:cd24137 161 QKMPFNLDDPYPLLVVNIGSGVSILAVHSKDNYKRVTGTSLGGGTFLGLCSLLTGCESFEEALEMASKGDSTQADKLVRD 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050 253 IYGGDYERFGLQGSAVASSFGNMMSKEKRESISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINMVSMK 332
Cdd:cd24137 241 IYGGDYERFGLPGWAVASSFGNMIYKEKRESVSKEDLARATLVTITNNIGSVARMCAVNEKINRVVFVGNFLRVNTLSMK 320
                       330       340       350
                ....*....|....*....|....*....|..
gi 19484050 333 LLAYAMDFWSKGQLKALFLEHEGYFGAVGALL 364
Cdd:cd24137 321 LLAYALDYWSKGQLKALFLEHEGYFGAVGALL 352
ASKHA_NBD_PanK-II_Pank1-like cd24122
nucleotide-binding domain (NBD) of the pantothenate kinase 1 (Pank1)-like subfamily; PanK (EC ...
13-364 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: 569.46  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050  13 WFGMDIGGTLVKLVYFEPKditaeeeqeevenlksirkyltsntaygktgirdvhlelknltmcgrkGNLHFIRFPTCAM 92
Cdd:cd24122   1 WFGLDIGGTLVKLVYFEPT------------------------------------------------GTLHFIRFETSRM 32
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050  93 HLFIQMGSEKNFSSLHTTLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSvgfNGKPECYYFENPTNPELC 172
Cdd:cd24122  33 EGFIQLAREKNLSSLIKTVCATGGGAYKFEKLFREELGLQLHKLDELDCLIRGINFLLR---HVPDECYYFENPSDPELC 109
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050 173 QK--KPYCLDNPYPMLLVNMGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALDMAAKGDSTNVDKLV 250
Cdd:cd24122 110 EKrvVPFDFSDPYPYLLVNIGSGVSILAVESPDNYERVSGTSLGGGTFLGLCCLLTGCETFEEALELAAKGDSTKVDMLV 189
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050 251 KDIYGGDYERFGLQGSAVASSFGNMMSKEKRESISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINMVS 330
Cdd:cd24122 190 GDIYGGDYEKFGLPGDTVASSFGKMVAKEKRESASKEDLARALLVMITNNIGSIARLCAKNEGIKRVVFVGNFLRHNPIA 269
                       330       340       350
                ....*....|....*....|....*....|....
gi 19484050 331 MKLLAYAMDFWSKGQLKALFLEHEGYFGAVGALL 364
Cdd:cd24122 270 MRLLAYAMDYWSKGEMKALFLEHEGYFGALGALL 303
ASKHA_NBD_PanK-II cd24016
nucleotide-binding domain (NBD) of type II pantothenate kinase (PanK-II) and similar proteins; ...
13-364 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: 516.82  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050  13 WFGMDIGGTLVKLVYFepkditaeeeqeevenlksirkyltsntaygktgirdvhlelknltmcgrkgnLHFIRFPTCAM 92
Cdd:cd24016   1 WFGIDIGGTLVKLVYF-----------------------------------------------------LHFIRFPTDQV 27
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050  93 HLFIQMGSEKNFSSLHTTLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSVGFNGKPECYYFENPTNPELC 172
Cdd:cd24016  28 VEFIQMGQDKNFSTLITKLCATGGGAGKFEEDFRTIGNLPLQKLDELDCLSQGLLYLDSVQFNGQAECYYFANASEPERC 107
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050 173 QKKPYCLDNPYPMLLVNMGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALDMAAKGDSTNVDKLVKD 252
Cdd:cd24016 108 QKMPFNLHDPYPYLFVNVGSGVSILAVDSKDNYKRVTGTSLGGGTFQGLCYLLTGCTDFEEALEMAQHGDSTTIDKLVRD 187
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050 253 IYGGDYERFGLQGSAVASSFGNMMSKEKRESISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINMVSMK 332
Cdd:cd24016 188 IYGGDYERFGLPGDAVASSFGNMLHKEKRADFSKEDLARATLGTITNNIGSMARMCARNEKIENVVFVGNFLRNNALLMK 267
                       330       340       350
                ....*....|....*....|....*....|..
gi 19484050 333 LLAYAMDFWSKGQLKALFLEHEGYFGAVGALL 364
Cdd:cd24016 268 LLAYATDLWSKGQLKALFVEHEGYFGAVGALL 299
Fumble pfam03630
Fumble; Fumble is required for cell division in Drosophila. Mutants lacking fumble exhibit ...
14-362 2.61e-163

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: 459.27  E-value: 2.61e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050    14 FGMDIGGTLVKLVYFEPKDITAEEEQeevenlksirkyltsntaygktgirdvhlelknltmcgrkGNLHFIRFPTCAMH 93
Cdd:pfam03630   1 FAIDIGGTLAKLVYFSPVPDSPKELG----------------------------------------GRLHFIKFETTKIE 40
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050    94 LFIQMGSEKNFSSLHT----TLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSvgfNGKPECYYFENPTNP 169
Cdd:pfam03630  41 DCLEFIKSLGLNSKGTdrglTVKATGGGAYKFYDLFKEKLGVKVDKEDEMECLIKGLNFLLT---NIPDEVFTYSDSPEY 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050   170 ELCQKKPyclDNPYPMLLVNMGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALDMAAKGDSTNVDKL 249
Cdd:pfam03630 118 FFQTVDN---NSIYPYLLVNIGSGVSILKVEGPDKFERVGGTSLGGGTFWGLCSLLTGAKSFDEMLELAEKGDNRNVDML 194
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050   250 VKDIYGGDYERFGLQGSAVASSFGNMMSKEKRESISK----EDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLR 325
Cdd:pfam03630 195 VGDIYGGDYEKIGLKSDTIASSFGKVFRKKFRESASNdaspEDIARSLLYMISNNIGQIAYLNAKLHGLKRIYFGGNFIR 274
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 19484050   326 INMVSMKLLAYAMDFWSKGQLKALFLEHEGYFGAVGA 362
Cdd:pfam03630 275 GHPITMKTLSYAINFWSKGELKALFLRHEGYLGALGA 311
ASKHA_NBD_PanK-II_euk cd24086
nucleotide-binding domain (NBD) of type II pantothenate kinase (PanK-II) and similar proteins ...
13-364 1.60e-140

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: 402.43  E-value: 1.60e-140
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050  13 WFGMDIGGTLVKLVYFEPKDITAEEEqeevenlksirkyltsntaygktgirDVHLELKNLTMCGRKGNLHFIRFPTCAM 92
Cdd:cd24086   1 RLGLDIGGTLAKLAYLTPIDIDEAEE--------------------------KESVLLKLLANSGEDGELHFISFPNKDL 54
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050  93 HLFIQMGSEKNF--SSLHTTLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSVGFngKPECYYFENPTNPE 170
Cdd:cd24086  55 EEFLNFLRDKNFedSSKGKVLYATGGGAYKYAELIEETLGVQLVKVDEMDSLVNGLHFLLSVLS--KDECFPFPNDSGPE 132
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050 171 LCQKKPYCLDNPYPMLLVNMGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALDMAAKGDSTNVDKLV 250
Cdd:cd24086 133 FLQKDPQLSDDLFPCLLVNIGSGVSILKVDSDGKYERVSGTSLGGGTFLGLASLLTGTNSFDELLELASRGDRANVDLLV 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050 251 KDIYGGDYERFGLQGSAVASSFGNMMSKEK-RESISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINMV 329
Cdd:cd24086 213 RDIYGGDYPYLGLPGDLLASSFGKLADDEKsREDFSKEDIARSLLRMIVNNIGYLAYLVAKLHNVKRVFFTGNFIRNNEL 292
                       330       340       350
                ....*....|....*....|....*....|....*
gi 19484050 330 SMKLLAYAMDFWSKGQLKALFLEHEGYFGAVGALL 364
Cdd:cd24086 293 ARKLIAEALNYWSKGSLNALFLRHDGYLGALGALL 327
panK_eukar TIGR00555
pantothenate kinase, eukaryotic/staphyloccocal type; This model describes a eukaryotic form of ...
12-365 8.37e-140

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: 399.47  E-value: 8.37e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050    12 PWFGMDIGGTLVKLVYFEPKditaeeeqeevenlkSIRKYLTSNTaygktgirdvhlelknltmcgrkGNLH-FIRFPTC 90
Cdd:TIGR00555   1 SRIGIDIGGTLIKVVYEEKK---------------GRRKFKTFET-----------------------TNIDkFIEWLKN 42
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050    91 AMHLFiqmgseknfsSLHTTLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSVGFNGKPECYYFEnptnpe 170
Cdd:TIGR00555  43 QIHRH----------SRITTLCATGGGAFKFAELIYESAGIQLHKFDEFDALIQGLNYLLKEEPKEKFTYYDFE------ 106
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050   171 lCQKKPYCLDNPYPMLLVNMGSGVSILAVYSkDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALDMAAKGDSTNVDKLV 250
Cdd:TIGR00555 107 -CQKKPIDLDDIYPYLLVNIGTGTSILYVDG-DNYERVGGTSLGGGTFLGLGKLLTGIQTFDELLEMAQHGDRTNVDLLV 184
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050   251 KDIYGGDYERFGLQGSAVASSFGNMMSKEKRESISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINMVS 330
Cdd:TIGR00555 185 GDIYGGDYSESGLDGSLTASSFGKVLSKHLDQSFSPEDIAASLLGLIGNNIGQIAYLCALRYNIDRIVFIGSFLRNNQLL 264
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 19484050   331 MKLLAYAMDFWSKgqlKALFLEHEGYFGAVGALLE 365
Cdd:TIGR00555 265 MKVLSYATNFWSK---KALFLEHEGYSGAIGALLS 296
ASKHA_NBD_PanK-II_Pank4 cd24123
nucleotide-binding domain (NBD) of pantothenate kinase 4 (Pank4) from type II pantothenate ...
14-364 2.16e-110

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: 326.05  E-value: 2.16e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050  14 FGMDIGGTLVKLVYFEPKDitaeeeqeevenlKSIRKYLTSNTAYGKTGIRDVHLELKNLTMCGRkgnLHFIRFPTCAMH 93
Cdd:cd24123   2 FAIDIGGSLAKLVYFSRVS-------------DKAASVSSSSGTSKGPSDEPLYEVSEQPELGGR---LHFVKFETKYIE 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050  94 LFIQMGSEKNFSSLHTTLC-----ATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSvgfNGKPECYYFENPTN 168
Cdd:cd24123  66 ECLDFIKDNLLHSRQGNKRgkvikATGGGAYKYADLIKEKLGVEVDKEDEMECLIKGCNFLLK---NIPDEVFTYDEHAK 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050 169 PELcqKKPYCLDNPYPMLLVNMGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALDMAAKGDSTNVDK 248
Cdd:cd24123 143 PEV--KFQSDPPDIFPYLLVNIGSGVSILKVDSEDKFERVGGTSLGGGTFWGLGSLLTGAKSFDELLELAEKGDNRNVDM 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050 249 LVKDIYGGDYERFGLQGSAVASSFGNMMSKEK---RESISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLR 325
Cdd:cd24123 221 LVGDIYGGDYSKIGLKSDTIASSFGKVARADKdarLEDFSPEDIAKSLLRMISNNIGQIAYLNAKLHGLKRIYFGGFFIR 300
                       330       340       350
                ....*....|....*....|....*....|....*....
gi 19484050 326 INMVSMKLLAYAMDFWSKGQLKALFLEHEGYFGAVGALL 364
Cdd:cd24123 301 GHPLTMHTISYAINFWSKGEMQALFLRHEGYLGAIGAFL 339
PLN02920 PLN02920
pantothenate kinase 1
16-364 1.60e-64

pantothenate kinase 1


Pssm-ID: 215498 [Multi-domain]  Cd Length: 398  Bit Score: 210.47  E-value: 1.60e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050   16 MDIGGTLVKLVYFEPKDitaeeeqeevENLKSIRKYLTSNTAYGKTGIRDVHLELKNLTMCgrkgnLHFIRFPTCAMHLF 95
Cdd:PLN02920  23 LDIGGSLIKLVYFSRNS----------GDSEDPRNDSSVKSDGVNGRLHFAKFETRKINDC-----LEFISSNKLHHGGF 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050   96 IQM---GSEKNFsslhttLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGllyvdsVGFNGKP---ECYYFENPtnp 169
Cdd:PLN02920  88 QHHenpTHDKNF------IKATGGGAYKFADLFKEKLGISLDKEDEMDCLVTG------ANFLLKAvhhEAFTYLDG--- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050  170 elcQKKPYCLDNP--YPMLLVNMGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALDMAAKGDSTNVD 247
Cdd:PLN02920 153 ---QKEFVQIDHNdlYPYLLVNIGSGVSMIKVDGDGKFERVSGTSVGGGTFWGLGKLLTKCKSFDELLELSHQGNNRVID 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050  248 KLVKDIYGG-DYERFGLQGSAVASSFGNMMSKEKR-ESISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLR 325
Cdd:PLN02920 230 MLVGDIYGGmDYSKIGLSSTTIASSFGKAISDNKElEDYKPEDVARSLLRMISNNIGQISYLNALRFGLKRIFFGGFFIR 309
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 19484050  326 INMVSMKLLAYAMDFWSKGQLKALFLEHEGYFGAVGALL 364
Cdd:PLN02920 310 GHSYTMDTISVAVHFWSKGEAKAMFLRHEGFLGALGAFM 348
PLN02902 PLN02902
pantothenate kinase
14-364 5.56e-63

pantothenate kinase


Pssm-ID: 215489 [Multi-domain]  Cd Length: 876  Bit Score: 215.91  E-value: 5.56e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050   14 FGMDIGGTLVKLVYFEPKDitaeeeqeeVENLKSIRKyltsNTAYGKTGIRDVHLelKNLTMCGrkGNLHFIRFPTCAMH 93
Cdd:PLN02902  56 LALDIGGSLIKLVYFSRHE---------DRSTDDKRK----RTIKERLGITNGNR--RSYPILG--GRLHFVKFETSKIN 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050   94 LFIQMGSEKNF-------------SSLHTTLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLlyvdsvgfNGKPEC 160
Cdd:PLN02902 119 ECLDFISSKQLhrggihswlskapPNGNGVIKATGGGAYKFADLFKERLGVSLDKEDEMDCLVAGA--------NFLLKA 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050  161 YYFENPTNPElCQKKPYCLD--NPYPMLLVNMGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALDMA 238
Cdd:PLN02902 191 IRHEAFTHME-GEKEFVQIDqnDLFPYLLVNIGSGVSMIKVDGDGKFERVSGTNVGGGTYWGLGRLLTKCKSFDELLELS 269
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050  239 AKGDSTNVDKLVKDIYGG-DYERFGLQGSAVASSFGNMMSKEKR-ESISKEDLARATLVTITNNIGSIARMCALNENIDR 316
Cdd:PLN02902 270 QRGDNSAIDMLVGDIYGGmDYSKIGLSASTIASSFGKVISENKElSDYRPEDISLSLLRMISYNIGQISYLNALRFGLKR 349
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 19484050  317 VVFVGNFLRINMVSMKLLAYAMDFWSKGQLKALFLEHEGYFGAVGALL 364
Cdd:PLN02902 350 IFFGGFFIRGHAYTMDTISFAVHFWSKGEAQAMFLRHEGFLGALGAFM 397
ASKHA_NBD_PanK-II_bac cd24085
nucleotide-binding domain (NBD) of type II pantothenate kinase (PanK-II) and similar proteins ...
15-364 4.35e-53

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: 176.60  E-value: 4.35e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050  15 GMDIGGTLVKLVYFEpkditaeeeqeevenlksirkyltsntaygktgirdvhlelknltmcgRKGNLHFIRFPTCAMHL 94
Cdd:cd24085   3 GIDAGGTLTKIVLLE------------------------------------------------NNGELKFKAFDSLKIEA 34
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050  95 ---FIQMGSEKNFSslhtTLCATGGGAFKFEEDfrmIADLQLHKLDELDCLIQGLLYVdsVGFNGKPecyyfenptnpel 171
Cdd:cd24085  35 lvkFLNELGINDIE----KIAVTGGGASRLPEN---IDGIPIVKVDEFEAIGRGALYL--LGEILDD------------- 92
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050 172 cqkkpycldnpypMLLVNMGSGVSILAVySKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALDMAAKGDSTNVDKLVK 251
Cdd:cd24085  93 -------------ALVVSIGTGTSIVLA-KNGTIRHVGGTGVGGGTLLGLGKLLLGVTDYDEITELARKGDRSNVDLTVG 158
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050 252 DIYGGDYErfGLQGSAVASSFGNMmskEKRESISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRiNMVSM 331
Cdd:cd24085 159 DIYGGGIG--PLPPDLTASNFGKL---ADDNKASREDLAAALINLVGETIGTLAALAARAEGVKDIVLVGSTLR-NPLLK 232
                       330       340       350
                ....*....|....*....|....*....|...
gi 19484050 332 KLLAYAMDFwskGQLKALFLEHEGYFGAVGALL 364
Cdd:cd24085 233 EVLERYTKL---YGVKPIFPENGEFAGAIGALL 262
PTZ00297 PTZ00297
pantothenate kinase; Provisional
16-362 5.14e-36

pantothenate kinase; Provisional


Pssm-ID: 140318 [Multi-domain]  Cd Length: 1452  Bit Score: 139.60  E-value: 5.14e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050    16 MDIGGTLVKLVYFEPKDITAeeeqeevenlksIRKYLT--SNTAYGKTGIRDVHL--------ELKNLTMCGRKGNLHFI 85
Cdd:PTZ00297 1044 IDIGGTFAKIAYVQPPGGFA------------FPTYIVheASSLSEKLGLRTFHFfadaeaaeSELRTRPHSRVGTLRFA 1111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050    86 RFPTCAMHLFIQMGSE----KNFSSLHTT-LCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSVGfngkPEC 160
Cdd:PTZ00297 1112 KIPSKQIPDFADYLAGshaiNYYKPQYRTkVRATGGGAFKYASVAKKVLGINFSVMREMDAVVKGLNLVIRVA----PES 1187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050   161 YYFENPTN----PELCQKKPYCLDNPYPMLLVNMGSGVSILAVYSKD-NYKRVTGTSLGGGTFLGLCCLLTGCETFEEAL 235
Cdd:PTZ00297 1188 IFTVDPSTgvhhPHQLVSPPGDGFSPFPCLLVNIGSGISIIKCLGPDgSHVRVGGSPIGGATFWGLVRTMTNVTSWEEVM 1267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050   236 D---MAAKGDSTNVDKLVKDIYGGDYERFG--LQGSAVASSFGNM----------------------------MSKEKRE 282
Cdd:PTZ00297 1268 EimrLDGPGDNKNVDLLVGDIYGYNAKDLPamLSVDTVASTFGKLgterfyemmrgvstahfsdddaageilsPKALKSP 1347
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050   283 SISKE-------------DLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINMVSMKLLAYAMDFWSKGQLKAL 349
Cdd:PTZ00297 1348 TVISElpvrngtkkasaiDIVRSLLNMISSNVTQLAYLHSRVQGVPNIFFAGGFVRDNPIIWSHISSTMKYWSKGECHAH 1427
                         410
                  ....*....|...
gi 19484050   350 FLEHEGYFGAVGA 362
Cdd:PTZ00297 1428 FLEHDGYLGALGC 1440
PRK13317 PRK13317
pantothenate kinase; Provisional
15-368 8.81e-36

pantothenate kinase; Provisional


Pssm-ID: 237346 [Multi-domain]  Cd Length: 277  Bit Score: 131.62  E-value: 8.81e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050   15 GMDIGGTLVKLVYFEPKditaeeeqeeveNLKSIRKYLTSNtaygktgIRDVHLELKNLTMCGRkgnlhfirfptcamhl 94
Cdd:PRK13317   6 GIDAGGTLTKIVYLEEK------------KQRTFKTEYSAE-------GKKVIDWLINLQDIEK---------------- 50
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050   95 fiqmgseknfsslhttLCATGGGAFKFEEdfRMIADLQLHKLDELDCLIQGLLYvdsvgfngkpecyyfenptnpeLCQK 174
Cdd:PRK13317  51 ----------------ICLTGGKAGYLQQ--LLNYGYPIAEFVEFEATGLGVRY----------------------LLKE 90
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050  175 KPYCLDNpypMLLVNMGSGVSILAVYSKDnYKRVTGTSLGGGTFLGLCCLLTGCETFEEALDMAAKGDSTNVDKLVKDIY 254
Cdd:PRK13317  91 EGHDLND---YIFTNIGTGTSIHYVDGNS-QRRVGGTGIGGGTIQGLSKLLTNISDYEQLIELAKHGDRNNIDLKVGDIY 166
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050  255 GGDYErfGLQGSAVASSFGNMMSKEKRESiSKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNflriNMVSMKLL 334
Cdd:PRK13317 167 KGPLP--PIPGDLTASNFGKVLHHLDSEF-TSSDILAGVIGLVGEVITTLSIQAAREKNIENIVYIGS----TLTNNPLL 239
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 19484050  335 AYAMDFWSKGQ-LKALFLEHEGYFGAVGALLELFK 368
Cdd:PRK13317 240 QEIIESYTKLRnCTPIFLENGGYSGAIGALLLATN 274
PanK COG5146
Pantothenate kinase [Coenzyme transport and metabolism]; Pantothenate kinase is part of the ...
15-364 1.76e-35

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: 130.78  E-value: 1.76e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050  15 GMDIGGTLVKLVYFEpkditaeeeqeevenlksirkyltsntaygktgirdvhlelknltmcgrKGNLHFIRFPTCAMHL 94
Cdd:COG5146   5 GIDAGGTLTKIAYLE-------------------------------------------------DGERRYKKFPSDEIES 35
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050  95 FIQ-MGSEKNFSslhtTLCATGGGAFKFEEdfrMIADLQLHKLDELDCLIQGllyvdsVGFNGKPECYYFENptnpelcq 173
Cdd:COG5146  36 VADwLNKFINIE----KIGLTGGRAEVLAE---KLNGDPKQYIVEFDATGKG------VRYLLKEEGHDIDK-------- 94
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050 174 kkpycldnpypMLLVNMGSGVSIlaVYSKDN-YKRVTGTSLGGGTFLGLCCLLTGCETFEEALDMAAKGDSTNVDKLVKD 252
Cdd:COG5146  95 -----------FIITNVGTGTSI--HYMDGDtQERVGGTGVGGGTLMGLSYLLTGISDFEEIVELAKKGDRDGIDLKVKD 161
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484050 253 IYGGDYErfGLQGSAVASSFGNMMSKEKrESISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINmvsmK 332
Cdd:COG5146 162 IYEGMEP--PIPGDLTASNFGKVLITLD-ESATKEDILAAIIGLVGETITTLSIQAAEEYDTETIVYIGSTLTNN----P 234
                       330       340       350
                ....*....|....*....|....*....|...
gi 19484050 333 LLAYAMDFWSKGQ-LKALFLEHEGYFGAVGALL 364
Cdd:COG5146 235 LLQEVIESYTILRgKKPIFLENGEFSGAIGALL 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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