NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1034568495|ref|XP_016871825|]
View 

pantothenate kinase 1 isoform X4 [Homo sapiens]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
9-360 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: 734.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495   9 WFGMDIGGTLVKLVYFEPKDITAEEEQEEVENLKSIRKYLTSNTAYGKTGIRDVHLELKNLTMCGRKGNLHFIRFPSCAM 88
Cdd:cd24135     1 WFGMDIGGTLVKLVYFEPKDITAEEEQEEVENLKSIRKYLTSNTAYGKTGIRDVHLELKNLTMCGRKGNLHFIRFPSCAM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495  89 HRFIQMGSEKNFSSLHTTLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSVGFNGKPECYYFENPTNPELC 168
Cdd:cd24135    81 HRFIQMGSEKNFSSLHTTLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSVGFNGQPECYYFENPTDPEQC 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495 169 QKKPYCLDNPYPMLLVNMGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALEMAAKGDSTNVDKLVKD 248
Cdd:cd24135   161 QKKPYCLDNPYPMLLVNIGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALEMAAKGDSTNVDKLVKD 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495 249 IYGGDYERFGLQGSAVASSFGNMMSKEKRDSISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINMVSMK 328
Cdd:cd24135   241 IYGGDYERFGLQGSAVASSFGHMMSKEKRDSISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINMVSMK 320
                         330       340       350
                  ....*....|....*....|....*....|..
gi 1034568495 329 LLAYAMDFWSKGQLKALFLEHEGYFGAVGALL 360
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 ...
9-360 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: 734.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495   9 WFGMDIGGTLVKLVYFEPKDITAEEEQEEVENLKSIRKYLTSNTAYGKTGIRDVHLELKNLTMCGRKGNLHFIRFPSCAM 88
Cdd:cd24135     1 WFGMDIGGTLVKLVYFEPKDITAEEEQEEVENLKSIRKYLTSNTAYGKTGIRDVHLELKNLTMCGRKGNLHFIRFPSCAM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495  89 HRFIQMGSEKNFSSLHTTLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSVGFNGKPECYYFENPTNPELC 168
Cdd:cd24135    81 HRFIQMGSEKNFSSLHTTLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSVGFNGQPECYYFENPTDPEQC 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495 169 QKKPYCLDNPYPMLLVNMGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALEMAAKGDSTNVDKLVKD 248
Cdd:cd24135   161 QKKPYCLDNPYPMLLVNIGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALEMAAKGDSTNVDKLVKD 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495 249 IYGGDYERFGLQGSAVASSFGNMMSKEKRDSISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINMVSMK 328
Cdd:cd24135   241 IYGGDYERFGLQGSAVASSFGHMMSKEKRDSISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINMVSMK 320
                         330       340       350
                  ....*....|....*....|....*....|..
gi 1034568495 329 LLAYAMDFWSKGQLKALFLEHEGYFGAVGALL 360
Cdd:cd24135   321 LLAYAMDFWSKGQLKALFLEHEGYFGAVGALL 352
Fumble pfam03630
Fumble; Fumble is required for cell division in Drosophila. Mutants lacking fumble exhibit ...
10-358 7.73e-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: 458.11  E-value: 7.73e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495  10 FGMDIGGTLVKLVYFEPKDITAEEEQeevenlksirkyltsntaygktgirdvhlelknltmcgrkGNLHFIRFPSCAMH 89
Cdd:pfam03630   1 FAIDIGGTLAKLVYFSPVPDSPKELG----------------------------------------GRLHFIKFETTKIE 40
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495  90 RFIQMGSEKNFSSLHT----TLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSvgfNGKPECYYFENPTNP 165
Cdd:pfam03630  41 DCLEFIKSLGLNSKGTdrglTVKATGGGAYKFYDLFKEKLGVKVDKEDEMECLIKGLNFLLT---NIPDEVFTYSDSPEY 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495 166 ELCQKKPyclDNPYPMLLVNMGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALEMAAKGDSTNVDKL 245
Cdd:pfam03630 118 FFQTVDN---NSIYPYLLVNIGSGVSILKVEGPDKFERVGGTSLGGGTFWGLCSLLTGAKSFDEMLELAEKGDNRNVDML 194
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495 246 VKDIYGGDYERFGLQGSAVASSFGNMMSKEKRDSISK----EDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLR 321
Cdd:pfam03630 195 VGDIYGGDYEKIGLKSDTIASSFGKVFRKKFRESASNdaspEDIARSLLYMISNNIGQIAYLNAKLHGLKRIYFGGNFIR 274
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1034568495 322 INMVSMKLLAYAMDFWSKGQLKALFLEHEGYFGAVGA 358
Cdd:pfam03630 275 GHPITMKTLSYAINFWSKGELKALFLRHEGYLGALGA 311
panK_eukar TIGR00555
pantothenate kinase, eukaryotic/staphyloccocal type; This model describes a eukaryotic form of ...
8-361 2.21e-141

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: 402.94  E-value: 2.21e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495   8 PWFGMDIGGTLVKLVYFEPKditaeeeqeevenlkSIRKYLTSNTaygktgirdvhlelknltmcgrkGNLH-FIRFPSC 86
Cdd:TIGR00555   1 SRIGIDIGGTLIKVVYEEKK---------------GRRKFKTFET-----------------------TNIDkFIEWLKN 42
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495  87 AMHRFiqmgseknfsSLHTTLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSVGFNGKPECYYFEnptnpe 166
Cdd:TIGR00555  43 QIHRH----------SRITTLCATGGGAFKFAELIYESAGIQLHKFDEFDALIQGLNYLLKEEPKEKFTYYDFE------ 106
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495 167 lCQKKPYCLDNPYPMLLVNMGSGVSILAVYSkDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALEMAAKGDSTNVDKLV 246
Cdd:TIGR00555 107 -CQKKPIDLDDIYPYLLVNIGTGTSILYVDG-DNYERVGGTSLGGGTFLGLGKLLTGIQTFDELLEMAQHGDRTNVDLLV 184
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495 247 KDIYGGDYERFGLQGSAVASSFGNMMSKEKRDSISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINMVS 326
Cdd:TIGR00555 185 GDIYGGDYSESGLDGSLTASSFGKVLSKHLDQSFSPEDIAASLLGLIGNNIGQIAYLCALRYNIDRIVFIGSFLRNNQLL 264
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1034568495 327 MKLLAYAMDFWSKgqlKALFLEHEGYFGAVGALLE 361
Cdd:TIGR00555 265 MKVLSYATNFWSK---KALFLEHEGYSGAIGALLS 296
PLN02920 PLN02920
pantothenate kinase 1
12-360 1.20e-64

pantothenate kinase 1


Pssm-ID: 215498 [Multi-domain]  Cd Length: 398  Bit Score: 210.85  E-value: 1.20e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495  12 MDIGGTLVKLVYFEPKDitaeeeqeevENLKSIRKYLTSNTAYGKTGIRDVHLELKNLTMCgrkgnLHFIRFPSCAMHRF 91
Cdd:PLN02920   23 LDIGGSLIKLVYFSRNS----------GDSEDPRNDSSVKSDGVNGRLHFAKFETRKINDC-----LEFISSNKLHHGGF 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495  92 IQM---GSEKNFsslhttLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGllyvdsVGFNGKP---ECYYFENPtnp 165
Cdd:PLN02920   88 QHHenpTHDKNF------IKATGGGAYKFADLFKEKLGISLDKEDEMDCLVTG------ANFLLKAvhhEAFTYLDG--- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495 166 elcQKKPYCLDNP--YPMLLVNMGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALEMAAKGDSTNVD 243
Cdd:PLN02920  153 ---QKEFVQIDHNdlYPYLLVNIGSGVSMIKVDGDGKFERVSGTSVGGGTFWGLGKLLTKCKSFDELLELSHQGNNRVID 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495 244 KLVKDIYGG-DYERFGLQGSAVASSFGNMMSKEKR-DSISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLR 321
Cdd:PLN02920  230 MLVGDIYGGmDYSKIGLSSTTIASSFGKAISDNKElEDYKPEDVARSLLRMISNNIGQISYLNALRFGLKRIFFGGFFIR 309
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1034568495 322 INMVSMKLLAYAMDFWSKGQLKALFLEHEGYFGAVGALL 360
Cdd:PLN02920  310 GHSYTMDTISVAVHFWSKGEAKAMFLRHEGFLGALGAFM 348
PanK COG5146
Pantothenate kinase [Coenzyme transport and metabolism]; Pantothenate kinase is part of the ...
11-360 8.84e-36

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: 131.16  E-value: 8.84e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495  11 GMDIGGTLVKLVYFEpkditaeeeqeevenlksirkyltsntaygktgirdvhlelknltmcgrKGNLHFIRFPSCAMHR 90
Cdd:COG5146     5 GIDAGGTLTKIAYLE-------------------------------------------------DGERRYKKFPSDEIES 35
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495  91 FIQ-MGSEKNFSslhtTLCATGGGAFKFEEdfrMIADLQLHKLDELDCLIQGllyvdsVGFNGKPECYYFENptnpelcq 169
Cdd:COG5146    36 VADwLNKFINIE----KIGLTGGRAEVLAE---KLNGDPKQYIVEFDATGKG------VRYLLKEEGHDIDK-------- 94
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495 170 kkpycldnpypMLLVNMGSGVSIlaVYSKDN-YKRVTGTSLGGGTFLGLCCLLTGCETFEEALEMAAKGDSTNVDKLVKD 248
Cdd:COG5146    95 -----------FIITNVGTGTSI--HYMDGDtQERVGGTGVGGGTLMGLSYLLTGISDFEEIVELAKKGDRDGIDLKVKD 161
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495 249 IYGGDYErfGLQGSAVASSFGNMMSKEKRDsISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINmvsmK 328
Cdd:COG5146   162 IYEGMEP--PIPGDLTASNFGKVLITLDES-ATKEDILAAIIGLVGETITTLSIQAAEEYDTETIVYIGSTLTNN----P 234
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1034568495 329 LLAYAMDFWSKGQ-LKALFLEHEGYFGAVGALL 360
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 ...
9-360 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: 734.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495   9 WFGMDIGGTLVKLVYFEPKDITAEEEQEEVENLKSIRKYLTSNTAYGKTGIRDVHLELKNLTMCGRKGNLHFIRFPSCAM 88
Cdd:cd24135     1 WFGMDIGGTLVKLVYFEPKDITAEEEQEEVENLKSIRKYLTSNTAYGKTGIRDVHLELKNLTMCGRKGNLHFIRFPSCAM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495  89 HRFIQMGSEKNFSSLHTTLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSVGFNGKPECYYFENPTNPELC 168
Cdd:cd24135    81 HRFIQMGSEKNFSSLHTTLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSVGFNGQPECYYFENPTDPEQC 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495 169 QKKPYCLDNPYPMLLVNMGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALEMAAKGDSTNVDKLVKD 248
Cdd:cd24135   161 QKKPYCLDNPYPMLLVNIGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALEMAAKGDSTNVDKLVKD 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495 249 IYGGDYERFGLQGSAVASSFGNMMSKEKRDSISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINMVSMK 328
Cdd:cd24135   241 IYGGDYERFGLQGSAVASSFGHMMSKEKRDSISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINMVSMK 320
                         330       340       350
                  ....*....|....*....|....*....|..
gi 1034568495 329 LLAYAMDFWSKGQLKALFLEHEGYFGAVGALL 360
Cdd:cd24135   321 LLAYAMDFWSKGQLKALFLEHEGYFGAVGALL 352
ASKHA_NBD_PanK-II_Pank2 cd24136
nucleotide-binding domain (NBD) of pantothenate kinase 2 (Pank2) from type II pantothenate ...
9-362 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: 641.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495   9 WFGMDIGGTLVKLVYFEPKDITAEEEQEEVENLKSIRKYLTSNTAYGKTGIRDVHLELKNLTMCGRKGNLHFIRFPSCAM 88
Cdd:cd24136     1 WFGLDIGGTLVKLVYFEPKDITAEEEEEEVENLKSIRKYLTSNVAYGSTGIRDVHLELKDLTLCGRKGNLHFIRFPTHDM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495  89 HRFIQMGSEKNFSSLHTTLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSVGFNGKPECYYFENPTNPELC 168
Cdd:cd24136    81 PAFIQMGRDKHFSSLHTTLCATGGGAYKFEQDFLTMGDLQLCKLDELDCLIKGVLYIDSVGFNGHSECYYFENPTDSEKC 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495 169 QKKPYCLDNPYPMLLVNMGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALEMAAKGDSTNVDKLVKD 248
Cdd:cd24136   161 QKLPFNLKNPYPLLLVNIGSGVSILAVYSKDNYKRVTGTSLGGGTFFGLCCLLTGCTTFEEALEMASRGDSTKVDKLVRD 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495 249 IYGGDYERFGLQGSAVASSFGNMMSKEKRDSISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINMVSMK 328
Cdd:cd24136   241 IYGGDYERFGLPGWAVASSFGNMMSKEKREAVSKEDLARATLITITNNIGSIARMCALNENINRVVFVGNFLRINTISMR 320
                         330       340       350
                  ....*....|....*....|....*....|....
gi 1034568495 329 LLAYAMDFWSKGQLKALFLEHEGYFGAVGALLEL 362
Cdd:cd24136   321 LLAYALDYWSKGQLKALFLEHEGYFGAVGALLEL 354
ASKHA_NBD_PanK-II_Pank3 cd24137
nucleotide-binding domain (NBD) of pantothenate kinase 3 (Pank3) from type II pantothenate ...
9-360 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: 571.18  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495   9 WFGMDIGGTLVKLVYFEPKDITAEEEQEEVENLKSIRKYLTSNTAYGKTGIRDVHLELKNLTMCGRKGNLHFIRFPSCAM 88
Cdd:cd24137     1 WFGMDIGGTLVKLSYFEPIDITAEEEQEEVESLKSIRKYLTSNVAYGSTGIRDVHLELKDLTLFGRRGNLHFIRFPTQDL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495  89 HRFIQMGSEKNFSSLHTTLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSVGFNGKPECYYFENPTNPELC 168
Cdd:cd24137    81 PTFIQMGRDKNFSTLQTVLCATGGGAYKFEKDFRTIGNLHLHKLDELDCLVKGLLYIDSVSFNGQAECYYFANASEPERC 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495 169 QKKPYCLDNPYPMLLVNMGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALEMAAKGDSTNVDKLVKD 248
Cdd:cd24137   161 QKMPFNLDDPYPLLVVNIGSGVSILAVHSKDNYKRVTGTSLGGGTFLGLCSLLTGCESFEEALEMASKGDSTQADKLVRD 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495 249 IYGGDYERFGLQGSAVASSFGNMMSKEKRDSISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINMVSMK 328
Cdd:cd24137   241 IYGGDYERFGLPGWAVASSFGNMIYKEKRESVSKEDLARATLVTITNNIGSVARMCAVNEKINRVVFVGNFLRVNTLSMK 320
                         330       340       350
                  ....*....|....*....|....*....|..
gi 1034568495 329 LLAYAMDFWSKGQLKALFLEHEGYFGAVGALL 360
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 ...
9-360 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: 567.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495   9 WFGMDIGGTLVKLVYFEPKditaeeeqeevenlksirkyltsntaygktgirdvhlelknltmcgrkGNLHFIRFPSCAM 88
Cdd:cd24122     1 WFGLDIGGTLVKLVYFEPT------------------------------------------------GTLHFIRFETSRM 32
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495  89 HRFIQMGSEKNFSSLHTTLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSvgfNGKPECYYFENPTNPELC 168
Cdd:cd24122    33 EGFIQLAREKNLSSLIKTVCATGGGAYKFEKLFREELGLQLHKLDELDCLIRGINFLLR---HVPDECYYFENPSDPELC 109
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495 169 QK--KPYCLDNPYPMLLVNMGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALEMAAKGDSTNVDKLV 246
Cdd:cd24122   110 EKrvVPFDFSDPYPYLLVNIGSGVSILAVESPDNYERVSGTSLGGGTFLGLCCLLTGCETFEEALELAAKGDSTKVDMLV 189
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495 247 KDIYGGDYERFGLQGSAVASSFGNMMSKEKRDSISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINMVS 326
Cdd:cd24122   190 GDIYGGDYEKFGLPGDTVASSFGKMVAKEKRESASKEDLARALLVMITNNIGSIARLCAKNEGIKRVVFVGNFLRHNPIA 269
                         330       340       350
                  ....*....|....*....|....*....|....
gi 1034568495 327 MKLLAYAMDFWSKGQLKALFLEHEGYFGAVGALL 360
Cdd:cd24122   270 MRLLAYAMDYWSKGEMKALFLEHEGYFGALGALL 303
ASKHA_NBD_PanK-II cd24016
nucleotide-binding domain (NBD) of type II pantothenate kinase (PanK-II) and similar proteins; ...
9-360 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: 517.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495   9 WFGMDIGGTLVKLVYFepkditaeeeqeevenlksirkyltsntaygktgirdvhlelknltmcgrkgnLHFIRFPSCAM 88
Cdd:cd24016     1 WFGIDIGGTLVKLVYF-----------------------------------------------------LHFIRFPTDQV 27
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495  89 HRFIQMGSEKNFSSLHTTLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSVGFNGKPECYYFENPTNPELC 168
Cdd:cd24016    28 VEFIQMGQDKNFSTLITKLCATGGGAGKFEEDFRTIGNLPLQKLDELDCLSQGLLYLDSVQFNGQAECYYFANASEPERC 107
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495 169 QKKPYCLDNPYPMLLVNMGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALEMAAKGDSTNVDKLVKD 248
Cdd:cd24016   108 QKMPFNLHDPYPYLFVNVGSGVSILAVDSKDNYKRVTGTSLGGGTFQGLCYLLTGCTDFEEALEMAQHGDSTTIDKLVRD 187
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495 249 IYGGDYERFGLQGSAVASSFGNMMSKEKRDSISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINMVSMK 328
Cdd:cd24016   188 IYGGDYERFGLPGDAVASSFGNMLHKEKRADFSKEDLARATLGTITNNIGSMARMCARNEKIENVVFVGNFLRNNALLMK 267
                         330       340       350
                  ....*....|....*....|....*....|..
gi 1034568495 329 LLAYAMDFWSKGQLKALFLEHEGYFGAVGALL 360
Cdd:cd24016   268 LLAYATDLWSKGQLKALFVEHEGYFGAVGALL 299
Fumble pfam03630
Fumble; Fumble is required for cell division in Drosophila. Mutants lacking fumble exhibit ...
10-358 7.73e-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: 458.11  E-value: 7.73e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495  10 FGMDIGGTLVKLVYFEPKDITAEEEQeevenlksirkyltsntaygktgirdvhlelknltmcgrkGNLHFIRFPSCAMH 89
Cdd:pfam03630   1 FAIDIGGTLAKLVYFSPVPDSPKELG----------------------------------------GRLHFIKFETTKIE 40
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495  90 RFIQMGSEKNFSSLHT----TLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSvgfNGKPECYYFENPTNP 165
Cdd:pfam03630  41 DCLEFIKSLGLNSKGTdrglTVKATGGGAYKFYDLFKEKLGVKVDKEDEMECLIKGLNFLLT---NIPDEVFTYSDSPEY 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495 166 ELCQKKPyclDNPYPMLLVNMGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALEMAAKGDSTNVDKL 245
Cdd:pfam03630 118 FFQTVDN---NSIYPYLLVNIGSGVSILKVEGPDKFERVGGTSLGGGTFWGLCSLLTGAKSFDEMLELAEKGDNRNVDML 194
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495 246 VKDIYGGDYERFGLQGSAVASSFGNMMSKEKRDSISK----EDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLR 321
Cdd:pfam03630 195 VGDIYGGDYEKIGLKSDTIASSFGKVFRKKFRESASNdaspEDIARSLLYMISNNIGQIAYLNAKLHGLKRIYFGGNFIR 274
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1034568495 322 INMVSMKLLAYAMDFWSKGQLKALFLEHEGYFGAVGA 358
Cdd:pfam03630 275 GHPITMKTLSYAINFWSKGELKALFLRHEGYLGALGA 311
panK_eukar TIGR00555
pantothenate kinase, eukaryotic/staphyloccocal type; This model describes a eukaryotic form of ...
8-361 2.21e-141

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: 402.94  E-value: 2.21e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495   8 PWFGMDIGGTLVKLVYFEPKditaeeeqeevenlkSIRKYLTSNTaygktgirdvhlelknltmcgrkGNLH-FIRFPSC 86
Cdd:TIGR00555   1 SRIGIDIGGTLIKVVYEEKK---------------GRRKFKTFET-----------------------TNIDkFIEWLKN 42
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495  87 AMHRFiqmgseknfsSLHTTLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSVGFNGKPECYYFEnptnpe 166
Cdd:TIGR00555  43 QIHRH----------SRITTLCATGGGAFKFAELIYESAGIQLHKFDEFDALIQGLNYLLKEEPKEKFTYYDFE------ 106
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495 167 lCQKKPYCLDNPYPMLLVNMGSGVSILAVYSkDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALEMAAKGDSTNVDKLV 246
Cdd:TIGR00555 107 -CQKKPIDLDDIYPYLLVNIGTGTSILYVDG-DNYERVGGTSLGGGTFLGLGKLLTGIQTFDELLEMAQHGDRTNVDLLV 184
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495 247 KDIYGGDYERFGLQGSAVASSFGNMMSKEKRDSISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINMVS 326
Cdd:TIGR00555 185 GDIYGGDYSESGLDGSLTASSFGKVLSKHLDQSFSPEDIAASLLGLIGNNIGQIAYLCALRYNIDRIVFIGSFLRNNQLL 264
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1034568495 327 MKLLAYAMDFWSKgqlKALFLEHEGYFGAVGALLE 361
Cdd:TIGR00555 265 MKVLSYATNFWSK---KALFLEHEGYSGAIGALLS 296
ASKHA_NBD_PanK-II_euk cd24086
nucleotide-binding domain (NBD) of type II pantothenate kinase (PanK-II) and similar proteins ...
9-360 1.47e-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: 402.04  E-value: 1.47e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495   9 WFGMDIGGTLVKLVYFEPKDITAEEEqeevenlksirkyltsntaygktgirDVHLELKNLTMCGRKGNLHFIRFPSCAM 88
Cdd:cd24086     1 RLGLDIGGTLAKLAYLTPIDIDEAEE--------------------------KESVLLKLLANSGEDGELHFISFPNKDL 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495  89 HRFIQMGSEKNF--SSLHTTLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSVGFngKPECYYFENPTNPE 166
Cdd:cd24086    55 EEFLNFLRDKNFedSSKGKVLYATGGGAYKYAELIEETLGVQLVKVDEMDSLVNGLHFLLSVLS--KDECFPFPNDSGPE 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495 167 LCQKKPYCLDNPYPMLLVNMGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALEMAAKGDSTNVDKLV 246
Cdd:cd24086   133 FLQKDPQLSDDLFPCLLVNIGSGVSILKVDSDGKYERVSGTSLGGGTFLGLASLLTGTNSFDELLELASRGDRANVDLLV 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495 247 KDIYGGDYERFGLQGSAVASSFGNMMSKEK-RDSISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINMV 325
Cdd:cd24086   213 RDIYGGDYPYLGLPGDLLASSFGKLADDEKsREDFSKEDIARSLLRMIVNNIGYLAYLVAKLHNVKRVFFTGNFIRNNEL 292
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1034568495 326 SMKLLAYAMDFWSKGQLKALFLEHEGYFGAVGALL 360
Cdd:cd24086   293 ARKLIAEALNYWSKGSLNALFLRHDGYLGALGALL 327
ASKHA_NBD_PanK-II_Pank4 cd24123
nucleotide-binding domain (NBD) of pantothenate kinase 4 (Pank4) from type II pantothenate ...
10-360 9.81e-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: 324.13  E-value: 9.81e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495  10 FGMDIGGTLVKLVYFEPKDitaeeeqeevenlKSIRKYLTSNTAYGKTGIRDVHLELKNLTMCGRkgnLHFIRFPSCAMH 89
Cdd:cd24123     2 FAIDIGGSLAKLVYFSRVS-------------DKAASVSSSSGTSKGPSDEPLYEVSEQPELGGR---LHFVKFETKYIE 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495  90 RFIQMGSEKNFSSLHTTLC-----ATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSvgfNGKPECYYFENPTN 164
Cdd:cd24123    66 ECLDFIKDNLLHSRQGNKRgkvikATGGGAYKYADLIKEKLGVEVDKEDEMECLIKGCNFLLK---NIPDEVFTYDEHAK 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495 165 PELcqKKPYCLDNPYPMLLVNMGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALEMAAKGDSTNVDK 244
Cdd:cd24123   143 PEV--KFQSDPPDIFPYLLVNIGSGVSILKVDSEDKFERVGGTSLGGGTFWGLGSLLTGAKSFDELLELAEKGDNRNVDM 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495 245 LVKDIYGGDYERFGLQGSAVASSFGNMMSKEK---RDSISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLR 321
Cdd:cd24123   221 LVGDIYGGDYSKIGLKSDTIASSFGKVARADKdarLEDFSPEDIAKSLLRMISNNIGQIAYLNAKLHGLKRIYFGGFFIR 300
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1034568495 322 INMVSMKLLAYAMDFWSKGQLKALFLEHEGYFGAVGALL 360
Cdd:cd24123   301 GHPLTMHTISYAINFWSKGEMQALFLRHEGYLGAIGAFL 339
PLN02920 PLN02920
pantothenate kinase 1
12-360 1.20e-64

pantothenate kinase 1


Pssm-ID: 215498 [Multi-domain]  Cd Length: 398  Bit Score: 210.85  E-value: 1.20e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495  12 MDIGGTLVKLVYFEPKDitaeeeqeevENLKSIRKYLTSNTAYGKTGIRDVHLELKNLTMCgrkgnLHFIRFPSCAMHRF 91
Cdd:PLN02920   23 LDIGGSLIKLVYFSRNS----------GDSEDPRNDSSVKSDGVNGRLHFAKFETRKINDC-----LEFISSNKLHHGGF 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495  92 IQM---GSEKNFsslhttLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGllyvdsVGFNGKP---ECYYFENPtnp 165
Cdd:PLN02920   88 QHHenpTHDKNF------IKATGGGAYKFADLFKEKLGISLDKEDEMDCLVTG------ANFLLKAvhhEAFTYLDG--- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495 166 elcQKKPYCLDNP--YPMLLVNMGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALEMAAKGDSTNVD 243
Cdd:PLN02920  153 ---QKEFVQIDHNdlYPYLLVNIGSGVSMIKVDGDGKFERVSGTSVGGGTFWGLGKLLTKCKSFDELLELSHQGNNRVID 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495 244 KLVKDIYGG-DYERFGLQGSAVASSFGNMMSKEKR-DSISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLR 321
Cdd:PLN02920  230 MLVGDIYGGmDYSKIGLSSTTIASSFGKAISDNKElEDYKPEDVARSLLRMISNNIGQISYLNALRFGLKRIFFGGFFIR 309
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1034568495 322 INMVSMKLLAYAMDFWSKGQLKALFLEHEGYFGAVGALL 360
Cdd:PLN02920  310 GHSYTMDTISVAVHFWSKGEAKAMFLRHEGFLGALGAFM 348
PLN02902 PLN02902
pantothenate kinase
10-360 2.95e-63

pantothenate kinase


Pssm-ID: 215489 [Multi-domain]  Cd Length: 876  Bit Score: 216.69  E-value: 2.95e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495  10 FGMDIGGTLVKLVYFEPKDitaeeeqeeVENLKSIRKyltsNTAYGKTGIRDVHLelKNLTMCGrkGNLHFIRFPSCAMH 89
Cdd:PLN02902   56 LALDIGGSLIKLVYFSRHE---------DRSTDDKRK----RTIKERLGITNGNR--RSYPILG--GRLHFVKFETSKIN 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495  90 RFIQMGSEKNF-------------SSLHTTLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLlyvdsvgfNGKPEC 156
Cdd:PLN02902  119 ECLDFISSKQLhrggihswlskapPNGNGVIKATGGGAYKFADLFKERLGVSLDKEDEMDCLVAGA--------NFLLKA 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495 157 YYFENPTNPElCQKKPYCLD--NPYPMLLVNMGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALEMA 234
Cdd:PLN02902  191 IRHEAFTHME-GEKEFVQIDqnDLFPYLLVNIGSGVSMIKVDGDGKFERVSGTNVGGGTYWGLGRLLTKCKSFDELLELS 269
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495 235 AKGDSTNVDKLVKDIYGG-DYERFGLQGSAVASSFGNMMSKEKR-DSISKEDLARATLVTITNNIGSIARMCALNENIDR 312
Cdd:PLN02902  270 QRGDNSAIDMLVGDIYGGmDYSKIGLSASTIASSFGKVISENKElSDYRPEDISLSLLRMISYNIGQISYLNALRFGLKR 349
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1034568495 313 VVFVGNFLRINMVSMKLLAYAMDFWSKGQLKALFLEHEGYFGAVGALL 360
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 ...
11-360 4.85e-54

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: 178.91  E-value: 4.85e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495  11 GMDIGGTLVKLVYFEpkditaeeeqeevenlksirkyltsntaygktgirdvhlelknltmcgRKGNLHFIRFPSCAMH- 89
Cdd:cd24085     3 GIDAGGTLTKIVLLE------------------------------------------------NNGELKFKAFDSLKIEa 34
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495  90 --RFIQMGSEKNFSslhtTLCATGGGAFKFEEDfrmIADLQLHKLDELDCLIQGLLYVdsVGFNGKPecyyfenptnpel 167
Cdd:cd24085    35 lvKFLNELGINDIE----KIAVTGGGASRLPEN---IDGIPIVKVDEFEAIGRGALYL--LGEILDD------------- 92
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495 168 cqkkpycldnpypMLLVNMGSGVSILAVySKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALEMAAKGDSTNVDKLVK 247
Cdd:cd24085    93 -------------ALVVSIGTGTSIVLA-KNGTIRHVGGTGVGGGTLLGLGKLLLGVTDYDEITELARKGDRSNVDLTVG 158
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495 248 DIYGGDYErfGLQGSAVASSFGNMmskEKRDSISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRiNMVSM 327
Cdd:cd24085   159 DIYGGGIG--PLPPDLTASNFGKL---ADDNKASREDLAAALINLVGETIGTLAALAARAEGVKDIVLVGSTLR-NPLLK 232
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1034568495 328 KLLAYAMDFwskGQLKALFLEHEGYFGAVGALL 360
Cdd:cd24085   233 EVLERYTKL---YGVKPIFPENGEFAGAIGALL 262
PTZ00297 PTZ00297
pantothenate kinase; Provisional
12-358 2.11e-38

pantothenate kinase; Provisional


Pssm-ID: 140318 [Multi-domain]  Cd Length: 1452  Bit Score: 146.54  E-value: 2.11e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495   12 MDIGGTLVKLVYFEPKDITAeeeqeevenlksIRKYLT--SNTAYGKTGIRDVHL--------ELKNLTMCGRKGNLHFI 81
Cdd:PTZ00297  1044 IDIGGTFAKIAYVQPPGGFA------------FPTYIVheASSLSEKLGLRTFHFfadaeaaeSELRTRPHSRVGTLRFA 1111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495   82 RFPSCAMHRFIQMGSE----KNFSSLHTT-LCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSVGfngkPEC 156
Cdd:PTZ00297  1112 KIPSKQIPDFADYLAGshaiNYYKPQYRTkVRATGGGAFKYASVAKKVLGINFSVMREMDAVVKGLNLVIRVA----PES 1187
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495  157 YYFENPTN----PELCQKKPYCLDNPYPMLLVNMGSGVSILAVYSKD-NYKRVTGTSLGGGTFLGLCCLLTGCETFEEAL 231
Cdd:PTZ00297  1188 IFTVDPSTgvhhPHQLVSPPGDGFSPFPCLLVNIGSGISIIKCLGPDgSHVRVGGSPIGGATFWGLVRTMTNVTSWEEVM 1267
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495  232 E---MAAKGDSTNVDKLVKDIYGGDYERFG--LQGSAVASSFGNMMSKEKRDSI-------------------------- 280
Cdd:PTZ00297  1268 EimrLDGPGDNKNVDLLVGDIYGYNAKDLPamLSVDTVASTFGKLGTERFYEMMrgvstahfsdddaageilspkalksp 1347
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495  281 ---------------SKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINMVSMKLLAYAMDFWSKGQLKAL 345
Cdd:PTZ00297  1348 tviselpvrngtkkaSAIDIVRSLLNMISSNVTQLAYLHSRVQGVPNIFFAGGFVRDNPIIWSHISSTMKYWSKGECHAH 1427
                          410
                   ....*....|...
gi 1034568495  346 FLEHEGYFGAVGA 358
Cdd:PTZ00297  1428 FLEHDGYLGALGC 1440
PRK13317 PRK13317
pantothenate kinase; Provisional
11-364 6.51e-36

pantothenate kinase; Provisional


Pssm-ID: 237346 [Multi-domain]  Cd Length: 277  Bit Score: 132.00  E-value: 6.51e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495  11 GMDIGGTLVKLVYFEPKditaeeeqeeveNLKSIRKYLTSNtaygktgIRDVHLELKNLTMCGRkgnlhfirfpscamhr 90
Cdd:PRK13317    6 GIDAGGTLTKIVYLEEK------------KQRTFKTEYSAE-------GKKVIDWLINLQDIEK---------------- 50
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495  91 fiqmgseknfsslhttLCATGGGAFKFEEdfRMIADLQLHKLDELDCLIQGLLYvdsvgfngkpecyyfenptnpeLCQK 170
Cdd:PRK13317   51 ----------------ICLTGGKAGYLQQ--LLNYGYPIAEFVEFEATGLGVRY----------------------LLKE 90
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495 171 KPYCLDNpypMLLVNMGSGVSILAVYSKDnYKRVTGTSLGGGTFLGLCCLLTGCETFEEALEMAAKGDSTNVDKLVKDIY 250
Cdd:PRK13317   91 EGHDLND---YIFTNIGTGTSIHYVDGNS-QRRVGGTGIGGGTIQGLSKLLTNISDYEQLIELAKHGDRNNIDLKVGDIY 166
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495 251 GGDYErfGLQGSAVASSFGNMMSkEKRDSISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNflriNMVSMKLL 330
Cdd:PRK13317  167 KGPLP--PIPGDLTASNFGKVLH-HLDSEFTSSDILAGVIGLVGEVITTLSIQAAREKNIENIVYIGS----TLTNNPLL 239
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1034568495 331 AYAMDFWSKGQ-LKALFLEHEGYFGAVGALLELFK 364
Cdd:PRK13317  240 QEIIESYTKLRnCTPIFLENGGYSGAIGALLLATN 274
PanK COG5146
Pantothenate kinase [Coenzyme transport and metabolism]; Pantothenate kinase is part of the ...
11-360 8.84e-36

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: 131.16  E-value: 8.84e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495  11 GMDIGGTLVKLVYFEpkditaeeeqeevenlksirkyltsntaygktgirdvhlelknltmcgrKGNLHFIRFPSCAMHR 90
Cdd:COG5146     5 GIDAGGTLTKIAYLE-------------------------------------------------DGERRYKKFPSDEIES 35
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495  91 FIQ-MGSEKNFSslhtTLCATGGGAFKFEEdfrMIADLQLHKLDELDCLIQGllyvdsVGFNGKPECYYFENptnpelcq 169
Cdd:COG5146    36 VADwLNKFINIE----KIGLTGGRAEVLAE---KLNGDPKQYIVEFDATGKG------VRYLLKEEGHDIDK-------- 94
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495 170 kkpycldnpypMLLVNMGSGVSIlaVYSKDN-YKRVTGTSLGGGTFLGLCCLLTGCETFEEALEMAAKGDSTNVDKLVKD 248
Cdd:COG5146    95 -----------FIITNVGTGTSI--HYMDGDtQERVGGTGVGGGTLMGLSYLLTGISDFEEIVELAKKGDRDGIDLKVKD 161
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568495 249 IYGGDYErfGLQGSAVASSFGNMMSKEKRDsISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINmvsmK 328
Cdd:COG5146   162 IYEGMEP--PIPGDLTASNFGKVLITLDES-ATKEDILAAIIGLVGETITTLSIQAAEEYDTETIVYIGSTLTNN----P 234
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1034568495 329 LLAYAMDFWSKGQ-LKALFLEHEGYFGAVGALL 360
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH