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Conserved domains on  [gi|564333466|ref|XP_006231338|]
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pantothenate kinase 1 isoform X1 [Rattus norvegicus]

Protein Classification

type II pantothenate kinase( domain architecture ID 10508179)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ASKHA_NBD_PanK-II_Pank1 cd24135
nucleotide-binding domain (NBD) of pantothenate kinase 1 (Pank1) from type II pantothenate ...
190-541 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: 756.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466 190 WFGMDIGGTLVKLVYFEPKDITAEEEQEEVENLKSIRKYLTSNTAYGKTGIRDVHLELKNLTMCGRKGNLHFIRFPTCAM 269
Cdd:cd24135    1 WFGMDIGGTLVKLVYFEPKDITAEEEQEEVENLKSIRKYLTSNTAYGKTGIRDVHLELKNLTMCGRKGNLHFIRFPSCAM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466 270 HMFIQMGSEKNFSSLHTTLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSVGFNGKPECYYFENPTNPELC 349
Cdd:cd24135   81 HRFIQMGSEKNFSSLHTTLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSVGFNGQPECYYFENPTDPEQC 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466 350 QKKPYCLDNPYPMLLVNMGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALDMAAKGDSTNVDKLVKD 429
Cdd:cd24135  161 QKKPYCLDNPYPMLLVNIGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALEMAAKGDSTNVDKLVKD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466 430 IYGGDYERFGLQGSAVASSFGNMMSKEKRESISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINMVSMK 509
Cdd:cd24135  241 IYGGDYERFGLQGSAVASSFGHMMSKEKRDSISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINMVSMK 320
                        330       340       350
                 ....*....|....*....|....*....|..
gi 564333466 510 LLAYAMDFWSKGQLKALFLEHEGYFGAVGALL 541
Cdd:cd24135  321 LLAYAMDFWSKGQLKALFLEHEGYFGAVGALL 352
PHA03321 super family cl33724
tegument protein VP11/12; Provisional
7-102 2.74e-03

tegument protein VP11/12; Provisional


The actual alignment was detected with superfamily member PHA03321:

Pssm-ID: 223041 [Multi-domain]  Cd Length: 694  Bit Score: 40.71  E-value: 2.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466   7 PRPGSAEVPAAARDAETLRAGAASPARRAQLAEDVGTPTGGGEERRGRQPPAAA---RRLRESKPQGGSEDRRTADrdlQ 83
Cdd:PHA03321 446 PRARPGSTPACARRARAQRARDAGPEYVDPLGALRRLPAGAAPPPEPAAAPSPAtyyTRMGGGPPRLPPRNRATET---L 522
                         90
                 ....*....|....*....
gi 564333466  84 RGCLsRSPRTAPPvPGMGD 102
Cdd:PHA03321 523 RPDW-GPPAAAPP-EQMED 539
 
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 ...
190-541 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: 756.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466 190 WFGMDIGGTLVKLVYFEPKDITAEEEQEEVENLKSIRKYLTSNTAYGKTGIRDVHLELKNLTMCGRKGNLHFIRFPTCAM 269
Cdd:cd24135    1 WFGMDIGGTLVKLVYFEPKDITAEEEQEEVENLKSIRKYLTSNTAYGKTGIRDVHLELKNLTMCGRKGNLHFIRFPSCAM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466 270 HMFIQMGSEKNFSSLHTTLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSVGFNGKPECYYFENPTNPELC 349
Cdd:cd24135   81 HRFIQMGSEKNFSSLHTTLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSVGFNGQPECYYFENPTDPEQC 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466 350 QKKPYCLDNPYPMLLVNMGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALDMAAKGDSTNVDKLVKD 429
Cdd:cd24135  161 QKKPYCLDNPYPMLLVNIGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALEMAAKGDSTNVDKLVKD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466 430 IYGGDYERFGLQGSAVASSFGNMMSKEKRESISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINMVSMK 509
Cdd:cd24135  241 IYGGDYERFGLQGSAVASSFGHMMSKEKRDSISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINMVSMK 320
                        330       340       350
                 ....*....|....*....|....*....|..
gi 564333466 510 LLAYAMDFWSKGQLKALFLEHEGYFGAVGALL 541
Cdd:cd24135  321 LLAYAMDFWSKGQLKALFLEHEGYFGAVGALL 352
Fumble pfam03630
Fumble; Fumble is required for cell division in Drosophila. Mutants lacking fumble exhibit ...
191-539 2.90e-167

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: 476.60  E-value: 2.90e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466  191 FGMDIGGTLVKLVYFEPKDITAEEEQeevenlksirkyltsntaygktgirdvhlelknltmcgrkGNLHFIRFPTCAMH 270
Cdd:pfam03630   1 FAIDIGGTLAKLVYFSPVPDSPKELG----------------------------------------GRLHFIKFETTKIE 40
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466  271 MFIQMGSEKNFSSLHT----TLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSvgfNGKPECYYFENPtnp 346
Cdd:pfam03630  41 DCLEFIKSLGLNSKGTdrglTVKATGGGAYKFYDLFKEKLGVKVDKEDEMECLIKGLNFLLT---NIPDEVFTYSDS--- 114
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466  347 elCQKKPYCLDN--PYPMLLVNMGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALDMAAKGDSTNVD 424
Cdd:pfam03630 115 --PEYFFQTVDNnsIYPYLLVNIGSGVSILKVEGPDKFERVGGTSLGGGTFWGLCSLLTGAKSFDEMLELAEKGDNRNVD 192
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466  425 KLVKDIYGGDYERFGLQGSAVASSFGNMMSKEKRESISK----EDLARATLVTITNNIGSIARMCALNENIDRVVFVGNF 500
Cdd:pfam03630 193 MLVGDIYGGDYEKIGLKSDTIASSFGKVFRKKFRESASNdaspEDIARSLLYMISNNIGQIAYLNAKLHGLKRIYFGGNF 272
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 564333466  501 LRINMVSMKLLAYAMDFWSKGQLKALFLEHEGYFGAVGA 539
Cdd:pfam03630 273 IRGHPITMKTLSYAINFWSKGELKALFLRHEGYLGALGA 311
panK_eukar TIGR00555
pantothenate kinase, eukaryotic/staphyloccocal type; This model describes a eukaryotic form of ...
189-542 5.78e-146

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: 421.81  E-value: 5.78e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466  189 PWFGMDIGGTLVKLVYFEPKditaeeeqeevenlkSIRKYLTSNTaygktgirdvhlelknltmcgrkGNLH-FIRFPTC 267
Cdd:TIGR00555   1 SRIGIDIGGTLIKVVYEEKK---------------GRRKFKTFET-----------------------TNIDkFIEWLKN 42
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466  268 AMHMFiqmgseknfsSLHTTLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSVGFNGKPECYYFEnptnpe 347
Cdd:TIGR00555  43 QIHRH----------SRITTLCATGGGAFKFAELIYESAGIQLHKFDEFDALIQGLNYLLKEEPKEKFTYYDFE------ 106
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466  348 lCQKKPYCLDNPYPMLLVNMGSGVSILAVYSkDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALDMAAKGDSTNVDKLV 427
Cdd:TIGR00555 107 -CQKKPIDLDDIYPYLLVNIGTGTSILYVDG-DNYERVGGTSLGGGTFLGLGKLLTGIQTFDELLEMAQHGDRTNVDLLV 184
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466  428 KDIYGGDYERFGLQGSAVASSFGNMMSKEKRESISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINMVS 507
Cdd:TIGR00555 185 GDIYGGDYSESGLDGSLTASSFGKVLSKHLDQSFSPEDIAASLLGLIGNNIGQIAYLCALRYNIDRIVFIGSFLRNNQLL 264
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 564333466  508 MKLLAYAMDFWSKgqlKALFLEHEGYFGAVGALLE 542
Cdd:TIGR00555 265 MKVLSYATNFWSK---KALFLEHEGYSGAIGALLS 296
PLN02920 PLN02920
pantothenate kinase 1
193-541 4.78e-65

pantothenate kinase 1


Pssm-ID: 215498 [Multi-domain]  Cd Length: 398  Bit Score: 217.02  E-value: 4.78e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466 193 MDIGGTLVKLVYFEPKDitaeeeqeevENLKSIRKYLTSNTAYGKTGIRDVHLELKNLTMCgrkgnLHFIRFPTCAMHMF 272
Cdd:PLN02920  23 LDIGGSLIKLVYFSRNS----------GDSEDPRNDSSVKSDGVNGRLHFAKFETRKINDC-----LEFISSNKLHHGGF 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466 273 IQM---GSEKNFsslhttLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGllyvdsVGFNGKP---ECYYFENPtnp 346
Cdd:PLN02920  88 QHHenpTHDKNF------IKATGGGAYKFADLFKEKLGISLDKEDEMDCLVTG------ANFLLKAvhhEAFTYLDG--- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466 347 elcQKKPYCLDNP--YPMLLVNMGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALDMAAKGDSTNVD 424
Cdd:PLN02920 153 ---QKEFVQIDHNdlYPYLLVNIGSGVSMIKVDGDGKFERVSGTSVGGGTFWGLGKLLTKCKSFDELLELSHQGNNRVID 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466 425 KLVKDIYGG-DYERFGLQGSAVASSFGNMMSKEKR-ESISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLR 502
Cdd:PLN02920 230 MLVGDIYGGmDYSKIGLSSTTIASSFGKAISDNKElEDYKPEDVARSLLRMISNNIGQISYLNALRFGLKRIFFGGFFIR 309
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 564333466 503 INMVSMKLLAYAMDFWSKGQLKALFLEHEGYFGAVGALL 541
Cdd:PLN02920 310 GHSYTMDTISVAVHFWSKGEAKAMFLRHEGFLGALGAFM 348
PanK COG5146
Pantothenate kinase [Coenzyme transport and metabolism]; Pantothenate kinase is part of the ...
192-541 2.82e-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: 136.17  E-value: 2.82e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466 192 GMDIGGTLVKLVYFEpkditaeeeqeevenlksirkyltsntaygktgirdvhlelknltmcgrKGNLHFIRFPTCAMHM 271
Cdd:COG5146    5 GIDAGGTLTKIAYLE-------------------------------------------------DGERRYKKFPSDEIES 35
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466 272 FIQ-MGSEKNFSslhtTLCATGGGAFKFEEdfrMIADLQLHKLDELDCLIQGllyvdsVGFNGKPECYYFENptnpelcq 350
Cdd:COG5146   36 VADwLNKFINIE----KIGLTGGRAEVLAE---KLNGDPKQYIVEFDATGKG------VRYLLKEEGHDIDK-------- 94
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466 351 kkpycldnpypMLLVNMGSGVSIlaVYSKDN-YKRVTGTSLGGGTFLGLCCLLTGCETFEEALDMAAKGDSTNVDKLVKD 429
Cdd:COG5146   95 -----------FIITNVGTGTSI--HYMDGDtQERVGGTGVGGGTLMGLSYLLTGISDFEEIVELAKKGDRDGIDLKVKD 161
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466 430 IYGGDYErfGLQGSAVASSFGNMMSKEKrESISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINmvsmK 509
Cdd:COG5146  162 IYEGMEP--PIPGDLTASNFGKVLITLD-ESATKEDILAAIIGLVGETITTLSIQAAEEYDTETIVYIGSTLTNN----P 234
                        330       340       350
                 ....*....|....*....|....*....|....
gi 564333466 510 LLAYAMDFWS--KGqLKALFLEHEGYFGAVGALL 541
Cdd:COG5146  235 LLQEVIESYTilRG-KKPIFLENGEFSGAIGALL 267
PHA03321 PHA03321
tegument protein VP11/12; Provisional
7-102 2.74e-03

tegument protein VP11/12; Provisional


Pssm-ID: 223041 [Multi-domain]  Cd Length: 694  Bit Score: 40.71  E-value: 2.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466   7 PRPGSAEVPAAARDAETLRAGAASPARRAQLAEDVGTPTGGGEERRGRQPPAAA---RRLRESKPQGGSEDRRTADrdlQ 83
Cdd:PHA03321 446 PRARPGSTPACARRARAQRARDAGPEYVDPLGALRRLPAGAAPPPEPAAAPSPAtyyTRMGGGPPRLPPRNRATET---L 522
                         90
                 ....*....|....*....
gi 564333466  84 RGCLsRSPRTAPPvPGMGD 102
Cdd:PHA03321 523 RPDW-GPPAAAPP-EQMED 539
 
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 ...
190-541 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: 756.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466 190 WFGMDIGGTLVKLVYFEPKDITAEEEQEEVENLKSIRKYLTSNTAYGKTGIRDVHLELKNLTMCGRKGNLHFIRFPTCAM 269
Cdd:cd24135    1 WFGMDIGGTLVKLVYFEPKDITAEEEQEEVENLKSIRKYLTSNTAYGKTGIRDVHLELKNLTMCGRKGNLHFIRFPSCAM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466 270 HMFIQMGSEKNFSSLHTTLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSVGFNGKPECYYFENPTNPELC 349
Cdd:cd24135   81 HRFIQMGSEKNFSSLHTTLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSVGFNGQPECYYFENPTDPEQC 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466 350 QKKPYCLDNPYPMLLVNMGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALDMAAKGDSTNVDKLVKD 429
Cdd:cd24135  161 QKKPYCLDNPYPMLLVNIGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALEMAAKGDSTNVDKLVKD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466 430 IYGGDYERFGLQGSAVASSFGNMMSKEKRESISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINMVSMK 509
Cdd:cd24135  241 IYGGDYERFGLQGSAVASSFGHMMSKEKRDSISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINMVSMK 320
                        330       340       350
                 ....*....|....*....|....*....|..
gi 564333466 510 LLAYAMDFWSKGQLKALFLEHEGYFGAVGALL 541
Cdd:cd24135  321 LLAYAMDFWSKGQLKALFLEHEGYFGAVGALL 352
ASKHA_NBD_PanK-II_Pank2 cd24136
nucleotide-binding domain (NBD) of pantothenate kinase 2 (Pank2) from type II pantothenate ...
190-543 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: 658.99  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466 190 WFGMDIGGTLVKLVYFEPKDITAEEEQEEVENLKSIRKYLTSNTAYGKTGIRDVHLELKNLTMCGRKGNLHFIRFPTCAM 269
Cdd:cd24136    1 WFGLDIGGTLVKLVYFEPKDITAEEEEEEVENLKSIRKYLTSNVAYGSTGIRDVHLELKDLTLCGRKGNLHFIRFPTHDM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466 270 HMFIQMGSEKNFSSLHTTLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSVGFNGKPECYYFENPTNPELC 349
Cdd:cd24136   81 PAFIQMGRDKHFSSLHTTLCATGGGAYKFEQDFLTMGDLQLCKLDELDCLIKGVLYIDSVGFNGHSECYYFENPTDSEKC 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466 350 QKKPYCLDNPYPMLLVNMGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALDMAAKGDSTNVDKLVKD 429
Cdd:cd24136  161 QKLPFNLKNPYPLLLVNIGSGVSILAVYSKDNYKRVTGTSLGGGTFFGLCCLLTGCTTFEEALEMASRGDSTKVDKLVRD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466 430 IYGGDYERFGLQGSAVASSFGNMMSKEKRESISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINMVSMK 509
Cdd:cd24136  241 IYGGDYERFGLPGWAVASSFGNMMSKEKREAVSKEDLARATLITITNNIGSIARMCALNENINRVVFVGNFLRINTISMR 320
                        330       340       350
                 ....*....|....*....|....*....|....
gi 564333466 510 LLAYAMDFWSKGQLKALFLEHEGYFGAVGALLEL 543
Cdd:cd24136  321 LLAYALDYWSKGQLKALFLEHEGYFGAVGALLEL 354
ASKHA_NBD_PanK-II_Pank3 cd24137
nucleotide-binding domain (NBD) of pantothenate kinase 3 (Pank3) from type II pantothenate ...
190-541 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: 586.20  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466 190 WFGMDIGGTLVKLVYFEPKDITAEEEQEEVENLKSIRKYLTSNTAYGKTGIRDVHLELKNLTMCGRKGNLHFIRFPTCAM 269
Cdd:cd24137    1 WFGMDIGGTLVKLSYFEPIDITAEEEQEEVESLKSIRKYLTSNVAYGSTGIRDVHLELKDLTLFGRRGNLHFIRFPTQDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466 270 HMFIQMGSEKNFSSLHTTLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSVGFNGKPECYYFENPTNPELC 349
Cdd:cd24137   81 PTFIQMGRDKNFSTLQTVLCATGGGAYKFEKDFRTIGNLHLHKLDELDCLVKGLLYIDSVSFNGQAECYYFANASEPERC 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466 350 QKKPYCLDNPYPMLLVNMGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALDMAAKGDSTNVDKLVKD 429
Cdd:cd24137  161 QKMPFNLDDPYPLLVVNIGSGVSILAVHSKDNYKRVTGTSLGGGTFLGLCSLLTGCESFEEALEMASKGDSTQADKLVRD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466 430 IYGGDYERFGLQGSAVASSFGNMMSKEKRESISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINMVSMK 509
Cdd:cd24137  241 IYGGDYERFGLPGWAVASSFGNMIYKEKRESVSKEDLARATLVTITNNIGSVARMCAVNEKINRVVFVGNFLRVNTLSMK 320
                        330       340       350
                 ....*....|....*....|....*....|..
gi 564333466 510 LLAYAMDFWSKGQLKALFLEHEGYFGAVGALL 541
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 ...
190-541 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: 581.02  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466 190 WFGMDIGGTLVKLVYFEPKditaeeeqeevenlksirkyltsntaygktgirdvhlelknltmcgrkGNLHFIRFPTCAM 269
Cdd:cd24122    1 WFGLDIGGTLVKLVYFEPT------------------------------------------------GTLHFIRFETSRM 32
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466 270 HMFIQMGSEKNFSSLHTTLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSvgfNGKPECYYFENPTNPELC 349
Cdd:cd24122   33 EGFIQLAREKNLSSLIKTVCATGGGAYKFEKLFREELGLQLHKLDELDCLIRGINFLLR---HVPDECYYFENPSDPELC 109
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466 350 QK--KPYCLDNPYPMLLVNMGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALDMAAKGDSTNVDKLV 427
Cdd:cd24122  110 EKrvVPFDFSDPYPYLLVNIGSGVSILAVESPDNYERVSGTSLGGGTFLGLCCLLTGCETFEEALELAAKGDSTKVDMLV 189
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466 428 KDIYGGDYERFGLQGSAVASSFGNMMSKEKRESISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINMVS 507
Cdd:cd24122  190 GDIYGGDYEKFGLPGDTVASSFGKMVAKEKRESASKEDLARALLVMITNNIGSIARLCAKNEGIKRVVFVGNFLRHNPIA 269
                        330       340       350
                 ....*....|....*....|....*....|....
gi 564333466 508 MKLLAYAMDFWSKGQLKALFLEHEGYFGAVGALL 541
Cdd:cd24122  270 MRLLAYAMDYWSKGEMKALFLEHEGYFGALGALL 303
ASKHA_NBD_PanK-II cd24016
nucleotide-binding domain (NBD) of type II pantothenate kinase (PanK-II) and similar proteins; ...
190-541 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: 533.38  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466 190 WFGMDIGGTLVKLVYFepkditaeeeqeevenlksirkyltsntaygktgirdvhlelknltmcgrkgnLHFIRFPTCAM 269
Cdd:cd24016    1 WFGIDIGGTLVKLVYF-----------------------------------------------------LHFIRFPTDQV 27
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466 270 HMFIQMGSEKNFSSLHTTLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSVGFNGKPECYYFENPTNPELC 349
Cdd:cd24016   28 VEFIQMGQDKNFSTLITKLCATGGGAGKFEEDFRTIGNLPLQKLDELDCLSQGLLYLDSVQFNGQAECYYFANASEPERC 107
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466 350 QKKPYCLDNPYPMLLVNMGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALDMAAKGDSTNVDKLVKD 429
Cdd:cd24016  108 QKMPFNLHDPYPYLFVNVGSGVSILAVDSKDNYKRVTGTSLGGGTFQGLCYLLTGCTDFEEALEMAQHGDSTTIDKLVRD 187
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466 430 IYGGDYERFGLQGSAVASSFGNMMSKEKRESISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINMVSMK 509
Cdd:cd24016  188 IYGGDYERFGLPGDAVASSFGNMLHKEKRADFSKEDLARATLGTITNNIGSMARMCARNEKIENVVFVGNFLRNNALLMK 267
                        330       340       350
                 ....*....|....*....|....*....|..
gi 564333466 510 LLAYAMDFWSKGQLKALFLEHEGYFGAVGALL 541
Cdd:cd24016  268 LLAYATDLWSKGQLKALFVEHEGYFGAVGALL 299
Fumble pfam03630
Fumble; Fumble is required for cell division in Drosophila. Mutants lacking fumble exhibit ...
191-539 2.90e-167

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: 476.60  E-value: 2.90e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466  191 FGMDIGGTLVKLVYFEPKDITAEEEQeevenlksirkyltsntaygktgirdvhlelknltmcgrkGNLHFIRFPTCAMH 270
Cdd:pfam03630   1 FAIDIGGTLAKLVYFSPVPDSPKELG----------------------------------------GRLHFIKFETTKIE 40
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466  271 MFIQMGSEKNFSSLHT----TLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSvgfNGKPECYYFENPtnp 346
Cdd:pfam03630  41 DCLEFIKSLGLNSKGTdrglTVKATGGGAYKFYDLFKEKLGVKVDKEDEMECLIKGLNFLLT---NIPDEVFTYSDS--- 114
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466  347 elCQKKPYCLDN--PYPMLLVNMGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALDMAAKGDSTNVD 424
Cdd:pfam03630 115 --PEYFFQTVDNnsIYPYLLVNIGSGVSILKVEGPDKFERVGGTSLGGGTFWGLCSLLTGAKSFDEMLELAEKGDNRNVD 192
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466  425 KLVKDIYGGDYERFGLQGSAVASSFGNMMSKEKRESISK----EDLARATLVTITNNIGSIARMCALNENIDRVVFVGNF 500
Cdd:pfam03630 193 MLVGDIYGGDYEKIGLKSDTIASSFGKVFRKKFRESASNdaspEDIARSLLYMISNNIGQIAYLNAKLHGLKRIYFGGNF 272
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 564333466  501 LRINMVSMKLLAYAMDFWSKGQLKALFLEHEGYFGAVGA 539
Cdd:pfam03630 273 IRGHPITMKTLSYAINFWSKGELKALFLRHEGYLGALGA 311
panK_eukar TIGR00555
pantothenate kinase, eukaryotic/staphyloccocal type; This model describes a eukaryotic form of ...
189-542 5.78e-146

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: 421.81  E-value: 5.78e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466  189 PWFGMDIGGTLVKLVYFEPKditaeeeqeevenlkSIRKYLTSNTaygktgirdvhlelknltmcgrkGNLH-FIRFPTC 267
Cdd:TIGR00555   1 SRIGIDIGGTLIKVVYEEKK---------------GRRKFKTFET-----------------------TNIDkFIEWLKN 42
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466  268 AMHMFiqmgseknfsSLHTTLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSVGFNGKPECYYFEnptnpe 347
Cdd:TIGR00555  43 QIHRH----------SRITTLCATGGGAFKFAELIYESAGIQLHKFDEFDALIQGLNYLLKEEPKEKFTYYDFE------ 106
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466  348 lCQKKPYCLDNPYPMLLVNMGSGVSILAVYSkDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALDMAAKGDSTNVDKLV 427
Cdd:TIGR00555 107 -CQKKPIDLDDIYPYLLVNIGTGTSILYVDG-DNYERVGGTSLGGGTFLGLGKLLTGIQTFDELLEMAQHGDRTNVDLLV 184
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466  428 KDIYGGDYERFGLQGSAVASSFGNMMSKEKRESISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINMVS 507
Cdd:TIGR00555 185 GDIYGGDYSESGLDGSLTASSFGKVLSKHLDQSFSPEDIAASLLGLIGNNIGQIAYLCALRYNIDRIVFIGSFLRNNQLL 264
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 564333466  508 MKLLAYAMDFWSKgqlKALFLEHEGYFGAVGALLE 542
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 ...
190-541 1.30e-145

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: 422.07  E-value: 1.30e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466 190 WFGMDIGGTLVKLVYFEPKDITAEEEqeevenlksirkyltsntaygktgirDVHLELKNLTMCGRKGNLHFIRFPTCAM 269
Cdd:cd24086    1 RLGLDIGGTLAKLAYLTPIDIDEAEE--------------------------KESVLLKLLANSGEDGELHFISFPNKDL 54
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466 270 HMFIQMGSEKNF--SSLHTTLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSVGFngKPECYYFENPTNPE 347
Cdd:cd24086   55 EEFLNFLRDKNFedSSKGKVLYATGGGAYKYAELIEETLGVQLVKVDEMDSLVNGLHFLLSVLS--KDECFPFPNDSGPE 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466 348 LCQKKPYCLDNPYPMLLVNMGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALDMAAKGDSTNVDKLV 427
Cdd:cd24086  133 FLQKDPQLSDDLFPCLLVNIGSGVSILKVDSDGKYERVSGTSLGGGTFLGLASLLTGTNSFDELLELASRGDRANVDLLV 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466 428 KDIYGGDYERFGLQGSAVASSFGNMMSKEK-RESISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINMV 506
Cdd:cd24086  213 RDIYGGDYPYLGLPGDLLASSFGKLADDEKsREDFSKEDIARSLLRMIVNNIGYLAYLVAKLHNVKRVFFTGNFIRNNEL 292
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 564333466 507 SMKLLAYAMDFWSKGQLKALFLEHEGYFGAVGALL 541
Cdd:cd24086  293 ARKLIAEALNYWSKGSLNALFLRHDGYLGALGALL 327
ASKHA_NBD_PanK-II_Pank4 cd24123
nucleotide-binding domain (NBD) of pantothenate kinase 4 (Pank4) from type II pantothenate ...
191-541 1.54e-111

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: 335.30  E-value: 1.54e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466 191 FGMDIGGTLVKLVYFEPKDitaeeeqeevenlKSIRKYLTSNTAYGKTGIRDVHLELKNLTMCGRkgnLHFIRFPTCAMH 270
Cdd:cd24123    2 FAIDIGGSLAKLVYFSRVS-------------DKAASVSSSSGTSKGPSDEPLYEVSEQPELGGR---LHFVKFETKYIE 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466 271 MFIQMGSEKNFSSLHTTLC-----ATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSvgfNGKPECYYFENPTN 345
Cdd:cd24123   66 ECLDFIKDNLLHSRQGNKRgkvikATGGGAYKYADLIKEKLGVEVDKEDEMECLIKGCNFLLK---NIPDEVFTYDEHAK 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466 346 PELcqKKPYCLDNPYPMLLVNMGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALDMAAKGDSTNVDK 425
Cdd:cd24123  143 PEV--KFQSDPPDIFPYLLVNIGSGVSILKVDSEDKFERVGGTSLGGGTFWGLGSLLTGAKSFDELLELAEKGDNRNVDM 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466 426 LVKDIYGGDYERFGLQGSAVASSFGNMMSKEK---RESISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLR 502
Cdd:cd24123  221 LVGDIYGGDYSKIGLKSDTIASSFGKVARADKdarLEDFSPEDIAKSLLRMISNNIGQIAYLNAKLHGLKRIYFGGFFIR 300
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 564333466 503 INMVSMKLLAYAMDFWSKGQLKALFLEHEGYFGAVGALL 541
Cdd:cd24123  301 GHPLTMHTISYAINFWSKGEMQALFLRHEGYLGAIGAFL 339
PLN02920 PLN02920
pantothenate kinase 1
193-541 4.78e-65

pantothenate kinase 1


Pssm-ID: 215498 [Multi-domain]  Cd Length: 398  Bit Score: 217.02  E-value: 4.78e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466 193 MDIGGTLVKLVYFEPKDitaeeeqeevENLKSIRKYLTSNTAYGKTGIRDVHLELKNLTMCgrkgnLHFIRFPTCAMHMF 272
Cdd:PLN02920  23 LDIGGSLIKLVYFSRNS----------GDSEDPRNDSSVKSDGVNGRLHFAKFETRKINDC-----LEFISSNKLHHGGF 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466 273 IQM---GSEKNFsslhttLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGllyvdsVGFNGKP---ECYYFENPtnp 346
Cdd:PLN02920  88 QHHenpTHDKNF------IKATGGGAYKFADLFKEKLGISLDKEDEMDCLVTG------ANFLLKAvhhEAFTYLDG--- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466 347 elcQKKPYCLDNP--YPMLLVNMGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALDMAAKGDSTNVD 424
Cdd:PLN02920 153 ---QKEFVQIDHNdlYPYLLVNIGSGVSMIKVDGDGKFERVSGTSVGGGTFWGLGKLLTKCKSFDELLELSHQGNNRVID 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466 425 KLVKDIYGG-DYERFGLQGSAVASSFGNMMSKEKR-ESISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLR 502
Cdd:PLN02920 230 MLVGDIYGGmDYSKIGLSSTTIASSFGKAISDNKElEDYKPEDVARSLLRMISNNIGQISYLNALRFGLKRIFFGGFFIR 309
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 564333466 503 INMVSMKLLAYAMDFWSKGQLKALFLEHEGYFGAVGALL 541
Cdd:PLN02920 310 GHSYTMDTISVAVHFWSKGEAKAMFLRHEGFLGALGAFM 348
PLN02902 PLN02902
pantothenate kinase
191-541 7.22e-60

pantothenate kinase


Pssm-ID: 215489 [Multi-domain]  Cd Length: 876  Bit Score: 212.83  E-value: 7.22e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466 191 FGMDIGGTLVKLVYFEPKDitaeEEQEEVENLKSIRKYLtsntaygktGIRDVHLelKNLTMCGrkGNLHFIRFPTCAMH 270
Cdd:PLN02902  56 LALDIGGSLIKLVYFSRHE----DRSTDDKRKRTIKERL---------GITNGNR--RSYPILG--GRLHFVKFETSKIN 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466 271 MFIQMGSEKNF-------------SSLHTTLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLlyvdsvgfNGKPEC 337
Cdd:PLN02902 119 ECLDFISSKQLhrggihswlskapPNGNGVIKATGGGAYKFADLFKERLGVSLDKEDEMDCLVAGA--------NFLLKA 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466 338 YYFENPTNPElCQKKPYCLD--NPYPMLLVNMGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALDMA 415
Cdd:PLN02902 191 IRHEAFTHME-GEKEFVQIDqnDLFPYLLVNIGSGVSMIKVDGDGKFERVSGTNVGGGTYWGLGRLLTKCKSFDELLELS 269
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466 416 AKGDSTNVDKLVKDIYGG-DYERFGLQGSAVASSFGNMMSKEKR-ESISKEDLARATLVTITNNIGSIARMCALNENIDR 493
Cdd:PLN02902 270 QRGDNSAIDMLVGDIYGGmDYSKIGLSASTIASSFGKVISENKElSDYRPEDISLSLLRMISYNIGQISYLNALRFGLKR 349
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 564333466 494 VVFVGNFLRINMVSMKLLAYAMDFWSKGQLKALFLEHEGYFGAVGALL 541
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 ...
192-541 4.36e-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: 181.23  E-value: 4.36e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466 192 GMDIGGTLVKLVYFEpkditaeeeqeevenlksirkyltsntaygktgirdvhlelknltmcgRKGNLHFIRFPTCAMHM 271
Cdd:cd24085    3 GIDAGGTLTKIVLLE------------------------------------------------NNGELKFKAFDSLKIEA 34
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466 272 ---FIQMGSEKNFSslhtTLCATGGGAFKFEEDfrmIADLQLHKLDELDCLIQGLLYVdsVGFNGKPecyyfenptnpel 348
Cdd:cd24085   35 lvkFLNELGINDIE----KIAVTGGGASRLPEN---IDGIPIVKVDEFEAIGRGALYL--LGEILDD------------- 92
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466 349 cqkkpycldnpypMLLVNMGSGVSILAVySKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALDMAAKGDSTNVDKLVK 428
Cdd:cd24085   93 -------------ALVVSIGTGTSIVLA-KNGTIRHVGGTGVGGGTLLGLGKLLLGVTDYDEITELARKGDRSNVDLTVG 158
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466 429 DIYGGDYErfGLQGSAVASSFGNMmskEKRESISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRiNMVSM 508
Cdd:cd24085  159 DIYGGGIG--PLPPDLTASNFGKL---ADDNKASREDLAAALINLVGETIGTLAALAARAEGVKDIVLVGSTLR-NPLLK 232
                        330       340       350
                 ....*....|....*....|....*....|...
gi 564333466 509 KLLAYAMDFwskGQLKALFLEHEGYFGAVGALL 541
Cdd:cd24085  233 EVLERYTKL---YGVKPIFPENGEFAGAIGALL 262
PRK13317 PRK13317
pantothenate kinase; Provisional
192-545 4.62e-37

pantothenate kinase; Provisional


Pssm-ID: 237346 [Multi-domain]  Cd Length: 277  Bit Score: 138.55  E-value: 4.62e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466 192 GMDIGGTLVKLVYFEPKditaeeeqeeveNLKSIRKYLTSNtaygktgIRDVHLELKNLTMCGRkgnlhfirfptcamhm 271
Cdd:PRK13317   6 GIDAGGTLTKIVYLEEK------------KQRTFKTEYSAE-------GKKVIDWLINLQDIEK---------------- 50
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466 272 fiqmgseknfsslhttLCATGGGAFKFEEdfRMIADLQLHKLDELDCLIQGLLYvdsvgfngkpecyyfenptnpeLCQK 351
Cdd:PRK13317  51 ----------------ICLTGGKAGYLQQ--LLNYGYPIAEFVEFEATGLGVRY----------------------LLKE 90
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466 352 KPYCLDNpypMLLVNMGSGVSILAVYSKDnYKRVTGTSLGGGTFLGLCCLLTGCETFEEALDMAAKGDSTNVDKLVKDIY 431
Cdd:PRK13317  91 EGHDLND---YIFTNIGTGTSIHYVDGNS-QRRVGGTGIGGGTIQGLSKLLTNISDYEQLIELAKHGDRNNIDLKVGDIY 166
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466 432 GGDYErfGLQGSAVASSFGNMMSKEKRESiSKEDLArATLVTITNN-IGSIARMCALNENIDRVVFVGNflriNMVSMKL 510
Cdd:PRK13317 167 KGPLP--PIPGDLTASNFGKVLHHLDSEF-TSSDIL-AGVIGLVGEvITTLSIQAAREKNIENIVYIGS----TLTNNPL 238
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 564333466 511 LAYAMDFWSKGQ-LKALFLEHEGYFGAVGALLELFK 545
Cdd:PRK13317 239 LQEIIESYTKLRnCTPIFLENGGYSGAIGALLLATN 274
PanK COG5146
Pantothenate kinase [Coenzyme transport and metabolism]; Pantothenate kinase is part of the ...
192-541 2.82e-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: 136.17  E-value: 2.82e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466 192 GMDIGGTLVKLVYFEpkditaeeeqeevenlksirkyltsntaygktgirdvhlelknltmcgrKGNLHFIRFPTCAMHM 271
Cdd:COG5146    5 GIDAGGTLTKIAYLE-------------------------------------------------DGERRYKKFPSDEIES 35
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466 272 FIQ-MGSEKNFSslhtTLCATGGGAFKFEEdfrMIADLQLHKLDELDCLIQGllyvdsVGFNGKPECYYFENptnpelcq 350
Cdd:COG5146   36 VADwLNKFINIE----KIGLTGGRAEVLAE---KLNGDPKQYIVEFDATGKG------VRYLLKEEGHDIDK-------- 94
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466 351 kkpycldnpypMLLVNMGSGVSIlaVYSKDN-YKRVTGTSLGGGTFLGLCCLLTGCETFEEALDMAAKGDSTNVDKLVKD 429
Cdd:COG5146   95 -----------FIITNVGTGTSI--HYMDGDtQERVGGTGVGGGTLMGLSYLLTGISDFEEIVELAKKGDRDGIDLKVKD 161
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466 430 IYGGDYErfGLQGSAVASSFGNMMSKEKrESISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINmvsmK 509
Cdd:COG5146  162 IYEGMEP--PIPGDLTASNFGKVLITLD-ESATKEDILAAIIGLVGETITTLSIQAAEEYDTETIVYIGSTLTNN----P 234
                        330       340       350
                 ....*....|....*....|....*....|....
gi 564333466 510 LLAYAMDFWS--KGqLKALFLEHEGYFGAVGALL 541
Cdd:COG5146  235 LLQEVIESYTilRG-KKPIFLENGEFSGAIGALL 267
PTZ00297 PTZ00297
pantothenate kinase; Provisional
193-539 1.13e-34

pantothenate kinase; Provisional


Pssm-ID: 140318 [Multi-domain]  Cd Length: 1452  Bit Score: 139.99  E-value: 1.13e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466  193 MDIGGTLVKLVYFEPKDITAeeeqeevenlksIRKYLT--SNTAYGKTGIRDVHL--------ELKNLTMCGRKGNLHFI 262
Cdd:PTZ00297 1044 IDIGGTFAKIAYVQPPGGFA------------FPTYIVheASSLSEKLGLRTFHFfadaeaaeSELRTRPHSRVGTLRFA 1111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466  263 RFPTCAMHMFIQMGSE----KNFSSLHTT-LCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSVGfngkPEC 337
Cdd:PTZ00297 1112 KIPSKQIPDFADYLAGshaiNYYKPQYRTkVRATGGGAFKYASVAKKVLGINFSVMREMDAVVKGLNLVIRVA----PES 1187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466  338 YYFENPTN----PELCQKKPYCLDNPYPMLLVNMGSGVSILAVYSKD-NYKRVTGTSLGGGTFLGLCCLLTGCETFEEAL 412
Cdd:PTZ00297 1188 IFTVDPSTgvhhPHQLVSPPGDGFSPFPCLLVNIGSGISIIKCLGPDgSHVRVGGSPIGGATFWGLVRTMTNVTSWEEVM 1267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466  413 D---MAAKGDSTNVDKLVKDIYGGDYERFG--LQGSAVASSFGNM----------------------------MSKEKRE 459
Cdd:PTZ00297 1268 EimrLDGPGDNKNVDLLVGDIYGYNAKDLPamLSVDTVASTFGKLgterfyemmrgvstahfsdddaageilsPKALKSP 1347
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466  460 SISKE-------------DLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINMVSMKLLAYAMDFWSKGQLKAL 526
Cdd:PTZ00297 1348 TVISElpvrngtkkasaiDIVRSLLNMISSNVTQLAYLHSRVQGVPNIFFAGGFVRDNPIIWSHISSTMKYWSKGECHAH 1427
                         410
                  ....*....|...
gi 564333466  527 FLEHEGYFGAVGA 539
Cdd:PTZ00297 1428 FLEHDGYLGALGC 1440
PHA03321 PHA03321
tegument protein VP11/12; Provisional
7-102 2.74e-03

tegument protein VP11/12; Provisional


Pssm-ID: 223041 [Multi-domain]  Cd Length: 694  Bit Score: 40.71  E-value: 2.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466   7 PRPGSAEVPAAARDAETLRAGAASPARRAQLAEDVGTPTGGGEERRGRQPPAAA---RRLRESKPQGGSEDRRTADrdlQ 83
Cdd:PHA03321 446 PRARPGSTPACARRARAQRARDAGPEYVDPLGALRRLPAGAAPPPEPAAAPSPAtyyTRMGGGPPRLPPRNRATET---L 522
                         90
                 ....*....|....*....
gi 564333466  84 RGCLsRSPRTAPPvPGMGD 102
Cdd:PHA03321 523 RPDW-GPPAAAPP-EQMED 539
PHA03378 PHA03378
EBNA-3B; Provisional
4-105 3.51e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 40.44  E-value: 3.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466   4 RRAPRPGSAEVPAAARDAETLRAGAASPARRAQLAEDVGTPTGGGEERR-------GRQPPAAARRLRESKPQGGSEDRR 76
Cdd:PHA03378 686 PIQWAPGTMQPPPRAPTPMRPPAAPPGRAQRPAAATGRARPPAAAPGRArppaaapGRARPPAAAPGRARPPAAAPGRAR 765
                         90       100
                 ....*....|....*....|....*....
gi 564333466  77 TADRDLQRGCLSRSPRtAPPVPGMGDRGA 105
Cdd:PHA03378 766 PPAAAPGAPTPQPPPQ-APPAPQQRPRGA 793
PHA03381 PHA03381
tegument protein VP22; Provisional
1-108 9.90e-03

tegument protein VP22; Provisional


Pssm-ID: 177618 [Multi-domain]  Cd Length: 290  Bit Score: 38.07  E-value: 9.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333466   1 MRGRRAPRP---GSAEVPAAARdaETLRAGAASPARrAQLAEDVGTPTGGGEERRGRqpPAAARRLRESKPQ-------- 69
Cdd:PHA03381   1 MASRRSPRPkphGTDEVEADVY--YDFISPDASPAR-VSFEEPADRARRGAGQARGR--SQAERRFHHYDEAradypyyt 75
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 564333466  70 -GGSEDRRTADRDLQRGCLSR-------SPRTAPPVPGMGDRGAQHE 108
Cdd:PHA03381  76 gSSSEDERPADPRPSRRPHAQpeasgpgPARGARGPAGSRGRGRRAE 122
 
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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