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Conserved domains on  [gi|386771479|ref|NP_001246848|]
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fumble, isoform G [Drosophila melanogaster]

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-like cd24122
nucleotide-binding domain (NBD) of the pantothenate kinase 1 (Pank1)-like subfamily; PanK (EC ...
30-378 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: 561.76  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479  30 WFGMDIGGTLTKLVYFEPKditpdeqdreagilrnirryltknsaygktghrdthlqmdnveirkrrGSLHFIRFQTTDM 109
Cdd:cd24122    1 WFGLDIGGTLVKLVYFEPT------------------------------------------------GTLHFIRFETSRM 32
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479 110 GNFLSLAKQKGMAELVTTVCATGGGAFKFEQDFRDQVNMKLAKFDELDTLIKGILFADLHNRTECYYYENARDILKSEK- 188
Cdd:cd24122   33 EGFIQLAREKNLSSLIKTVCATGGGAYKFEKLFREELGLQLHKLDELDCLIRGINFLLRHVPDECYYFENPSDPELCEKr 112
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479 189 -QQFNFSQPFPFILVNVGSGVSILAVYGPDNYKRISGTSLGGGTFLGLCCLLTGCTSFEEAIQLATKGDNRKVDKLVKDI 267
Cdd:cd24122  113 vVPFDFSDPYPYLLVNIGSGVSILAVESPDNYERVSGTSLGGGTFLGLCCLLTGCETFEEALELAAKGDSTKVDMLVGDI 192
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479 268 YGGDYNRFGLPGDLVASSFGQMHLNDKRVSVSREDLANATLVTITNNIGSIARMCALNEKIDRVVFVGNFLRVNPISMKL 347
Cdd:cd24122  193 YGGDYEKFGLPGDTVASSFGKMVAKEKRESASKEDLARALLVMITNNIGSIARLCAKNEGIKRVVFVGNFLRHNPIAMRL 272
                        330       340       350
                 ....*....|....*....|....*....|.
gi 386771479 348 LAYAMEFWSNGTMKGLFLEHEGYFGALGCLL 378
Cdd:cd24122  273 LAYAMDYWSKGEMKALFLEHEGYFGALGALL 303
 
Name Accession Description Interval E-value
ASKHA_NBD_PanK-II_Pank1-like cd24122
nucleotide-binding domain (NBD) of the pantothenate kinase 1 (Pank1)-like subfamily; PanK (EC ...
30-378 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: 561.76  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479  30 WFGMDIGGTLTKLVYFEPKditpdeqdreagilrnirryltknsaygktghrdthlqmdnveirkrrGSLHFIRFQTTDM 109
Cdd:cd24122    1 WFGLDIGGTLVKLVYFEPT------------------------------------------------GTLHFIRFETSRM 32
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479 110 GNFLSLAKQKGMAELVTTVCATGGGAFKFEQDFRDQVNMKLAKFDELDTLIKGILFADLHNRTECYYYENARDILKSEK- 188
Cdd:cd24122   33 EGFIQLAREKNLSSLIKTVCATGGGAYKFEKLFREELGLQLHKLDELDCLIRGINFLLRHVPDECYYFENPSDPELCEKr 112
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479 189 -QQFNFSQPFPFILVNVGSGVSILAVYGPDNYKRISGTSLGGGTFLGLCCLLTGCTSFEEAIQLATKGDNRKVDKLVKDI 267
Cdd:cd24122  113 vVPFDFSDPYPYLLVNIGSGVSILAVESPDNYERVSGTSLGGGTFLGLCCLLTGCETFEEALELAAKGDSTKVDMLVGDI 192
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479 268 YGGDYNRFGLPGDLVASSFGQMHLNDKRVSVSREDLANATLVTITNNIGSIARMCALNEKIDRVVFVGNFLRVNPISMKL 347
Cdd:cd24122  193 YGGDYEKFGLPGDTVASSFGKMVAKEKRESASKEDLARALLVMITNNIGSIARLCAKNEGIKRVVFVGNFLRHNPIAMRL 272
                        330       340       350
                 ....*....|....*....|....*....|.
gi 386771479 348 LAYAMEFWSNGTMKGLFLEHEGYFGALGCLL 378
Cdd:cd24122  273 LAYAMDYWSKGEMKALFLEHEGYFGALGALL 303
Fumble pfam03630
Fumble; Fumble is required for cell division in Drosophila. Mutants lacking fumble exhibit ...
31-376 2.32e-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: 471.98  E-value: 2.32e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479   31 FGMDIGGTLTKLVYFEPKDITPDEQDreagilrnirryltknsaygktghrdthlqmdnveirkrrGSLHFIRFQTTDMG 110
Cdd:pfam03630   1 FAIDIGGTLAKLVYFSPVPDSPKELG----------------------------------------GRLHFIKFETTKIE 40
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479  111 NFLSLAKQKGMAELVT----TVCATGGGAFKFEQDFRDQVNMKLAKFDELDTLIKGILFADLHNRTECYYYENARdilKS 186
Cdd:pfam03630  41 DCLEFIKSLGLNSKGTdrglTVKATGGGAYKFYDLFKEKLGVKVDKEDEMECLIKGLNFLLTNIPDEVFTYSDSP---EY 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479  187 EKQQFNFSQPFPFILVNVGSGVSILAVYGPDNYKRISGTSLGGGTFLGLCCLLTGCTSFEEAIQLATKGDNRKVDKLVKD 266
Cdd:pfam03630 118 FFQTVDNNSIYPYLLVNIGSGVSILKVEGPDKFERVGGTSLGGGTFWGLCSLLTGAKSFDEMLELAEKGDNRNVDMLVGD 197
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479  267 IYGGDYNRFGLPGDLVASSFGQMHLNDKRVSV----SREDLANATLVTITNNIGSIARMCALNEKIDRVVFVGNFLRVNP 342
Cdd:pfam03630 198 IYGGDYEKIGLKSDTIASSFGKVFRKKFRESAsndaSPEDIARSLLYMISNNIGQIAYLNAKLHGLKRIYFGGNFIRGHP 277
                         330       340       350
                  ....*....|....*....|....*....|....
gi 386771479  343 ISMKLLAYAMEFWSNGTMKGLFLEHEGYFGALGC 376
Cdd:pfam03630 278 ITMKTLSYAINFWSKGELKALFLRHEGYLGALGA 311
panK_eukar TIGR00555
pantothenate kinase, eukaryotic/staphyloccocal type; This model describes a eukaryotic form of ...
29-378 5.71e-110

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: 325.51  E-value: 5.71e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479   29 PWFGMDIGGTLTKLVYFEPKditpdeqdreagilrnirryltknsaygktghrdthlqmdnveirkrrGSLHFIRFQTTD 108
Cdd:TIGR00555   1 SRIGIDIGGTLIKVVYEEKK------------------------------------------------GRRKFKTFETTN 32
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479  109 MGNFLSLAK-QKGMAELVTTVCATGGGAFKFEQDFRDQVNMKLAKFDELDTLIKGILFADLHNRTECYYYENArdilKSE 187
Cdd:TIGR00555  33 IDKFIEWLKnQIHRHSRITTLCATGGGAFKFAELIYESAGIQLHKFDEFDALIQGLNYLLKEEPKEKFTYYDF----ECQ 108
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479  188 KQQFNFSQPFPFILVNVGSGVSILAVYGpDNYKRISGTSLGGGTFLGLCCLLTGCTSFEEAIQLATKGDNRKVDKLVKDI 267
Cdd:TIGR00555 109 KKPIDLDDIYPYLLVNIGTGTSILYVDG-DNYERVGGTSLGGGTFLGLGKLLTGIQTFDELLEMAQHGDRTNVDLLVGDI 187
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479  268 YGGDYNRFGLPGDLVASSFGQMHLNDKRVSVSREDLANATLVTITNNIGSIARMCALNEKIDRVVFVGNFLRVNPISMKL 347
Cdd:TIGR00555 188 YGGDYSESGLDGSLTASSFGKVLSKHLDQSFSPEDIAASLLGLIGNNIGQIAYLCALRYNIDRIVFIGSFLRNNQLLMKV 267
                         330       340       350
                  ....*....|....*....|....*....|.
gi 386771479  348 LAYAMEFWSngtMKGLFLEHEGYFGALGCLL 378
Cdd:TIGR00555 268 LSYATNFWS---KKALFLEHEGYSGAIGALL 295
PLN02902 PLN02902
pantothenate kinase
31-381 3.96e-69

pantothenate kinase


Pssm-ID: 215489 [Multi-domain]  Cd Length: 876  Bit Score: 234.79  E-value: 3.96e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479  31 FGMDIGGTLTKLVYFEPKDITPDEQDREagilRNIRRYLTKNSaygktGHRDTHLQMDnveirkrrGSLHFIRFQTTDMG 110
Cdd:PLN02902  56 LALDIGGSLIKLVYFSRHEDRSTDDKRK----RTIKERLGITN-----GNRRSYPILG--------GRLHFVKFETSKIN 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479 111 NFLSLAKQKGM-------------AELVTTVCATGGGAFKFEQDFRDQVNMKLAKFDELDTLIKGILFADLHNRTECYYY 177
Cdd:PLN02902 119 ECLDFISSKQLhrggihswlskapPNGNGVIKATGGGAYKFADLFKERLGVSLDKEDEMDCLVAGANFLLKAIRHEAFTH 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479 178 enardiLKSEKQ--QFNFSQPFPFILVNVGSGVSILAVYGPDNYKRISGTSLGGGTFLGLCCLLTGCTSFEEAIQLATKG 255
Cdd:PLN02902 199 ------MEGEKEfvQIDQNDLFPYLLVNIGSGVSMIKVDGDGKFERVSGTNVGGGTYWGLGRLLTKCKSFDELLELSQRG 272
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479 256 DNRKVDKLVKDIYGG-DYNRFGLPGDLVASSFGQMHLNDKRVSVSR-EDLANATLVTITNNIGSIARMCALNEKIDRVVF 333
Cdd:PLN02902 273 DNSAIDMLVGDIYGGmDYSKIGLSASTIASSFGKVISENKELSDYRpEDISLSLLRMISYNIGQISYLNALRFGLKRIFF 352
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 386771479 334 VGNFLRVNPISMKLLAYAMEFWSNGTMKGLFLEHEGYFGALGCLLQFN 381
Cdd:PLN02902 353 GGFFIRGHAYTMDTISFAVHFWSKGEAQAMFLRHEGFLGALGAFMSYE 400
PanK COG5146
Pantothenate kinase [Coenzyme transport and metabolism]; Pantothenate kinase is part of the ...
32-378 1.02e-40

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: 145.80  E-value: 1.02e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479  32 GMDIGGTLTKLVYFEpkditpdeqdreagilrnirryltknsaygktghrdthlqmdnveirkrRGSLHFIRFQTTDMGN 111
Cdd:COG5146    5 GIDAGGTLTKIAYLE-------------------------------------------------DGERRYKKFPSDEIES 35
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479 112 FLS-LAKQKGMAElvttVCATGGGAFKFEQDFRDqvnMKLAKFDELDTLIKGILFadlhnrtecyyyenardILKSEKQQ 190
Cdd:COG5146   36 VADwLNKFINIEK----IGLTGGRAEVLAEKLNG---DPKQYIVEFDATGKGVRY-----------------LLKEEGHD 91
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479 191 FNfsqpfPFILVNVGSGVSILAVYGpDNYKRISGTSLGGGTFLGLCCLLTGCTSFEEAIQLATKGDNRKVDKLVKDIYGG 270
Cdd:COG5146   92 ID-----KFIITNVGTGTSIHYMDG-DTQERVGGTGVGGGTLMGLSYLLTGISDFEEIVELAKKGDRDGIDLKVKDIYEG 165
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479 271 DYNrfGLPGDLVASSFGQMHLNDKRvSVSREDLANATLVTITNNIGSIARMCALNEKIDRVVFVGNFLRVNPismkLLAY 350
Cdd:COG5146  166 MEP--PIPGDLTASNFGKVLITLDE-SATKEDILAAIIGLVGETITTLSIQAAEEYDTETIVYIGSTLTNNP----LLQE 238
                        330       340       350
                 ....*....|....*....|....*....|.
gi 386771479 351 AMEFWSngTMKGL---FLEHEGYFGALGCLL 378
Cdd:COG5146  239 VIESYT--ILRGKkpiFLENGEFSGAIGALL 267
 
Name Accession Description Interval E-value
ASKHA_NBD_PanK-II_Pank1-like cd24122
nucleotide-binding domain (NBD) of the pantothenate kinase 1 (Pank1)-like subfamily; PanK (EC ...
30-378 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: 561.76  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479  30 WFGMDIGGTLTKLVYFEPKditpdeqdreagilrnirryltknsaygktghrdthlqmdnveirkrrGSLHFIRFQTTDM 109
Cdd:cd24122    1 WFGLDIGGTLVKLVYFEPT------------------------------------------------GTLHFIRFETSRM 32
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479 110 GNFLSLAKQKGMAELVTTVCATGGGAFKFEQDFRDQVNMKLAKFDELDTLIKGILFADLHNRTECYYYENARDILKSEK- 188
Cdd:cd24122   33 EGFIQLAREKNLSSLIKTVCATGGGAYKFEKLFREELGLQLHKLDELDCLIRGINFLLRHVPDECYYFENPSDPELCEKr 112
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479 189 -QQFNFSQPFPFILVNVGSGVSILAVYGPDNYKRISGTSLGGGTFLGLCCLLTGCTSFEEAIQLATKGDNRKVDKLVKDI 267
Cdd:cd24122  113 vVPFDFSDPYPYLLVNIGSGVSILAVESPDNYERVSGTSLGGGTFLGLCCLLTGCETFEEALELAAKGDSTKVDMLVGDI 192
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479 268 YGGDYNRFGLPGDLVASSFGQMHLNDKRVSVSREDLANATLVTITNNIGSIARMCALNEKIDRVVFVGNFLRVNPISMKL 347
Cdd:cd24122  193 YGGDYEKFGLPGDTVASSFGKMVAKEKRESASKEDLARALLVMITNNIGSIARLCAKNEGIKRVVFVGNFLRHNPIAMRL 272
                        330       340       350
                 ....*....|....*....|....*....|.
gi 386771479 348 LAYAMEFWSNGTMKGLFLEHEGYFGALGCLL 378
Cdd:cd24122  273 LAYAMDYWSKGEMKALFLEHEGYFGALGALL 303
ASKHA_NBD_PanK-II_Pank1 cd24135
nucleotide-binding domain (NBD) of pantothenate kinase 1 (Pank1) from type II pantothenate ...
30-378 1.36e-179

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: 504.53  E-value: 1.36e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479  30 WFGMDIGGTLTKLVYFEPKDITPDEQDREAGILRNIRRYLTKNSAYGKTGHRDTHLQMDNVEIRKRRGSLHFIRFQTTDM 109
Cdd:cd24135    1 WFGMDIGGTLVKLVYFEPKDITAEEEQEEVENLKSIRKYLTSNTAYGKTGIRDVHLELKNLTMCGRKGNLHFIRFPSCAM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479 110 GNFLSLAKQKGMAELVTTVCATGGGAFKFEQDFRDQVNMKLAKFDELDTLIKGILFAD---LHNRTECYYYENARDILKS 186
Cdd:cd24135   81 HRFIQMGSEKNFSSLHTTLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDsvgFNGQPECYYFENPTDPEQC 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479 187 EKQQFNFSQPFPFILVNVGSGVSILAVYGPDNYKRISGTSLGGGTFLGLCCLLTGCTSFEEAIQLATKGDNRKVDKLVKD 266
Cdd:cd24135  161 QKKPYCLDNPYPMLLVNIGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALEMAAKGDSTNVDKLVKD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479 267 IYGGDYNRFGLPGDLVASSFGQMHLNDKRVSVSREDLANATLVTITNNIGSIARMCALNEKIDRVVFVGNFLRVNPISMK 346
Cdd:cd24135  241 IYGGDYERFGLQGSAVASSFGHMMSKEKRDSISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINMVSMK 320
                        330       340       350
                 ....*....|....*....|....*....|..
gi 386771479 347 LLAYAMEFWSNGTMKGLFLEHEGYFGALGCLL 378
Cdd:cd24135  321 LLAYAMDFWSKGQLKALFLEHEGYFGAVGALL 352
ASKHA_NBD_PanK-II_Pank2 cd24136
nucleotide-binding domain (NBD) of pantothenate kinase 2 (Pank2) from type II pantothenate ...
30-380 3.83e-179

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: 503.76  E-value: 3.83e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479  30 WFGMDIGGTLTKLVYFEPKDITPDEQDREAGILRNIRRYLTKNSAYGKTGHRDTHLQMDNVEIRKRRGSLHFIRFQTTDM 109
Cdd:cd24136    1 WFGLDIGGTLVKLVYFEPKDITAEEEEEEVENLKSIRKYLTSNVAYGSTGIRDVHLELKDLTLCGRKGNLHFIRFPTHDM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479 110 GNFLSLAKQKGMAELVTTVCATGGGAFKFEQDFRDQVNMKLAKFDELDTLIKGILFAD---LHNRTECYYYENARDILKS 186
Cdd:cd24136   81 PAFIQMGRDKHFSSLHTTLCATGGGAYKFEQDFLTMGDLQLCKLDELDCLIKGVLYIDsvgFNGHSECYYFENPTDSEKC 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479 187 EKQQFNFSQPFPFILVNVGSGVSILAVYGPDNYKRISGTSLGGGTFLGLCCLLTGCTSFEEAIQLATKGDNRKVDKLVKD 266
Cdd:cd24136  161 QKLPFNLKNPYPLLLVNIGSGVSILAVYSKDNYKRVTGTSLGGGTFFGLCCLLTGCTTFEEALEMASRGDSTKVDKLVRD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479 267 IYGGDYNRFGLPGDLVASSFGQMHLNDKRVSVSREDLANATLVTITNNIGSIARMCALNEKIDRVVFVGNFLRVNPISMK 346
Cdd:cd24136  241 IYGGDYERFGLPGWAVASSFGNMMSKEKREAVSKEDLARATLITITNNIGSIARMCALNENINRVVFVGNFLRINTISMR 320
                        330       340       350
                 ....*....|....*....|....*....|....
gi 386771479 347 LLAYAMEFWSNGTMKGLFLEHEGYFGALGCLLQF 380
Cdd:cd24136  321 LLAYALDYWSKGQLKALFLEHEGYFGAVGALLEL 354
Fumble pfam03630
Fumble; Fumble is required for cell division in Drosophila. Mutants lacking fumble exhibit ...
31-376 2.32e-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: 471.98  E-value: 2.32e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479   31 FGMDIGGTLTKLVYFEPKDITPDEQDreagilrnirryltknsaygktghrdthlqmdnveirkrrGSLHFIRFQTTDMG 110
Cdd:pfam03630   1 FAIDIGGTLAKLVYFSPVPDSPKELG----------------------------------------GRLHFIKFETTKIE 40
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479  111 NFLSLAKQKGMAELVT----TVCATGGGAFKFEQDFRDQVNMKLAKFDELDTLIKGILFADLHNRTECYYYENARdilKS 186
Cdd:pfam03630  41 DCLEFIKSLGLNSKGTdrglTVKATGGGAYKFYDLFKEKLGVKVDKEDEMECLIKGLNFLLTNIPDEVFTYSDSP---EY 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479  187 EKQQFNFSQPFPFILVNVGSGVSILAVYGPDNYKRISGTSLGGGTFLGLCCLLTGCTSFEEAIQLATKGDNRKVDKLVKD 266
Cdd:pfam03630 118 FFQTVDNNSIYPYLLVNIGSGVSILKVEGPDKFERVGGTSLGGGTFWGLCSLLTGAKSFDEMLELAEKGDNRNVDMLVGD 197
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479  267 IYGGDYNRFGLPGDLVASSFGQMHLNDKRVSV----SREDLANATLVTITNNIGSIARMCALNEKIDRVVFVGNFLRVNP 342
Cdd:pfam03630 198 IYGGDYEKIGLKSDTIASSFGKVFRKKFRESAsndaSPEDIARSLLYMISNNIGQIAYLNAKLHGLKRIYFGGNFIRGHP 277
                         330       340       350
                  ....*....|....*....|....*....|....
gi 386771479  343 ISMKLLAYAMEFWSNGTMKGLFLEHEGYFGALGC 376
Cdd:pfam03630 278 ITMKTLSYAINFWSKGELKALFLRHEGYLGALGA 311
ASKHA_NBD_PanK-II_Pank3 cd24137
nucleotide-binding domain (NBD) of pantothenate kinase 3 (Pank3) from type II pantothenate ...
30-378 7.68e-163

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: 462.17  E-value: 7.68e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479  30 WFGMDIGGTLTKLVYFEPKDITPDEQDREAGILRNIRRYLTKNSAYGKTGHRDTHLQMDNVEIRKRRGSLHFIRFQTTDM 109
Cdd:cd24137    1 WFGMDIGGTLVKLSYFEPIDITAEEEQEEVESLKSIRKYLTSNVAYGSTGIRDVHLELKDLTLFGRRGNLHFIRFPTQDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479 110 GNFLSLAKQKGMAELVTTVCATGGGAFKFEQDFRDQVNMKLAKFDELDTLIKGILFAD---LHNRTECYYYENARDILKS 186
Cdd:cd24137   81 PTFIQMGRDKNFSTLQTVLCATGGGAYKFEKDFRTIGNLHLHKLDELDCLVKGLLYIDsvsFNGQAECYYFANASEPERC 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479 187 EKQQFNFSQPFPFILVNVGSGVSILAVYGPDNYKRISGTSLGGGTFLGLCCLLTGCTSFEEAIQLATKGDNRKVDKLVKD 266
Cdd:cd24137  161 QKMPFNLDDPYPLLVVNIGSGVSILAVHSKDNYKRVTGTSLGGGTFLGLCSLLTGCESFEEALEMASKGDSTQADKLVRD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479 267 IYGGDYNRFGLPGDLVASSFGQMHLNDKRVSVSREDLANATLVTITNNIGSIARMCALNEKIDRVVFVGNFLRVNPISMK 346
Cdd:cd24137  241 IYGGDYERFGLPGWAVASSFGNMIYKEKRESVSKEDLARATLVTITNNIGSVARMCAVNEKINRVVFVGNFLRVNTLSMK 320
                        330       340       350
                 ....*....|....*....|....*....|..
gi 386771479 347 LLAYAMEFWSNGTMKGLFLEHEGYFGALGCLL 378
Cdd:cd24137  321 LLAYALDYWSKGQLKALFLEHEGYFGAVGALL 352
ASKHA_NBD_PanK-II cd24016
nucleotide-binding domain (NBD) of type II pantothenate kinase (PanK-II) and similar proteins; ...
30-378 6.82e-134

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: 386.62  E-value: 6.82e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479  30 WFGMDIGGTLTKLVYFepkditpdeqdreagilrnirryltknsaygktghrdthlqmdnveirkrrgsLHFIRFQTTDM 109
Cdd:cd24016    1 WFGIDIGGTLVKLVYF-----------------------------------------------------LHFIRFPTDQV 27
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479 110 GNFLSLAKQKGMAELVTTVCATGGGAFKFEQDFRDQVNMKLAKFDELDTLIKGILFAD---LHNRTECYYYENARDILKS 186
Cdd:cd24016   28 VEFIQMGQDKNFSTLITKLCATGGGAGKFEEDFRTIGNLPLQKLDELDCLSQGLLYLDsvqFNGQAECYYFANASEPERC 107
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479 187 EKQQFNFSQPFPFILVNVGSGVSILAVYGPDNYKRISGTSLGGGTFLGLCCLLTGCTSFEEAIQLATKGDNRKVDKLVKD 266
Cdd:cd24016  108 QKMPFNLHDPYPYLFVNVGSGVSILAVDSKDNYKRVTGTSLGGGTFQGLCYLLTGCTDFEEALEMAQHGDSTTIDKLVRD 187
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479 267 IYGGDYNRFGLPGDLVASSFGQMHLNDKRVSVSREDLANATLVTITNNIGSIARMCALNEKIDRVVFVGNFLRVNPISMK 346
Cdd:cd24016  188 IYGGDYERFGLPGDAVASSFGNMLHKEKRADFSKEDLARATLGTITNNIGSMARMCARNEKIENVVFVGNFLRNNALLMK 267
                        330       340       350
                 ....*....|....*....|....*....|..
gi 386771479 347 LLAYAMEFWSNGTMKGLFLEHEGYFGALGCLL 378
Cdd:cd24016  268 LLAYATDLWSKGQLKALFVEHEGYFGAVGALL 299
ASKHA_NBD_PanK-II_euk cd24086
nucleotide-binding domain (NBD) of type II pantothenate kinase (PanK-II) and similar proteins ...
30-378 7.57e-126

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: 366.99  E-value: 7.57e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479  30 WFGMDIGGTLTKLVYFEPKDIT--PDEQDREAGILRNIRRYltknsaygktghrdthlqmdnveirkrrGSLHFIRFQTT 107
Cdd:cd24086    1 RLGLDIGGTLAKLAYLTPIDIDeaEEKESVLLKLLANSGED----------------------------GELHFISFPNK 52
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479 108 DMGNFLSLAKQKGMAEL--VTTVCATGGGAFKFEQDFRDQVNMKLAKFDELDTLIKGILFADLHN-RTECYYYENARDIL 184
Cdd:cd24086   53 DLEEFLNFLRDKNFEDSskGKVLYATGGGAYKYAELIEETLGVQLVKVDEMDSLVNGLHFLLSVLsKDECFPFPNDSGPE 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479 185 KSEKQQFNFSQPFPFILVNVGSGVSILAVYGPDNYKRISGTSLGGGTFLGLCCLLTGCTSFEEAIQLATKGDNRKVDKLV 264
Cdd:cd24086  133 FLQKDPQLSDDLFPCLLVNIGSGVSILKVDSDGKYERVSGTSLGGGTFLGLASLLTGTNSFDELLELASRGDRANVDLLV 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479 265 KDIYGGDYNRFGLPGDLVASSFGQM-HLNDKRVSVSREDLANATLVTITNNIGSIARMCALNEKIDRVVFVGNFLRVNPI 343
Cdd:cd24086  213 RDIYGGDYPYLGLPGDLLASSFGKLaDDEKSREDFSKEDIARSLLRMIVNNIGYLAYLVAKLHNVKRVFFTGNFIRNNEL 292
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 386771479 344 SMKLLAYAMEFWSNGTMKGLFLEHEGYFGALGCLL 378
Cdd:cd24086  293 ARKLIAEALNYWSKGSLNALFLRHDGYLGALGALL 327
ASKHA_NBD_PanK-II_Pank4 cd24123
nucleotide-binding domain (NBD) of pantothenate kinase 4 (Pank4) from type II pantothenate ...
31-378 7.33e-113

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: 334.53  E-value: 7.33e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479  31 FGMDIGGTLTKLVYFEP-KDITPDEQDREAGILRNIRRYLTKNSAYGKTGHRdthlqmdnveirkrrgsLHFIRFQTTDM 109
Cdd:cd24123    2 FAIDIGGSLAKLVYFSRvSDKAASVSSSSGTSKGPSDEPLYEVSEQPELGGR-----------------LHFVKFETKYI 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479 110 GNFLSLAKQK------GMAELVTtVCATGGGAFKFEQDFRDQVNMKLAKFDELDTLIKGILFADLHNRTECYYYEnardi 183
Cdd:cd24123   65 EECLDFIKDNllhsrqGNKRGKV-IKATGGGAYKYADLIKEKLGVEVDKEDEMECLIKGCNFLLKNIPDEVFTYD----- 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479 184 lKSEKQQFNF----SQPFPFILVNVGSGVSILAVYGPDNYKRISGTSLGGGTFLGLCCLLTGCTSFEEAIQLATKGDNRK 259
Cdd:cd24123  139 -EHAKPEVKFqsdpPDIFPYLLVNIGSGVSILKVDSEDKFERVGGTSLGGGTFWGLGSLLTGAKSFDELLELAEKGDNRN 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479 260 VDKLVKDIYGGDYNRFGLPGDLVASSFG---QMHLNDKRVSVSREDLANATLVTITNNIGSIARMCALNEKIDRVVFVGN 336
Cdd:cd24123  218 VDMLVGDIYGGDYSKIGLKSDTIASSFGkvaRADKDARLEDFSPEDIAKSLLRMISNNIGQIAYLNAKLHGLKRIYFGGF 297
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 386771479 337 FLRVNPISMKLLAYAMEFWSNGTMKGLFLEHEGYFGALGCLL 378
Cdd:cd24123  298 FIRGHPLTMHTISYAINFWSKGEMQALFLRHEGYLGAIGAFL 339
panK_eukar TIGR00555
pantothenate kinase, eukaryotic/staphyloccocal type; This model describes a eukaryotic form of ...
29-378 5.71e-110

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: 325.51  E-value: 5.71e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479   29 PWFGMDIGGTLTKLVYFEPKditpdeqdreagilrnirryltknsaygktghrdthlqmdnveirkrrGSLHFIRFQTTD 108
Cdd:TIGR00555   1 SRIGIDIGGTLIKVVYEEKK------------------------------------------------GRRKFKTFETTN 32
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479  109 MGNFLSLAK-QKGMAELVTTVCATGGGAFKFEQDFRDQVNMKLAKFDELDTLIKGILFADLHNRTECYYYENArdilKSE 187
Cdd:TIGR00555  33 IDKFIEWLKnQIHRHSRITTLCATGGGAFKFAELIYESAGIQLHKFDEFDALIQGLNYLLKEEPKEKFTYYDF----ECQ 108
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479  188 KQQFNFSQPFPFILVNVGSGVSILAVYGpDNYKRISGTSLGGGTFLGLCCLLTGCTSFEEAIQLATKGDNRKVDKLVKDI 267
Cdd:TIGR00555 109 KKPIDLDDIYPYLLVNIGTGTSILYVDG-DNYERVGGTSLGGGTFLGLGKLLTGIQTFDELLEMAQHGDRTNVDLLVGDI 187
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479  268 YGGDYNRFGLPGDLVASSFGQMHLNDKRVSVSREDLANATLVTITNNIGSIARMCALNEKIDRVVFVGNFLRVNPISMKL 347
Cdd:TIGR00555 188 YGGDYSESGLDGSLTASSFGKVLSKHLDQSFSPEDIAASLLGLIGNNIGQIAYLCALRYNIDRIVFIGSFLRNNQLLMKV 267
                         330       340       350
                  ....*....|....*....|....*....|.
gi 386771479  348 LAYAMEFWSngtMKGLFLEHEGYFGALGCLL 378
Cdd:TIGR00555 268 LSYATNFWS---KKALFLEHEGYSGAIGALL 295
PLN02902 PLN02902
pantothenate kinase
31-381 3.96e-69

pantothenate kinase


Pssm-ID: 215489 [Multi-domain]  Cd Length: 876  Bit Score: 234.79  E-value: 3.96e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479  31 FGMDIGGTLTKLVYFEPKDITPDEQDREagilRNIRRYLTKNSaygktGHRDTHLQMDnveirkrrGSLHFIRFQTTDMG 110
Cdd:PLN02902  56 LALDIGGSLIKLVYFSRHEDRSTDDKRK----RTIKERLGITN-----GNRRSYPILG--------GRLHFVKFETSKIN 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479 111 NFLSLAKQKGM-------------AELVTTVCATGGGAFKFEQDFRDQVNMKLAKFDELDTLIKGILFADLHNRTECYYY 177
Cdd:PLN02902 119 ECLDFISSKQLhrggihswlskapPNGNGVIKATGGGAYKFADLFKERLGVSLDKEDEMDCLVAGANFLLKAIRHEAFTH 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479 178 enardiLKSEKQ--QFNFSQPFPFILVNVGSGVSILAVYGPDNYKRISGTSLGGGTFLGLCCLLTGCTSFEEAIQLATKG 255
Cdd:PLN02902 199 ------MEGEKEfvQIDQNDLFPYLLVNIGSGVSMIKVDGDGKFERVSGTNVGGGTYWGLGRLLTKCKSFDELLELSQRG 272
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479 256 DNRKVDKLVKDIYGG-DYNRFGLPGDLVASSFGQMHLNDKRVSVSR-EDLANATLVTITNNIGSIARMCALNEKIDRVVF 333
Cdd:PLN02902 273 DNSAIDMLVGDIYGGmDYSKIGLSASTIASSFGKVISENKELSDYRpEDISLSLLRMISYNIGQISYLNALRFGLKRIFF 352
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 386771479 334 VGNFLRVNPISMKLLAYAMEFWSNGTMKGLFLEHEGYFGALGCLLQFN 381
Cdd:PLN02902 353 GGFFIRGHAYTMDTISFAVHFWSKGEAQAMFLRHEGFLGALGAFMSYE 400
PLN02920 PLN02920
pantothenate kinase 1
33-409 2.02e-68

pantothenate kinase 1


Pssm-ID: 215498 [Multi-domain]  Cd Length: 398  Bit Score: 222.41  E-value: 2.02e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479  33 MDIGGTLTKLVYFEPKDitPDEQDREAGILRnirrylTKNSAYGKtghrdthLQMDNVEIRKRRGSLHFIRFQTTDMGNF 112
Cdd:PLN02920  23 LDIGGSLIKLVYFSRNS--GDSEDPRNDSSV------KSDGVNGR-------LHFAKFETRKINDCLEFISSNKLHHGGF 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479 113 lslAKQKGMAELVTTVCATGGGAFKFEQDFRDQVNMKLAKFDELDTLIKGILFADLHNRTECYYYENArdilKSEKQQFN 192
Cdd:PLN02920  88 ---QHHENPTHDKNFIKATGGGAYKFADLFKEKLGISLDKEDEMDCLVTGANFLLKAVHHEAFTYLDG----QKEFVQID 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479 193 FSQPFPFILVNVGSGVSILAVYGPDNYKRISGTSLGGGTFLGLCCLLTGCTSFEEAIQLATKGDNRKVDKLVKDIYGG-D 271
Cdd:PLN02920 161 HNDLYPYLLVNIGSGVSMIKVDGDGKFERVSGTSVGGGTFWGLGKLLTKCKSFDELLELSHQGNNRVIDMLVGDIYGGmD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479 272 YNRFGLPGDLVASSFGQMHLNDKRVSVSR-EDLANATLVTITNNIGSIARMCALNEKIDRVVFVGNFLRVNPISMKLLAY 350
Cdd:PLN02920 241 YSKIGLSSTTIASSFGKAISDNKELEDYKpEDVARSLLRMISNNIGQISYLNALRFGLKRIFFGGFFIRGHSYTMDTISV 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 386771479 351 AMEFWSNGTMKGLFLEHEGYFGALGCLLQFNGElaaALNDGVEHSIHTESDSASEAAQT 409
Cdd:PLN02920 321 AVHFWSKGEAKAMFLRHEGFLGALGAFMSYEKH---SLDDLMVNQVVQLPVNASSGTDT 376
ASKHA_NBD_PanK-II_bac cd24085
nucleotide-binding domain (NBD) of type II pantothenate kinase (PanK-II) and similar proteins ...
32-378 4.92e-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: 180.46  E-value: 4.92e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479  32 GMDIGGTLTKLVYFEPKditpdeqdreagilrnirryltknsaygktghrdthlqmdnveirkrrGSLHFIRFQTTDMGN 111
Cdd:cd24085    3 GIDAGGTLTKIVLLENN------------------------------------------------GELKFKAFDSLKIEA 34
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479 112 FLSLAKQKGMAElVTTVCATGGGAFKFEQDFrdqVNMKLAKFDELDTLIKGILFadlhnrtecyyyenardILKSEKQqf 191
Cdd:cd24085   35 LVKFLNELGIND-IEKIAVTGGGASRLPENI---DGIPIVKVDEFEAIGRGALY-----------------LLGEILD-- 91
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479 192 nfsqpfPFILVNVGSGVSILAVYGpDNYKRISGTSLGGGTFLGLCCLLTGCTSFEEAIQLATKGDNRKVDKLVKDIYGGD 271
Cdd:cd24085   92 ------DALVVSIGTGTSIVLAKN-GTIRHVGGTGVGGGTLLGLGKLLLGVTDYDEITELARKGDRSNVDLTVGDIYGGG 164
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479 272 YnrFGLPGDLVASSFGQMHLNDKrvsVSREDLANATLVTITNNIGSIARMCALNEKIDRVVFVGNFLRvNPISMKLLAYA 351
Cdd:cd24085  165 I--GPLPPDLTASNFGKLADDNK---ASREDLAAALINLVGETIGTLAALAARAEGVKDIVLVGSTLR-NPLLKEVLERY 238
                        330       340
                 ....*....|....*....|....*..
gi 386771479 352 MEFwsnGTMKGLFLEHEGYFGALGCLL 378
Cdd:cd24085  239 TKL---YGVKPIFPENGEFAGAIGALL 262
PTZ00297 PTZ00297
pantothenate kinase; Provisional
33-405 1.15e-43

pantothenate kinase; Provisional


Pssm-ID: 140318 [Multi-domain]  Cd Length: 1452  Bit Score: 163.87  E-value: 1.15e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479   33 MDIGGTLTKLVYFEPK--DITPDEQDREAGILRNirryltknsaygKTGHRDTHLQMD----NVEIRKRR----GSLHFI 102
Cdd:PTZ00297 1044 IDIGGTFAKIAYVQPPggFAFPTYIVHEASSLSE------------KLGLRTFHFFADaeaaESELRTRPhsrvGTLRFA 1111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479  103 RFQTTDMGNFLS-LAKQKGMA----ELVTTVCATGGGAFKFEQDFRDQVNMKLAKFDELDTLIKGILFADLHNRTECYYY 177
Cdd:PTZ00297 1112 KIPSKQIPDFADyLAGSHAINyykpQYRTKVRATGGGAFKYASVAKKVLGINFSVMREMDAVVKGLNLVIRVAPESIFTV 1191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479  178 ENARDI-----LKSEKQQfNFSqPFPFILVNVGSGVSILAVYGPD-NYKRISGTSLGGGTFLGLCCLLTGCTSFEEAIQ- 250
Cdd:PTZ00297 1192 DPSTGVhhphqLVSPPGD-GFS-PFPCLLVNIGSGISIIKCLGPDgSHVRVGGSPIGGATFWGLVRTMTNVTSWEEVMEi 1269
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479  251 --LATKGDNRKVDKLVKDIYGgdYNRFGLPG----DLVASSFGQM---HLNDKRVSVSRE-------------------- 301
Cdd:PTZ00297 1270 mrLDGPGDNKNVDLLVGDIYG--YNAKDLPAmlsvDTVASTFGKLgteRFYEMMRGVSTAhfsdddaageilspkalksp 1347
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479  302 ------------------DLANATLVTITNNIGSIARMCALNEKIDRVVFVGNFLRVNPISMKLLAYAMEFWSNGTMKGL 363
Cdd:PTZ00297 1348 tviselpvrngtkkasaiDIVRSLLNMISSNVTQLAYLHSRVQGVPNIFFAGGFVRDNPIIWSHISSTMKYWSKGECHAH 1427
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 386771479  364 FLEHEGYFGALGCllqfngelaaALNDgvehsihTESDSASE 405
Cdd:PTZ00297 1428 FLEHDGYLGALGC----------ATLD-------PDGDAASE 1452
PanK COG5146
Pantothenate kinase [Coenzyme transport and metabolism]; Pantothenate kinase is part of the ...
32-378 1.02e-40

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: 145.80  E-value: 1.02e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479  32 GMDIGGTLTKLVYFEpkditpdeqdreagilrnirryltknsaygktghrdthlqmdnveirkrRGSLHFIRFQTTDMGN 111
Cdd:COG5146    5 GIDAGGTLTKIAYLE-------------------------------------------------DGERRYKKFPSDEIES 35
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479 112 FLS-LAKQKGMAElvttVCATGGGAFKFEQDFRDqvnMKLAKFDELDTLIKGILFadlhnrtecyyyenardILKSEKQQ 190
Cdd:COG5146   36 VADwLNKFINIEK----IGLTGGRAEVLAEKLNG---DPKQYIVEFDATGKGVRY-----------------LLKEEGHD 91
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479 191 FNfsqpfPFILVNVGSGVSILAVYGpDNYKRISGTSLGGGTFLGLCCLLTGCTSFEEAIQLATKGDNRKVDKLVKDIYGG 270
Cdd:COG5146   92 ID-----KFIITNVGTGTSIHYMDG-DTQERVGGTGVGGGTLMGLSYLLTGISDFEEIVELAKKGDRDGIDLKVKDIYEG 165
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479 271 DYNrfGLPGDLVASSFGQMHLNDKRvSVSREDLANATLVTITNNIGSIARMCALNEKIDRVVFVGNFLRVNPismkLLAY 350
Cdd:COG5146  166 MEP--PIPGDLTASNFGKVLITLDE-SATKEDILAAIIGLVGETITTLSIQAAEEYDTETIVYIGSTLTNNP----LLQE 238
                        330       340       350
                 ....*....|....*....|....*....|.
gi 386771479 351 AMEFWSngTMKGL---FLEHEGYFGALGCLL 378
Cdd:COG5146  239 VIESYT--ILRGKkpiFLENGEFSGAIGALL 267
PRK13317 PRK13317
pantothenate kinase; Provisional
32-380 2.72e-36

pantothenate kinase; Provisional


Pssm-ID: 237346 [Multi-domain]  Cd Length: 277  Bit Score: 134.31  E-value: 2.72e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479  32 GMDIGGTLTKLVYFEPKDItpdeqdreagilrnirRYLTknSAYGKTGHRDTHLQMDNVEIRKrrgslhfirfqttdmgn 111
Cdd:PRK13317   6 GIDAGGTLTKIVYLEEKKQ----------------RTFK--TEYSAEGKKVIDWLINLQDIEK----------------- 50
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479 112 flslakqkgmaelvttVCATGGGAFKFEQDFRDQVnmKLAKFDELDTLIKGILFadlhnrtecyyyenardILKSEKQQF 191
Cdd:PRK13317  51 ----------------ICLTGGKAGYLQQLLNYGY--PIAEFVEFEATGLGVRY-----------------LLKEEGHDL 95
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479 192 NfsqpfPFILVNVGSGVSILAVYGpDNYKRISGTSLGGGTFLGLCCLLTGCTSFEEAIQLATKGDNRKVDKLVKDIYGGD 271
Cdd:PRK13317  96 N-----DYIFTNIGTGTSIHYVDG-NSQRRVGGTGIGGGTIQGLSKLLTNISDYEQLIELAKHGDRNNIDLKVGDIYKGP 169
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771479 272 YNrfGLPGDLVASSFGQMhLNDKRVSVSREDLANATLVTITNNIGSIARMCALNEKIDRVVFVGNFLRVNPismkLLAYA 351
Cdd:PRK13317 170 LP--PIPGDLTASNFGKV-LHHLDSEFTSSDILAGVIGLVGEVITTLSIQAAREKNIENIVYIGSTLTNNP----LLQEI 242
                        330       340       350
                 ....*....|....*....|....*....|..
gi 386771479 352 MEFWSNgtMKG---LFLEHEGYFGALGCLLQF 380
Cdd:PRK13317 243 IESYTK--LRNctpIFLENGGYSGAIGALLLA 272
 
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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