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Conserved domains on  [gi|24430167|ref|NP_079236|]
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pantothenate kinase 2, mitochondrial isoform 2 [Homo sapiens]

Protein Classification

type II pantothenate kinase( domain architecture ID 10508179)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ASKHA_ATPase-like super family cl49607
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ...
1-275 0e+00

ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA superfamily, also known as actin-like ATPase domain superfamily, includes acetate and sugar kinases, heat-shock cognate 70 (Hsp70) and actin family proteins. They either function as conformational hydrolases (e.g. Hsp70, actin) that perform simple ATP hydrolysis, or as metabolite kinases (e.g. glycerol kinase) that catalyze the transfer of a phosphoryl group from ATP to their cognate substrates. Both activities depend on the presence of specific metal cations. ASKHA superfamily members share a common core fold that includes an actin-like ATPase domain consisting of two subdomains (denoted I _ II) with highly similar ribonuclease (RNase) H-like folds. The fold of each subdomain is characterized by a central five strand beta-sheet and flanking alpha-helices. The two subdomains form an active site cleft in which ATP binds at the bottom. Another common feature of ASKHA superfamily members is the coupling of phosphoryl-group transfer to conformational rearrangement, leading to domain closure. Substrate binding triggers protein motion.


The actual alignment was detected with superfamily member cd24136:

Pssm-ID: 483947 [Multi-domain]  Cd Length: 354  Bit Score: 566.16  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24430167   1 MPAFIQMGRDKNFSSLHTVFCATGGGAYKFEQDFLTIGDLQLCKLDELDCLIKGILYIDSVGFNGRSQCYYFENPADSEK 80
Cdd:cd24136  80 MPAFIQMGRDKHFSSLHTTLCATGGGAYKFEQDFLTMGDLQLCKLDELDCLIKGVLYIDSVGFNGHSECYYFENPTDSEK 159
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24430167  81 CQKLPFDLKNPYPLLLVNIGSGVSILAVYSKDNYKRVTGTSLGGGTFFGLCCLLTGCTTFEEALEMASRGDSTKVDKLVR 160
Cdd:cd24136 160 CQKLPFNLKNPYPLLLVNIGSGVSILAVYSKDNYKRVTGTSLGGGTFFGLCCLLTGCTTFEEALEMASRGDSTKVDKLVR 239
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24430167 161 DIYGGDYERFGLPGWAVASSFGNMMSKEKREAVSKEDLARATLITITNNIGSIARMCALNENINQVVFVGNFLRINTIAM 240
Cdd:cd24136 240 DIYGGDYERFGLPGWAVASSFGNMMSKEKREAVSKEDLARATLITITNNIGSIARMCALNENINRVVFVGNFLRINTISM 319
                       250       260       270
                ....*....|....*....|....*....|....*
gi 24430167 241 RLLAYALDYWSKGQLKALFSEHEGYFGAVGALLEL 275
Cdd:cd24136 320 RLLAYALDYWSKGQLKALFLEHEGYFGAVGALLEL 354
 
Name Accession Description Interval E-value
ASKHA_NBD_PanK-II_Pank2 cd24136
nucleotide-binding domain (NBD) of pantothenate kinase 2 (Pank2) from type II pantothenate ...
1-275 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: 566.16  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24430167   1 MPAFIQMGRDKNFSSLHTVFCATGGGAYKFEQDFLTIGDLQLCKLDELDCLIKGILYIDSVGFNGRSQCYYFENPADSEK 80
Cdd:cd24136  80 MPAFIQMGRDKHFSSLHTTLCATGGGAYKFEQDFLTMGDLQLCKLDELDCLIKGVLYIDSVGFNGHSECYYFENPTDSEK 159
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24430167  81 CQKLPFDLKNPYPLLLVNIGSGVSILAVYSKDNYKRVTGTSLGGGTFFGLCCLLTGCTTFEEALEMASRGDSTKVDKLVR 160
Cdd:cd24136 160 CQKLPFNLKNPYPLLLVNIGSGVSILAVYSKDNYKRVTGTSLGGGTFFGLCCLLTGCTTFEEALEMASRGDSTKVDKLVR 239
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24430167 161 DIYGGDYERFGLPGWAVASSFGNMMSKEKREAVSKEDLARATLITITNNIGSIARMCALNENINQVVFVGNFLRINTIAM 240
Cdd:cd24136 240 DIYGGDYERFGLPGWAVASSFGNMMSKEKREAVSKEDLARATLITITNNIGSIARMCALNENINRVVFVGNFLRINTISM 319
                       250       260       270
                ....*....|....*....|....*....|....*
gi 24430167 241 RLLAYALDYWSKGQLKALFSEHEGYFGAVGALLEL 275
Cdd:cd24136 320 RLLAYALDYWSKGQLKALFLEHEGYFGAVGALLEL 354
Fumble pfam03630
Fumble; Fumble is required for cell division in Drosophila. Mutants lacking fumble exhibit ...
1-271 4.32e-144

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: 406.88  E-value: 4.32e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24430167     1 MPAFIQMGRDKNFSSLHT----VFCATGGGAYKFEQDFLTIGDLQLCKLDELDCLIKGILYIDSvgfNGRSQCYYFEnpa 76
Cdd:pfam03630  39 IEDCLEFIKSLGLNSKGTdrglTVKATGGGAYKFYDLFKEKLGVKVDKEDEMECLIKGLNFLLT---NIPDEVFTYS--- 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24430167    77 DSEKCQKLPFDLKNPYPLLLVNIGSGVSILAVYSKDNYKRVTGTSLGGGTFFGLCCLLTGCTTFEEALEMASRGDSTKVD 156
Cdd:pfam03630 113 DSPEYFFQTVDNNSIYPYLLVNIGSGVSILKVEGPDKFERVGGTSLGGGTFWGLCSLLTGAKSFDEMLELAEKGDNRNVD 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24430167   157 KLVRDIYGGDYERFGLPGWAVASSFGNMMSKEKREAVSK----EDLARATLITITNNIGSIARMCALNENINQVVFVGNF 232
Cdd:pfam03630 193 MLVGDIYGGDYEKIGLKSDTIASSFGKVFRKKFRESASNdaspEDIARSLLYMISNNIGQIAYLNAKLHGLKRIYFGGNF 272
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 24430167   233 LRINTIAMRLLAYALDYWSKGQLKALFSEHEGYFGAVGA 271
Cdd:pfam03630 273 IRGHPITMKTLSYAINFWSKGELKALFLRHEGYLGALGA 311
panK_eukar TIGR00555
pantothenate kinase, eukaryotic/staphyloccocal type; This model describes a eukaryotic form of ...
15-274 1.62e-114

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: 331.29  E-value: 1.62e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24430167    15 SLHTVFCATGGGAYKFEQDFLTIGDLQLCKLDELDCLIKGILYIDSVGFNGRSQCYYFEnpadsekCQKLPFDLKNPYPL 94
Cdd:TIGR00555  48 SRITTLCATGGGAFKFAELIYESAGIQLHKFDEFDALIQGLNYLLKEEPKEKFTYYDFE-------CQKKPIDLDDIYPY 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24430167    95 LLVNIGSGVSILAVYSkDNYKRVTGTSLGGGTFFGLCCLLTGCTTFEEALEMASRGDSTKVDKLVRDIYGGDYERFGLPG 174
Cdd:TIGR00555 121 LLVNIGTGTSILYVDG-DNYERVGGTSLGGGTFLGLGKLLTGIQTFDELLEMAQHGDRTNVDLLVGDIYGGDYSESGLDG 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24430167   175 WAVASSFGNMMSKEKREAVSKEDLARATLITITNNIGSIARMCALNENINQVVFVGNFLRINTIAMRLLAYALDYWSKgq 254
Cdd:TIGR00555 200 SLTASSFGKVLSKHLDQSFSPEDIAASLLGLIGNNIGQIAYLCALRYNIDRIVFIGSFLRNNQLLMKVLSYATNFWSK-- 277
                         250       260
                  ....*....|....*....|
gi 24430167   255 lKALFSEHEGYFGAVGALLE 274
Cdd:TIGR00555 278 -KALFLEHEGYSGAIGALLS 296
PLN02920 PLN02920
pantothenate kinase 1
8-273 1.83e-59

pantothenate kinase 1


Pssm-ID: 215498 [Multi-domain]  Cd Length: 398  Bit Score: 193.91  E-value: 1.83e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24430167    8 GRDKNFSSlhtvfcATGGGAYKFEQDFLTIGDLQLCKLDELDCLIKGILYIDSvGFNGRSQCYYfenpaDSEKcQKLPFD 87
Cdd:PLN02920  94 THDKNFIK------ATGGGAYKFADLFKEKLGISLDKEDEMDCLVTGANFLLK-AVHHEAFTYL-----DGQK-EFVQID 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24430167   88 LKNPYPLLLVNIGSGVSILAVYSKDNYKRVTGTSLGGGTFFGLCCLLTGCTTFEEALEMASRGDSTKVDKLVRDIYGG-D 166
Cdd:PLN02920 161 HNDLYPYLLVNIGSGVSMIKVDGDGKFERVSGTSVGGGTFWGLGKLLTKCKSFDELLELSHQGNNRVIDMLVGDIYGGmD 240
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24430167  167 YERFGLPGWAVASSFGNMMSKEKR-EAVSKEDLARATLITITNNIGSIARMCALNENINQVVFVGNFLRINTIAMRLLAY 245
Cdd:PLN02920 241 YSKIGLSSTTIASSFGKAISDNKElEDYKPEDVARSLLRMISNNIGQISYLNALRFGLKRIFFGGFFIRGHSYTMDTISV 320
                        250       260
                 ....*....|....*....|....*...
gi 24430167  246 ALDYWSKGQLKALFSEHEGYFGAVGALL 273
Cdd:PLN02920 321 AVHFWSKGEAKAMFLRHEGFLGALGAFM 348
PanK COG5146
Pantothenate kinase [Coenzyme transport and metabolism]; Pantothenate kinase is part of the ...
19-273 1.37e-31

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: 117.68  E-value: 1.37e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24430167  19 VFCATGGGAyKFEQDFLTIGDLQlcKLDELDCLIKGILYIdsvgfngrsqcyyfenpadsekcqkLPFDLKNPYPLLLVN 98
Cdd:COG5146  48 KIGLTGGRA-EVLAEKLNGDPKQ--YIVEFDATGKGVRYL-------------------------LKEEGHDIDKFIITN 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24430167  99 IGSGVSIlaVYSKDN-YKRVTGTSLGGGTFFGLCCLLTGCTTFEEALEMASRGDSTKVDKLVRDIYGGDYErfGLPGWAV 177
Cdd:COG5146 100 VGTGTSI--HYMDGDtQERVGGTGVGGGTLMGLSYLLTGISDFEEIVELAKKGDRDGIDLKVKDIYEGMEP--PIPGDLT 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24430167 178 ASSFGNMMSKEKREAvSKEDLARATLITITNNIGSIARMCALNENINQVVFVGNFLRINTIAMRLLAyalDYWSKGQLKA 257
Cdd:COG5146 176 ASNFGKVLITLDESA-TKEDILAAIIGLVGETITTLSIQAAEEYDTETIVYIGSTLTNNPLLQEVIE---SYTILRGKKP 251
                       250
                ....*....|....*.
gi 24430167 258 LFSEHEGYFGAVGALL 273
Cdd:COG5146 252 IFLENGEFSGAIGALL 267
 
Name Accession Description Interval E-value
ASKHA_NBD_PanK-II_Pank2 cd24136
nucleotide-binding domain (NBD) of pantothenate kinase 2 (Pank2) from type II pantothenate ...
1-275 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: 566.16  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24430167   1 MPAFIQMGRDKNFSSLHTVFCATGGGAYKFEQDFLTIGDLQLCKLDELDCLIKGILYIDSVGFNGRSQCYYFENPADSEK 80
Cdd:cd24136  80 MPAFIQMGRDKHFSSLHTTLCATGGGAYKFEQDFLTMGDLQLCKLDELDCLIKGVLYIDSVGFNGHSECYYFENPTDSEK 159
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24430167  81 CQKLPFDLKNPYPLLLVNIGSGVSILAVYSKDNYKRVTGTSLGGGTFFGLCCLLTGCTTFEEALEMASRGDSTKVDKLVR 160
Cdd:cd24136 160 CQKLPFNLKNPYPLLLVNIGSGVSILAVYSKDNYKRVTGTSLGGGTFFGLCCLLTGCTTFEEALEMASRGDSTKVDKLVR 239
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24430167 161 DIYGGDYERFGLPGWAVASSFGNMMSKEKREAVSKEDLARATLITITNNIGSIARMCALNENINQVVFVGNFLRINTIAM 240
Cdd:cd24136 240 DIYGGDYERFGLPGWAVASSFGNMMSKEKREAVSKEDLARATLITITNNIGSIARMCALNENINRVVFVGNFLRINTISM 319
                       250       260       270
                ....*....|....*....|....*....|....*
gi 24430167 241 RLLAYALDYWSKGQLKALFSEHEGYFGAVGALLEL 275
Cdd:cd24136 320 RLLAYALDYWSKGQLKALFLEHEGYFGAVGALLEL 354
ASKHA_NBD_PanK-II_Pank1-like cd24122
nucleotide-binding domain (NBD) of the pantothenate kinase 1 (Pank1)-like subfamily; PanK (EC ...
1-273 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: 515.53  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24430167   1 MPAFIQMGRDKNFSSLHTVFCATGGGAYKFEQDFLTIGDLQLCKLDELDCLIKGILYIDSvgfNGRSQCYYFENPADSEK 80
Cdd:cd24122  32 MEGFIQLAREKNLSSLIKTVCATGGGAYKFEKLFREELGLQLHKLDELDCLIRGINFLLR---HVPDECYYFENPSDPEL 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24430167  81 CQK--LPFDLKNPYPLLLVNIGSGVSILAVYSKDNYKRVTGTSLGGGTFFGLCCLLTGCTTFEEALEMASRGDSTKVDKL 158
Cdd:cd24122 109 CEKrvVPFDFSDPYPYLLVNIGSGVSILAVESPDNYERVSGTSLGGGTFLGLCCLLTGCETFEEALELAAKGDSTKVDML 188
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24430167 159 VRDIYGGDYERFGLPGWAVASSFGNMMSKEKREAVSKEDLARATLITITNNIGSIARMCALNENINQVVFVGNFLRINTI 238
Cdd:cd24122 189 VGDIYGGDYEKFGLPGDTVASSFGKMVAKEKRESASKEDLARALLVMITNNIGSIARLCAKNEGIKRVVFVGNFLRHNPI 268
                       250       260       270
                ....*....|....*....|....*....|....*
gi 24430167 239 AMRLLAYALDYWSKGQLKALFSEHEGYFGAVGALL 273
Cdd:cd24122 269 AMRLLAYAMDYWSKGEMKALFLEHEGYFGALGALL 303
ASKHA_NBD_PanK-II_Pank1 cd24135
nucleotide-binding domain (NBD) of pantothenate kinase 1 (Pank1) from type II pantothenate ...
1-273 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: 503.38  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24430167   1 MPAFIQMGRDKNFSSLHTVFCATGGGAYKFEQDFLTIGDLQLCKLDELDCLIKGILYIDSVGFNGRSQCYYFENPADSEK 80
Cdd:cd24135  80 MHRFIQMGSEKNFSSLHTTLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSVGFNGQPECYYFENPTDPEQ 159
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24430167  81 CQKLPFDLKNPYPLLLVNIGSGVSILAVYSKDNYKRVTGTSLGGGTFFGLCCLLTGCTTFEEALEMASRGDSTKVDKLVR 160
Cdd:cd24135 160 CQKKPYCLDNPYPMLLVNIGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALEMAAKGDSTNVDKLVK 239
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24430167 161 DIYGGDYERFGLPGWAVASSFGNMMSKEKREAVSKEDLARATLITITNNIGSIARMCALNENINQVVFVGNFLRINTIAM 240
Cdd:cd24135 240 DIYGGDYERFGLQGSAVASSFGHMMSKEKRDSISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINMVSM 319
                       250       260       270
                ....*....|....*....|....*....|...
gi 24430167 241 RLLAYALDYWSKGQLKALFSEHEGYFGAVGALL 273
Cdd:cd24135 320 KLLAYAMDFWSKGQLKALFLEHEGYFGAVGALL 352
ASKHA_NBD_PanK-II cd24016
nucleotide-binding domain (NBD) of type II pantothenate kinase (PanK-II) and similar proteins; ...
1-273 3.07e-177

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: 490.24  E-value: 3.07e-177
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24430167   1 MPAFIQMGRDKNFSSLHTVFCATGGGAYKFEQDFLTIGDLQLCKLDELDCLIKGILYIDSVGFNGRSQCYYFENPADSEK 80
Cdd:cd24016  27 VVEFIQMGQDKNFSTLITKLCATGGGAGKFEEDFRTIGNLPLQKLDELDCLSQGLLYLDSVQFNGQAECYYFANASEPER 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24430167  81 CQKLPFDLKNPYPLLLVNIGSGVSILAVYSKDNYKRVTGTSLGGGTFFGLCCLLTGCTTFEEALEMASRGDSTKVDKLVR 160
Cdd:cd24016 107 CQKMPFNLHDPYPYLFVNVGSGVSILAVDSKDNYKRVTGTSLGGGTFQGLCYLLTGCTDFEEALEMAQHGDSTTIDKLVR 186
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24430167 161 DIYGGDYERFGLPGWAVASSFGNMMSKEKREAVSKEDLARATLITITNNIGSIARMCALNENINQVVFVGNFLRINTIAM 240
Cdd:cd24016 187 DIYGGDYERFGLPGDAVASSFGNMLHKEKRADFSKEDLARATLGTITNNIGSMARMCARNEKIENVVFVGNFLRNNALLM 266
                       250       260       270
                ....*....|....*....|....*....|...
gi 24430167 241 RLLAYALDYWSKGQLKALFSEHEGYFGAVGALL 273
Cdd:cd24016 267 KLLAYATDLWSKGQLKALFVEHEGYFGAVGALL 299
ASKHA_NBD_PanK-II_Pank3 cd24137
nucleotide-binding domain (NBD) of pantothenate kinase 3 (Pank3) from type II pantothenate ...
1-273 1.33e-166

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: 465.63  E-value: 1.33e-166
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24430167   1 MPAFIQMGRDKNFSSLHTVFCATGGGAYKFEQDFLTIGDLQLCKLDELDCLIKGILYIDSVGFNGRSQCYYFENPADSEK 80
Cdd:cd24137  80 LPTFIQMGRDKNFSTLQTVLCATGGGAYKFEKDFRTIGNLHLHKLDELDCLVKGLLYIDSVSFNGQAECYYFANASEPER 159
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24430167  81 CQKLPFDLKNPYPLLLVNIGSGVSILAVYSKDNYKRVTGTSLGGGTFFGLCCLLTGCTTFEEALEMASRGDSTKVDKLVR 160
Cdd:cd24137 160 CQKMPFNLDDPYPLLVVNIGSGVSILAVHSKDNYKRVTGTSLGGGTFLGLCSLLTGCESFEEALEMASKGDSTQADKLVR 239
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24430167 161 DIYGGDYERFGLPGWAVASSFGNMMSKEKREAVSKEDLARATLITITNNIGSIARMCALNENINQVVFVGNFLRINTIAM 240
Cdd:cd24137 240 DIYGGDYERFGLPGWAVASSFGNMIYKEKRESVSKEDLARATLVTITNNIGSVARMCAVNEKINRVVFVGNFLRVNTLSM 319
                       250       260       270
                ....*....|....*....|....*....|...
gi 24430167 241 RLLAYALDYWSKGQLKALFSEHEGYFGAVGALL 273
Cdd:cd24137 320 KLLAYALDYWSKGQLKALFLEHEGYFGAVGALL 352
Fumble pfam03630
Fumble; Fumble is required for cell division in Drosophila. Mutants lacking fumble exhibit ...
1-271 4.32e-144

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: 406.88  E-value: 4.32e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24430167     1 MPAFIQMGRDKNFSSLHT----VFCATGGGAYKFEQDFLTIGDLQLCKLDELDCLIKGILYIDSvgfNGRSQCYYFEnpa 76
Cdd:pfam03630  39 IEDCLEFIKSLGLNSKGTdrglTVKATGGGAYKFYDLFKEKLGVKVDKEDEMECLIKGLNFLLT---NIPDEVFTYS--- 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24430167    77 DSEKCQKLPFDLKNPYPLLLVNIGSGVSILAVYSKDNYKRVTGTSLGGGTFFGLCCLLTGCTTFEEALEMASRGDSTKVD 156
Cdd:pfam03630 113 DSPEYFFQTVDNNSIYPYLLVNIGSGVSILKVEGPDKFERVGGTSLGGGTFWGLCSLLTGAKSFDEMLELAEKGDNRNVD 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24430167   157 KLVRDIYGGDYERFGLPGWAVASSFGNMMSKEKREAVSK----EDLARATLITITNNIGSIARMCALNENINQVVFVGNF 232
Cdd:pfam03630 193 MLVGDIYGGDYEKIGLKSDTIASSFGKVFRKKFRESASNdaspEDIARSLLYMISNNIGQIAYLNAKLHGLKRIYFGGNF 272
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 24430167   233 LRINTIAMRLLAYALDYWSKGQLKALFSEHEGYFGAVGA 271
Cdd:pfam03630 273 IRGHPITMKTLSYAINFWSKGELKALFLRHEGYLGALGA 311
ASKHA_NBD_PanK-II_euk cd24086
nucleotide-binding domain (NBD) of type II pantothenate kinase (PanK-II) and similar proteins ...
1-273 4.76e-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: 361.60  E-value: 4.76e-126
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24430167   1 MPAFIQMGRDKNF--SSLHTVFCATGGGAYKFEQDFLTIGDLQLCKLDELDCLIKGILYIDSVGFNgrSQCYYFENPADS 78
Cdd:cd24086  54 LEEFLNFLRDKNFedSSKGKVLYATGGGAYKYAELIEETLGVQLVKVDEMDSLVNGLHFLLSVLSK--DECFPFPNDSGP 131
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24430167  79 EKCQKLPFDLKNPYPLLLVNIGSGVSILAVYSKDNYKRVTGTSLGGGTFFGLCCLLTGCTTFEEALEMASRGDSTKVDKL 158
Cdd:cd24086 132 EFLQKDPQLSDDLFPCLLVNIGSGVSILKVDSDGKYERVSGTSLGGGTFLGLASLLTGTNSFDELLELASRGDRANVDLL 211
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24430167 159 VRDIYGGDYERFGLPGWAVASSFGNMMSKEK-REAVSKEDLARATLITITNNIGSIARMCALNENINQVVFVGNFLRINT 237
Cdd:cd24086 212 VRDIYGGDYPYLGLPGDLLASSFGKLADDEKsREDFSKEDIARSLLRMIVNNIGYLAYLVAKLHNVKRVFFTGNFIRNNE 291
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 24430167 238 IAMRLLAYALDYWSKGQLKALFSEHEGYFGAVGALL 273
Cdd:cd24086 292 LARKLIAEALNYWSKGSLNALFLRHDGYLGALGALL 327
panK_eukar TIGR00555
pantothenate kinase, eukaryotic/staphyloccocal type; This model describes a eukaryotic form of ...
15-274 1.62e-114

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: 331.29  E-value: 1.62e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24430167    15 SLHTVFCATGGGAYKFEQDFLTIGDLQLCKLDELDCLIKGILYIDSVGFNGRSQCYYFEnpadsekCQKLPFDLKNPYPL 94
Cdd:TIGR00555  48 SRITTLCATGGGAFKFAELIYESAGIQLHKFDEFDALIQGLNYLLKEEPKEKFTYYDFE-------CQKKPIDLDDIYPY 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24430167    95 LLVNIGSGVSILAVYSkDNYKRVTGTSLGGGTFFGLCCLLTGCTTFEEALEMASRGDSTKVDKLVRDIYGGDYERFGLPG 174
Cdd:TIGR00555 121 LLVNIGTGTSILYVDG-DNYERVGGTSLGGGTFLGLGKLLTGIQTFDELLEMAQHGDRTNVDLLVGDIYGGDYSESGLDG 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24430167   175 WAVASSFGNMMSKEKREAVSKEDLARATLITITNNIGSIARMCALNENINQVVFVGNFLRINTIAMRLLAYALDYWSKgq 254
Cdd:TIGR00555 200 SLTASSFGKVLSKHLDQSFSPEDIAASLLGLIGNNIGQIAYLCALRYNIDRIVFIGSFLRNNQLLMKVLSYATNFWSK-- 277
                         250       260
                  ....*....|....*....|
gi 24430167   255 lKALFSEHEGYFGAVGALLE 274
Cdd:TIGR00555 278 -KALFLEHEGYSGAIGALLS 296
ASKHA_NBD_PanK-II_Pank4 cd24123
nucleotide-binding domain (NBD) of pantothenate kinase 4 (Pank4) from type II pantothenate ...
22-273 1.27e-97

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: 289.84  E-value: 1.27e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24430167  22 ATGGGAYKFEQDFLTIGDLQLCKLDELDCLIKGilyidsVGF---NGRSQCYYFENpaDSEKCQKLPFDLKNPYPLLLVN 98
Cdd:cd24123  90 ATGGGAYKYADLIKEKLGVEVDKEDEMECLIKG------CNFllkNIPDEVFTYDE--HAKPEVKFQSDPPDIFPYLLVN 161
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24430167  99 IGSGVSILAVYSKDNYKRVTGTSLGGGTFFGLCCLLTGCTTFEEALEMASRGDSTKVDKLVRDIYGGDYERFGLPGWAVA 178
Cdd:cd24123 162 IGSGVSILKVDSEDKFERVGGTSLGGGTFWGLGSLLTGAKSFDELLELAEKGDNRNVDMLVGDIYGGDYSKIGLKSDTIA 241
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24430167 179 SSFGNMMSKEK---REAVSKEDLARATLITITNNIGSIARMCALNENINQVVFVGNFLRINTIAMRLLAYALDYWSKGQL 255
Cdd:cd24123 242 SSFGKVARADKdarLEDFSPEDIAKSLLRMISNNIGQIAYLNAKLHGLKRIYFGGFFIRGHPLTMHTISYAINFWSKGEM 321
                       250
                ....*....|....*...
gi 24430167 256 KALFSEHEGYFGAVGALL 273
Cdd:cd24123 322 QALFLRHEGYLGAIGAFL 339
PLN02920 PLN02920
pantothenate kinase 1
8-273 1.83e-59

pantothenate kinase 1


Pssm-ID: 215498 [Multi-domain]  Cd Length: 398  Bit Score: 193.91  E-value: 1.83e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24430167    8 GRDKNFSSlhtvfcATGGGAYKFEQDFLTIGDLQLCKLDELDCLIKGILYIDSvGFNGRSQCYYfenpaDSEKcQKLPFD 87
Cdd:PLN02920  94 THDKNFIK------ATGGGAYKFADLFKEKLGISLDKEDEMDCLVTGANFLLK-AVHHEAFTYL-----DGQK-EFVQID 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24430167   88 LKNPYPLLLVNIGSGVSILAVYSKDNYKRVTGTSLGGGTFFGLCCLLTGCTTFEEALEMASRGDSTKVDKLVRDIYGG-D 166
Cdd:PLN02920 161 HNDLYPYLLVNIGSGVSMIKVDGDGKFERVSGTSVGGGTFWGLGKLLTKCKSFDELLELSHQGNNRVIDMLVGDIYGGmD 240
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24430167  167 YERFGLPGWAVASSFGNMMSKEKR-EAVSKEDLARATLITITNNIGSIARMCALNENINQVVFVGNFLRINTIAMRLLAY 245
Cdd:PLN02920 241 YSKIGLSSTTIASSFGKAISDNKElEDYKPEDVARSLLRMISNNIGQISYLNALRFGLKRIFFGGFFIRGHSYTMDTISV 320
                        250       260
                 ....*....|....*....|....*...
gi 24430167  246 ALDYWSKGQLKALFSEHEGYFGAVGALL 273
Cdd:PLN02920 321 AVHFWSKGEAKAMFLRHEGFLGALGAFM 348
PLN02902 PLN02902
pantothenate kinase
22-273 5.10e-58

pantothenate kinase


Pssm-ID: 215489 [Multi-domain]  Cd Length: 876  Bit Score: 198.58  E-value: 5.10e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24430167   22 ATGGGAYKFEQDFLTIGDLQLCKLDELDCLIKGILYIDSVGfngRSQCYyfeNPADSEKcQKLPFDLKNPYPLLLVNIGS 101
Cdd:PLN02902 151 ATGGGAYKFADLFKERLGVSLDKEDEMDCLVAGANFLLKAI---RHEAF---THMEGEK-EFVQIDQNDLFPYLLVNIGS 223
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24430167  102 GVSILAVYSKDNYKRVTGTSLGGGTFFGLCCLLTGCTTFEEALEMASRGDSTKVDKLVRDIYGG-DYERFGLPGWAVASS 180
Cdd:PLN02902 224 GVSMIKVDGDGKFERVSGTNVGGGTYWGLGRLLTKCKSFDELLELSQRGDNSAIDMLVGDIYGGmDYSKIGLSASTIASS 303
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24430167  181 FGNMMSKEKR-EAVSKEDLARATLITITNNIGSIARMCALNENINQVVFVGNFLRINTIAMRLLAYALDYWSKGQLKALF 259
Cdd:PLN02902 304 FGKVISENKElSDYRPEDISLSLLRMISYNIGQISYLNALRFGLKRIFFGGFFIRGHAYTMDTISFAVHFWSKGEAQAMF 383
                        250
                 ....*....|....
gi 24430167  260 SEHEGYFGAVGALL 273
Cdd:PLN02902 384 LRHEGFLGALGAFM 397
ASKHA_NBD_PanK-II_bac cd24085
nucleotide-binding domain (NBD) of type II pantothenate kinase (PanK-II) and similar proteins ...
21-273 2.12e-50

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: 166.59  E-value: 2.12e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24430167  21 CATGGGAYKFEQDFLtigDLQLCKLDELDCLIKGILYIdsvgfngrsqcyYFENPADSekcqklpfdlknpyplLLVNIG 100
Cdd:cd24085  51 AVTGGGASRLPENID---GIPIVKVDEFEAIGRGALYL------------LGEILDDA----------------LVVSIG 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24430167 101 SGVSILAVySKDNYKRVTGTSLGGGTFFGLCCLLTGCTTFEEALEMASRGDSTKVDKLVRDIYGGDYErfGLPGWAVASS 180
Cdd:cd24085 100 TGTSIVLA-KNGTIRHVGGTGVGGGTLLGLGKLLLGVTDYDEITELARKGDRSNVDLTVGDIYGGGIG--PLPPDLTASN 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24430167 181 FGNMmskEKREAVSKEDLARATLITITNNIGSIARMCALNENINQVVFVGNFLRINTIAMRLLAYALDYwskgQLKALFS 260
Cdd:cd24085 177 FGKL---ADDNKASREDLAAALINLVGETIGTLAALAARAEGVKDIVLVGSTLRNPLLKEVLERYTKLY----GVKPIFP 249
                       250
                ....*....|...
gi 24430167 261 EHEGYFGAVGALL 273
Cdd:cd24085 250 ENGEFAGAIGALL 262
PTZ00297 PTZ00297
pantothenate kinase; Provisional
22-271 3.02e-33

pantothenate kinase; Provisional


Pssm-ID: 140318 [Multi-domain]  Cd Length: 1452  Bit Score: 128.43  E-value: 3.02e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24430167    22 ATGGGAYKFEQDFLTIGDLQLCKLDELDCLIKGI-LYIDSVgfngrSQCYYFENPADSE----KCQKLPFDLKNPYPLLL 96
Cdd:PTZ00297 1144 ATGGGAFKYASVAKKVLGINFSVMREMDAVVKGLnLVIRVA-----PESIFTVDPSTGVhhphQLVSPPGDGFSPFPCLL 1218
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24430167    97 VNIGSGVSILAVYSKD-NYKRVTGTSLGGGTFFGLCCLLTGCTTFEEALE---MASRGDSTKVDKLVRDIYGgdYERFGL 172
Cdd:PTZ00297 1219 VNIGSGISIIKCLGPDgSHVRVGGSPIGGATFWGLVRTMTNVTSWEEVMEimrLDGPGDNKNVDLLVGDIYG--YNAKDL 1296
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24430167   173 PGW----AVASSFGNMMSKEKRE-----------------------------------------AVSKEDLARATLITIT 207
Cdd:PTZ00297 1297 PAMlsvdTVASTFGKLGTERFYEmmrgvstahfsdddaageilspkalksptviselpvrngtkKASAIDIVRSLLNMIS 1376
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24430167   208 NNIGSIARMCALNENINQVVFVGNFLRINTIAMRLLAYALDYWSKGQLKALFSEHEGYFGAVGA 271
Cdd:PTZ00297 1377 SNVTQLAYLHSRVQGVPNIFFAGGFVRDNPIIWSHISSTMKYWSKGECHAHFLEHDGYLGALGC 1440
PRK13317 PRK13317
pantothenate kinase; Provisional
20-273 3.02e-33

pantothenate kinase; Provisional


Pssm-ID: 237346 [Multi-domain]  Cd Length: 277  Bit Score: 122.37  E-value: 3.02e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24430167   20 FCATGGGAYKFEQdfLTIGDLQLCKLDELDCLIKGILYIdsvgfngrsqcyyfenpadsEKCQKLPFDlknpyPLLLVNI 99
Cdd:PRK13317  51 ICLTGGKAGYLQQ--LLNYGYPIAEFVEFEATGLGVRYL--------------------LKEEGHDLN-----DYIFTNI 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24430167  100 GSGVSILAVYSKDnYKRVTGTSLGGGTFFGLCCLLTGCTTFEEALEMASRGDSTKVDKLVRDIYGGDYErfGLPGWAVAS 179
Cdd:PRK13317 104 GTGTSIHYVDGNS-QRRVGGTGIGGGTIQGLSKLLTNISDYEQLIELAKHGDRNNIDLKVGDIYKGPLP--PIPGDLTAS 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24430167  180 SFGNMMSKEKREAvSKEDLArATLITITNN-IGSIARMCALNENINQVVFVGNFLRINTIAMRLLAyalDYWSKGQLKAL 258
Cdd:PRK13317 181 NFGKVLHHLDSEF-TSSDIL-AGVIGLVGEvITTLSIQAAREKNIENIVYIGSTLTNNPLLQEIIE---SYTKLRNCTPI 255
                        250
                 ....*....|....*
gi 24430167  259 FSEHEGYFGAVGALL 273
Cdd:PRK13317 256 FLENGGYSGAIGALL 270
PanK COG5146
Pantothenate kinase [Coenzyme transport and metabolism]; Pantothenate kinase is part of the ...
19-273 1.37e-31

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: 117.68  E-value: 1.37e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24430167  19 VFCATGGGAyKFEQDFLTIGDLQlcKLDELDCLIKGILYIdsvgfngrsqcyyfenpadsekcqkLPFDLKNPYPLLLVN 98
Cdd:COG5146  48 KIGLTGGRA-EVLAEKLNGDPKQ--YIVEFDATGKGVRYL-------------------------LKEEGHDIDKFIITN 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24430167  99 IGSGVSIlaVYSKDN-YKRVTGTSLGGGTFFGLCCLLTGCTTFEEALEMASRGDSTKVDKLVRDIYGGDYErfGLPGWAV 177
Cdd:COG5146 100 VGTGTSI--HYMDGDtQERVGGTGVGGGTLMGLSYLLTGISDFEEIVELAKKGDRDGIDLKVKDIYEGMEP--PIPGDLT 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24430167 178 ASSFGNMMSKEKREAvSKEDLARATLITITNNIGSIARMCALNENINQVVFVGNFLRINTIAMRLLAyalDYWSKGQLKA 257
Cdd:COG5146 176 ASNFGKVLITLDESA-TKEDILAAIIGLVGETITTLSIQAAEEYDTETIVYIGSTLTNNPLLQEVIE---SYTILRGKKP 251
                       250
                ....*....|....*.
gi 24430167 258 LFSEHEGYFGAVGALL 273
Cdd:COG5146 252 IFLENGEFSGAIGALL 267
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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