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Conserved domains on  [gi|1024249294|ref|NP_001311122|]
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pantothenate kinase 2, mitochondrial isoform 6 [Homo sapiens]

Protein Classification

acetate and sugar kinases/Hsc70/actin family protein( domain architecture ID 99298)

acetate and sugar kinases/Hsc70/actin (ASKHA) family protein catalyzes phosphoryl transfer from ATP to their respective substrates

CATH:  3.30.420.40
Gene Ontology:  GO:0000166
PubMed:  8800467|7781919

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 ...
 1-128 7.03e-94

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 cd24122:

Pssm-ID: 483947 [Multi-domain]  Cd Length: 303  Bit Score: 272.86  E-value: 7.03e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249294   1 MASRGDSTKVDKLVRDIYGGDYERFGLPGWAVASSFGNMMSKEKREAVSKEDLARATLITITNNIGSIARMCALNENINQ 80
Cdd:cd24122   176 LAAKGDSTKVDMLVGDIYGGDYEKFGLPGDTVASSFGKMVAKEKRESASKEDLARALLVMITNNIGSIARLCAKNEGIKR 255

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1024249294  81 VVFVGNFLRINTIAMRLLAYALDYWSKGQLKALFSEHEGYFGAVGALL 128
Cdd:cd24122   256 VVFVGNFLRHNPIAMRLLAYAMDYWSKGEMKALFLEHEGYFGALGALL 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 ...
 1-128 7.03e-94

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: 272.86  E-value: 7.03e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249294   1 MASRGDSTKVDKLVRDIYGGDYERFGLPGWAVASSFGNMMSKEKREAVSKEDLARATLITITNNIGSIARMCALNENINQ 80
Cdd:cd24122   176 LAAKGDSTKVDMLVGDIYGGDYEKFGLPGDTVASSFGKMVAKEKRESASKEDLARALLVMITNNIGSIARLCAKNEGIKR 255

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1024249294  81 VVFVGNFLRINTIAMRLLAYALDYWSKGQLKALFSEHEGYFGAVGALL 128
Cdd:cd24122   256 VVFVGNFLRHNPIAMRLLAYAMDYWSKGEMKALFLEHEGYFGALGALL 303
Fumble pfam03630
Fumble; Fumble is required for cell division in Drosophila. Mutants lacking fumble exhibit ...
 1-126 4.07e-74

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: 222.75  E-value: 4.07e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249294   1 MASRGDSTKVDKLVRDIYGGDYERFGLPGWAVASSFGNMMSKEKREAVSK----EDLARATLITITNNIGSIARMCALNE 76
Cdd:pfam03630 182 LAEKGDNRNVDMLVGDIYGGDYEKIGLKSDTIASSFGKVFRKKFRESASNdaspEDIARSLLYMISNNIGQIAYLNAKLH 261

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1024249294  77 NINQVVFVGNFLRINTIAMRLLAYALDYWSKGQLKALFSEHEGYFGAVGA 126
Cdd:pfam03630 262 GLKRIYFGGNFIRGHPITMKTLSYAINFWSKGELKALFLRHEGYLGALGA 311
PLN02920 PLN02920
pantothenate kinase 1
 1-128 1.12e-28

pantothenate kinase 1


Pssm-ID: 215498 [Multi-domain]  Cd Length: 398  Bit Score: 107.62  E-value: 1.12e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249294   1 MASRGDSTKVDKLVRDIYGG-DYERFGLPGWAVASSFGNMMSKEKR-EAVSKEDLARATLITITNNIGSIARMCALNENI 78
Cdd:PLN02920  219 LSHQGNNRVIDMLVGDIYGGmDYSKIGLSSTTIASSFGKAISDNKElEDYKPEDVARSLLRMISNNIGQISYLNALRFGL 298

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1024249294  79 NQVVFVGNFLRINTIAMRLLAYALDYWSKGQLKALFSEHEGYFGAVGALL 128
Cdd:PLN02920  299 KRIFFGGFFIRGHSYTMDTISVAVHFWSKGEAKAMFLRHEGFLGALGAFM 348
 
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 ...
 1-128 7.03e-94

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: 272.86  E-value: 7.03e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249294   1 MASRGDSTKVDKLVRDIYGGDYERFGLPGWAVASSFGNMMSKEKREAVSKEDLARATLITITNNIGSIARMCALNENINQ 80
Cdd:cd24122   176 LAAKGDSTKVDMLVGDIYGGDYEKFGLPGDTVASSFGKMVAKEKRESASKEDLARALLVMITNNIGSIARLCAKNEGIKR 255

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1024249294  81 VVFVGNFLRINTIAMRLLAYALDYWSKGQLKALFSEHEGYFGAVGALL 128
Cdd:cd24122   256 VVFVGNFLRHNPIAMRLLAYAMDYWSKGEMKALFLEHEGYFGALGALL 303
ASKHA_NBD_PanK-II_Pank2 cd24136
nucleotide-binding domain (NBD) of pantothenate kinase 2 (Pank2) from type II pantothenate ...
 1-130 2.11e-92

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: 271.10  E-value: 2.11e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249294   1 MASRGDSTKVDKLVRDIYGGDYERFGLPGWAVASSFGNMMSKEKREAVSKEDLARATLITITNNIGSIARMCALNENINQ 80
Cdd:cd24136   225 MASRGDSTKVDKLVRDIYGGDYERFGLPGWAVASSFGNMMSKEKREAVSKEDLARATLITITNNIGSIARMCALNENINR 304

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1024249294  81 VVFVGNFLRINTIAMRLLAYALDYWSKGQLKALFSEHEGYFGAVGALLEL 130
Cdd:cd24136   305 VVFVGNFLRINTISMRLLAYALDYWSKGQLKALFLEHEGYFGAVGALLEL 354
ASKHA_NBD_PanK-II_Pank1 cd24135
nucleotide-binding domain (NBD) of pantothenate kinase 1 (Pank1) from type II pantothenate ...
 1-128 1.48e-80

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: 240.67  E-value: 1.48e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249294   1 MASRGDSTKVDKLVRDIYGGDYERFGLPGWAVASSFGNMMSKEKREAVSKEDLARATLITITNNIGSIARMCALNENINQ 80
Cdd:cd24135   225 MAAKGDSTNVDKLVKDIYGGDYERFGLQGSAVASSFGHMMSKEKRDSISKEDLARATLVTITNNIGSIARMCALNENIDR 304

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1024249294  81 VVFVGNFLRINTIAMRLLAYALDYWSKGQLKALFSEHEGYFGAVGALL 128
Cdd:cd24135   305 VVFVGNFLRINMVSMKLLAYAMDFWSKGQLKALFLEHEGYFGAVGALL 352
ASKHA_NBD_PanK-II cd24016
nucleotide-binding domain (NBD) of type II pantothenate kinase (PanK-II) and similar proteins; ...
 1-128 1.02e-79

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: 236.78  E-value: 1.02e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249294   1 MASRGDSTKVDKLVRDIYGGDYERFGLPGWAVASSFGNMMSKEKREAVSKEDLARATLITITNNIGSIARMCALNENINQ 80
Cdd:cd24016   172 MAQHGDSTTIDKLVRDIYGGDYERFGLPGDAVASSFGNMLHKEKRADFSKEDLARATLGTITNNIGSMARMCARNEKIEN 251

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1024249294  81 VVFVGNFLRINTIAMRLLAYALDYWSKGQLKALFSEHEGYFGAVGALL 128
Cdd:cd24016   252 VVFVGNFLRNNALLMKLLAYATDLWSKGQLKALFVEHEGYFGAVGALL 299
ASKHA_NBD_PanK-II_Pank3 cd24137
nucleotide-binding domain (NBD) of pantothenate kinase 3 (Pank3) from type II pantothenate ...
 1-128 4.86e-76

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: 229.51  E-value: 4.86e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249294   1 MASRGDSTKVDKLVRDIYGGDYERFGLPGWAVASSFGNMMSKEKREAVSKEDLARATLITITNNIGSIARMCALNENINQ 80
Cdd:cd24137   225 MASKGDSTQADKLVRDIYGGDYERFGLPGWAVASSFGNMIYKEKRESVSKEDLARATLVTITNNIGSVARMCAVNEKINR 304

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1024249294  81 VVFVGNFLRINTIAMRLLAYALDYWSKGQLKALFSEHEGYFGAVGALL 128
Cdd:cd24137   305 VVFVGNFLRVNTLSMKLLAYALDYWSKGQLKALFLEHEGYFGAVGALL 352
Fumble pfam03630
Fumble; Fumble is required for cell division in Drosophila. Mutants lacking fumble exhibit ...
 1-126 4.07e-74

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: 222.75  E-value: 4.07e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249294   1 MASRGDSTKVDKLVRDIYGGDYERFGLPGWAVASSFGNMMSKEKREAVSK----EDLARATLITITNNIGSIARMCALNE 76
Cdd:pfam03630 182 LAEKGDNRNVDMLVGDIYGGDYEKIGLKSDTIASSFGKVFRKKFRESASNdaspEDIARSLLYMISNNIGQIAYLNAKLH 261

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1024249294  77 NINQVVFVGNFLRINTIAMRLLAYALDYWSKGQLKALFSEHEGYFGAVGA 126
Cdd:pfam03630 262 GLKRIYFGGNFIRGHPITMKTLSYAINFWSKGELKALFLRHEGYLGALGA 311
ASKHA_NBD_PanK-II_euk cd24086
nucleotide-binding domain (NBD) of type II pantothenate kinase (PanK-II) and similar proteins ...
 1-128 5.32e-58

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: 182.48  E-value: 5.32e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249294   1 MASRGDSTKVDKLVRDIYGGDYERFGLPGWAVASSFGNMMSKEK-REAVSKEDLARATLITITNNIGSIARMCALNENIN 79
Cdd:cd24086   199 LASRGDRANVDLLVRDIYGGDYPYLGLPGDLLASSFGKLADDEKsREDFSKEDIARSLLRMIVNNIGYLAYLVAKLHNVK 278

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1024249294  80 QVVFVGNFLRINTIAMRLLAYALDYWSKGQLKALFSEHEGYFGAVGALL 128
Cdd:cd24086   279 RVFFTGNFIRNNELARKLIAEALNYWSKGSLNALFLRHDGYLGALGALL 327
ASKHA_NBD_PanK-II_Pank4 cd24123
nucleotide-binding domain (NBD) of pantothenate kinase 4 (Pank4) from type II pantothenate ...
 1-128 4.65e-50

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: 162.34  E-value: 4.65e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249294   1 MASRGDSTKVDKLVRDIYGGDYERFGLPGWAVASSFGNMMSKEK---REAVSKEDLARATLITITNNIGSIARMCALNEN 77
Cdd:cd24123   209 LAEKGDNRNVDMLVGDIYGGDYSKIGLKSDTIASSFGKVARADKdarLEDFSPEDIAKSLLRMISNNIGQIAYLNAKLHG 288

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1024249294  78 INQVVFVGNFLRINTIAMRLLAYALDYWSKGQLKALFSEHEGYFGAVGALL 128
Cdd:cd24123   289 LKRIYFGGFFIRGHPLTMHTISYAINFWSKGEMQALFLRHEGYLGAIGAFL 339
PLN02920 PLN02920
pantothenate kinase 1
 1-128 1.12e-28

pantothenate kinase 1


Pssm-ID: 215498 [Multi-domain]  Cd Length: 398  Bit Score: 107.62  E-value: 1.12e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249294   1 MASRGDSTKVDKLVRDIYGG-DYERFGLPGWAVASSFGNMMSKEKR-EAVSKEDLARATLITITNNIGSIARMCALNENI 78
Cdd:PLN02920  219 LSHQGNNRVIDMLVGDIYGGmDYSKIGLSSTTIASSFGKAISDNKElEDYKPEDVARSLLRMISNNIGQISYLNALRFGL 298

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1024249294  79 NQVVFVGNFLRINTIAMRLLAYALDYWSKGQLKALFSEHEGYFGAVGALL 128
Cdd:PLN02920  299 KRIFFGGFFIRGHSYTMDTISVAVHFWSKGEAKAMFLRHEGFLGALGAFM 348
PLN02902 PLN02902
pantothenate kinase
 1-128 1.72e-28

pantothenate kinase


Pssm-ID: 215489 [Multi-domain]  Cd Length: 876  Bit Score: 108.83  E-value: 1.72e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249294   1 MASRGDSTKVDKLVRDIYGG-DYERFGLPGWAVASSFGNMMSKEKR-EAVSKEDLARATLITITNNIGSIARMCALNENI 78
Cdd:PLN02902  268 LSQRGDNSAIDMLVGDIYGGmDYSKIGLSASTIASSFGKVISENKElSDYRPEDISLSLLRMISYNIGQISYLNALRFGL 347

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1024249294  79 NQVVFVGNFLRINTIAMRLLAYALDYWSKGQLKALFSEHEGYFGAVGALL 128
Cdd:PLN02902  348 KRIFFGGFFIRGHAYTMDTISFAVHFWSKGEAQAMFLRHEGFLGALGAFM 397
ASKHA_NBD_PanK-II_bac cd24085
nucleotide-binding domain (NBD) of type II pantothenate kinase (PanK-II) and similar proteins ...
 1-128 1.69e-23

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: 91.47  E-value: 1.69e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249294   1 MASRGDSTKVDKLVRDIYGGDYErfGLPGWAVASSFGNMmskEKREAVSKEDLARATLITITNNIGSIARMCALNENINQ 80
Cdd:cd24085   144 LARKGDRSNVDLTVGDIYGGGIG--PLPPDLTASNFGKL---ADDNKASREDLAAALINLVGETIGTLAALAARAEGVKD 218

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1024249294  81 VVFVGNFLRINTIAMRLLAYALDYwskgQLKALFSEHEGYFGAVGALL 128
Cdd:cd24085   219 IVLVGSTLRNPLLKEVLERYTKLY----GVKPIFPENGEFAGAIGALL 262
PTZ00297 PTZ00297
pantothenate kinase; Provisional
 5-126 1.23e-14

pantothenate kinase; Provisional


Pssm-ID: 140318 [Multi-domain]  Cd Length: 1452  Bit Score: 69.11  E-value: 1.23e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249294    5 GDSTKVDKLVRDIYGgdYERFGLPGW----AVASSFGNMMSKEKRE---------------------------------- 46
Cdd:PTZ00297  1276 GDNKNVDLLVGDIYG--YNAKDLPAMlsvdTVASTFGKLGTERFYEmmrgvstahfsdddaageilspkalksptvisel 1353

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249294   47 -------AVSKEDLARATLITITNNIGSIARMCALNENINQVVFVGNFLRINTIAMRLLAYALDYWSKGQLKALFSEHEG 119
Cdd:PTZ00297  1354 pvrngtkKASAIDIVRSLLNMISSNVTQLAYLHSRVQGVPNIFFAGGFVRDNPIIWSHISSTMKYWSKGECHAHFLEHDG 1433


                   ....*..
gi 1024249294  120 YFGAVGA 126
Cdd:PTZ00297  1434 YLGALGC 1440
PRK13317 PRK13317
pantothenate kinase; Provisional
 1-128 1.87e-14

pantothenate kinase; Provisional


Pssm-ID: 237346 [Multi-domain]  Cd Length: 277  Bit Score: 67.67  E-value: 1.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249294   1 MASRGDSTKVDKLVRDIYGGDYErfGLPGWAVASSFGNMMSKEKREAvSKEDLArATLITITNN-IGSIARMCALNENIN 79
Cdd:PRK13317  149 LAKHGDRNNIDLKVGDIYKGPLP--PIPGDLTASNFGKVLHHLDSEF-TSSDIL-AGVIGLVGEvITTLSIQAAREKNIE 224

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1024249294  80 QVVFVGNFLRINTIAMRLLAyalDYWSKGQLKALFSEHEGYFGAVGALL 128
Cdd:PRK13317  225 NIVYIGSTLTNNPLLQEIIE---SYTKLRNCTPIFLENGGYSGAIGALL 270
 
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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