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Conserved domains on  [gi|85838513|ref|NP_705902|]
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pantothenate kinase 2, mitochondrial isoform 1 precursor [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

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 ...
213-566 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: 750.29  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513 213 WFGLDIGGTLVKLVYFEPKDITAEEEEEEVESLKSIRKYLTSNVAYGSTGIRDVHLELKDLTLCGRKGNLHFIRFPTHDM 292
Cdd:cd24136   1 WFGLDIGGTLVKLVYFEPKDITAEEEEEEVENLKSIRKYLTSNVAYGSTGIRDVHLELKDLTLCGRKGNLHFIRFPTHDM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513 293 PAFIQMGRDKNFSSLHTVFCATGGGAYKFEQDFLTIGDLQLCKLDELDCLIKGILYIDSVGFNGRSQCYYFENPADSEKC 372
Cdd:cd24136  81 PAFIQMGRDKHFSSLHTTLCATGGGAYKFEQDFLTMGDLQLCKLDELDCLIKGVLYIDSVGFNGHSECYYFENPTDSEKC 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513 373 QKLPFDLKNPYPLLLVNIGSGVSILAVYSKDNYKRVTGTSLGGGTFFGLCCLLTGCTTFEEALEMASRGDSTKVDKLVRD 452
Cdd:cd24136 161 QKLPFNLKNPYPLLLVNIGSGVSILAVYSKDNYKRVTGTSLGGGTFFGLCCLLTGCTTFEEALEMASRGDSTKVDKLVRD 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513 453 IYGGDYERFGLPGWAVASSFGNMMSKEKREAVSKEDLARATLITITNNIGSIARMCALNENINQVVFVGNFLRINTIAMR 532
Cdd:cd24136 241 IYGGDYERFGLPGWAVASSFGNMMSKEKREAVSKEDLARATLITITNNIGSIARMCALNENINRVVFVGNFLRINTISMR 320
                       330       340       350
                ....*....|....*....|....*....|....
gi 85838513 533 LLAYALDYWSKGQLKALFSEHEGYFGAVGALLEL 566
Cdd:cd24136 321 LLAYALDYWSKGQLKALFLEHEGYFGAVGALLEL 354
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
8-209 7.81e-04

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.47  E-value: 7.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513     8 HPRVHWAAPPSLSSGLHRLLFLRG--TRIPSSTTLSPPRH--------DSLSLDGGTVNPPRVREPTGREAFGPSPASSD 77
Cdd:PHA03307  676 PPRALEACPARLESWLRELRDLRDavYLARLRGDLPVAGGreervaavRAVSLVARTVAPLVRYSPRRARARASAWDITD 755
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513    78 WLPARWRngrgGRPrARLCSGWTAAEEARRNPTLGGLLGRQRLLLRMGGGRLGAPMERHGRASATSVSSAGEQAAGDPEG 157
Cdd:PHA03307  756 ALFSNPS----LVP-AKLAEALALLEPAEPQRGAGSSPPVRAEAAFRRPGRLRRSGPAADAASRTASKRKSRSHTPDGGS 830
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 85838513   158 RRQEPLRRRASSASVPAVGASAEGTRRDRLGSYSGPTSVSRQRVESLRKKRP 209
Cdd:PHA03307  831 ESSGPARPPGAAARPPPARSSESSKSKPAAAGGRARGKNGRRRPRPPEPRAR 882
 
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 ...
213-566 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: 750.29  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513 213 WFGLDIGGTLVKLVYFEPKDITAEEEEEEVESLKSIRKYLTSNVAYGSTGIRDVHLELKDLTLCGRKGNLHFIRFPTHDM 292
Cdd:cd24136   1 WFGLDIGGTLVKLVYFEPKDITAEEEEEEVENLKSIRKYLTSNVAYGSTGIRDVHLELKDLTLCGRKGNLHFIRFPTHDM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513 293 PAFIQMGRDKNFSSLHTVFCATGGGAYKFEQDFLTIGDLQLCKLDELDCLIKGILYIDSVGFNGRSQCYYFENPADSEKC 372
Cdd:cd24136  81 PAFIQMGRDKHFSSLHTTLCATGGGAYKFEQDFLTMGDLQLCKLDELDCLIKGVLYIDSVGFNGHSECYYFENPTDSEKC 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513 373 QKLPFDLKNPYPLLLVNIGSGVSILAVYSKDNYKRVTGTSLGGGTFFGLCCLLTGCTTFEEALEMASRGDSTKVDKLVRD 452
Cdd:cd24136 161 QKLPFNLKNPYPLLLVNIGSGVSILAVYSKDNYKRVTGTSLGGGTFFGLCCLLTGCTTFEEALEMASRGDSTKVDKLVRD 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513 453 IYGGDYERFGLPGWAVASSFGNMMSKEKREAVSKEDLARATLITITNNIGSIARMCALNENINQVVFVGNFLRINTIAMR 532
Cdd:cd24136 241 IYGGDYERFGLPGWAVASSFGNMMSKEKREAVSKEDLARATLITITNNIGSIARMCALNENINRVVFVGNFLRINTISMR 320
                       330       340       350
                ....*....|....*....|....*....|....
gi 85838513 533 LLAYALDYWSKGQLKALFSEHEGYFGAVGALLEL 566
Cdd:cd24136 321 LLAYALDYWSKGQLKALFLEHEGYFGAVGALLEL 354
Fumble pfam03630
Fumble; Fumble is required for cell division in Drosophila. Mutants lacking fumble exhibit ...
214-562 1.12e-162

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: 465.43  E-value: 1.12e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513   214 FGLDIGGTLVKLVYFEPKDITAEEEEeeveslksirkyltsnvaygstgirdvhlelkdltlcgrkGNLHFIRFPTHDMP 293
Cdd:pfam03630   1 FAIDIGGTLAKLVYFSPVPDSPKELG----------------------------------------GRLHFIKFETTKIE 40
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513   294 AFIQMGRDKNFSSLHT----VFCATGGGAYKFEQDFLTIGDLQLCKLDELDCLIKGILYIDSvgfNGRSQCYYFEnpaDS 369
Cdd:pfam03630  41 DCLEFIKSLGLNSKGTdrglTVKATGGGAYKFYDLFKEKLGVKVDKEDEMECLIKGLNFLLT---NIPDEVFTYS---DS 114
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513   370 EKCQKLPFDLKNPYPLLLVNIGSGVSILAVYSKDNYKRVTGTSLGGGTFFGLCCLLTGCTTFEEALEMASRGDSTKVDKL 449
Cdd:pfam03630 115 PEYFFQTVDNNSIYPYLLVNIGSGVSILKVEGPDKFERVGGTSLGGGTFWGLCSLLTGAKSFDEMLELAEKGDNRNVDML 194
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513   450 VRDIYGGDYERFGLPGWAVASSFGNMMSKEKREAVSK----EDLARATLITITNNIGSIARMCALNENINQVVFVGNFLR 525
Cdd:pfam03630 195 VGDIYGGDYEKIGLKSDTIASSFGKVFRKKFRESASNdaspEDIARSLLYMISNNIGQIAYLNAKLHGLKRIYFGGNFIR 274
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 85838513   526 INTIAMRLLAYALDYWSKGQLKALFSEHEGYFGAVGA 562
Cdd:pfam03630 275 GHPITMKTLSYAINFWSKGELKALFLRHEGYLGALGA 311
panK_eukar TIGR00555
pantothenate kinase, eukaryotic/staphyloccocal type; This model describes a eukaryotic form of ...
212-565 4.60e-127

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: 374.43  E-value: 4.60e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513   212 PWFGLDIGGTLVKLVYFEPKditaeeeeeeveslkSIRKYLTSNvaygstgirdvhlelkdltlcgrKGNLH-FIRFPTH 290
Cdd:TIGR00555   1 SRIGIDIGGTLIKVVYEEKK---------------GRRKFKTFE-----------------------TTNIDkFIEWLKN 42
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513   291 DMPAFiqmgrdknfsSLHTVFCATGGGAYKFEQDFLTIGDLQLCKLDELDCLIKGILYIDSVGFNGRSQCYYFEnpadse 370
Cdd:TIGR00555  43 QIHRH----------SRITTLCATGGGAFKFAELIYESAGIQLHKFDEFDALIQGLNYLLKEEPKEKFTYYDFE------ 106
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513   371 kCQKLPFDLKNPYPLLLVNIGSGVSILAVYSkDNYKRVTGTSLGGGTFFGLCCLLTGCTTFEEALEMASRGDSTKVDKLV 450
Cdd:TIGR00555 107 -CQKKPIDLDDIYPYLLVNIGTGTSILYVDG-DNYERVGGTSLGGGTFLGLGKLLTGIQTFDELLEMAQHGDRTNVDLLV 184
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513   451 RDIYGGDYERFGLPGWAVASSFGNMMSKEKREAVSKEDLARATLITITNNIGSIARMCALNENINQVVFVGNFLRINTIA 530
Cdd:TIGR00555 185 GDIYGGDYSESGLDGSLTASSFGKVLSKHLDQSFSPEDIAASLLGLIGNNIGQIAYLCALRYNIDRIVFIGSFLRNNQLL 264
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 85838513   531 MRLLAYALDYWSKgqlKALFSEHEGYFGAVGALLE 565
Cdd:TIGR00555 265 MKVLSYATNFWSK---KALFLEHEGYSGAIGALLS 296
PLN02920 PLN02920
pantothenate kinase 1
216-564 4.02e-63

pantothenate kinase 1


Pssm-ID: 215498 [Multi-domain]  Cd Length: 398  Bit Score: 212.39  E-value: 4.02e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513  216 LDIGGTLVKLVYFEPKDITAEEEEEEVESLKSIRKYLTSNVAYGSTGIRDVhLELKdltlcgRKGNLHFIRFPTHDMPaf 295
Cdd:PLN02920  23 LDIGGSLIKLVYFSRNSGDSEDPRNDSSVKSDGVNGRLHFAKFETRKINDC-LEFI------SSNKLHHGGFQHHENP-- 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513  296 iqmGRDKNFSSlhtvfcATGGGAYKFEQDFLTIGDLQLCKLDELDCLIKGILYIDSVgFNGRSQCYYfenpaDSEKcQKL 375
Cdd:PLN02920  94 ---THDKNFIK------ATGGGAYKFADLFKEKLGISLDKEDEMDCLVTGANFLLKA-VHHEAFTYL-----DGQK-EFV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513  376 PFDLKNPYPLLLVNIGSGVSILAVYSKDNYKRVTGTSLGGGTFFGLCCLLTGCTTFEEALEMASRGDSTKVDKLVRDIYG 455
Cdd:PLN02920 158 QIDHNDLYPYLLVNIGSGVSMIKVDGDGKFERVSGTSVGGGTFWGLGKLLTKCKSFDELLELSHQGNNRVIDMLVGDIYG 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513  456 G-DYERFGLPGWAVASSFGNMMSKEKR-EAVSKEDLARATLITITNNIGSIARMCALNENINQVVFVGNFLRINTIAMRL 533
Cdd:PLN02920 238 GmDYSKIGLSSTTIASSFGKAISDNKElEDYKPEDVARSLLRMISNNIGQISYLNALRFGLKRIFFGGFFIRGHSYTMDT 317
                        330       340       350
                 ....*....|....*....|....*....|.
gi 85838513  534 LAYALDYWSKGQLKALFSEHEGYFGAVGALL 564
Cdd:PLN02920 318 ISVAVHFWSKGEAKAMFLRHEGFLGALGAFM 348
PanK COG5146
Pantothenate kinase [Coenzyme transport and metabolism]; Pantothenate kinase is part of the ...
215-564 1.49e-35

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: 134.25  E-value: 1.49e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513 215 GLDIGGTLVKLVYFEpkditaeeeeeeveslksirkyltsnvaygstgirdvhlelkdltlcgrKGNLHFIRFPTHDMPA 294
Cdd:COG5146   5 GIDAGGTLTKIAYLE-------------------------------------------------DGERRYKKFPSDEIES 35
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513 295 FIQ-MGRDKNFSSLhtvfCATGGGAyKFEQDFLTIGDLQlcKLDELDCLIKGILYIdsvgfngrsqcyyfenpadsekcq 373
Cdd:COG5146  36 VADwLNKFINIEKI----GLTGGRA-EVLAEKLNGDPKQ--YIVEFDATGKGVRYL------------------------ 84
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513 374 kLPFDLKNPYPLLLVNIGSGVSIlaVYSKDN-YKRVTGTSLGGGTFFGLCCLLTGCTTFEEALEMASRGDSTKVDKLVRD 452
Cdd:COG5146  85 -LKEEGHDIDKFIITNVGTGTSI--HYMDGDtQERVGGTGVGGGTLMGLSYLLTGISDFEEIVELAKKGDRDGIDLKVKD 161
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513 453 IYGGDYErfGLPGWAVASSFGNMMSKEKREAvSKEDLARATLITITNNIGSIARMCALNENINQVVFVGNFLRINTIAMR 532
Cdd:COG5146 162 IYEGMEP--PIPGDLTASNFGKVLITLDESA-TKEDILAAIIGLVGETITTLSIQAAEEYDTETIVYIGSTLTNNPLLQE 238
                       330       340       350
                ....*....|....*....|....*....|..
gi 85838513 533 LLAyalDYWSKGQLKALFSEHEGYFGAVGALL 564
Cdd:COG5146 239 VIE---SYTILRGKKPIFLENGEFSGAIGALL 267
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
8-209 7.81e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.47  E-value: 7.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513     8 HPRVHWAAPPSLSSGLHRLLFLRG--TRIPSSTTLSPPRH--------DSLSLDGGTVNPPRVREPTGREAFGPSPASSD 77
Cdd:PHA03307  676 PPRALEACPARLESWLRELRDLRDavYLARLRGDLPVAGGreervaavRAVSLVARTVAPLVRYSPRRARARASAWDITD 755
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513    78 WLPARWRngrgGRPrARLCSGWTAAEEARRNPTLGGLLGRQRLLLRMGGGRLGAPMERHGRASATSVSSAGEQAAGDPEG 157
Cdd:PHA03307  756 ALFSNPS----LVP-AKLAEALALLEPAEPQRGAGSSPPVRAEAAFRRPGRLRRSGPAADAASRTASKRKSRSHTPDGGS 830
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 85838513   158 RRQEPLRRRASSASVPAVGASAEGTRRDRLGSYSGPTSVSRQRVESLRKKRP 209
Cdd:PHA03307  831 ESSGPARPPGAAARPPPARSSESSKSKPAAAGGRARGKNGRRRPRPPEPRAR 882
 
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 ...
213-566 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: 750.29  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513 213 WFGLDIGGTLVKLVYFEPKDITAEEEEEEVESLKSIRKYLTSNVAYGSTGIRDVHLELKDLTLCGRKGNLHFIRFPTHDM 292
Cdd:cd24136   1 WFGLDIGGTLVKLVYFEPKDITAEEEEEEVENLKSIRKYLTSNVAYGSTGIRDVHLELKDLTLCGRKGNLHFIRFPTHDM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513 293 PAFIQMGRDKNFSSLHTVFCATGGGAYKFEQDFLTIGDLQLCKLDELDCLIKGILYIDSVGFNGRSQCYYFENPADSEKC 372
Cdd:cd24136  81 PAFIQMGRDKHFSSLHTTLCATGGGAYKFEQDFLTMGDLQLCKLDELDCLIKGVLYIDSVGFNGHSECYYFENPTDSEKC 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513 373 QKLPFDLKNPYPLLLVNIGSGVSILAVYSKDNYKRVTGTSLGGGTFFGLCCLLTGCTTFEEALEMASRGDSTKVDKLVRD 452
Cdd:cd24136 161 QKLPFNLKNPYPLLLVNIGSGVSILAVYSKDNYKRVTGTSLGGGTFFGLCCLLTGCTTFEEALEMASRGDSTKVDKLVRD 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513 453 IYGGDYERFGLPGWAVASSFGNMMSKEKREAVSKEDLARATLITITNNIGSIARMCALNENINQVVFVGNFLRINTIAMR 532
Cdd:cd24136 241 IYGGDYERFGLPGWAVASSFGNMMSKEKREAVSKEDLARATLITITNNIGSIARMCALNENINRVVFVGNFLRINTISMR 320
                       330       340       350
                ....*....|....*....|....*....|....
gi 85838513 533 LLAYALDYWSKGQLKALFSEHEGYFGAVGALLEL 566
Cdd:cd24136 321 LLAYALDYWSKGQLKALFLEHEGYFGAVGALLEL 354
ASKHA_NBD_PanK-II_Pank1 cd24135
nucleotide-binding domain (NBD) of pantothenate kinase 1 (Pank1) from type II pantothenate ...
213-564 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: 665.16  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513 213 WFGLDIGGTLVKLVYFEPKDITAEEEEEEVESLKSIRKYLTSNVAYGSTGIRDVHLELKDLTLCGRKGNLHFIRFPTHDM 292
Cdd:cd24135   1 WFGMDIGGTLVKLVYFEPKDITAEEEQEEVENLKSIRKYLTSNTAYGKTGIRDVHLELKNLTMCGRKGNLHFIRFPSCAM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513 293 PAFIQMGRDKNFSSLHTVFCATGGGAYKFEQDFLTIGDLQLCKLDELDCLIKGILYIDSVGFNGRSQCYYFENPADSEKC 372
Cdd:cd24135  81 HRFIQMGSEKNFSSLHTTLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSVGFNGQPECYYFENPTDPEQC 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513 373 QKLPFDLKNPYPLLLVNIGSGVSILAVYSKDNYKRVTGTSLGGGTFFGLCCLLTGCTTFEEALEMASRGDSTKVDKLVRD 452
Cdd:cd24135 161 QKKPYCLDNPYPMLLVNIGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALEMAAKGDSTNVDKLVKD 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513 453 IYGGDYERFGLPGWAVASSFGNMMSKEKREAVSKEDLARATLITITNNIGSIARMCALNENINQVVFVGNFLRINTIAMR 532
Cdd:cd24135 241 IYGGDYERFGLQGSAVASSFGHMMSKEKRDSISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINMVSMK 320
                       330       340       350
                ....*....|....*....|....*....|..
gi 85838513 533 LLAYALDYWSKGQLKALFSEHEGYFGAVGALL 564
Cdd:cd24135 321 LLAYAMDFWSKGQLKALFLEHEGYFGAVGALL 352
ASKHA_NBD_PanK-II_Pank3 cd24137
nucleotide-binding domain (NBD) of pantothenate kinase 3 (Pank3) from type II pantothenate ...
213-564 0e+00

nucleotide-binding domain (NBD) of pantothenate kinase 3 (Pank3) from type II pantothenate kinase (PanK-II) subfamily; PanK (EC 2.7.1.33), also called pantothenic acid kinase, is the first enzyme in the Coenzyme A (CoA) biosynthetic pathway. It catalyzes the phosphorylation of pantothenate (vitamin B5) to form 4'-phosphopantothenate at the expense of a molecule of adenosine triphosphate (ATP), which is the rate-limiting step in CoA biosynthesis. It cannot utilize a phosphoryl donor other than ATP. Three distinct types of PanK have been identified, PanK-I, PanK-II and PanK-III. Eukaryotic PanK-II enzymes often occur as different isoforms, such as PanK1, PanK2, PanK3 and PanK4. The model corresponds to PanK3.


Pssm-ID: 466987 [Multi-domain]  Cd Length: 353  Bit Score: 610.85  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513 213 WFGLDIGGTLVKLVYFEPKDITAEEEEEEVESLKSIRKYLTSNVAYGSTGIRDVHLELKDLTLCGRKGNLHFIRFPTHDM 292
Cdd:cd24137   1 WFGMDIGGTLVKLSYFEPIDITAEEEQEEVESLKSIRKYLTSNVAYGSTGIRDVHLELKDLTLFGRRGNLHFIRFPTQDL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513 293 PAFIQMGRDKNFSSLHTVFCATGGGAYKFEQDFLTIGDLQLCKLDELDCLIKGILYIDSVGFNGRSQCYYFENPADSEKC 372
Cdd:cd24137  81 PTFIQMGRDKNFSTLQTVLCATGGGAYKFEKDFRTIGNLHLHKLDELDCLVKGLLYIDSVSFNGQAECYYFANASEPERC 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513 373 QKLPFDLKNPYPLLLVNIGSGVSILAVYSKDNYKRVTGTSLGGGTFFGLCCLLTGCTTFEEALEMASRGDSTKVDKLVRD 452
Cdd:cd24137 161 QKMPFNLDDPYPLLVVNIGSGVSILAVHSKDNYKRVTGTSLGGGTFLGLCSLLTGCESFEEALEMASKGDSTQADKLVRD 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513 453 IYGGDYERFGLPGWAVASSFGNMMSKEKREAVSKEDLARATLITITNNIGSIARMCALNENINQVVFVGNFLRINTIAMR 532
Cdd:cd24137 241 IYGGDYERFGLPGWAVASSFGNMIYKEKRESVSKEDLARATLVTITNNIGSVARMCAVNEKINRVVFVGNFLRVNTLSMK 320
                       330       340       350
                ....*....|....*....|....*....|..
gi 85838513 533 LLAYALDYWSKGQLKALFSEHEGYFGAVGALL 564
Cdd:cd24137 321 LLAYALDYWSKGQLKALFLEHEGYFGAVGALL 352
ASKHA_NBD_PanK-II_Pank1-like cd24122
nucleotide-binding domain (NBD) of the pantothenate kinase 1 (Pank1)-like subfamily; PanK (EC ...
213-564 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: 579.09  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513 213 WFGLDIGGTLVKLVYFEPKditaeeeeeeveslksirkyltsnvaygstgirdvhlelkdltlcgrkGNLHFIRFPTHDM 292
Cdd:cd24122   1 WFGLDIGGTLVKLVYFEPT------------------------------------------------GTLHFIRFETSRM 32
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513 293 PAFIQMGRDKNFSSLHTVFCATGGGAYKFEQDFLTIGDLQLCKLDELDCLIKGILYIDSvgfNGRSQCYYFENPADSEKC 372
Cdd:cd24122  33 EGFIQLAREKNLSSLIKTVCATGGGAYKFEKLFREELGLQLHKLDELDCLIRGINFLLR---HVPDECYYFENPSDPELC 109
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513 373 QK--LPFDLKNPYPLLLVNIGSGVSILAVYSKDNYKRVTGTSLGGGTFFGLCCLLTGCTTFEEALEMASRGDSTKVDKLV 450
Cdd:cd24122 110 EKrvVPFDFSDPYPYLLVNIGSGVSILAVESPDNYERVSGTSLGGGTFLGLCCLLTGCETFEEALELAAKGDSTKVDMLV 189
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513 451 RDIYGGDYERFGLPGWAVASSFGNMMSKEKREAVSKEDLARATLITITNNIGSIARMCALNENINQVVFVGNFLRINTIA 530
Cdd:cd24122 190 GDIYGGDYEKFGLPGDTVASSFGKMVAKEKRESASKEDLARALLVMITNNIGSIARLCAKNEGIKRVVFVGNFLRHNPIA 269
                       330       340       350
                ....*....|....*....|....*....|....
gi 85838513 531 MRLLAYALDYWSKGQLKALFSEHEGYFGAVGALL 564
Cdd:cd24122 270 MRLLAYAMDYWSKGEMKALFLEHEGYFGALGALL 303
ASKHA_NBD_PanK-II cd24016
nucleotide-binding domain (NBD) of type II pantothenate kinase (PanK-II) and similar proteins; ...
213-564 0e+00

nucleotide-binding domain (NBD) of type II pantothenate kinase (PanK-II) and similar proteins; PanK (EC 2.7.1.33), also called pantothenic acid kinase, is the first enzyme in the Coenzyme A (CoA) biosynthetic pathway. It catalyzes the phosphorylation of pantothenate (vitamin B5) to form 4'-phosphopantothenate at the expense of a molecule of adenosine triphosphate (ATP), which is the rate-limiting step in CoA biosynthesis. It cannot utilize a phosphoryl donor other than ATP. Three distinct types of PanK have been identified, PanK-I, PanK-II and PanK-III. Eukaryotic PanK-II enzymes often occur as different isoforms, such as PanK1, PanK2, PanK3 and PanK4. The model corresponds to PanK-II that belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.


Pssm-ID: 466866 [Multi-domain]  Cd Length: 299  Bit Score: 538.39  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513 213 WFGLDIGGTLVKLVYFepkditaeeeeeeveslksirkyltsnvaygstgirdvhlelkdltlcgrkgnLHFIRFPTHDM 292
Cdd:cd24016   1 WFGIDIGGTLVKLVYF-----------------------------------------------------LHFIRFPTDQV 27
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513 293 PAFIQMGRDKNFSSLHTVFCATGGGAYKFEQDFLTIGDLQLCKLDELDCLIKGILYIDSVGFNGRSQCYYFENPADSEKC 372
Cdd:cd24016  28 VEFIQMGQDKNFSTLITKLCATGGGAGKFEEDFRTIGNLPLQKLDELDCLSQGLLYLDSVQFNGQAECYYFANASEPERC 107
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513 373 QKLPFDLKNPYPLLLVNIGSGVSILAVYSKDNYKRVTGTSLGGGTFFGLCCLLTGCTTFEEALEMASRGDSTKVDKLVRD 452
Cdd:cd24016 108 QKMPFNLHDPYPYLFVNVGSGVSILAVDSKDNYKRVTGTSLGGGTFQGLCYLLTGCTDFEEALEMAQHGDSTTIDKLVRD 187
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513 453 IYGGDYERFGLPGWAVASSFGNMMSKEKREAVSKEDLARATLITITNNIGSIARMCALNENINQVVFVGNFLRINTIAMR 532
Cdd:cd24016 188 IYGGDYERFGLPGDAVASSFGNMLHKEKRADFSKEDLARATLGTITNNIGSMARMCARNEKIENVVFVGNFLRNNALLMK 267
                       330       340       350
                ....*....|....*....|....*....|..
gi 85838513 533 LLAYALDYWSKGQLKALFSEHEGYFGAVGALL 564
Cdd:cd24016 268 LLAYATDLWSKGQLKALFVEHEGYFGAVGALL 299
Fumble pfam03630
Fumble; Fumble is required for cell division in Drosophila. Mutants lacking fumble exhibit ...
214-562 1.12e-162

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: 465.43  E-value: 1.12e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513   214 FGLDIGGTLVKLVYFEPKDITAEEEEeeveslksirkyltsnvaygstgirdvhlelkdltlcgrkGNLHFIRFPTHDMP 293
Cdd:pfam03630   1 FAIDIGGTLAKLVYFSPVPDSPKELG----------------------------------------GRLHFIKFETTKIE 40
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513   294 AFIQMGRDKNFSSLHT----VFCATGGGAYKFEQDFLTIGDLQLCKLDELDCLIKGILYIDSvgfNGRSQCYYFEnpaDS 369
Cdd:pfam03630  41 DCLEFIKSLGLNSKGTdrglTVKATGGGAYKFYDLFKEKLGVKVDKEDEMECLIKGLNFLLT---NIPDEVFTYS---DS 114
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513   370 EKCQKLPFDLKNPYPLLLVNIGSGVSILAVYSKDNYKRVTGTSLGGGTFFGLCCLLTGCTTFEEALEMASRGDSTKVDKL 449
Cdd:pfam03630 115 PEYFFQTVDNNSIYPYLLVNIGSGVSILKVEGPDKFERVGGTSLGGGTFWGLCSLLTGAKSFDEMLELAEKGDNRNVDML 194
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513   450 VRDIYGGDYERFGLPGWAVASSFGNMMSKEKREAVSK----EDLARATLITITNNIGSIARMCALNENINQVVFVGNFLR 525
Cdd:pfam03630 195 VGDIYGGDYEKIGLKSDTIASSFGKVFRKKFRESASNdaspEDIARSLLYMISNNIGQIAYLNAKLHGLKRIYFGGNFIR 274
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 85838513   526 INTIAMRLLAYALDYWSKGQLKALFSEHEGYFGAVGA 562
Cdd:pfam03630 275 GHPITMKTLSYAINFWSKGELKALFLRHEGYLGALGA 311
ASKHA_NBD_PanK-II_euk cd24086
nucleotide-binding domain (NBD) of type II pantothenate kinase (PanK-II) and similar proteins ...
213-564 1.45e-149

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: 432.86  E-value: 1.45e-149
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513 213 WFGLDIGGTLVKLVYFEPKDITAEEEeeeveslksirkyltsnvaygstgirDVHLELKDLTLCGRKGNLHFIRFPTHDM 292
Cdd:cd24086   1 RLGLDIGGTLAKLAYLTPIDIDEAEE--------------------------KESVLLKLLANSGEDGELHFISFPNKDL 54
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513 293 PAFIQMGRDKNF--SSLHTVFCATGGGAYKFEQDFLTIGDLQLCKLDELDCLIKGILYIDSVGFNgrSQCYYFENPADSE 370
Cdd:cd24086  55 EEFLNFLRDKNFedSSKGKVLYATGGGAYKYAELIEETLGVQLVKVDEMDSLVNGLHFLLSVLSK--DECFPFPNDSGPE 132
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513 371 KCQKLPFDLKNPYPLLLVNIGSGVSILAVYSKDNYKRVTGTSLGGGTFFGLCCLLTGCTTFEEALEMASRGDSTKVDKLV 450
Cdd:cd24086 133 FLQKDPQLSDDLFPCLLVNIGSGVSILKVDSDGKYERVSGTSLGGGTFLGLASLLTGTNSFDELLELASRGDRANVDLLV 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513 451 RDIYGGDYERFGLPGWAVASSFGNMMSKEK-REAVSKEDLARATLITITNNIGSIARMCALNENINQVVFVGNFLRINTI 529
Cdd:cd24086 213 RDIYGGDYPYLGLPGDLLASSFGKLADDEKsREDFSKEDIARSLLRMIVNNIGYLAYLVAKLHNVKRVFFTGNFIRNNEL 292
                       330       340       350
                ....*....|....*....|....*....|....*
gi 85838513 530 AMRLLAYALDYWSKGQLKALFSEHEGYFGAVGALL 564
Cdd:cd24086 293 ARKLIAEALNYWSKGSLNALFLRHDGYLGALGALL 327
panK_eukar TIGR00555
pantothenate kinase, eukaryotic/staphyloccocal type; This model describes a eukaryotic form of ...
212-565 4.60e-127

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: 374.43  E-value: 4.60e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513   212 PWFGLDIGGTLVKLVYFEPKditaeeeeeeveslkSIRKYLTSNvaygstgirdvhlelkdltlcgrKGNLH-FIRFPTH 290
Cdd:TIGR00555   1 SRIGIDIGGTLIKVVYEEKK---------------GRRKFKTFE-----------------------TTNIDkFIEWLKN 42
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513   291 DMPAFiqmgrdknfsSLHTVFCATGGGAYKFEQDFLTIGDLQLCKLDELDCLIKGILYIDSVGFNGRSQCYYFEnpadse 370
Cdd:TIGR00555  43 QIHRH----------SRITTLCATGGGAFKFAELIYESAGIQLHKFDEFDALIQGLNYLLKEEPKEKFTYYDFE------ 106
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513   371 kCQKLPFDLKNPYPLLLVNIGSGVSILAVYSkDNYKRVTGTSLGGGTFFGLCCLLTGCTTFEEALEMASRGDSTKVDKLV 450
Cdd:TIGR00555 107 -CQKKPIDLDDIYPYLLVNIGTGTSILYVDG-DNYERVGGTSLGGGTFLGLGKLLTGIQTFDELLEMAQHGDRTNVDLLV 184
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513   451 RDIYGGDYERFGLPGWAVASSFGNMMSKEKREAVSKEDLARATLITITNNIGSIARMCALNENINQVVFVGNFLRINTIA 530
Cdd:TIGR00555 185 GDIYGGDYSESGLDGSLTASSFGKVLSKHLDQSFSPEDIAASLLGLIGNNIGQIAYLCALRYNIDRIVFIGSFLRNNQLL 264
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 85838513   531 MRLLAYALDYWSKgqlKALFSEHEGYFGAVGALLE 565
Cdd:TIGR00555 265 MKVLSYATNFWSK---KALFLEHEGYSGAIGALLS 296
ASKHA_NBD_PanK-II_Pank4 cd24123
nucleotide-binding domain (NBD) of pantothenate kinase 4 (Pank4) from type II pantothenate ...
214-564 4.82e-109

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: 329.91  E-value: 4.82e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513 214 FGLDIGGTLVKLVYFEPKDitaeeeeeeveslKSIRKYLTSNVAYGSTGIRDVHLELKDLTLCGRkgnLHFIRFPTHDMP 293
Cdd:cd24123   2 FAIDIGGSLAKLVYFSRVS-------------DKAASVSSSSGTSKGPSDEPLYEVSEQPELGGR---LHFVKFETKYIE 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513 294 AFIQMGRDKNFSSLH-----TVFCATGGGAYKFEQDFLTIGDLQLCKLDELDCLIKGilyidsVGF---NGRSQCYYFEN 365
Cdd:cd24123  66 ECLDFIKDNLLHSRQgnkrgKVIKATGGGAYKYADLIKEKLGVEVDKEDEMECLIKG------CNFllkNIPDEVFTYDE 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513 366 paDSEKCQKLPFDLKNPYPLLLVNIGSGVSILAVYSKDNYKRVTGTSLGGGTFFGLCCLLTGCTTFEEALEMASRGDSTK 445
Cdd:cd24123 140 --HAKPEVKFQSDPPDIFPYLLVNIGSGVSILKVDSEDKFERVGGTSLGGGTFWGLGSLLTGAKSFDELLELAEKGDNRN 217
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513 446 VDKLVRDIYGGDYERFGLPGWAVASSFGNMMSKEK---REAVSKEDLARATLITITNNIGSIARMCALNENINQVVFVGN 522
Cdd:cd24123 218 VDMLVGDIYGGDYSKIGLKSDTIASSFGKVARADKdarLEDFSPEDIAKSLLRMISNNIGQIAYLNAKLHGLKRIYFGGF 297
                       330       340       350       360
                ....*....|....*....|....*....|....*....|..
gi 85838513 523 FLRINTIAMRLLAYALDYWSKGQLKALFSEHEGYFGAVGALL 564
Cdd:cd24123 298 FIRGHPLTMHTISYAINFWSKGEMQALFLRHEGYLGAIGAFL 339
PLN02920 PLN02920
pantothenate kinase 1
216-564 4.02e-63

pantothenate kinase 1


Pssm-ID: 215498 [Multi-domain]  Cd Length: 398  Bit Score: 212.39  E-value: 4.02e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513  216 LDIGGTLVKLVYFEPKDITAEEEEEEVESLKSIRKYLTSNVAYGSTGIRDVhLELKdltlcgRKGNLHFIRFPTHDMPaf 295
Cdd:PLN02920  23 LDIGGSLIKLVYFSRNSGDSEDPRNDSSVKSDGVNGRLHFAKFETRKINDC-LEFI------SSNKLHHGGFQHHENP-- 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513  296 iqmGRDKNFSSlhtvfcATGGGAYKFEQDFLTIGDLQLCKLDELDCLIKGILYIDSVgFNGRSQCYYfenpaDSEKcQKL 375
Cdd:PLN02920  94 ---THDKNFIK------ATGGGAYKFADLFKEKLGISLDKEDEMDCLVTGANFLLKA-VHHEAFTYL-----DGQK-EFV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513  376 PFDLKNPYPLLLVNIGSGVSILAVYSKDNYKRVTGTSLGGGTFFGLCCLLTGCTTFEEALEMASRGDSTKVDKLVRDIYG 455
Cdd:PLN02920 158 QIDHNDLYPYLLVNIGSGVSMIKVDGDGKFERVSGTSVGGGTFWGLGKLLTKCKSFDELLELSHQGNNRVIDMLVGDIYG 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513  456 G-DYERFGLPGWAVASSFGNMMSKEKR-EAVSKEDLARATLITITNNIGSIARMCALNENINQVVFVGNFLRINTIAMRL 533
Cdd:PLN02920 238 GmDYSKIGLSSTTIASSFGKAISDNKElEDYKPEDVARSLLRMISNNIGQISYLNALRFGLKRIFFGGFFIRGHSYTMDT 317
                        330       340       350
                 ....*....|....*....|....*....|.
gi 85838513  534 LAYALDYWSKGQLKALFSEHEGYFGAVGALL 564
Cdd:PLN02920 318 ISVAVHFWSKGEAKAMFLRHEGFLGALGAFM 348
PLN02902 PLN02902
pantothenate kinase
162-564 6.40e-59

pantothenate kinase


Pssm-ID: 215489 [Multi-domain]  Cd Length: 876  Bit Score: 210.91  E-value: 6.40e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513  162 PLRRRASSASVPAVGASAEGTRRDRlgsysGPTSVSRQRVESLRKkrplfpwFGLDIGGTLVKLVYFEPKDitaeeeeee 241
Cdd:PLN02902  16 SIHRSGSRPQLDLSKAAIQGNLEER-----DPTILLPNQSDDISH-------LALDIGGSLIKLVYFSRHE--------- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513  242 VESLKSIRKYLTSNVAYGSTGIRDVHLELkdltlcgrKGNLHFIRFPTHDMPA---FI---QMGR-------DKNFSSLH 308
Cdd:PLN02902  75 DRSTDDKRKRTIKERLGITNGNRRSYPIL--------GGRLHFVKFETSKINEcldFIsskQLHRggihswlSKAPPNGN 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513  309 TVFCATGGGAYKFEQDFLTIGDLQLCKLDELDCLIKGILYIDSVgfnGRSQCYyfeNPADSEKcQKLPFDLKNPYPLLLV 388
Cdd:PLN02902 147 GVIKATGGGAYKFADLFKERLGVSLDKEDEMDCLVAGANFLLKA---IRHEAF---THMEGEK-EFVQIDQNDLFPYLLV 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513  389 NIGSGVSILAVYSKDNYKRVTGTSLGGGTFFGLCCLLTGCTTFEEALEMASRGDSTKVDKLVRDIYGG-DYERFGLPGWA 467
Cdd:PLN02902 220 NIGSGVSMIKVDGDGKFERVSGTNVGGGTYWGLGRLLTKCKSFDELLELSQRGDNSAIDMLVGDIYGGmDYSKIGLSAST 299
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513  468 VASSFGNMMSKEKR-EAVSKEDLARATLITITNNIGSIARMCALNENINQVVFVGNFLRINTIAMRLLAYALDYWSKGQL 546
Cdd:PLN02902 300 IASSFGKVISENKElSDYRPEDISLSLLRMISYNIGQISYLNALRFGLKRIFFGGFFIRGHAYTMDTISFAVHFWSKGEA 379
                        410
                 ....*....|....*...
gi 85838513  547 KALFSEHEGYFGAVGALL 564
Cdd:PLN02902 380 QAMFLRHEGFLGALGAFM 397
ASKHA_NBD_PanK-II_bac cd24085
nucleotide-binding domain (NBD) of type II pantothenate kinase (PanK-II) and similar proteins ...
215-564 3.99e-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: 184.31  E-value: 3.99e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513 215 GLDIGGTLVKLVYFEpkditaeeeeeeveslksirkyltsnvaygstgirdvhlelkdltlcgRKGNLHFIRFPTHDMPA 294
Cdd:cd24085   3 GIDAGGTLTKIVLLE------------------------------------------------NNGELKFKAFDSLKIEA 34
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513 295 ---FIQMGRDKNFSSLhtvfCATGGGAYKFEQDFLtigDLQLCKLDELDCLIKGILYIdsvgfngrsqcyYFENPADSek 371
Cdd:cd24085  35 lvkFLNELGINDIEKI----AVTGGGASRLPENID---GIPIVKVDEFEAIGRGALYL------------LGEILDDA-- 93
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513 372 cqklpfdlknpyplLLVNIGSGVSILAVySKDNYKRVTGTSLGGGTFFGLCCLLTGCTTFEEALEMASRGDSTKVDKLVR 451
Cdd:cd24085  94 --------------LVVSIGTGTSIVLA-KNGTIRHVGGTGVGGGTLLGLGKLLLGVTDYDEITELARKGDRSNVDLTVG 158
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513 452 DIYGGDYErfGLPGWAVASSFGNMmskEKREAVSKEDLARATLITITNNIGSIARMCALNENINQVVFVGNFLRINTIAM 531
Cdd:cd24085 159 DIYGGGIG--PLPPDLTASNFGKL---ADDNKASREDLAAALINLVGETIGTLAALAARAEGVKDIVLVGSTLRNPLLKE 233
                       330       340       350
                ....*....|....*....|....*....|...
gi 85838513 532 RLLAYALDYwskgQLKALFSEHEGYFGAVGALL 564
Cdd:cd24085 234 VLERYTKLY----GVKPIFPENGEFAGAIGALL 262
PRK13317 PRK13317
pantothenate kinase; Provisional
215-564 5.57e-36

pantothenate kinase; Provisional


Pssm-ID: 237346 [Multi-domain]  Cd Length: 277  Bit Score: 135.85  E-value: 5.57e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513  215 GLDIGGTLVKLVYFEPKDItaeeeeeeveslKSIRKYLTSNVAYgstgirdVHLELKDLTLCGRkgnlhfirfpthdmpa 294
Cdd:PRK13317   6 GIDAGGTLTKIVYLEEKKQ------------RTFKTEYSAEGKK-------VIDWLINLQDIEK---------------- 50
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513  295 fiqmgrdknfsslhtvFCATGGGAYKFEQdfLTIGDLQLCKLDELDCLIKGILYIdsvgfngrsqcyyfenpadsEKCQK 374
Cdd:PRK13317  51 ----------------ICLTGGKAGYLQQ--LLNYGYPIAEFVEFEATGLGVRYL--------------------LKEEG 92
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513  375 LPFDlknpyPLLLVNIGSGVSILAVYSKDnYKRVTGTSLGGGTFFGLCCLLTGCTTFEEALEMASRGDSTKVDKLVRDIY 454
Cdd:PRK13317  93 HDLN-----DYIFTNIGTGTSIHYVDGNS-QRRVGGTGIGGGTIQGLSKLLTNISDYEQLIELAKHGDRNNIDLKVGDIY 166
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513  455 GGDYErfGLPGWAVASSFGNMMSKEKREAvSKEDLArATLITITNN-IGSIARMCALNENINQVVFVGNFLRINTIAMRL 533
Cdd:PRK13317 167 KGPLP--PIPGDLTASNFGKVLHHLDSEF-TSSDIL-AGVIGLVGEvITTLSIQAAREKNIENIVYIGSTLTNNPLLQEI 242
                        330       340       350
                 ....*....|....*....|....*....|.
gi 85838513  534 LAyalDYWSKGQLKALFSEHEGYFGAVGALL 564
Cdd:PRK13317 243 IE---SYTKLRNCTPIFLENGGYSGAIGALL 270
PanK COG5146
Pantothenate kinase [Coenzyme transport and metabolism]; Pantothenate kinase is part of the ...
215-564 1.49e-35

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: 134.25  E-value: 1.49e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513 215 GLDIGGTLVKLVYFEpkditaeeeeeeveslksirkyltsnvaygstgirdvhlelkdltlcgrKGNLHFIRFPTHDMPA 294
Cdd:COG5146   5 GIDAGGTLTKIAYLE-------------------------------------------------DGERRYKKFPSDEIES 35
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513 295 FIQ-MGRDKNFSSLhtvfCATGGGAyKFEQDFLTIGDLQlcKLDELDCLIKGILYIdsvgfngrsqcyyfenpadsekcq 373
Cdd:COG5146  36 VADwLNKFINIEKI----GLTGGRA-EVLAEKLNGDPKQ--YIVEFDATGKGVRYL------------------------ 84
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513 374 kLPFDLKNPYPLLLVNIGSGVSIlaVYSKDN-YKRVTGTSLGGGTFFGLCCLLTGCTTFEEALEMASRGDSTKVDKLVRD 452
Cdd:COG5146  85 -LKEEGHDIDKFIITNVGTGTSI--HYMDGDtQERVGGTGVGGGTLMGLSYLLTGISDFEEIVELAKKGDRDGIDLKVKD 161
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513 453 IYGGDYErfGLPGWAVASSFGNMMSKEKREAvSKEDLARATLITITNNIGSIARMCALNENINQVVFVGNFLRINTIAMR 532
Cdd:COG5146 162 IYEGMEP--PIPGDLTASNFGKVLITLDESA-TKEDILAAIIGLVGETITTLSIQAAEEYDTETIVYIGSTLTNNPLLQE 238
                       330       340       350
                ....*....|....*....|....*....|..
gi 85838513 533 LLAyalDYWSKGQLKALFSEHEGYFGAVGALL 564
Cdd:COG5146 239 VIE---SYTILRGKKPIFLENGEFSGAIGALL 267
PTZ00297 PTZ00297
pantothenate kinase; Provisional
161-562 3.84e-34

pantothenate kinase; Provisional


Pssm-ID: 140318 [Multi-domain]  Cd Length: 1452  Bit Score: 138.45  E-value: 3.84e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513   161 EPLRRRASSASVPAVGASAEGTRRDrlgSYSGPTSVSRQRVESLRKkrPLfpwfGLDIGGTLVKLVYFEPKDITAeeeee 240
Cdd:PTZ00297  998 ERFYSDVETTPLPTPCADLQEDVSD---VESSGTKLSSDCDFSLQV--PV----TIDIGGTFAKIAYVQPPGGFA----- 1063
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513   241 eveslksIRKYLTSNVAYGST--GIRDVHL---------ELKDLTLcGRKGNLHFIRFPTHDMPAF------IQMgrDKN 303
Cdd:PTZ00297 1064 -------FPTYIVHEASSLSEklGLRTFHFfadaeaaesELRTRPH-SRVGTLRFAKIPSKQIPDFadylagSHA--INY 1133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513   304 FS-SLHTVFCATGGGAYKFEQDFLTIGDLQLCKLDELDCLIKGILYIDSVGfngrSQCYYFENPADSE----KCQKLPFD 378
Cdd:PTZ00297 1134 YKpQYRTKVRATGGGAFKYASVAKKVLGINFSVMREMDAVVKGLNLVIRVA----PESIFTVDPSTGVhhphQLVSPPGD 1209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513   379 LKNPYPLLLVNIGSGVSILAVYSKD-NYKRVTGTSLGGGTFFGLCCLLTGCTTFEEALE---MASRGDSTKVDKLVRDIY 454
Cdd:PTZ00297 1210 GFSPFPCLLVNIGSGISIIKCLGPDgSHVRVGGSPIGGATFWGLVRTMTNVTSWEEVMEimrLDGPGDNKNVDLLVGDIY 1289
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513   455 GgdYERFGLPGW----AVASSFGNMMSKEKRE-----------------------------------------AVSKEDL 489
Cdd:PTZ00297 1290 G--YNAKDLPAMlsvdTVASTFGKLGTERFYEmmrgvstahfsdddaageilspkalksptviselpvrngtkKASAIDI 1367
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 85838513   490 ARATLITITNNIGSIARMCALNENINQVVFVGNFLRINTIAMRLLAYALDYWSKGQLKALFSEHEGYFGAVGA 562
Cdd:PTZ00297 1368 VRSLLNMISSNVTQLAYLHSRVQGVPNIFFAGGFVRDNPIIWSHISSTMKYWSKGECHAHFLEHDGYLGALGC 1440
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
8-209 7.81e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.47  E-value: 7.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513     8 HPRVHWAAPPSLSSGLHRLLFLRG--TRIPSSTTLSPPRH--------DSLSLDGGTVNPPRVREPTGREAFGPSPASSD 77
Cdd:PHA03307  676 PPRALEACPARLESWLRELRDLRDavYLARLRGDLPVAGGreervaavRAVSLVARTVAPLVRYSPRRARARASAWDITD 755
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85838513    78 WLPARWRngrgGRPrARLCSGWTAAEEARRNPTLGGLLGRQRLLLRMGGGRLGAPMERHGRASATSVSSAGEQAAGDPEG 157
Cdd:PHA03307  756 ALFSNPS----LVP-AKLAEALALLEPAEPQRGAGSSPPVRAEAAFRRPGRLRRSGPAADAASRTASKRKSRSHTPDGGS 830
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 85838513   158 RRQEPLRRRASSASVPAVGASAEGTRRDRLGSYSGPTSVSRQRVESLRKKRP 209
Cdd:PHA03307  831 ESSGPARPPGAAARPPPARSSESSKSKPAAAGGRARGKNGRRRPRPPEPRAR 882
 
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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