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Conserved domains on  [gi|1426138158|ref|NP_060686|]
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4'-phosphopantetheine phosphatase [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ASKHA_NBD_PanK-II_Pank4 cd24123
nucleotide-binding domain (NBD) of pantothenate kinase 4 (Pank4) from type II pantothenate ...
36-366 0e+00

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: 645.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158  36 RFAIDIGGSLTKLAYYSTVQHKVAKVRSFDHSGKdtEREHEPPYEISVQEEITARLHFIKFENTYIEACLDFIKDHLV-- 113
Cdd:cd24123     1 HFAIDIGGSLAKLVYFSRVSDKAASVSSSSGTSK--GPSDEPLYEVSEQPELGGRLHFVKFETKYIEECLDFIKDNLLhs 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 114 ---NTETKVIQATGGGAYKFKDLIEEKLRLKVDKEDVMTCLIKGCNFVLKNIPHEAFVYQKDSDPEFRFQTNHPHIFPYL 190
Cdd:cd24123    79 rqgNKRGKVIKATGGGAYKYADLIKEKLGVEVDKEDEMECLIKGCNFLLKNIPDEVFTYDEHAKPEVKFQSDPPDIFPYL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 191 LVNIGSGVSIVKVETEDRFEWVGGSSIGGGTFWGLGALLTKTKKFDELLHLASRGQHSNVDMLVRDVYGGAHQTLGLSGN 270
Cdd:cd24123   159 LVNIGSGVSILKVDSEDKFERVGGTSLGGGTFWGLGSLLTGAKSFDELLELAEKGDNRNVDMLVGDIYGGDYSKIGLKSD 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 271 LIASSFGKSATAD-----QEFSKEDMAKSLLHMISNDIGQLACLHARLHSLDRVYFGGFFIRGHPVTMRTITYSINFFSK 345
Cdd:cd24123   239 TIASSFGKVARADkdarlEDFSPEDIAKSLLRMISNNIGQIAYLNAKLHGLKRIYFGGFFIRGHPLTMHTISYAINFWSK 318
                         330       340
                  ....*....|....*....|.
gi 1426138158 346 GEVQALFLRHEGYLGAIGAFL 366
Cdd:cd24123   319 GEMQALFLRHEGYLGAIGAFL 339
PLN02902 super family cl27475
pantothenate kinase
17-771 0e+00

pantothenate kinase


The actual alignment was detected with superfamily member PLN02902:

Pssm-ID: 215489 [Multi-domain]  Cd Length: 876  Bit Score: 616.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158  17 DKSITLPPDEifrnlENAKRFAIDIGGSLTKLAYYSTVQHkvakvRSFDHSGKDTERE-------HEPPYEIsvqeeITA 89
Cdd:PLN02902   41 DPTILLPNQS-----DDISHLALDIGGSLIKLVYFSRHED-----RSTDDKRKRTIKErlgitngNRRSYPI-----LGG 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158  90 RLHFIKFENTYIEACLDFIKD--------HLVNTETK-----VIQATGGGAYKFKDLIEEKLRLKVDKEDVMTCLIKGCN 156
Cdd:PLN02902  106 RLHFVKFETSKINECLDFISSkqlhrggiHSWLSKAPpngngVIKATGGGAYKFADLFKERLGVSLDKEDEMDCLVAGAN 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 157 FVLKNIPHEAFVYQkDSDPEFrFQTNHPHIFPYLLVNIGSGVSIVKVETEDRFEWVGGSSIGGGTFWGLGALLTKTKKFD 236
Cdd:PLN02902  186 FLLKAIRHEAFTHM-EGEKEF-VQIDQNDLFPYLLVNIGSGVSMIKVDGDGKFERVSGTNVGGGTYWGLGRLLTKCKSFD 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 237 ELLHLASRGQHSNVDMLVRDVYGGA-HQTLGLSGNLIASSFGKSATADQEFS---KEDMAKSLLHMISNDIGQLACLHAR 312
Cdd:PLN02902  264 ELLELSQRGDNSAIDMLVGDIYGGMdYSKIGLSASTIASSFGKVISENKELSdyrPEDISLSLLRMISYNIGQISYLNAL 343
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 313 LHSLDRVYFGGFFIRGHPVTMRTITYSINFFSKGEVQALFLRHEGYLGAIGAFLK------------------------- 367
Cdd:PLN02902  344 RFGLKRIFFGGFFIRGHAYTMDTISFAVHFWSKGEAQAMFLRHEGFLGALGAFMSyekhglddlmahqlverfpmgapyt 423
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 368 GAEQDNP------NQYSWGENYAGSSGLMSASPELGPAQRARSGTF-------DLLEMD---------RLERPLVDLPLL 425
Cdd:PLN02902  424 GGNIHGPplgdlnEKISWMEKFVQKGTEITAPVPMGPPGTTGLGGFevpssrgGSLRSDasalnvgvlHLVPTLEVFPLL 503
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 426 LDPPSYVPDTVDLTDDAlARKYWLTCFEEALDGVVKRAVASQPDSVDAAERAEKFRQKYWNKLQTLRQQPFAYGTLTVRS 505
Cdd:PLN02902  504 ADPKTYEPNTIDLSDQS-EREYWFKVLSEHLPDLVDKAVASEGGTDDAKRRGDAFARAFSAHLARLMEEPAAYGKLGLAN 582
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 506 LLDTREHCLNEFNFPDPYSKVKQRENGVALRCFPGVVRSLDALGWEERQLALVKGLLAGNVFDWGAKAVSAVLESDPYFG 585
Cdd:PLN02902  583 LLELREECLREFHFVDAYRSIKQRENEASLAVLPDLLAELDSMTEETRLLTLIEGVLAANIFDWGSRACVELYHKGTIIE 662
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 586 FEEAKRKLQERPWLVDSYSEWLQRLKGP------PHKCALIFADNSGIDIILGVFPFVRELLLRGTEVILACNSGPALND 659
Cdd:PLN02902  663 IYRMSRNKMQRPWRVDDFDAFKERMLGSggkkpkPHKRALLFVDNSGADVVLGMLPLARELLRRGTEVVLVANSLPALND 742
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 660 VTHSE-SLIVAE-----------RIAG---MDPVVHSALQEE------RLLLVQTGSSSPCLDLSRLDKGLAALVRErgA 718
Cdd:PLN02902  743 VTAMElPDIVAEaakhcdilrraAEAGgllVDAMVNTDDGSKddstsvPLMVVENGCGSPCIDLRQVSSELAAAAKD--A 820
                         810       820       830       840       850
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1426138158 719 DLVVIEGMGRAVHTNYHAALRCESLKLAVIKNAWLAERL-GGRLFSVIFKYEVP 771
Cdd:PLN02902  821 DLIVLEGMGRALHTNFNARFKCEALKLAMVKNQRLAEKLiNGNIYDCVCRYEPA 874
 
Name Accession Description Interval E-value
ASKHA_NBD_PanK-II_Pank4 cd24123
nucleotide-binding domain (NBD) of pantothenate kinase 4 (Pank4) from type II pantothenate ...
36-366 0e+00

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: 645.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158  36 RFAIDIGGSLTKLAYYSTVQHKVAKVRSFDHSGKdtEREHEPPYEISVQEEITARLHFIKFENTYIEACLDFIKDHLV-- 113
Cdd:cd24123     1 HFAIDIGGSLAKLVYFSRVSDKAASVSSSSGTSK--GPSDEPLYEVSEQPELGGRLHFVKFETKYIEECLDFIKDNLLhs 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 114 ---NTETKVIQATGGGAYKFKDLIEEKLRLKVDKEDVMTCLIKGCNFVLKNIPHEAFVYQKDSDPEFRFQTNHPHIFPYL 190
Cdd:cd24123    79 rqgNKRGKVIKATGGGAYKYADLIKEKLGVEVDKEDEMECLIKGCNFLLKNIPDEVFTYDEHAKPEVKFQSDPPDIFPYL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 191 LVNIGSGVSIVKVETEDRFEWVGGSSIGGGTFWGLGALLTKTKKFDELLHLASRGQHSNVDMLVRDVYGGAHQTLGLSGN 270
Cdd:cd24123   159 LVNIGSGVSILKVDSEDKFERVGGTSLGGGTFWGLGSLLTGAKSFDELLELAEKGDNRNVDMLVGDIYGGDYSKIGLKSD 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 271 LIASSFGKSATAD-----QEFSKEDMAKSLLHMISNDIGQLACLHARLHSLDRVYFGGFFIRGHPVTMRTITYSINFFSK 345
Cdd:cd24123   239 TIASSFGKVARADkdarlEDFSPEDIAKSLLRMISNNIGQIAYLNAKLHGLKRIYFGGFFIRGHPLTMHTISYAINFWSK 318
                         330       340
                  ....*....|....*....|.
gi 1426138158 346 GEVQALFLRHEGYLGAIGAFL 366
Cdd:cd24123   319 GEMQALFLRHEGYLGAIGAFL 339
PLN02902 PLN02902
pantothenate kinase
17-771 0e+00

pantothenate kinase


Pssm-ID: 215489 [Multi-domain]  Cd Length: 876  Bit Score: 616.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158  17 DKSITLPPDEifrnlENAKRFAIDIGGSLTKLAYYSTVQHkvakvRSFDHSGKDTERE-------HEPPYEIsvqeeITA 89
Cdd:PLN02902   41 DPTILLPNQS-----DDISHLALDIGGSLIKLVYFSRHED-----RSTDDKRKRTIKErlgitngNRRSYPI-----LGG 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158  90 RLHFIKFENTYIEACLDFIKD--------HLVNTETK-----VIQATGGGAYKFKDLIEEKLRLKVDKEDVMTCLIKGCN 156
Cdd:PLN02902  106 RLHFVKFETSKINECLDFISSkqlhrggiHSWLSKAPpngngVIKATGGGAYKFADLFKERLGVSLDKEDEMDCLVAGAN 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 157 FVLKNIPHEAFVYQkDSDPEFrFQTNHPHIFPYLLVNIGSGVSIVKVETEDRFEWVGGSSIGGGTFWGLGALLTKTKKFD 236
Cdd:PLN02902  186 FLLKAIRHEAFTHM-EGEKEF-VQIDQNDLFPYLLVNIGSGVSMIKVDGDGKFERVSGTNVGGGTYWGLGRLLTKCKSFD 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 237 ELLHLASRGQHSNVDMLVRDVYGGA-HQTLGLSGNLIASSFGKSATADQEFS---KEDMAKSLLHMISNDIGQLACLHAR 312
Cdd:PLN02902  264 ELLELSQRGDNSAIDMLVGDIYGGMdYSKIGLSASTIASSFGKVISENKELSdyrPEDISLSLLRMISYNIGQISYLNAL 343
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 313 LHSLDRVYFGGFFIRGHPVTMRTITYSINFFSKGEVQALFLRHEGYLGAIGAFLK------------------------- 367
Cdd:PLN02902  344 RFGLKRIFFGGFFIRGHAYTMDTISFAVHFWSKGEAQAMFLRHEGFLGALGAFMSyekhglddlmahqlverfpmgapyt 423
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 368 GAEQDNP------NQYSWGENYAGSSGLMSASPELGPAQRARSGTF-------DLLEMD---------RLERPLVDLPLL 425
Cdd:PLN02902  424 GGNIHGPplgdlnEKISWMEKFVQKGTEITAPVPMGPPGTTGLGGFevpssrgGSLRSDasalnvgvlHLVPTLEVFPLL 503
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 426 LDPPSYVPDTVDLTDDAlARKYWLTCFEEALDGVVKRAVASQPDSVDAAERAEKFRQKYWNKLQTLRQQPFAYGTLTVRS 505
Cdd:PLN02902  504 ADPKTYEPNTIDLSDQS-EREYWFKVLSEHLPDLVDKAVASEGGTDDAKRRGDAFARAFSAHLARLMEEPAAYGKLGLAN 582
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 506 LLDTREHCLNEFNFPDPYSKVKQRENGVALRCFPGVVRSLDALGWEERQLALVKGLLAGNVFDWGAKAVSAVLESDPYFG 585
Cdd:PLN02902  583 LLELREECLREFHFVDAYRSIKQRENEASLAVLPDLLAELDSMTEETRLLTLIEGVLAANIFDWGSRACVELYHKGTIIE 662
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 586 FEEAKRKLQERPWLVDSYSEWLQRLKGP------PHKCALIFADNSGIDIILGVFPFVRELLLRGTEVILACNSGPALND 659
Cdd:PLN02902  663 IYRMSRNKMQRPWRVDDFDAFKERMLGSggkkpkPHKRALLFVDNSGADVVLGMLPLARELLRRGTEVVLVANSLPALND 742
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 660 VTHSE-SLIVAE-----------RIAG---MDPVVHSALQEE------RLLLVQTGSSSPCLDLSRLDKGLAALVRErgA 718
Cdd:PLN02902  743 VTAMElPDIVAEaakhcdilrraAEAGgllVDAMVNTDDGSKddstsvPLMVVENGCGSPCIDLRQVSSELAAAAKD--A 820
                         810       820       830       840       850
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1426138158 719 DLVVIEGMGRAVHTNYHAALRCESLKLAVIKNAWLAERL-GGRLFSVIFKYEVP 771
Cdd:PLN02902  821 DLIVLEGMGRALHTNFNARFKCEALKLAMVKNQRLAEKLiNGNIYDCVCRYEPA 874
Fumble pfam03630
Fumble; Fumble is required for cell division in Drosophila. Mutants lacking fumble exhibit ...
37-364 8.42e-177

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: 508.96  E-value: 8.42e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158  37 FAIDIGGSLTKLAYYSTVQHKvakvrsfdhsgkdtereheppyeisvQEEITARLHFIKFENTYIEACLDFIKDHLVNTE 116
Cdd:pfam03630   1 FAIDIGGTLAKLVYFSPVPDS--------------------------PKELGGRLHFIKFETTKIEDCLEFIKSLGLNSK 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 117 TK----VIQATGGGAYKFKDLIEEKLRLKVDKEDVMTCLIKGCNFVLKNIPHEAFVYqkDSDPEFRFQT-NHPHIFPYLL 191
Cdd:pfam03630  55 GTdrglTVKATGGGAYKFYDLFKEKLGVKVDKEDEMECLIKGLNFLLTNIPDEVFTY--SDSPEYFFQTvDNNSIYPYLL 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 192 VNIGSGVSIVKVETEDRFEWVGGSSIGGGTFWGLGALLTKTKKFDELLHLASRGQHSNVDMLVRDVYGGAHQTLGLSGNL 271
Cdd:pfam03630 133 VNIGSGVSILKVEGPDKFERVGGTSLGGGTFWGLCSLLTGAKSFDEMLELAEKGDNRNVDMLVGDIYGGDYEKIGLKSDT 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 272 IASSFGKSATADQEF------SKEDMAKSLLHMISNDIGQLACLHARLHSLDRVYFGGFFIRGHPVTMRTITYSINFFSK 345
Cdd:pfam03630 213 IASSFGKVFRKKFREsasndaSPEDIARSLLYMISNNIGQIAYLNAKLHGLKRIYFGGNFIRGHPITMKTLSYAINFWSK 292
                         330
                  ....*....|....*....
gi 1426138158 346 GEVQALFLRHEGYLGAIGA 364
Cdd:pfam03630 293 GELKALFLRHEGYLGALGA 311
PLN02920 PLN02920
pantothenate kinase 1
21-366 8.98e-110

pantothenate kinase 1


Pssm-ID: 215498 [Multi-domain]  Cd Length: 398  Bit Score: 339.90  E-value: 8.98e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158  21 TLPPDEIfrnlenaKRFAIDIGGSLTKLAYYStvqhkvakvrsfdhsgKDTEREHEPPYEISVQEEIT-ARLHFIKFENT 99
Cdd:PLN02920   12 NSSPIQI-------SHLALDIGGSLIKLVYFS----------------RNSGDSEDPRNDSSVKSDGVnGRLHFAKFETR 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 100 YIEACLDFIKDHLV--------NTETK---VIQATGGGAYKFKDLIEEKLRLKVDKEDVMTCLIKGCNFVLKNIPHEAFV 168
Cdd:PLN02920   69 KINDCLEFISSNKLhhggfqhhENPTHdknFIKATGGGAYKFADLFKEKLGISLDKEDEMDCLVTGANFLLKAVHHEAFT 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 169 YQkDSDPEFrFQTNHPHIFPYLLVNIGSGVSIVKVETEDRFEWVGGSSIGGGTFWGLGALLTKTKKFDELLHLASRGQHS 248
Cdd:PLN02920  149 YL-DGQKEF-VQIDHNDLYPYLLVNIGSGVSMIKVDGDGKFERVSGTSVGGGTFWGLGKLLTKCKSFDELLELSHQGNNR 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 249 NVDMLVRDVYGGA-HQTLGLSGNLIASSFGKSATADQE---FSKEDMAKSLLHMISNDIGQLACLHARLHSLDRVYFGGF 324
Cdd:PLN02920  227 VIDMLVGDIYGGMdYSKIGLSSTTIASSFGKAISDNKEledYKPEDVARSLLRMISNNIGQISYLNALRFGLKRIFFGGF 306
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1426138158 325 FIRGHPVTMRTITYSINFFSKGEVQALFLRHEGYLGAIGAFL 366
Cdd:PLN02920  307 FIRGHSYTMDTISVAVHFWSKGEAKAMFLRHEGFLGALGAFM 348
ARMT1-like_dom pfam01937
Damage-control phosphatase ARMT1-like domain; This domain is widely distributed in all domains ...
451-760 3.70e-59

Damage-control phosphatase ARMT1-like domain; This domain is widely distributed in all domains of life and occur in stand-alone form and as C-terminal fusions to pantothenate kinase (PanK) in plants and animals. They are metal-dependent phosphatases involved in metabolic damage-control processes termed "damage pre-emption" or "housecleaning". S.cerevisiae Damage-control phosphatase YMR027W and the human orthologue Damage-control phosphatase ARMT1 (also known as C6orf211) are involved in response to DNA damage, a damage pre-emption function. Crystal structure of Damage-control phosphatase At2g17340 from Arabidopsis revealed a novel protein fold and several conserved residues coordinating a metal ion (probably Mg2+), which exhibits a high degree of conservation, suggesting that the metal-binding site is central for the function.


Pssm-ID: 396496  Cd Length: 303  Bit Score: 202.88  E-value: 3.70e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 451 CFEEALDGVVKRAVasqpDSVDAAERAEKFRQKYWNKLQTLRQQPFAYGTLT--VRSLLDTREHCLNEFNFPDPYSKVKQ 528
Cdd:pfam01937   1 TAPERLPCILTQAI----DDLELATDDEEELKKIIGELAELKAELQTDKPLPplPFAECYLYRRLLEALGNYDPFKEQKE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 529 RENGVALRCFPGVVRSLdalgwEERQLALVKGLLAGNVFDWGAKAvSAVLESDpyfgFEEAKRKLQERPWLVDSYSEWLQ 608
Cdd:pfam01937  77 LSNEKALAAVPELAERL-----EELFKELLKISLWGNAIDLGLLA-GADSQKD----QESELREALERPLLVDDTDALWE 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 609 RLKGPPHKCALIFADNSGIDIILGVFpFVRELL--LRGTEVILACNSGPALNDVTHSESLIVAERIAGMDPVVHSALQEE 686
Cdd:pfam01937 147 LLKGKRAKRVDYVLDNAGFELVFDLL-LAEFLLrsGLATKVVLHVKGIPFVNDVTMEDAEWLLEQLSALGAGLDELLALG 225
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1426138158 687 RLLLVQTGSSSPCLDLSRLDKGLAALVRErgADLVVIEGMG--RAVHTNYHAALRCESLKLAVIKNAWLAERLGGR 760
Cdd:pfam01937 226 KLIDTGSDFWTPGTDFWEMSPELYEELEK--ADLVIFKGDLnyRKLTGDRDWPPTCPILFLRTAKCDVVAGLLVGL 299
DUF89 COG1578
House-cleaning carbohydrate phosphatase, DUF89 family [Defense mechanisms];
520-767 5.62e-25

House-cleaning carbohydrate phosphatase, DUF89 family [Defense mechanisms];


Pssm-ID: 441186  Cd Length: 282  Bit Score: 105.29  E-value: 5.62e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 520 PDPYSKVKQRENGVALRCFPGVVRSLDALgwEERQLALVKGLLAGNVFDWGAKAVSavlesdpyFGFEEAKRKLQERPWL 599
Cdd:COG1578    67 DDPYKELKERSNELALELLPELKERIESS--EDPLETALKLAVAGNIIDFGVKGVS--------FDLEETIKEVLEKPFA 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 600 VDSYSEWLQRLKgpphkCA---LIFADNSG-IdiilgVF--PFVRELLLRGTEVILACNSGPALNDVTHSEslivAERiA 673
Cdd:COG1578   137 IDDTEELKERLK-----KAkrvLYLGDNAGeI-----VFdkLLIEELKKLGLEVTYAVRGGPILNDATLED----AKE-A 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 674 GMDPVVHsalqeerllLVQTGSSSPCLDLSRLDKGLAALVRErgADLVVIEGMGravhtNYhaalrcESLK--------- 744
Cdd:COG1578   202 GLDKVAR---------VITTGSDAPGTVLEECSEEFKELFDE--ADLIISKGQG-----NY------ETLSeekdkpiff 259
                         250       260
                  ....*....|....*....|...
gi 1426138158 745 LAVIKNAWLAERLGGRLFSVIFK 767
Cdd:COG1578   260 LLKAKCEVVARDLGVPVGDLVFK 282
 
Name Accession Description Interval E-value
ASKHA_NBD_PanK-II_Pank4 cd24123
nucleotide-binding domain (NBD) of pantothenate kinase 4 (Pank4) from type II pantothenate ...
36-366 0e+00

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: 645.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158  36 RFAIDIGGSLTKLAYYSTVQHKVAKVRSFDHSGKdtEREHEPPYEISVQEEITARLHFIKFENTYIEACLDFIKDHLV-- 113
Cdd:cd24123     1 HFAIDIGGSLAKLVYFSRVSDKAASVSSSSGTSK--GPSDEPLYEVSEQPELGGRLHFVKFETKYIEECLDFIKDNLLhs 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 114 ---NTETKVIQATGGGAYKFKDLIEEKLRLKVDKEDVMTCLIKGCNFVLKNIPHEAFVYQKDSDPEFRFQTNHPHIFPYL 190
Cdd:cd24123    79 rqgNKRGKVIKATGGGAYKYADLIKEKLGVEVDKEDEMECLIKGCNFLLKNIPDEVFTYDEHAKPEVKFQSDPPDIFPYL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 191 LVNIGSGVSIVKVETEDRFEWVGGSSIGGGTFWGLGALLTKTKKFDELLHLASRGQHSNVDMLVRDVYGGAHQTLGLSGN 270
Cdd:cd24123   159 LVNIGSGVSILKVDSEDKFERVGGTSLGGGTFWGLGSLLTGAKSFDELLELAEKGDNRNVDMLVGDIYGGDYSKIGLKSD 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 271 LIASSFGKSATAD-----QEFSKEDMAKSLLHMISNDIGQLACLHARLHSLDRVYFGGFFIRGHPVTMRTITYSINFFSK 345
Cdd:cd24123   239 TIASSFGKVARADkdarlEDFSPEDIAKSLLRMISNNIGQIAYLNAKLHGLKRIYFGGFFIRGHPLTMHTISYAINFWSK 318
                         330       340
                  ....*....|....*....|.
gi 1426138158 346 GEVQALFLRHEGYLGAIGAFL 366
Cdd:cd24123   319 GEMQALFLRHEGYLGAIGAFL 339
PLN02902 PLN02902
pantothenate kinase
17-771 0e+00

pantothenate kinase


Pssm-ID: 215489 [Multi-domain]  Cd Length: 876  Bit Score: 616.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158  17 DKSITLPPDEifrnlENAKRFAIDIGGSLTKLAYYSTVQHkvakvRSFDHSGKDTERE-------HEPPYEIsvqeeITA 89
Cdd:PLN02902   41 DPTILLPNQS-----DDISHLALDIGGSLIKLVYFSRHED-----RSTDDKRKRTIKErlgitngNRRSYPI-----LGG 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158  90 RLHFIKFENTYIEACLDFIKD--------HLVNTETK-----VIQATGGGAYKFKDLIEEKLRLKVDKEDVMTCLIKGCN 156
Cdd:PLN02902  106 RLHFVKFETSKINECLDFISSkqlhrggiHSWLSKAPpngngVIKATGGGAYKFADLFKERLGVSLDKEDEMDCLVAGAN 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 157 FVLKNIPHEAFVYQkDSDPEFrFQTNHPHIFPYLLVNIGSGVSIVKVETEDRFEWVGGSSIGGGTFWGLGALLTKTKKFD 236
Cdd:PLN02902  186 FLLKAIRHEAFTHM-EGEKEF-VQIDQNDLFPYLLVNIGSGVSMIKVDGDGKFERVSGTNVGGGTYWGLGRLLTKCKSFD 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 237 ELLHLASRGQHSNVDMLVRDVYGGA-HQTLGLSGNLIASSFGKSATADQEFS---KEDMAKSLLHMISNDIGQLACLHAR 312
Cdd:PLN02902  264 ELLELSQRGDNSAIDMLVGDIYGGMdYSKIGLSASTIASSFGKVISENKELSdyrPEDISLSLLRMISYNIGQISYLNAL 343
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 313 LHSLDRVYFGGFFIRGHPVTMRTITYSINFFSKGEVQALFLRHEGYLGAIGAFLK------------------------- 367
Cdd:PLN02902  344 RFGLKRIFFGGFFIRGHAYTMDTISFAVHFWSKGEAQAMFLRHEGFLGALGAFMSyekhglddlmahqlverfpmgapyt 423
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 368 GAEQDNP------NQYSWGENYAGSSGLMSASPELGPAQRARSGTF-------DLLEMD---------RLERPLVDLPLL 425
Cdd:PLN02902  424 GGNIHGPplgdlnEKISWMEKFVQKGTEITAPVPMGPPGTTGLGGFevpssrgGSLRSDasalnvgvlHLVPTLEVFPLL 503
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 426 LDPPSYVPDTVDLTDDAlARKYWLTCFEEALDGVVKRAVASQPDSVDAAERAEKFRQKYWNKLQTLRQQPFAYGTLTVRS 505
Cdd:PLN02902  504 ADPKTYEPNTIDLSDQS-EREYWFKVLSEHLPDLVDKAVASEGGTDDAKRRGDAFARAFSAHLARLMEEPAAYGKLGLAN 582
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 506 LLDTREHCLNEFNFPDPYSKVKQRENGVALRCFPGVVRSLDALGWEERQLALVKGLLAGNVFDWGAKAVSAVLESDPYFG 585
Cdd:PLN02902  583 LLELREECLREFHFVDAYRSIKQRENEASLAVLPDLLAELDSMTEETRLLTLIEGVLAANIFDWGSRACVELYHKGTIIE 662
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 586 FEEAKRKLQERPWLVDSYSEWLQRLKGP------PHKCALIFADNSGIDIILGVFPFVRELLLRGTEVILACNSGPALND 659
Cdd:PLN02902  663 IYRMSRNKMQRPWRVDDFDAFKERMLGSggkkpkPHKRALLFVDNSGADVVLGMLPLARELLRRGTEVVLVANSLPALND 742
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 660 VTHSE-SLIVAE-----------RIAG---MDPVVHSALQEE------RLLLVQTGSSSPCLDLSRLDKGLAALVRErgA 718
Cdd:PLN02902  743 VTAMElPDIVAEaakhcdilrraAEAGgllVDAMVNTDDGSKddstsvPLMVVENGCGSPCIDLRQVSSELAAAAKD--A 820
                         810       820       830       840       850
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1426138158 719 DLVVIEGMGRAVHTNYHAALRCESLKLAVIKNAWLAERL-GGRLFSVIFKYEVP 771
Cdd:PLN02902  821 DLIVLEGMGRALHTNFNARFKCEALKLAMVKNQRLAEKLiNGNIYDCVCRYEPA 874
Fumble pfam03630
Fumble; Fumble is required for cell division in Drosophila. Mutants lacking fumble exhibit ...
37-364 8.42e-177

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: 508.96  E-value: 8.42e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158  37 FAIDIGGSLTKLAYYSTVQHKvakvrsfdhsgkdtereheppyeisvQEEITARLHFIKFENTYIEACLDFIKDHLVNTE 116
Cdd:pfam03630   1 FAIDIGGTLAKLVYFSPVPDS--------------------------PKELGGRLHFIKFETTKIEDCLEFIKSLGLNSK 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 117 TK----VIQATGGGAYKFKDLIEEKLRLKVDKEDVMTCLIKGCNFVLKNIPHEAFVYqkDSDPEFRFQT-NHPHIFPYLL 191
Cdd:pfam03630  55 GTdrglTVKATGGGAYKFYDLFKEKLGVKVDKEDEMECLIKGLNFLLTNIPDEVFTY--SDSPEYFFQTvDNNSIYPYLL 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 192 VNIGSGVSIVKVETEDRFEWVGGSSIGGGTFWGLGALLTKTKKFDELLHLASRGQHSNVDMLVRDVYGGAHQTLGLSGNL 271
Cdd:pfam03630 133 VNIGSGVSILKVEGPDKFERVGGTSLGGGTFWGLCSLLTGAKSFDEMLELAEKGDNRNVDMLVGDIYGGDYEKIGLKSDT 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 272 IASSFGKSATADQEF------SKEDMAKSLLHMISNDIGQLACLHARLHSLDRVYFGGFFIRGHPVTMRTITYSINFFSK 345
Cdd:pfam03630 213 IASSFGKVFRKKFREsasndaSPEDIARSLLYMISNNIGQIAYLNAKLHGLKRIYFGGNFIRGHPITMKTLSYAINFWSK 292
                         330
                  ....*....|....*....
gi 1426138158 346 GEVQALFLRHEGYLGAIGA 364
Cdd:pfam03630 293 GELKALFLRHEGYLGALGA 311
ASKHA_NBD_PanK-II_euk cd24086
nucleotide-binding domain (NBD) of type II pantothenate kinase (PanK-II) and similar proteins ...
36-366 2.74e-142

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: 421.30  E-value: 2.74e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158  36 RFAIDIGGSLTKLAYYSTVQHKVAKVRSFDHSgkdtereheppyEISVQEEITARLHFIKFENTYIEACLDFIKDHL--V 113
Cdd:cd24086     1 RLGLDIGGTLAKLAYLTPIDIDEAEEKESVLL------------KLLANSGEDGELHFISFPNKDLEEFLNFLRDKNfeD 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 114 NTETKVIQATGGGAYKFKDLIEEKLRLKVDKEDVMTCLIKGCNFVLKN-IPHEAFVYQKDSDPEFR--FQTNHPHIFPYL 190
Cdd:cd24086    69 SSKGKVLYATGGGAYKYAELIEETLGVQLVKVDEMDSLVNGLHFLLSVlSKDECFPFPNDSGPEFLqkDPQLSDDLFPCL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 191 LVNIGSGVSIVKVETEDRFEWVGGSSIGGGTFWGLGALLTKTKKFDELLHLASRGQHSNVDMLVRDVYGGAHQTLGLSGN 270
Cdd:cd24086   149 LVNIGSGVSILKVDSDGKYERVSGTSLGGGTFLGLASLLTGTNSFDELLELASRGDRANVDLLVRDIYGGDYPYLGLPGD 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 271 LIASSFGKSATADQ---EFSKEDMAKSLLHMISNDIGQLACLHARLHSLDRVYFGGFFIRGHPVTMRTITYSINFFSKGE 347
Cdd:cd24086   229 LLASSFGKLADDEKsreDFSKEDIARSLLRMIVNNIGYLAYLVAKLHNVKRVFFTGNFIRNNELARKLIAEALNYWSKGS 308
                         330
                  ....*....|....*....
gi 1426138158 348 VQALFLRHEGYLGAIGAFL 366
Cdd:cd24086   309 LNALFLRHDGYLGALGALL 327
ASKHA_NBD_PanK-II_Pank1-like cd24122
nucleotide-binding domain (NBD) of the pantothenate kinase 1 (Pank1)-like subfamily; PanK (EC ...
37-366 5.35e-126

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: 378.40  E-value: 5.35e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158  37 FAIDIGGSLTKLAYYstvqhkvakvrsfdhsgkdterehEPpyeisvqeeiTARLHFIKFENTYIEACLDFIKDHLVNTE 116
Cdd:cd24122     2 FGLDIGGTLVKLVYF------------------------EP----------TGTLHFIRFETSRMEGFIQLAREKNLSSL 47
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 117 TKVIQATGGGAYKFKDLIEEKLRLKVDKEDVMTCLIKGCNFVLKNIPHEAFVYQKDSDPEFR----FQTNHPHIFPYLLV 192
Cdd:cd24122    48 IKTVCATGGGAYKFEKLFREELGLQLHKLDELDCLIRGINFLLRHVPDECYYFENPSDPELCekrvVPFDFSDPYPYLLV 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 193 NIGSGVSIVKVETEDRFEWVGGSSIGGGTFWGLGALLTKTKKFDELLHLASRGQHSNVDMLVRDVYGGAHQTLGLSGNLI 272
Cdd:cd24122   128 NIGSGVSILAVESPDNYERVSGTSLGGGTFLGLCCLLTGCETFEEALELAAKGDSTKVDMLVGDIYGGDYEKFGLPGDTV 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 273 ASSFGKSATAD--QEFSKEDMAKSLLHMISNDIGQLACLHARLHSLDRVYFGGFFIRGHPVTMRTITYSINFFSKGEVQA 350
Cdd:cd24122   208 ASSFGKMVAKEkrESASKEDLARALLVMITNNIGSIARLCAKNEGIKRVVFVGNFLRHNPIAMRLLAYAMDYWSKGEMKA 287
                         330
                  ....*....|....*.
gi 1426138158 351 LFLRHEGYLGAIGAFL 366
Cdd:cd24122   288 LFLEHEGYFGALGALL 303
PLN02920 PLN02920
pantothenate kinase 1
21-366 8.98e-110

pantothenate kinase 1


Pssm-ID: 215498 [Multi-domain]  Cd Length: 398  Bit Score: 339.90  E-value: 8.98e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158  21 TLPPDEIfrnlenaKRFAIDIGGSLTKLAYYStvqhkvakvrsfdhsgKDTEREHEPPYEISVQEEIT-ARLHFIKFENT 99
Cdd:PLN02920   12 NSSPIQI-------SHLALDIGGSLIKLVYFS----------------RNSGDSEDPRNDSSVKSDGVnGRLHFAKFETR 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 100 YIEACLDFIKDHLV--------NTETK---VIQATGGGAYKFKDLIEEKLRLKVDKEDVMTCLIKGCNFVLKNIPHEAFV 168
Cdd:PLN02920   69 KINDCLEFISSNKLhhggfqhhENPTHdknFIKATGGGAYKFADLFKEKLGISLDKEDEMDCLVTGANFLLKAVHHEAFT 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 169 YQkDSDPEFrFQTNHPHIFPYLLVNIGSGVSIVKVETEDRFEWVGGSSIGGGTFWGLGALLTKTKKFDELLHLASRGQHS 248
Cdd:PLN02920  149 YL-DGQKEF-VQIDHNDLYPYLLVNIGSGVSMIKVDGDGKFERVSGTSVGGGTFWGLGKLLTKCKSFDELLELSHQGNNR 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 249 NVDMLVRDVYGGA-HQTLGLSGNLIASSFGKSATADQE---FSKEDMAKSLLHMISNDIGQLACLHARLHSLDRVYFGGF 324
Cdd:PLN02920  227 VIDMLVGDIYGGMdYSKIGLSSTTIASSFGKAISDNKEledYKPEDVARSLLRMISNNIGQISYLNALRFGLKRIFFGGF 306
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1426138158 325 FIRGHPVTMRTITYSINFFSKGEVQALFLRHEGYLGAIGAFL 366
Cdd:PLN02920  307 FIRGHSYTMDTISVAVHFWSKGEAKAMFLRHEGFLGALGAFM 348
ASKHA_NBD_PanK-II_Pank1 cd24135
nucleotide-binding domain (NBD) of pantothenate kinase 1 (Pank1) from type II pantothenate ...
37-366 2.81e-67

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: 226.42  E-value: 2.81e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158  37 FAIDIGGSLTKLAYYS-------TVQHKVAKVRSFDHS-------GKDTEREHEPPYEISVQEEITARLHFIKFENTYIE 102
Cdd:cd24135     2 FGMDIGGTLVKLVYFEpkditaeEEQEEVENLKSIRKYltsntayGKTGIRDVHLELKNLTMCGRKGNLHFIRFPSCAMH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 103 ACLDFIKDHLVNTETKVIQATGGGAYKFKDLIEEKLRLKVDKEDVMTCLIKGCNFVLK---NIPHEAFVYQKDSDPEF-- 177
Cdd:cd24135    82 RFIQMGSEKNFSSLHTTLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSvgfNGQPECYYFENPTDPEQcq 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 178 --RFQTNHPhiFPYLLVNIGSGVSIVKVETEDRFEWVGGSSIGGGTFWGLGALLTKTKKFDELLHLASRGQHSNVDMLVR 255
Cdd:cd24135   162 kkPYCLDNP--YPMLLVNIGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALEMAAKGDSTNVDKLVK 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 256 DVYGGAHQTLGLSGNLIASSFGKSATADQE--FSKEDMAKSLLHMISNDIGQLACLHARLHSLDRVYFGGFFIRGHPVTM 333
Cdd:cd24135   240 DIYGGDYERFGLQGSAVASSFGHMMSKEKRdsISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINMVSM 319
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1426138158 334 RTITYSINFFSKGEVQALFLRHEGYLGAIGAFL 366
Cdd:cd24135   320 KLLAYAMDFWSKGQLKALFLEHEGYFGAVGALL 352
ASKHA_NBD_PanK-II_Pank2 cd24136
nucleotide-binding domain (NBD) of pantothenate kinase 2 (Pank2) from type II pantothenate ...
37-367 2.56e-64

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: 218.71  E-value: 2.56e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158  37 FAIDIGGSLTKLAYYS----TVQHKVAKVRSFDHSGK----DTEREHEPPYEISVQ-EEIT-----ARLHFIKFENTYIE 102
Cdd:cd24136     2 FGLDIGGTLVKLVYFEpkdiTAEEEEEEVENLKSIRKyltsNVAYGSTGIRDVHLElKDLTlcgrkGNLHFIRFPTHDMP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 103 ACLDFIKDHLVNTETKVIQATGGGAYKFKDLIEEKLRLKVDKEDVMTCLIKGCNFVLK---NIPHEAFVYQKDSDPE--- 176
Cdd:cd24136    82 AFIQMGRDKHFSSLHTTLCATGGGAYKFEQDFLTMGDLQLCKLDELDCLIKGVLYIDSvgfNGHSECYYFENPTDSEkcq 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 177 -FRFQTNHPhiFPYLLVNIGSGVSIVKVETEDRFEWVGGSSIGGGTFWGLGALLTKTKKFDELLHLASRGQHSNVDMLVR 255
Cdd:cd24136   162 kLPFNLKNP--YPLLLVNIGSGVSILAVYSKDNYKRVTGTSLGGGTFFGLCCLLTGCTTFEEALEMASRGDSTKVDKLVR 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 256 DVYGGAHQTLGLSGNLIASSFGK--SATADQEFSKEDMAKSLLHMISNDIGQLACLHARLHSLDRVYFGGFFIRGHPVTM 333
Cdd:cd24136   240 DIYGGDYERFGLPGWAVASSFGNmmSKEKREAVSKEDLARATLITITNNIGSIARMCALNENINRVVFVGNFLRINTISM 319
                         330       340       350
                  ....*....|....*....|....*....|....
gi 1426138158 334 RTITYSINFFSKGEVQALFLRHEGYLGAIGAFLK 367
Cdd:cd24136   320 RLLAYALDYWSKGQLKALFLEHEGYFGAVGALLE 353
ASKHA_NBD_PanK-II_Pank3 cd24137
nucleotide-binding domain (NBD) of pantothenate kinase 3 (Pank3) from type II pantothenate ...
37-366 7.76e-62

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: 211.79  E-value: 7.76e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158  37 FAIDIGGSLTKLAYYSTV-------QHKVAKVRSFDHS-------GKDTEREHEPPYEISVQEEITARLHFIKFENTYIE 102
Cdd:cd24137     2 FGMDIGGTLVKLSYFEPIditaeeeQEEVESLKSIRKYltsnvayGSTGIRDVHLELKDLTLFGRRGNLHFIRFPTQDLP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 103 ACLDFIKDHLVNTETKVIQATGGGAYKFKDLIEEKLRLKVDKEDVMTCLIKGCNFVLK---NIPHEAFVYQKDSDPE--- 176
Cdd:cd24137    82 TFIQMGRDKNFSTLQTVLCATGGGAYKFEKDFRTIGNLHLHKLDELDCLVKGLLYIDSvsfNGQAECYYFANASEPErcq 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 177 -FRFQTNHPhiFPYLLVNIGSGVSIVKVETEDRFEWVGGSSIGGGTFWGLGALLTKTKKFDELLHLASRGQHSNVDMLVR 255
Cdd:cd24137   162 kMPFNLDDP--YPLLVVNIGSGVSILAVHSKDNYKRVTGTSLGGGTFLGLCSLLTGCESFEEALEMASKGDSTQADKLVR 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 256 DVYGGAHQTLGLSGNLIASSFGKSATADQE--FSKEDMAKSLLHMISNDIGQLACLHARLHSLDRVYFGGFFIRGHPVTM 333
Cdd:cd24137   240 DIYGGDYERFGLPGWAVASSFGNMIYKEKResVSKEDLARATLVTITNNIGSVARMCAVNEKINRVVFVGNFLRVNTLSM 319
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1426138158 334 RTITYSINFFSKGEVQALFLRHEGYLGAIGAFL 366
Cdd:cd24137   320 KLLAYALDYWSKGQLKALFLEHEGYFGAVGALL 352
ASKHA_NBD_PanK-II cd24016
nucleotide-binding domain (NBD) of type II pantothenate kinase (PanK-II) and similar proteins; ...
37-366 7.92e-61

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: 207.12  E-value: 7.92e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158  37 FAIDIGGSLTKLAYYstvqhkvakvrsfdhsgkdtereheppyeisvqeeitarLHFIKFENTYIEACLDFIKDHLVNTE 116
Cdd:cd24016     2 FGIDIGGTLVKLVYF---------------------------------------LHFIRFPTDQVVEFIQMGQDKNFSTL 42
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 117 TKVIQATGGGAYKFKDLIEEKLRLKVDKEDVMTCLIKGCNFVLK---NIPHEAFVYQKDSDPEF--RFQTNHPHIFPYLL 191
Cdd:cd24016    43 ITKLCATGGGAGKFEEDFRTIGNLPLQKLDELDCLSQGLLYLDSvqfNGQAECYYFANASEPERcqKMPFNLHDPYPYLF 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 192 VNIGSGVSIVKVETEDRFEWVGGSSIGGGTFWGLGALLTKTKKFDELLHLASRGQHSNVDMLVRDVYGGAHQTLGLSGNL 271
Cdd:cd24016   123 VNVGSGVSILAVDSKDNYKRVTGTSLGGGTFQGLCYLLTGCTDFEEALEMAQHGDSTTIDKLVRDIYGGDYERFGLPGDA 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 272 IASSFGK--SATADQEFSKEDMAKSLLHMISNDIGQLACLHARLHSLDRVYFGGFFIRGHPVTMRTITYSINFFSKGEVQ 349
Cdd:cd24016   203 VASSFGNmlHKEKRADFSKEDLARATLGTITNNIGSMARMCARNEKIENVVFVGNFLRNNALLMKLLAYATDLWSKGQLK 282
                         330
                  ....*....|....*..
gi 1426138158 350 ALFLRHEGYLGAIGAFL 366
Cdd:cd24016   283 ALFVEHEGYFGAVGALL 299
ARMT1-like_dom pfam01937
Damage-control phosphatase ARMT1-like domain; This domain is widely distributed in all domains ...
451-760 3.70e-59

Damage-control phosphatase ARMT1-like domain; This domain is widely distributed in all domains of life and occur in stand-alone form and as C-terminal fusions to pantothenate kinase (PanK) in plants and animals. They are metal-dependent phosphatases involved in metabolic damage-control processes termed "damage pre-emption" or "housecleaning". S.cerevisiae Damage-control phosphatase YMR027W and the human orthologue Damage-control phosphatase ARMT1 (also known as C6orf211) are involved in response to DNA damage, a damage pre-emption function. Crystal structure of Damage-control phosphatase At2g17340 from Arabidopsis revealed a novel protein fold and several conserved residues coordinating a metal ion (probably Mg2+), which exhibits a high degree of conservation, suggesting that the metal-binding site is central for the function.


Pssm-ID: 396496  Cd Length: 303  Bit Score: 202.88  E-value: 3.70e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 451 CFEEALDGVVKRAVasqpDSVDAAERAEKFRQKYWNKLQTLRQQPFAYGTLT--VRSLLDTREHCLNEFNFPDPYSKVKQ 528
Cdd:pfam01937   1 TAPERLPCILTQAI----DDLELATDDEEELKKIIGELAELKAELQTDKPLPplPFAECYLYRRLLEALGNYDPFKEQKE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 529 RENGVALRCFPGVVRSLdalgwEERQLALVKGLLAGNVFDWGAKAvSAVLESDpyfgFEEAKRKLQERPWLVDSYSEWLQ 608
Cdd:pfam01937  77 LSNEKALAAVPELAERL-----EELFKELLKISLWGNAIDLGLLA-GADSQKD----QESELREALERPLLVDDTDALWE 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 609 RLKGPPHKCALIFADNSGIDIILGVFpFVRELL--LRGTEVILACNSGPALNDVTHSESLIVAERIAGMDPVVHSALQEE 686
Cdd:pfam01937 147 LLKGKRAKRVDYVLDNAGFELVFDLL-LAEFLLrsGLATKVVLHVKGIPFVNDVTMEDAEWLLEQLSALGAGLDELLALG 225
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1426138158 687 RLLLVQTGSSSPCLDLSRLDKGLAALVRErgADLVVIEGMG--RAVHTNYHAALRCESLKLAVIKNAWLAERLGGR 760
Cdd:pfam01937 226 KLIDTGSDFWTPGTDFWEMSPELYEELEK--ADLVIFKGDLnyRKLTGDRDWPPTCPILFLRTAKCDVVAGLLVGL 299
ASKHA_NBD_PanK-II_bac cd24085
nucleotide-binding domain (NBD) of type II pantothenate kinase (PanK-II) and similar proteins ...
38-366 1.44e-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: 177.76  E-value: 1.44e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158  38 AIDIGGSLTKLAYYstvqhkvakvrsfDHSGKdtereheppyeisvqeeitarLHFIKFENTYIEACLDFIKdHLVNTET 117
Cdd:cd24085     3 GIDAGGTLTKIVLL-------------ENNGE---------------------LKFKAFDSLKIEALVKFLN-ELGINDI 47
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 118 KVIQATGGGAYKFKDLIEEklrLKVDKEDVMTCLIKGCNFVLKNIPHeafvyqkdsdpefrfqtnhphifPYLLVNIGSG 197
Cdd:cd24085    48 EKIAVTGGGASRLPENIDG---IPIVKVDEFEAIGRGALYLLGEILD-----------------------DALVVSIGTG 101
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 198 VSIVKVEtEDRFEWVGGSSIGGGTFWGLGALLTKTKKFDELLHLASRGQHSNVDMLVRDVYGGahqTLG-LSGNLIASSF 276
Cdd:cd24085   102 TSIVLAK-NGTIRHVGGTGVGGGTLLGLGKLLLGVTDYDEITELARKGDRSNVDLTVGDIYGG---GIGpLPPDLTASNF 177
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 277 GKsATADQEFSKEDMAKSLLHMISNDIGQLACLHARLHSLDRVYFGGFFIRGhPVTMRTITYSINFFskgEVQALFLRHE 356
Cdd:cd24085   178 GK-LADDNKASREDLAAALINLVGETIGTLAALAARAEGVKDIVLVGSTLRN-PLLKEVLERYTKLY---GVKPIFPENG 252
                         330
                  ....*....|
gi 1426138158 357 GYLGAIGAFL 366
Cdd:cd24085   253 EFAGAIGALL 262
PTZ00297 PTZ00297
pantothenate kinase; Provisional
38-376 1.60e-47

pantothenate kinase; Provisional


Pssm-ID: 140318 [Multi-domain]  Cd Length: 1452  Bit Score: 182.75  E-value: 1.60e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158   38 AIDIGGSLTKLAY-----YSTVQHKVAK----------VRSFDHSGKDTEREHEPPyeiSVQEEITARLHFIKFENTYIE 102
Cdd:PTZ00297  1043 TIDIGGTFAKIAYvqppgGFAFPTYIVHeasslseklgLRTFHFFADAEAAESELR---TRPHSRVGTLRFAKIPSKQIP 1119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158  103 ACLDFI-KDHLVN----TETKVIQATGGGAYKFKDLIEEKLRLKVDKEDVMTCLIKGCNFVLKNIPHEAFVYqkdsDPEf 177
Cdd:PTZ00297  1120 DFADYLaGSHAINyykpQYRTKVRATGGGAFKYASVAKKVLGINFSVMREMDAVVKGLNLVIRVAPESIFTV----DPS- 1194
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158  178 rFQTNHPH-----------IFPYLLVNIGSGVSIVKVETED-RFEWVGGSSIGGGTFWGLGALLTKTKKFDELLH---LA 242
Cdd:PTZ00297  1195 -TGVHHPHqlvsppgdgfsPFPCLLVNIGSGISIIKCLGPDgSHVRVGGSPIGGATFWGLVRTMTNVTSWEEVMEimrLD 1273
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158  243 SRGQHSNVDMLVRDVYGGAHQTLG--LSGNLIASSFGKSAT---------------ADQEFSKE---------------- 289
Cdd:PTZ00297  1274 GPGDNKNVDLLVGDIYGYNAKDLPamLSVDTVASTFGKLGTerfyemmrgvstahfSDDDAAGEilspkalksptvisel 1353
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158  290 ------------DMAKSLLHMISNDIGQLACLHARLHSLDRVYFGGFFIRGHPVTMRTITYSINFFSKGEVQALFLRHEG 357
Cdd:PTZ00297  1354 pvrngtkkasaiDIVRSLLNMISSNVTQLAYLHSRVQGVPNIFFAGGFVRDNPIIWSHISSTMKYWSKGECHAHFLEHDG 1433
                          410
                   ....*....|....*....
gi 1426138158  358 YLGAIGAFLKGAEQDNPNQ 376
Cdd:PTZ00297  1434 YLGALGCATLDPDGDAASE 1452
PRK13317 PRK13317
pantothenate kinase; Provisional
39-370 2.83e-36

pantothenate kinase; Provisional


Pssm-ID: 237346 [Multi-domain]  Cd Length: 277  Bit Score: 138.16  E-value: 2.83e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158  39 IDIGGSLTKLAYystvqhkvakvrsFDHSGKdtereheppyeisvqeeitarLHFIKFENTYIEacldFIKDHLVNTET- 117
Cdd:PRK13317    7 IDAGGTLTKIVY-------------LEEKKQ---------------------RTFKTEYSAEGK----KVIDWLINLQDi 48
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 118 KVIQATGGGAYKFKDLIeeKLRLKVDKEDVMTCLIKGCNFVLKNIPHeafvyqkdsdpefrfqtnhpHIFPYLLVNIGSG 197
Cdd:PRK13317   49 EKICLTGGKAGYLQQLL--NYGYPIAEFVEFEATGLGVRYLLKEEGH--------------------DLNDYIFTNIGTG 106
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 198 VSIVKVEtEDRFEWVGGSSIGGGTFWGLGALLTKTKKFDELLHLASRGQHSNVDMLVRDVYGGAhqTLGLSGNLIASSFG 277
Cdd:PRK13317  107 TSIHYVD-GNSQRRVGGTGIGGGTIQGLSKLLTNISDYEQLIELAKHGDRNNIDLKVGDIYKGP--LPPIPGDLTASNFG 183
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 278 K-SATADQEFSKEDMAKSLLHMISNDIGQLACLHARLHSL-DRVYFGGFF--------IRGHPVTMRTITysinffskge 347
Cdd:PRK13317  184 KvLHHLDSEFTSSDILAGVIGLVGEVITTLSIQAAREKNIeNIVYIGSTLtnnpllqeIIESYTKLRNCT---------- 253
                         330       340
                  ....*....|....*....|...
gi 1426138158 348 vqALFLRHEGYLGAIGAFLKGAE 370
Cdd:PRK13317  254 --PIFLENGGYSGAIGALLLATN 274
DUF89 COG1578
House-cleaning carbohydrate phosphatase, DUF89 family [Defense mechanisms];
520-767 5.62e-25

House-cleaning carbohydrate phosphatase, DUF89 family [Defense mechanisms];


Pssm-ID: 441186  Cd Length: 282  Bit Score: 105.29  E-value: 5.62e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 520 PDPYSKVKQRENGVALRCFPGVVRSLDALgwEERQLALVKGLLAGNVFDWGAKAVSavlesdpyFGFEEAKRKLQERPWL 599
Cdd:COG1578    67 DDPYKELKERSNELALELLPELKERIESS--EDPLETALKLAVAGNIIDFGVKGVS--------FDLEETIKEVLEKPFA 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 600 VDSYSEWLQRLKgpphkCA---LIFADNSG-IdiilgVF--PFVRELLLRGTEVILACNSGPALNDVTHSEslivAERiA 673
Cdd:COG1578   137 IDDTEELKERLK-----KAkrvLYLGDNAGeI-----VFdkLLIEELKKLGLEVTYAVRGGPILNDATLED----AKE-A 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426138158 674 GMDPVVHsalqeerllLVQTGSSSPCLDLSRLDKGLAALVRErgADLVVIEGMGravhtNYhaalrcESLK--------- 744
Cdd:COG1578   202 GLDKVAR---------VITTGSDAPGTVLEECSEEFKELFDE--ADLIISKGQG-----NY------ETLSeekdkpiff 259
                         250       260
                  ....*....|....*....|...
gi 1426138158 745 LAVIKNAWLAERLGGRLFSVIFK 767
Cdd:COG1578   260 LLKAKCEVVARDLGVPVGDLVFK 282
 
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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