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Conserved domains on  [gi|530378682|ref|XP_005248298|]
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NAD kinase 2, mitochondrial isoform X1 [Homo sapiens]

Protein Classification

diacylglycerol kinase catalytic domain-containing protein( domain architecture ID 546)

diacylglycerol kinase catalytic domain-containing protein is involved in the conversion of diacylglycerol (DAG) to phosphatidic acid (PA), utilizing ATP as a source of the phosphate

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DAGK_cat super family cl01255
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
96-340 3.73e-18

Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts as a protein kinase C activator. The catalytic domain is assumed from the finding of bacterial homologs. YegS is the Escherichia coli protein in this family whose crystal structure reveals an active site in the inter-domain cleft formed by four conserved sequence motifs, revealing a novel metal-binding site. The residues of this site are conserved across the family.


The actual alignment was detected with superfamily member PLN02929:

Pssm-ID: 445337 [Multi-domain]  Cd Length: 301  Bit Score: 84.70  E-value: 3.73e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378682  96 DLKQLLALKGSS-------YSGLLERHHIHTKNVEHIIDSLRNEGIEVRLVKRREYdEETVRWADAVIAAGGDGTmLLAA 168
Cdd:PLN02929   3 DVYPFRQLEGSGratnpkvLEYLEDRHKVHKDTVNFCKDILQQKSVDWECVLRNEL-SQPIRDVDLVVAVGGDGT-LLQA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378682 169 SKVLDRLKPVIGVNTDP---------------ERSEGHLCLPVRYthSFPEALQKFYRGEFRWLWRQRIRLYLEGTginp 233
Cdd:PLN02929  81 SHFLDDSIPVLGVNSDPtqkdeveeysdefdaRRSTGHLCAATAE--DFEQVLDDVLFGRLKPTELSRISTVVNGT---- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378682 234 vpvdlheqqlslnqhnralnierahderseasgpqLLPVRALNEVFIGE---SLSSRMSYSWavavdnlrrsiPTLKGla 310
Cdd:PLN02929 155 -----------------------------------LLETPALNDVLIAHpspAAVSRFSFRV-----------GRQGG-- 186
                        250       260       270
                 ....*....|....*....|....*....|
gi 530378682 311 syyeisvDDGPWEKQKSSGLNLCTGTGSKA 340
Cdd:PLN02929 187 -------SSGPLINVRSSGLRVSTAAGSTA 209
 
Name Accession Description Interval E-value
PLN02929 PLN02929
NADH kinase
96-340 3.73e-18

NADH kinase


Pssm-ID: 215502 [Multi-domain]  Cd Length: 301  Bit Score: 84.70  E-value: 3.73e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378682  96 DLKQLLALKGSS-------YSGLLERHHIHTKNVEHIIDSLRNEGIEVRLVKRREYdEETVRWADAVIAAGGDGTmLLAA 168
Cdd:PLN02929   3 DVYPFRQLEGSGratnpkvLEYLEDRHKVHKDTVNFCKDILQQKSVDWECVLRNEL-SQPIRDVDLVVAVGGDGT-LLQA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378682 169 SKVLDRLKPVIGVNTDP---------------ERSEGHLCLPVRYthSFPEALQKFYRGEFRWLWRQRIRLYLEGTginp 233
Cdd:PLN02929  81 SHFLDDSIPVLGVNSDPtqkdeveeysdefdaRRSTGHLCAATAE--DFEQVLDDVLFGRLKPTELSRISTVVNGT---- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378682 234 vpvdlheqqlslnqhnralnierahderseasgpqLLPVRALNEVFIGE---SLSSRMSYSWavavdnlrrsiPTLKGla 310
Cdd:PLN02929 155 -----------------------------------LLETPALNDVLIAHpspAAVSRFSFRV-----------GRQGG-- 186
                        250       260       270
                 ....*....|....*....|....*....|
gi 530378682 311 syyeisvDDGPWEKQKSSGLNLCTGTGSKA 340
Cdd:PLN02929 187 -------SSGPLINVRSSGLRVSTAAGSTA 209
NadK COG0061
NAD kinase [Coenzyme transport and metabolism];
122-343 6.36e-12

NAD kinase [Coenzyme transport and metabolism];


Pssm-ID: 439831 [Multi-domain]  Cd Length: 279  Bit Score: 65.93  E-value: 6.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378682 122 VEHIIDSLRNEGIEVRLVKRREYD----EETVRWADAVIAAGGDGTMLLAASKVLDRLKPVIGVN-------TDPERSEg 190
Cdd:COG0061   19 AEELAELLEERGIEVVLDEDTAVPgvplEELGEEADLVIVLGGDGTLLRAARLLAPLGIPILGINlgrlgflTEIEPEE- 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378682 191 hlclpvrythsFPEALQKFYRGEFRWLWRQRIRLYlegtginpvpvdlheqqlslnqhnralnIERAHDERSEAsgpqll 270
Cdd:COG0061   98 -----------LEEALERLLAGEYEVEERLLLEAT----------------------------VDRDGEVVHEA------ 132
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530378682 271 pvRALNEVFIGESLSSRMsyswavavdnlrrsiptLKglasyYEISVDDGPWEKQKSSGLNLCTGTGSKAWSF 343
Cdd:COG0061  133 --LALNEVVVLRGSIARM-----------------IE-----LEVYIDGEFLEEFRGDGLIVSTPTGSTAYNL 181
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
120-181 1.25e-04

Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts as a protein kinase C activator. The catalytic domain is assumed from the finding of bacterial homologs. YegS is the Escherichia coli protein in this family whose crystal structure reveals an active site in the inter-domain cleft formed by four conserved sequence motifs, revealing a novel metal-binding site. The residues of this site are conserved across the family.


Pssm-ID: 425868 [Multi-domain]  Cd Length: 125  Bit Score: 41.80  E-value: 1.25e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530378682  120 KNVEHIIDSLRNEGIEVRLV--KRREYDEETVRWA-----DAVIAAGGDGTMLLAASkVLDRL--KPVIGV 181
Cdd:pfam00781  17 KLLRKVRPLLNKAGVEVELVltEGPGDALELAREAaedgyDRIVVAGGDGTVNEVLN-GLAGLatRPPLGI 86
 
Name Accession Description Interval E-value
PLN02929 PLN02929
NADH kinase
96-340 3.73e-18

NADH kinase


Pssm-ID: 215502 [Multi-domain]  Cd Length: 301  Bit Score: 84.70  E-value: 3.73e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378682  96 DLKQLLALKGSS-------YSGLLERHHIHTKNVEHIIDSLRNEGIEVRLVKRREYdEETVRWADAVIAAGGDGTmLLAA 168
Cdd:PLN02929   3 DVYPFRQLEGSGratnpkvLEYLEDRHKVHKDTVNFCKDILQQKSVDWECVLRNEL-SQPIRDVDLVVAVGGDGT-LLQA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378682 169 SKVLDRLKPVIGVNTDP---------------ERSEGHLCLPVRYthSFPEALQKFYRGEFRWLWRQRIRLYLEGTginp 233
Cdd:PLN02929  81 SHFLDDSIPVLGVNSDPtqkdeveeysdefdaRRSTGHLCAATAE--DFEQVLDDVLFGRLKPTELSRISTVVNGT---- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378682 234 vpvdlheqqlslnqhnralnierahderseasgpqLLPVRALNEVFIGE---SLSSRMSYSWavavdnlrrsiPTLKGla 310
Cdd:PLN02929 155 -----------------------------------LLETPALNDVLIAHpspAAVSRFSFRV-----------GRQGG-- 186
                        250       260       270
                 ....*....|....*....|....*....|
gi 530378682 311 syyeisvDDGPWEKQKSSGLNLCTGTGSKA 340
Cdd:PLN02929 187 -------SSGPLINVRSSGLRVSTAAGSTA 209
NadK COG0061
NAD kinase [Coenzyme transport and metabolism];
122-343 6.36e-12

NAD kinase [Coenzyme transport and metabolism];


Pssm-ID: 439831 [Multi-domain]  Cd Length: 279  Bit Score: 65.93  E-value: 6.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378682 122 VEHIIDSLRNEGIEVRLVKRREYD----EETVRWADAVIAAGGDGTMLLAASKVLDRLKPVIGVN-------TDPERSEg 190
Cdd:COG0061   19 AEELAELLEERGIEVVLDEDTAVPgvplEELGEEADLVIVLGGDGTLLRAARLLAPLGIPILGINlgrlgflTEIEPEE- 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378682 191 hlclpvrythsFPEALQKFYRGEFRWLWRQRIRLYlegtginpvpvdlheqqlslnqhnralnIERAHDERSEAsgpqll 270
Cdd:COG0061   98 -----------LEEALERLLAGEYEVEERLLLEAT----------------------------VDRDGEVVHEA------ 132
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530378682 271 pvRALNEVFIGESLSSRMsyswavavdnlrrsiptLKglasyYEISVDDGPWEKQKSSGLNLCTGTGSKAWSF 343
Cdd:COG0061  133 --LALNEVVVLRGSIARM-----------------IE-----LEVYIDGEFLEEFRGDGLIVSTPTGSTAYNL 181
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
120-181 1.25e-04

Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts as a protein kinase C activator. The catalytic domain is assumed from the finding of bacterial homologs. YegS is the Escherichia coli protein in this family whose crystal structure reveals an active site in the inter-domain cleft formed by four conserved sequence motifs, revealing a novel metal-binding site. The residues of this site are conserved across the family.


Pssm-ID: 425868 [Multi-domain]  Cd Length: 125  Bit Score: 41.80  E-value: 1.25e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530378682  120 KNVEHIIDSLRNEGIEVRLV--KRREYDEETVRWA-----DAVIAAGGDGTMLLAASkVLDRL--KPVIGV 181
Cdd:pfam00781  17 KLLRKVRPLLNKAGVEVELVltEGPGDALELAREAaedgyDRIVVAGGDGTVNEVLN-GLAGLatRPPLGI 86
NAD_kinase pfam01513
ATP-NAD kinase N-terminal domain; Members of this family include ATP-NAD kinases EC:2.7.1.23, ...
152-183 2.43e-04

ATP-NAD kinase N-terminal domain; Members of this family include ATP-NAD kinases EC:2.7.1.23, which catalyzes the phosphorylation of NAD to NADP utilizing ATP and other nucleoside triphosphates as well as inorganic polyphosphate as a source of phosphorus. Also includes NADH kinases EC:2.7.1.86.


Pssm-ID: 426300 [Multi-domain]  Cd Length: 128  Bit Score: 40.81  E-value: 2.43e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 530378682  152 ADAVIAAGGDGTMLLAASKVLDRLKPVIGVNT 183
Cdd:pfam01513  74 VDLIIVLGGDGTALRAARLLQKAVIPILGVNT 105
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
120-181 5.09e-04

Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, General function prediction only];


Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 41.76  E-value: 5.09e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530378682 120 KNVEHIIDSLRNEGIEVRLVKRREYDE--ETVRWA-----DAVIAAGGDGTMLLAASKVLDRlKPVIGV 181
Cdd:COG1597   20 RLLERLVAALRAAGLEVEVLETESPGDatELAREAaaegaDLVVAAGGDGTVNEVANGLAGT-GPPLGI 87
ppnK PRK01231
NAD(+) kinase;
122-342 5.13e-04

NAD(+) kinase;


Pssm-ID: 179257 [Multi-domain]  Cd Length: 295  Bit Score: 41.87  E-value: 5.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378682 122 VEHIIDSLRNEGIEVRL---------------VKRREYDEEtvrwADAVIAAGGDGTMLLAASKVLDRLKPVIGVN---- 182
Cdd:PRK01231  22 LRRLKDFLLDRGLEVILdeetaevlpghglqtVSRKLLGEV----CDLVIVVGGDGSLLGAARALARHNVPVLGINrgrl 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378682 183 ---TD--PERSEGHLclpvrythsfPEALQKFYRGEFRWLwrqrirlyLEGTginpvpvdlheqqlslnqhnralnIERA 257
Cdd:PRK01231  98 gflTDirPDELEFKL----------AEVLDGHYQEEERFL--------LEAE------------------------VRRG 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378682 258 HDERSEASgpqllpvrALNEVFIGESLSSRMsyswavaVDnlrrsiptlkglasyYEISVDDGPWEKQKSSGLNLCTGTG 337
Cdd:PRK01231 136 GEVIGQGD--------ALNDVVLHPGKSTRM-------IE---------------FELYIDGQFVCSQRSDGLIVSTPTG 185

                 ....*
gi 530378682 338 SKAWS 342
Cdd:PRK01231 186 STAYA 190
ppnK PRK01911
inorganic polyphosphate/ATP-NAD kinase; Provisional
122-215 1.55e-03

inorganic polyphosphate/ATP-NAD kinase; Provisional


Pssm-ID: 179352 [Multi-domain]  Cd Length: 292  Bit Score: 40.29  E-value: 1.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378682 122 VEHIIDSLRNEGIEVrLVKRREYD------------------EETVRWADAVIAAGGDGTMLLAASKVLDRLKPVIGVNT 183
Cdd:PRK01911  18 IQELFDELEERGAEV-LIEEKFLDflkqdlkfhpsydtfsdnEELDGSADMVISIGGDGTFLRTATYVGNSNIPILGINT 96
                         90       100       110
                 ....*....|....*....|....*....|...
gi 530378682 184 dperseGHL-CLPVRYTHSFPEALQKFYRGEFR 215
Cdd:PRK01911  97 ------GRLgFLATVSKEEIEETIDELLNGDYT 123
 
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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