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Conserved domains on  [gi|1370488453|ref|XP_024310128|]
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NAD kinase 2, mitochondrial isoform X2 [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 ...
 2-177 7.16e-06

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: 46.57  E-value: 7.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488453   2 LLAASKVLDRLKPVIGVNTDP---------------ERSEGHLCLPVRYthSFPEALQKFYRGEFRWLWRQRIRLYLEGT 66
Cdd:PLN02929   77 LLQASHFLDDSIPVLGVNSDPtqkdeveeysdefdaRRSTGHLCAATAE--DFEQVLDDVLFGRLKPTELSRISTVVNGT 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488453  67 ginpvpvdlheqqlslnqhnralnierahderseasgpqLLPVRALNEVFIGE---SLSSRMSYSWavavdnlrrsiPTL 143
Cdd:PLN02929  155 ---------------------------------------LLETPALNDVLIAHpspAAVSRFSFRV-----------GRQ 184

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1370488453 144 KGlasyyeisvDDGPWEKQKSSGLNLCTGTGSKA 177
Cdd:PLN02929  185 GG---------SSGPLINVRSSGLRVSTAAGSTA 209
 
Name Accession Description Interval E-value
PLN02929 PLN02929
NADH kinase
 2-177 7.16e-06

NADH kinase


Pssm-ID: 215502 [Multi-domain]  Cd Length: 301  Bit Score: 46.57  E-value: 7.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488453   2 LLAASKVLDRLKPVIGVNTDP---------------ERSEGHLCLPVRYthSFPEALQKFYRGEFRWLWRQRIRLYLEGT 66
Cdd:PLN02929   77 LLQASHFLDDSIPVLGVNSDPtqkdeveeysdefdaRRSTGHLCAATAE--DFEQVLDDVLFGRLKPTELSRISTVVNGT 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488453  67 ginpvpvdlheqqlslnqhnralnierahderseasgpqLLPVRALNEVFIGE---SLSSRMSYSWavavdnlrrsiPTL 143
Cdd:PLN02929  155 ---------------------------------------LLETPALNDVLIAHpspAAVSRFSFRV-----------GRQ 184

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1370488453 144 KGlasyyeisvDDGPWEKQKSSGLNLCTGTGSKA 177
Cdd:PLN02929  185 GG---------SSGPLINVRSSGLRVSTAAGSTA 209
 
Name Accession Description Interval E-value
PLN02929 PLN02929
NADH kinase
 2-177 7.16e-06

NADH kinase


Pssm-ID: 215502 [Multi-domain]  Cd Length: 301  Bit Score: 46.57  E-value: 7.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488453   2 LLAASKVLDRLKPVIGVNTDP---------------ERSEGHLCLPVRYthSFPEALQKFYRGEFRWLWRQRIRLYLEGT 66
Cdd:PLN02929   77 LLQASHFLDDSIPVLGVNSDPtqkdeveeysdefdaRRSTGHLCAATAE--DFEQVLDDVLFGRLKPTELSRISTVVNGT 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488453  67 ginpvpvdlheqqlslnqhnralnierahderseasgpqLLPVRALNEVFIGE---SLSSRMSYSWavavdnlrrsiPTL 143
Cdd:PLN02929  155 ---------------------------------------LLETPALNDVLIAHpspAAVSRFSFRV-----------GRQ 184

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1370488453 144 KGlasyyeisvDDGPWEKQKSSGLNLCTGTGSKA 177
Cdd:PLN02929  185 GG---------SSGPLINVRSSGLRVSTAAGSTA 209
 
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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