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Conserved domains on  [gi|194115180|gb|EDW37223|]
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GL25642 [Drosophila persimilis]

Protein Classification

P-mevalo_kinase domain-containing protein( domain architecture ID 10018760)

P-mevalo_kinase domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Pmev_kin_anim TIGR01223
phosphomevalonate kinase, animal type; This enzyme is part of the mevalonate pathway, one of ...
 4-185 3.31e-84

phosphomevalonate kinase, animal type; This enzyme is part of the mevalonate pathway, one of two alternative pathways for the biosynthesis of IPP. In an example of nonorthologous gene displacement, two different types of phosphomevalonate kinase are found. One is this type, found in animals. The other is the ERG8 type, found in plants and fungi (TIGR01219) and in Gram-positive bacteria (TIGR01220). [Central intermediary metabolism, Other]


:

Pssm-ID: 130290  Cd Length: 182  Bit Score: 246.53  E-value: 3.31e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194115180    4 IVLISGKRKCGKDYISERLQKRLTNRA-IIVRISEPIKSEWARKLQLDLSALLSDGPYKEQYRRDMIVWSDEVRNKDYGY 82
Cdd:TIGR01223   1 VLLFSGKRKSGKDFVTEALQSRLGADVcAVLRLSGPLKEQYAQEHGLNFQRLLDTSTYKEAFRKDMIRWGEEKRQADPGF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194115180   83 FCRaAMEEAPldQIAYVIVSDVRRKNDIKWFRETYGQNMVrTVRLTSRPETRQARGWTFTKGIDDVPSECDLDDYDSFDF 162
Cdd:TIGR01223  81 FCR-KIVEGI--SQPIWLVSDTRRVSDIQWFREAYGAVTQ-TVRVVALEQSRQQRGWVFTPGVDDAESECGLDNFGDFDW 156

                         170       180
                  ....*....|....*....|....*
gi 194115180  163 VVPNE--DENDQGFIDQLLDMLQLK 185
Cdd:TIGR01223 157 VIENHgvEQRLEEQLENLIEFIRSR 181
 
Name Accession Description Interval E-value
Pmev_kin_anim TIGR01223
phosphomevalonate kinase, animal type; This enzyme is part of the mevalonate pathway, one of ...
 4-185 3.31e-84

phosphomevalonate kinase, animal type; This enzyme is part of the mevalonate pathway, one of two alternative pathways for the biosynthesis of IPP. In an example of nonorthologous gene displacement, two different types of phosphomevalonate kinase are found. One is this type, found in animals. The other is the ERG8 type, found in plants and fungi (TIGR01219) and in Gram-positive bacteria (TIGR01220). [Central intermediary metabolism, Other]


Pssm-ID: 130290  Cd Length: 182  Bit Score: 246.53  E-value: 3.31e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194115180    4 IVLISGKRKCGKDYISERLQKRLTNRA-IIVRISEPIKSEWARKLQLDLSALLSDGPYKEQYRRDMIVWSDEVRNKDYGY 82
Cdd:TIGR01223   1 VLLFSGKRKSGKDFVTEALQSRLGADVcAVLRLSGPLKEQYAQEHGLNFQRLLDTSTYKEAFRKDMIRWGEEKRQADPGF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194115180   83 FCRaAMEEAPldQIAYVIVSDVRRKNDIKWFRETYGQNMVrTVRLTSRPETRQARGWTFTKGIDDVPSECDLDDYDSFDF 162
Cdd:TIGR01223  81 FCR-KIVEGI--SQPIWLVSDTRRVSDIQWFREAYGAVTQ-TVRVVALEQSRQQRGWVFTPGVDDAESECGLDNFGDFDW 156

                         170       180
                  ....*....|....*....|....*
gi 194115180  163 VVPNE--DENDQGFIDQLLDMLQLK 185
Cdd:TIGR01223 157 VIENHgvEQRLEEQLENLIEFIRSR 181
P-mevalo_kinase pfam04275
Phosphomevalonate kinase; Phosphomevalonate kinase (EC:2.7.4.2) catalyzes the phosphorylation ...
 7-118 3.07e-61

Phosphomevalonate kinase; Phosphomevalonate kinase (EC:2.7.4.2) catalyzes the phosphorylation of 5-phosphomevalonate into 5-diphosphomevalonate, an essential step in isoprenoid biosynthesis via the mevalonate pathway. This family represents the animal type of the enzyme. The other is the ERG8 type, found in plants and fungi, and some bacteria (see pfam00288).


Pssm-ID: 461247  Cd Length: 112  Bit Score: 185.47  E-value: 3.07e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194115180    7 ISGKRKCGKDYISERLQKRL-TNRAIIVRISEPIKSEWARKLQLDLSALLSDGPYKEQYRRDMIVWSDEVRNKDYGYFCR 85
Cdd:pfam04275   1 FSGKRKSGKDYVTELLQERLgGDRCAVLRISGPIKQQYAKEHGLDLDELLSDGPYKEQYRKDMIRWGEEKRNKDPGYFCR 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 194115180   86 AAMEEAPLDQiAYVIVSDVRRKNDIKWFRETYG 118
Cdd:pfam04275  81 AAIEMADAQK-PVWIVSDARRKTDLQWFRENYP 112
 
Name Accession Description Interval E-value
Pmev_kin_anim TIGR01223
phosphomevalonate kinase, animal type; This enzyme is part of the mevalonate pathway, one of ...
 4-185 3.31e-84

phosphomevalonate kinase, animal type; This enzyme is part of the mevalonate pathway, one of two alternative pathways for the biosynthesis of IPP. In an example of nonorthologous gene displacement, two different types of phosphomevalonate kinase are found. One is this type, found in animals. The other is the ERG8 type, found in plants and fungi (TIGR01219) and in Gram-positive bacteria (TIGR01220). [Central intermediary metabolism, Other]


Pssm-ID: 130290  Cd Length: 182  Bit Score: 246.53  E-value: 3.31e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194115180    4 IVLISGKRKCGKDYISERLQKRLTNRA-IIVRISEPIKSEWARKLQLDLSALLSDGPYKEQYRRDMIVWSDEVRNKDYGY 82
Cdd:TIGR01223   1 VLLFSGKRKSGKDFVTEALQSRLGADVcAVLRLSGPLKEQYAQEHGLNFQRLLDTSTYKEAFRKDMIRWGEEKRQADPGF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194115180   83 FCRaAMEEAPldQIAYVIVSDVRRKNDIKWFRETYGQNMVrTVRLTSRPETRQARGWTFTKGIDDVPSECDLDDYDSFDF 162
Cdd:TIGR01223  81 FCR-KIVEGI--SQPIWLVSDTRRVSDIQWFREAYGAVTQ-TVRVVALEQSRQQRGWVFTPGVDDAESECGLDNFGDFDW 156

                         170       180
                  ....*....|....*....|....*
gi 194115180  163 VVPNE--DENDQGFIDQLLDMLQLK 185
Cdd:TIGR01223 157 VIENHgvEQRLEEQLENLIEFIRSR 181
P-mevalo_kinase pfam04275
Phosphomevalonate kinase; Phosphomevalonate kinase (EC:2.7.4.2) catalyzes the phosphorylation ...
 7-118 3.07e-61

Phosphomevalonate kinase; Phosphomevalonate kinase (EC:2.7.4.2) catalyzes the phosphorylation of 5-phosphomevalonate into 5-diphosphomevalonate, an essential step in isoprenoid biosynthesis via the mevalonate pathway. This family represents the animal type of the enzyme. The other is the ERG8 type, found in plants and fungi, and some bacteria (see pfam00288).


Pssm-ID: 461247  Cd Length: 112  Bit Score: 185.47  E-value: 3.07e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194115180    7 ISGKRKCGKDYISERLQKRL-TNRAIIVRISEPIKSEWARKLQLDLSALLSDGPYKEQYRRDMIVWSDEVRNKDYGYFCR 85
Cdd:pfam04275   1 FSGKRKSGKDYVTELLQERLgGDRCAVLRISGPIKQQYAKEHGLDLDELLSDGPYKEQYRKDMIRWGEEKRNKDPGYFCR 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 194115180   86 AAMEEAPLDQiAYVIVSDVRRKNDIKWFRETYG 118
Cdd:pfam04275  81 AAIEMADAQK-PVWIVSDARRKTDLQWFRENYP 112
 
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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