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Conserved domains on  [gi|1622830039|ref|XP_028684387|]
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phosphomevalonate kinase isoform X3 [Macaca mulatta]

Protein Classification

P-mevalo_kinase domain-containing protein( domain architecture ID 10515312)

P-mevalo_kinase domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
P-mevalo_kinase super family cl04466
Phosphomevalonate kinase; Phosphomevalonate kinase (EC:2.7.4.2) catalyzes the phosphorylation ...
3-88 1.14e-36

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).


The actual alignment was detected with superfamily member pfam04275:

Pssm-ID: 471038  Cd Length: 112  Bit Score: 121.91  E-value: 1.14e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622830039   3 FGQEHGLNFQRLLDASTYKEAFRKDMIRWGEEKRQADPGFFCRKIVEGI--SQPIWhpvllvtcvpplqLVSDTRRVSDI 80
Cdd:pfam04275  38 YAKEHGLDLDELLSDGPYKEQYRKDMIRWGEEKRNKDPGYFCRAAIEMAdaQKPVW-------------IVSDARRKTDL 104

                  ....*...
gi 1622830039  81 QWFREAYG 88
Cdd:pfam04275 105 QWFRENYP 112
 
Name Accession Description Interval E-value
P-mevalo_kinase pfam04275
Phosphomevalonate kinase; Phosphomevalonate kinase (EC:2.7.4.2) catalyzes the phosphorylation ...
3-88 1.14e-36

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: 121.91  E-value: 1.14e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622830039   3 FGQEHGLNFQRLLDASTYKEAFRKDMIRWGEEKRQADPGFFCRKIVEGI--SQPIWhpvllvtcvpplqLVSDTRRVSDI 80
Cdd:pfam04275  38 YAKEHGLDLDELLSDGPYKEQYRKDMIRWGEEKRNKDPGYFCRAAIEMAdaQKPVW-------------IVSDARRKTDL 104

                  ....*...
gi 1622830039  81 QWFREAYG 88
Cdd:pfam04275 105 QWFRENYP 112
Pmev_kin_anim TIGR01223
phosphomevalonate kinase, animal type; This enzyme is part of the mevalonate pathway, one of ...
9-151 4.57e-32

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: 112.87  E-value: 4.57e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622830039   9 LNFQRLLDASTYKEAFRKDMIRWGEEKRQADPGFFCRKIVEGISQPiwhpvllvtcvppLQLVSDTRRVSDIQWFREAYG 88
Cdd:TIGR01223  47 LNFQRLLDTSTYKEAFRKDMIRWGEEKRQADPGFFCRKIVEGISQP-------------IWLVSDTRRVSDIQWFREAYG 113
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622830039  89 AMTQTVRVVALEQSRQQRGWVFTPGVDDAESECGLDNFGGFDWVIENHGDEQRLEEQLENLIE 151
Cdd:TIGR01223 114 AVTQTVRVVALEQSRQQRGWVFTPGVDDAESECGLDNFGDFDWVIENHGVEQRLEEQLENLIE 176
 
Name Accession Description Interval E-value
P-mevalo_kinase pfam04275
Phosphomevalonate kinase; Phosphomevalonate kinase (EC:2.7.4.2) catalyzes the phosphorylation ...
3-88 1.14e-36

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: 121.91  E-value: 1.14e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622830039   3 FGQEHGLNFQRLLDASTYKEAFRKDMIRWGEEKRQADPGFFCRKIVEGI--SQPIWhpvllvtcvpplqLVSDTRRVSDI 80
Cdd:pfam04275  38 YAKEHGLDLDELLSDGPYKEQYRKDMIRWGEEKRNKDPGYFCRAAIEMAdaQKPVW-------------IVSDARRKTDL 104

                  ....*...
gi 1622830039  81 QWFREAYG 88
Cdd:pfam04275 105 QWFRENYP 112
Pmev_kin_anim TIGR01223
phosphomevalonate kinase, animal type; This enzyme is part of the mevalonate pathway, one of ...
9-151 4.57e-32

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: 112.87  E-value: 4.57e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622830039   9 LNFQRLLDASTYKEAFRKDMIRWGEEKRQADPGFFCRKIVEGISQPiwhpvllvtcvppLQLVSDTRRVSDIQWFREAYG 88
Cdd:TIGR01223  47 LNFQRLLDTSTYKEAFRKDMIRWGEEKRQADPGFFCRKIVEGISQP-------------IWLVSDTRRVSDIQWFREAYG 113
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622830039  89 AMTQTVRVVALEQSRQQRGWVFTPGVDDAESECGLDNFGGFDWVIENHGDEQRLEEQLENLIE 151
Cdd:TIGR01223 114 AVTQTVRVVALEQSRQQRGWVFTPGVDDAESECGLDNFGDFDWVIENHGVEQRLEEQLENLIE 176
 
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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