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Conserved domains on  [gi|613107343|gb|EZX15679|]
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hypothetical protein V069_00616 [Staphylococcus aureus C0637]

Protein Classification

YmfK family protein( domain architecture ID 10486782)

YmfK family protein is a DUF3388 domain-containing protein with an N-terminal ACT domain

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DUF3388 pfam11868
Protein of unknown function (DUF3388); This family of proteins are functionally ...
 75-261 2.93e-123

Protein of unknown function (DUF3388); This family of proteins are functionally uncharacterized. This protein is found in bacteria. Proteins in this family are typically between 261 to 275 amino acids in length. This protein is found associated with pfam01842.


:

Pssm-ID: 432145  Cd Length: 190  Bit Score: 349.04  E-value: 2.93e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613107343   75 ITKLKKPELRDRLAVRHGRYIEQDAKDKKTFRFEREDLGLLVDFLAELFKEEGHKLIGIRGMPRVGKTESIVAGSVCAHK 154
Cdd:pfam11868   1 VTKLRKPKLRDRLAVRHGRYIQRDADDKKTFRFVREELGLLVDFMAELFKEEGHKLIGIRGMPRVGKTESIVAASVCANK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613107343  155 RWLFISSTLIKQTVRSSLIKGEYDANHVYIIDGAVTARESNPKHQELVNEVMTLPSIKVVEHPDLFVETSTCTMEDFDYI 234
Cdd:pfam11868  81 RWLFVSSTLLKQTVRSQLIKDEYNANNIFIIDGIVSTRRANEKHWQLIREIMRLPATKVVEHPDIFVQETEYTLDDFDYI 160

                         170       180
                  ....*....|....*....|....*..
gi 613107343  235 IELRENENQEIHYEEMKKQTVQSKNNL 261
Cdd:pfam11868 161 IELRNDDNEEITYEIVEKPDMFQQDGF 187
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 18-74 7.02e-03

ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme. The ACT domain is found in: D-3-phosphoglycerate dehydrogenase EC:1.1.1.95, which is inhibited by serine. Aspartokinase EC:2.7.2.4, which is regulated by lysine. Acetolactate synthase small regulatory subunit, which is inhibited by valine. Phenylalanine-4-hydroxylase EC:1.14.16.1, which is regulated by phenylalanine. Prephenate dehydrogenase EC:4.2.1.51. formyltetrahydrofolate deformylase EC:3.5.1.10, which is activated by methionine and inhibited by glycine. GTP pyrophosphokinase EC:2.7.6.5


:

Pssm-ID: 426468 [Multi-domain]  Cd Length: 66  Bit Score: 34.59  E-value: 7.02e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 613107343   18 NRPGLLGDVSSLLGMLGISIVTINGVDQGKRGLLIKTDNLEKVERFEQIARGINEIE 74
Cdd:pfam01842   9 DRPGLLARVLGALADRGINITSIEQGTSEDKGGIVFVVIVVDEEDLEEVLEALKKLE 65
 
Name Accession Description Interval E-value
DUF3388 pfam11868
Protein of unknown function (DUF3388); This family of proteins are functionally ...
 75-261 2.93e-123

Protein of unknown function (DUF3388); This family of proteins are functionally uncharacterized. This protein is found in bacteria. Proteins in this family are typically between 261 to 275 amino acids in length. This protein is found associated with pfam01842.


Pssm-ID: 432145  Cd Length: 190  Bit Score: 349.04  E-value: 2.93e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613107343   75 ITKLKKPELRDRLAVRHGRYIEQDAKDKKTFRFEREDLGLLVDFLAELFKEEGHKLIGIRGMPRVGKTESIVAGSVCAHK 154
Cdd:pfam11868   1 VTKLRKPKLRDRLAVRHGRYIQRDADDKKTFRFVREELGLLVDFMAELFKEEGHKLIGIRGMPRVGKTESIVAASVCANK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613107343  155 RWLFISSTLIKQTVRSSLIKGEYDANHVYIIDGAVTARESNPKHQELVNEVMTLPSIKVVEHPDLFVETSTCTMEDFDYI 234
Cdd:pfam11868  81 RWLFVSSTLLKQTVRSQLIKDEYNANNIFIIDGIVSTRRANEKHWQLIREIMRLPATKVVEHPDIFVQETEYTLDDFDYI 160

                         170       180
                  ....*....|....*....|....*..
gi 613107343  235 IELRENENQEIHYEEMKKQTVQSKNNL 261
Cdd:pfam11868 161 IELRNDDNEEITYEIVEKPDMFQQDGF 187
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 18-74 7.02e-03

ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme. The ACT domain is found in: D-3-phosphoglycerate dehydrogenase EC:1.1.1.95, which is inhibited by serine. Aspartokinase EC:2.7.2.4, which is regulated by lysine. Acetolactate synthase small regulatory subunit, which is inhibited by valine. Phenylalanine-4-hydroxylase EC:1.14.16.1, which is regulated by phenylalanine. Prephenate dehydrogenase EC:4.2.1.51. formyltetrahydrofolate deformylase EC:3.5.1.10, which is activated by methionine and inhibited by glycine. GTP pyrophosphokinase EC:2.7.6.5


Pssm-ID: 426468 [Multi-domain]  Cd Length: 66  Bit Score: 34.59  E-value: 7.02e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 613107343   18 NRPGLLGDVSSLLGMLGISIVTINGVDQGKRGLLIKTDNLEKVERFEQIARGINEIE 74
Cdd:pfam01842   9 DRPGLLARVLGALADRGINITSIEQGTSEDKGGIVFVVIVVDEEDLEEVLEALKKLE 65
 
Name Accession Description Interval E-value
DUF3388 pfam11868
Protein of unknown function (DUF3388); This family of proteins are functionally ...
 75-261 2.93e-123

Protein of unknown function (DUF3388); This family of proteins are functionally uncharacterized. This protein is found in bacteria. Proteins in this family are typically between 261 to 275 amino acids in length. This protein is found associated with pfam01842.


Pssm-ID: 432145  Cd Length: 190  Bit Score: 349.04  E-value: 2.93e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613107343   75 ITKLKKPELRDRLAVRHGRYIEQDAKDKKTFRFEREDLGLLVDFLAELFKEEGHKLIGIRGMPRVGKTESIVAGSVCAHK 154
Cdd:pfam11868   1 VTKLRKPKLRDRLAVRHGRYIQRDADDKKTFRFVREELGLLVDFMAELFKEEGHKLIGIRGMPRVGKTESIVAASVCANK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613107343  155 RWLFISSTLIKQTVRSSLIKGEYDANHVYIIDGAVTARESNPKHQELVNEVMTLPSIKVVEHPDLFVETSTCTMEDFDYI 234
Cdd:pfam11868  81 RWLFVSSTLLKQTVRSQLIKDEYNANNIFIIDGIVSTRRANEKHWQLIREIMRLPATKVVEHPDIFVQETEYTLDDFDYI 160

                         170       180
                  ....*....|....*....|....*..
gi 613107343  235 IELRENENQEIHYEEMKKQTVQSKNNL 261
Cdd:pfam11868 161 IELRNDDNEEITYEIVEKPDMFQQDGF 187
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 18-74 7.02e-03

ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme. The ACT domain is found in: D-3-phosphoglycerate dehydrogenase EC:1.1.1.95, which is inhibited by serine. Aspartokinase EC:2.7.2.4, which is regulated by lysine. Acetolactate synthase small regulatory subunit, which is inhibited by valine. Phenylalanine-4-hydroxylase EC:1.14.16.1, which is regulated by phenylalanine. Prephenate dehydrogenase EC:4.2.1.51. formyltetrahydrofolate deformylase EC:3.5.1.10, which is activated by methionine and inhibited by glycine. GTP pyrophosphokinase EC:2.7.6.5


Pssm-ID: 426468 [Multi-domain]  Cd Length: 66  Bit Score: 34.59  E-value: 7.02e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 613107343   18 NRPGLLGDVSSLLGMLGISIVTINGVDQGKRGLLIKTDNLEKVERFEQIARGINEIE 74
Cdd:pfam01842   9 DRPGLLARVLGALADRGINITSIEQGTSEDKGGIVFVVIVVDEEDLEEVLEALKKLE 65
 
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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