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Conserved domains on  [gi|497720448|ref|WP_010034632|]
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hypothetical protein [Gemmata obscuriglobus]

Protein Classification

ACTx2 family protein( domain architecture ID 11469125)

ACTx2 family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ACTx2 COG4747
ACT domain-containing protein [General function prediction only];
25-155 7.64e-41

ACT domain-containing protein [General function prediction only];


:

Pssm-ID: 443781 [Multi-domain]  Cd Length: 129  Bit Score: 133.73  E-value: 7.64e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497720448  25 RQFNVFLANRMGALLDLVRRFEQTDIRVVSLTVVETADCAIIRLVPSHYERGYEILTDAKFAFTESDLLVVKLPDDDRPL 104
Cdd:COG4747    1 KQISVFLENKPGRLAEVTRLLGDAGINIRALSIADTSDFGILRLIVDDPEKAREVLKEAGFTVSETDVLAVELPDRPGGL 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 497720448 105 LTITKALLSAEIDICYMYPLLIGVGplGNTAIAVYVDDFETAAAALEAQGF 155
Cdd:COG4747   81 AEILKALAEAGINIEYMYAFVGRPG--GKAVLILRVDDLEKAIEVLKENGI 129
 
Name Accession Description Interval E-value
ACTx2 COG4747
ACT domain-containing protein [General function prediction only];
25-155 7.64e-41

ACT domain-containing protein [General function prediction only];


Pssm-ID: 443781 [Multi-domain]  Cd Length: 129  Bit Score: 133.73  E-value: 7.64e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497720448  25 RQFNVFLANRMGALLDLVRRFEQTDIRVVSLTVVETADCAIIRLVPSHYERGYEILTDAKFAFTESDLLVVKLPDDDRPL 104
Cdd:COG4747    1 KQISVFLENKPGRLAEVTRLLGDAGINIRALSIADTSDFGILRLIVDDPEKAREVLKEAGFTVSETDVLAVELPDRPGGL 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 497720448 105 LTITKALLSAEIDICYMYPLLIGVGplGNTAIAVYVDDFETAAAALEAQGF 155
Cdd:COG4747   81 AEILKALAEAGINIEYMYAFVGRPG--GKAVLILRVDDLEKAIEVLKENGI 129
ACT_Bt0572_1 cd04908
N-terminal ACT domain of a novel protein composed almost entirely of two tandem ACT domains; ...
 24-86 4.06e-13

N-terminal ACT domain of a novel protein composed almost entirely of two tandem ACT domains; Included in this CD is the N-terminal ACT domain of a novel protein composed almost entirely of two tandem ACT domains as seen in the uncharacterized structure (pdb 2F06) of the Bt0572 protein from Bacteroides thetaiotaomicron and related ACT domains. These tandem ACT domain proteins belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153180  Cd Length: 66  Bit Score: 60.67  E-value: 4.06e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497720448  24 VRQFNVFLANRMGALLDLVRRFEQTDIRVVSLTVVETADCAIIRLVPSHYERGYEILTDAKFA 86
Cdd:cd04908    1 IKQLSVFLENKPGRLAAVTEILSEAGINIRALSIADTSEFGILRLIVSDPDKAKEALKEAGFA 63
ACT_8 pfam19571
ACT domain pair; This entry represents a pair of ACT domains. These domains bind to amino ...
 23-165 6.89e-12

ACT domain pair; This entry represents a pair of ACT domains. These domains bind to amino acids and often form regulatory subunits of enzymes. Proteins in this family are found in bacteria and archaea. Proteins in this family are approximately 140 amino acids in length.


Pssm-ID: 437403 [Multi-domain]  Cd Length: 141  Bit Score: 59.45  E-value: 6.89e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497720448   23 SVRQFNVFLANRMGALLDLVRRFEQTDIRVVSLTVVETADCAIIRLVPSHYERGYEILTDAKFAFTESDLLVVKLpdDDR 102
Cdd:pfam19571   2 TIHQLSVFVENKSGTLLKVLELLKEAGIQLIASTISDTVEYGIYRIICSEPTRAYEVLKEAGISVALSDVFAITL--DNQ 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497720448  103 P--LLTITKALLSAEIDICYMYPLLigvgpLGNTAIAVY-VDDFETAAAALEAQGFTLFTESDLSE 165
Cdd:pfam19571  80 PgrAADAIRLFSEEGIGISYLYSFL-----LGGKGILVFrTDNAERAREVIILNKLDFVAEKNLME 140
 
Name Accession Description Interval E-value
ACTx2 COG4747
ACT domain-containing protein [General function prediction only];
25-155 7.64e-41

ACT domain-containing protein [General function prediction only];


Pssm-ID: 443781 [Multi-domain]  Cd Length: 129  Bit Score: 133.73  E-value: 7.64e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497720448  25 RQFNVFLANRMGALLDLVRRFEQTDIRVVSLTVVETADCAIIRLVPSHYERGYEILTDAKFAFTESDLLVVKLPDDDRPL 104
Cdd:COG4747    1 KQISVFLENKPGRLAEVTRLLGDAGINIRALSIADTSDFGILRLIVDDPEKAREVLKEAGFTVSETDVLAVELPDRPGGL 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 497720448 105 LTITKALLSAEIDICYMYPLLIGVGplGNTAIAVYVDDFETAAAALEAQGF 155
Cdd:COG4747   81 AEILKALAEAGINIEYMYAFVGRPG--GKAVLILRVDDLEKAIEVLKENGI 129
ACT_Bt0572_1 cd04908
N-terminal ACT domain of a novel protein composed almost entirely of two tandem ACT domains; ...
 24-86 4.06e-13

N-terminal ACT domain of a novel protein composed almost entirely of two tandem ACT domains; Included in this CD is the N-terminal ACT domain of a novel protein composed almost entirely of two tandem ACT domains as seen in the uncharacterized structure (pdb 2F06) of the Bt0572 protein from Bacteroides thetaiotaomicron and related ACT domains. These tandem ACT domain proteins belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153180  Cd Length: 66  Bit Score: 60.67  E-value: 4.06e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497720448  24 VRQFNVFLANRMGALLDLVRRFEQTDIRVVSLTVVETADCAIIRLVPSHYERGYEILTDAKFA 86
Cdd:cd04908    1 IKQLSVFLENKPGRLAAVTEILSEAGINIRALSIADTSEFGILRLIVSDPDKAKEALKEAGFA 63
ACT_8 pfam19571
ACT domain pair; This entry represents a pair of ACT domains. These domains bind to amino ...
 23-165 6.89e-12

ACT domain pair; This entry represents a pair of ACT domains. These domains bind to amino acids and often form regulatory subunits of enzymes. Proteins in this family are found in bacteria and archaea. Proteins in this family are approximately 140 amino acids in length.


Pssm-ID: 437403 [Multi-domain]  Cd Length: 141  Bit Score: 59.45  E-value: 6.89e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497720448   23 SVRQFNVFLANRMGALLDLVRRFEQTDIRVVSLTVVETADCAIIRLVPSHYERGYEILTDAKFAFTESDLLVVKLpdDDR 102
Cdd:pfam19571   2 TIHQLSVFVENKSGTLLKVLELLKEAGIQLIASTISDTVEYGIYRIICSEPTRAYEVLKEAGISVALSDVFAITL--DNQ 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497720448  103 P--LLTITKALLSAEIDICYMYPLLigvgpLGNTAIAVY-VDDFETAAAALEAQGFTLFTESDLSE 165
Cdd:pfam19571  80 PgrAADAIRLFSEEGIGISYLYSFL-----LGGKGILVFrTDNAERAREVIILNKLDFVAEKNLME 140
ACT_PDH-BS-like cd04889
C-terminal ACT domain of the monofunctional, NAD dependent, prephenate dehydrogenase (PDH) ...
 29-81 6.83e-05

C-terminal ACT domain of the monofunctional, NAD dependent, prephenate dehydrogenase (PDH) enzyme that catalyzes the formation of 4-hydroxyphenylpyruvate from prephenate; Included in this CD is the C-terminal ACT domain of the monofunctional, NAD dependent, prephenate dehydrogenase (PDH) enzyme that catalyzes the formation of 4-hydroxyphenylpyruvate from prephenate, found in Bacillus subtilis (BS) and other Firmicutes, Deinococci, and Bacteroidetes. PDH is the first enzyme in the aromatic amino acid pathway specific for the biosynthesis of tyrosine. This enzyme is feedback inhibited by tyrosine in B. subtilis and other microorganisms. Both phenylalanine and tryptophan have been shown to be inhibitors of this activity in B. subtilis. Bifunctional chorismate mutase-PDH (TyrA) enzymes such as those seen in Escherichia coli do not contain an ACT domain. Also included in this CD is the N-terminal ACT domain of a novel protein composed almost entirely of two tandem ACT domains as seen in the uncharacterized structure (pdb 2F06) of the Bt0572 protein from Bacteroides thetaiotaomicron and related ACT domains. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153161  Cd Length: 56  Bit Score: 38.64  E-value: 6.83e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 497720448  29 VFLANRMGALLDLVRRFEQTDIRVVSLTVVETA-DCAIIRLVPSHYERGYEILT 81
Cdd:cd04889    3 VFVENKPGRLAEVTEILAEAGINIKAISIAETRgEFGILRLIFSDPERAKEVLK 56
 
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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