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Conserved domains on  [gi|446291047|ref|WP_000368902|]
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MULTISPECIES: ACT domain-containing protein [Staphylococcus]

Protein Classification

ACT domain-containing protein( domain architecture ID 11480277)

ACT domain-containing protein similar to Bacillus subtilis UPF0735 ACT domain-containing protein YszB

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK04435 PRK04435
ACT domain-containing protein;
3-150 1.32e-65

ACT domain-containing protein;


:

Pssm-ID: 179848 [Multi-domain]  Cd Length: 147  Bit Score: 196.57  E-value: 1.32e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291047   3 NKDYKKFYLIREDVLPESVVKTLKIKDALKSDPTLSIYDAVKQFDLSRSAFYKYRETIFPVDDkMLDHREFTLILYVTDI 82
Cdd:PRK04435   1 NKMKKKFYLVREDVLPEAVEKTLKAKELLKSGKVKSINEAVKQVGISRSAFYKYKDYVFPFDE-MVKGKIITLSLLLEDR 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446291047  83 VGMLARVLDVISKLELSVLTIHQSIPMEEKATITLSLNAKSKETSVEDVIGALRNLDYVSKVELISMS 150
Cdd:PRK04435  80 SGTLSKVLNVIAEAGGNILTINQSIPLQGRANVTISIDTSSMEGDIDELLEKLRNLDGVEKVELIGME 147
 
Name Accession Description Interval E-value
PRK04435 PRK04435
ACT domain-containing protein;
3-150 1.32e-65

ACT domain-containing protein;


Pssm-ID: 179848 [Multi-domain]  Cd Length: 147  Bit Score: 196.57  E-value: 1.32e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291047   3 NKDYKKFYLIREDVLPESVVKTLKIKDALKSDPTLSIYDAVKQFDLSRSAFYKYRETIFPVDDkMLDHREFTLILYVTDI 82
Cdd:PRK04435   1 NKMKKKFYLVREDVLPEAVEKTLKAKELLKSGKVKSINEAVKQVGISRSAFYKYKDYVFPFDE-MVKGKIITLSLLLEDR 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446291047  83 VGMLARVLDVISKLELSVLTIHQSIPMEEKATITLSLNAKSKETSVEDVIGALRNLDYVSKVELISMS 150
Cdd:PRK04435  80 SGTLSKVLNVIAEAGGNILTINQSIPLQGRANVTISIDTSSMEGDIDELLEKLRNLDGVEKVELIGME 147
PheB COG4492
ACT domain-containing protein, UPF0735 family [General function prediction only];
3-150 3.87e-59

ACT domain-containing protein, UPF0735 family [General function prediction only];


Pssm-ID: 443581 [Multi-domain]  Cd Length: 147  Bit Score: 179.95  E-value: 3.87e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291047   3 NKDYKKFYLIREDVLPESVVKTLKIKDALKSDPTLSIYDAVKQFDLSRSAFYKYRETIFPVDDkMLDHREFTLILYVTDI 82
Cdd:COG4492    1 MKKEKKFYLVREDILPEAILKVVEAKELLESGEVKTVNEAVKKVGISRSAFYKYKDYVFPFYE-MSKGKIITLSLLLEDE 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446291047  83 VGMLARVLDVISKLELSVLTIHQSIPMEEKATITLSLNAKSKETSVEDVIGALRNLDYVSKVELISMS 150
Cdd:COG4492   80 PGVLSSVLNIIAEAGGNILTINQSIPIQGIANVTISIETSDMTIDIEELLEELRELEGVRKVEILGRE 147
ACT_PheB-BS cd04888
C-terminal ACT domain of a small (~147 a.a.) putative phenylalanine biosynthetic pathway ...
 73-148 1.72e-21

C-terminal ACT domain of a small (~147 a.a.) putative phenylalanine biosynthetic pathway protein described in Bacillus subtilis (BS) PheB (PheB-BS) and related domains; This CD includes the C-terminal ACT domain of a small (~147 a.a.) putative phenylalanine biosynthetic pathway protein described in Bacillus subtilis (BS) PheB (PheB-BS) and other related ACT domains. In B. subtilis, the upstream gene of pheB, pheA encodes prephenate dehydratase (PDT). The presumed product of the pheB gene is chorismate mutase (CM). The deduced product of the B. subtilis pheB gene, however, has no significant homology to the CM portion of the bifunctional CM-PDT of Escherichia coli. The presence of an ACT domain lends support to the prediction that these proteins function as a phenylalanine-binding regulatory protein. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153160  Cd Length: 76  Bit Score: 82.24  E-value: 1.72e-21
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446291047  73 FTLILYVTDIVGMLARVLDVISKLELSVLTIHQSIPMEEKATITLSLNAKSKETSVEDVIGALRNLDYVSKVELIS 148
Cdd:cd04888    1 VTLSLLLEHRPGVLSKVLNTIAQVRGNVLTINQNIPIHGRANVTISIDTSTMNGDIDELLEELREIDGVEKVELVG 76
ACT_4 pfam13291
ACT domain; ACT domains bind to amino acids and regulate associated enzyme domains. These ACT ...
 74-145 1.25e-03

ACT domain; ACT domains bind to amino acids and regulate associated enzyme domains. These ACT domains are found at the C-terminus of the RelA protein.


Pssm-ID: 463831 [Multi-domain]  Cd Length: 79  Bit Score: 35.61  E-value: 1.25e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446291047   74 TLILYVTDIVGMLARVLDVISKLELSVLTIH-QSIPMEEKATITLSLNAKSKETsVEDVIGALRNLDYVSKVE 145
Cdd:pfam13291   7 DLEVEAIDRPGLLADITQVISEEKANIVSVNaKTRKKDGTAEIKITLEVKDVEH-LERLMAKLRRIPGVIDVE 78
 
Name Accession Description Interval E-value
PRK04435 PRK04435
ACT domain-containing protein;
3-150 1.32e-65

ACT domain-containing protein;


Pssm-ID: 179848 [Multi-domain]  Cd Length: 147  Bit Score: 196.57  E-value: 1.32e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291047   3 NKDYKKFYLIREDVLPESVVKTLKIKDALKSDPTLSIYDAVKQFDLSRSAFYKYRETIFPVDDkMLDHREFTLILYVTDI 82
Cdd:PRK04435   1 NKMKKKFYLVREDVLPEAVEKTLKAKELLKSGKVKSINEAVKQVGISRSAFYKYKDYVFPFDE-MVKGKIITLSLLLEDR 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446291047  83 VGMLARVLDVISKLELSVLTIHQSIPMEEKATITLSLNAKSKETSVEDVIGALRNLDYVSKVELISMS 150
Cdd:PRK04435  80 SGTLSKVLNVIAEAGGNILTINQSIPLQGRANVTISIDTSSMEGDIDELLEKLRNLDGVEKVELIGME 147
PheB COG4492
ACT domain-containing protein, UPF0735 family [General function prediction only];
3-150 3.87e-59

ACT domain-containing protein, UPF0735 family [General function prediction only];


Pssm-ID: 443581 [Multi-domain]  Cd Length: 147  Bit Score: 179.95  E-value: 3.87e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291047   3 NKDYKKFYLIREDVLPESVVKTLKIKDALKSDPTLSIYDAVKQFDLSRSAFYKYRETIFPVDDkMLDHREFTLILYVTDI 82
Cdd:COG4492    1 MKKEKKFYLVREDILPEAILKVVEAKELLESGEVKTVNEAVKKVGISRSAFYKYKDYVFPFYE-MSKGKIITLSLLLEDE 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446291047  83 VGMLARVLDVISKLELSVLTIHQSIPMEEKATITLSLNAKSKETSVEDVIGALRNLDYVSKVELISMS 150
Cdd:COG4492   80 PGVLSSVLNIIAEAGGNILTINQSIPIQGIANVTISIETSDMTIDIEELLEELRELEGVRKVEILGRE 147
ACT_PheB-BS cd04888
C-terminal ACT domain of a small (~147 a.a.) putative phenylalanine biosynthetic pathway ...
 73-148 1.72e-21

C-terminal ACT domain of a small (~147 a.a.) putative phenylalanine biosynthetic pathway protein described in Bacillus subtilis (BS) PheB (PheB-BS) and related domains; This CD includes the C-terminal ACT domain of a small (~147 a.a.) putative phenylalanine biosynthetic pathway protein described in Bacillus subtilis (BS) PheB (PheB-BS) and other related ACT domains. In B. subtilis, the upstream gene of pheB, pheA encodes prephenate dehydratase (PDT). The presumed product of the pheB gene is chorismate mutase (CM). The deduced product of the B. subtilis pheB gene, however, has no significant homology to the CM portion of the bifunctional CM-PDT of Escherichia coli. The presence of an ACT domain lends support to the prediction that these proteins function as a phenylalanine-binding regulatory protein. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153160  Cd Length: 76  Bit Score: 82.24  E-value: 1.72e-21
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446291047  73 FTLILYVTDIVGMLARVLDVISKLELSVLTIHQSIPMEEKATITLSLNAKSKETSVEDVIGALRNLDYVSKVELIS 148
Cdd:cd04888    1 VTLSLLLEHRPGVLSKVLNTIAQVRGNVLTINQNIPIHGRANVTISIDTSTMNGDIDELLEELREIDGVEKVELVG 76
SpoT COG0317
(p)ppGpp synthase/hydrolase, HD superfamily [Signal transduction mechanisms, Transcription];
57-145 3.55e-04

(p)ppGpp synthase/hydrolase, HD superfamily [Signal transduction mechanisms, Transcription];


Pssm-ID: 440086 [Multi-domain]  Cd Length: 722  Bit Score: 39.37  E-value: 3.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446291047  57 RETIFPVDdkmldhreftLILYVTDIVGMLARVLDVISKLELSVLTIHQSIPMEEKATITLSLNAKSKEtSVEDVIGALR 136
Cdd:COG0317  641 SSGVFPVD----------IRIEALDRPGLLADITSVIAEEKINILSVNTRSRDDGTATIRFTVEVRDLD-HLARVLRKLR 709


                 ....*....
gi 446291047 137 NLDYVSKVE 145
Cdd:COG0317  710 KVPGVISVR 718
ACT_Af1403 cd04874
N-terminal ACT domain of the yet uncharacterized, small (~133 a.a.), putative amino acid ...
 73-146 5.96e-04

N-terminal ACT domain of the yet uncharacterized, small (~133 a.a.), putative amino acid binding protein, Af1403, and related domains; This CD includes the N-terminal ACT domain of the yet uncharacterized, small (~133 a.a.), putative amino acid binding protein, Af1403, from Archaeoglobus fulgidus and other related archeal ACT domains. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153146 [Multi-domain]  Cd Length: 72  Bit Score: 36.51  E-value: 5.96e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446291047  73 FTLILYVTDIVGMLARVLDVISKLELSVLTIHQSIPMEEKATITLSLNAKSketSVEDVIGALRNLDYVSKVEL 146
Cdd:cd04874    1 IALSIIAEDKPGVLRDLTGVIAEHGGNITYTQQFIEREGKARIYMELEGVG---DIEELVEELRSLPIVREVEI 71
ACT_4 pfam13291
ACT domain; ACT domains bind to amino acids and regulate associated enzyme domains. These ACT ...
 74-145 1.25e-03

ACT domain; ACT domains bind to amino acids and regulate associated enzyme domains. These ACT domains are found at the C-terminus of the RelA protein.


Pssm-ID: 463831 [Multi-domain]  Cd Length: 79  Bit Score: 35.61  E-value: 1.25e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446291047   74 TLILYVTDIVGMLARVLDVISKLELSVLTIH-QSIPMEEKATITLSLNAKSKETsVEDVIGALRNLDYVSKVE 145
Cdd:pfam13291   7 DLEVEAIDRPGLLADITQVISEEKANIVSVNaKTRKKDGTAEIKITLEVKDVEH-LERLMAKLRRIPGVIDVE 78
ACT_ThrD-II-like cd04886
C-terminal ACT domain of biodegradative (catabolic) threonine dehydratase II (ThrD-II) and ...
 75-140 2.19e-03

C-terminal ACT domain of biodegradative (catabolic) threonine dehydratase II (ThrD-II) and other related ACT domains; This CD includes the C-terminal ACT domain of biodegradative (catabolic) threonine dehydratase II (ThrD-II) and other related ACT domains. The Escherichia coli tdcB gene product, ThrD-II, anaerobically catalyzes the pyridoxal phosphate-dependent dehydration of L-threonine and L-serine to ammonia and to alpha-ketobutyrate and pyruvate, respectively. Tetrameric ThrD-II is subject to allosteric activation by AMP, inhibition by alpha-keto acids, and catabolite inactivation by several metabolites of glycolysis and the citric acid cycle. Also included in this CD are N-terminal ACT domains present in smaller (~170 a.a.) archaeal proteins of unknown function. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153158 [Multi-domain]  Cd Length: 73  Bit Score: 34.83  E-value: 2.19e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446291047  75 LILYVTDIVGMLARVLDVISKLELSVLTI-HQ----SIPMEEkATITLSLNAKSKEtSVEDVIGALRNLDY 140
Cdd:cd04886    1 LRVELPDRPGQLAKLLAVIAEAGANIIEVsHDrafkTLPLGE-VEVELTLETRGAE-HIEEIIAALREAGY 69
ACT cd02116
ACT domains are commonly involved in specifically binding an amino acid or other small ligand ...
 75-132 5.10e-03

ACT domains are commonly involved in specifically binding an amino acid or other small ligand leading to regulation of the enzyme; Members of this CD belong to the superfamily of ACT regulatory domains. Pairs of ACT domains are commonly involved in specifically binding an amino acid or other small ligand leading to regulation of the enzyme. The ACT domain has been detected in a number of diverse proteins; some of these proteins are involved in amino acid and purine biosynthesis, phenylalanine hydroxylation, regulation of bacterial metabolism and transcription, and many remain to be characterized. ACT domain-containing enzymes involved in amino acid and purine synthesis are in many cases allosteric enzymes with complex regulation enforced by the binding of ligands. The ACT domain is commonly involved in the binding of a small regulatory molecule, such as the amino acids L-Ser and L-Phe in the case of D-3-phosphoglycerate dehydrogenase and the bifunctional chorismate mutase-prephenate dehydratase enzyme (P-protein), respectively. Aspartokinases typically consist of two C-terminal ACT domains in a tandem repeat, but the second ACT domain is inserted within the first, resulting in, what is normally the terminal beta strand of ACT2, formed from a region N-terminal of ACT1. ACT domain repeats have been shown to have nonequivalent ligand-binding sites with complex regulatory patterns such as those seen in the bifunctional enzyme, aspartokinase-homoserine dehydrogenase (ThrA). In other enzymes, such as phenylalanine hydroxylases, the ACT domain appears to function as a flexible small module providing allosteric regulation via transmission of conformational changes, these conformational changes are not necessarily initiated by regulatory ligand binding at the ACT domain itself. ACT domains are present either singularly, N- or C-terminal, or in pairs present C-terminal or between two catalytic domains. Unique to cyanobacteria are four ACT domains C-terminal to an aspartokinase domain. A few proteins are composed almost entirely of ACT domain repeats as seen in the four ACT domain protein, the ACR protein, found in higher plants; and the two ACT domain protein, the glycine cleavage system transcriptional repressor (GcvR) protein, found in some bacteria. Also seen are single ACT domain proteins similar to the Streptococcus pneumoniae ACT domain protein (uncharacterized pdb structure 1ZPV) found in both bacteria and archaea. Purportedly, the ACT domain is an evolutionarily mobile ligand binding regulatory module that has been fused to different enzymes at various times.


Pssm-ID: 153139 [Multi-domain]  Cd Length: 60  Bit Score: 33.80  E-value: 5.10e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446291047  75 LILYVTDIVGMLARVLDVISKLELSVLTIHQS-IPMEEKATITLSLNAKSKETSVEDVI 132
Cdd:cd02116    1 LTVSGPDRPGLLAKVLSVLAEAGINITSIEQRtSGDGGEADIFIVVDGDGDLEKLLEAL 59
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 74-138 7.93e-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: 33.43  E-value: 7.93e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446291047   74 TLILYVTDIVGMLARVLDVISKLELSVLTIHQSiPMEEKATITLSLNAKSkETSVEDVIGALRNL 138
Cdd:pfam01842   2 VLEVLVPDRPGLLARVLGALADRGINITSIEQG-TSEDKGGIVFVVIVVD-EEDLEEVLEALKKL 64
 
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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