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Conserved domains on  [gi|288965811|pdb|3KYJ|A]
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Chain A, Putative histidine protein kinase

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CheA super family cl33989
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
7-130 7.78e-24

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


The actual alignment was detected with superfamily member COG0643:

Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 95.63  E-value: 7.78e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3KYJ_A        7 DEMDEIWALYADDGAQALDAMEASLLALQAGEDAAAHVGPLFRAVHTFKGNSRVLGLSVVESRAHLCEDLIGLVRDAGVP 86
Cdd:COG0643   1 MDMDELLEIFLEEARELLEQLEEGLLALEQDPDDPELLNAIFRAAHTLKGSAGMLGLDALAELAHALEDLLDALRNGELA 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
3KYJ_A       87 MDGEIVEILLFASDTLRAMLEETAASRAdvEGTGSEALMDQLRS 130
Cdd:COG0643  81 LTPELIDLLLEALDALRALLDALEAGGE--PPADISALLARLDA 122
 
Name Accession Description Interval E-value
CheA COG0643
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
7-130 7.78e-24

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 95.63  E-value: 7.78e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3KYJ_A        7 DEMDEIWALYADDGAQALDAMEASLLALQAGEDAAAHVGPLFRAVHTFKGNSRVLGLSVVESRAHLCEDLIGLVRDAGVP 86
Cdd:COG0643   1 MDMDELLEIFLEEARELLEQLEEGLLALEQDPDDPELLNAIFRAAHTLKGSAGMLGLDALAELAHALEDLLDALRNGELA 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
3KYJ_A       87 MDGEIVEILLFASDTLRAMLEETAASRAdvEGTGSEALMDQLRS 130
Cdd:COG0643  81 LTPELIDLLLEALDALRALLDALEAGGE--PPADISALLARLDA 122
HPT cd00088
Histidine Phosphotransfer domain, involved in signalling through a two part component systems ...
 9-107 1.75e-10

Histidine Phosphotransfer domain, involved in signalling through a two part component systems in which an autophosphorylating histidine protein kinase serves as a phosphoryl donor to a response regulator protein; the response regulator protein is modulated by phosphorylation and dephosphorylation of a conserved aspartic acid residue; two-component proteins are abundant in most eubacteria; In E. coli there are 62 two-component proteins involved in a variety of processes such as chemotaxis, osmoregulation, metabolism and transport 1; also present in both Gram positive and Gram negative pathogenic bacteria where they regulate basic housekeeping functions and control expression of toxins and other proteins important for pathogenesis; in archaea and eukaryotes, two-component pathways constitute a very small number of all signaling systems; in fungi they mediate environmental stress responses and, in pathogenic yeast, hyphal development. In Dictyostelium and in plants, they are involved in important processes such as osmoregulation, cell growth, and differentiation; to date two-component proteins have not been identified in animals; in most prokaryotic systems, the output response is effected directly by the RR, which functions as a transcription factor while in eukaryotic systems, two-component proteins are found at the beginning of signaling pathways where they interface with more conventional eukaryotic signaling strategies such as MAP kinase and cyclic nucleotide cascades


Pssm-ID: 238041 [Multi-domain]  Cd Length: 94  Bit Score: 53.92  E-value: 1.75e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3KYJ_A        9 MDEIWALYADDGAQALDAMEASLLALQAGEDaaahVGPLFRAVHTFKGNSRVLGLSVVESRAHLCEDLIGLVRDaGVPMD 88
Cdd:cd00088   1 MEELLELFLEEAEELLEELERALLELEDAED----LNEIFRAAHTLKGSAASLGLQRLAQLAHQLEDLLDALRD-GLEVT 75

                        90
                ....*....|....*....
3KYJ_A       89 GEIVEILLFASDTLRAMLE 107
Cdd:cd00088  76 PELIDLLLDALDALKAELE 94
PRK10547 PRK10547
chemotaxis protein CheA; Provisional
 6-107 8.76e-07

chemotaxis protein CheA; Provisional


Pssm-ID: 236712 [Multi-domain]  Cd Length: 670  Bit Score: 47.03  E-value: 8.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3KYJ_A         6 FDEMDEiwaLYADdgaqaldaMEASLLALQAGEDAAAHVGPLFRAVHTFKGNSRVLGLSVVESRAHLCEDLIGLVRDAGV 85
Cdd:PRK10547  11 FDEADE---LLAD--------MEQHLLVLDPEAPDAEQLNAIFRAAHSIKGGAGTFGFTVLQETTHLMENLLDEARRGEM 79

                         90       100
                 ....*....|....*....|..
3KYJ_A        86 PMDGEIVEILLFASDTLRAMLE 107
Cdd:PRK10547  80 QLNTDIINLFLETKDIMQEQLD 101
HPT smart00073
Histidine Phosphotransfer domain; Contains an active histidine residue that mediates ...
 15-103 4.72e-06

Histidine Phosphotransfer domain; Contains an active histidine residue that mediates phosphotransfer reactions. Domain detected only in eubacteria. This alignment is an extension to that shown in the Cell structure paper.


Pssm-ID: 197502 [Multi-domain]  Cd Length: 92  Bit Score: 42.24  E-value: 4.72e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3KYJ_A          15 LYADDGAQALDAMEASLLALQAGEDAAAhVGPLFRAVHTFKGNSRVLGLSVVESRAHLCEDLIGLVRDAGVPMDGEIVEI 94
Cdd:smart00073   5 LFREELAEFLQSLEEGLLELEKALDAQD-VNEIFRAAHTLKGSAGSLGLQQLAQLCHQLENLLDALRSGEVELTPDLLDL 83


                   ....*....
3KYJ_A          95 LLFASDTLR 103
Cdd:smart00073  84 LLELVDVLK 92
Hpt pfam01627
Hpt domain; The histidine-containing phosphotransfer (HPt) domain is a novel protein module ...
 11-95 3.69e-04

Hpt domain; The histidine-containing phosphotransfer (HPt) domain is a novel protein module with an active histidine residue that mediates phosphotransfer reactions in the two-component signaling systems. A multistep phosphorelay involving the HPt domain has been suggested for these signaling pathways. The crystal structure of the HPt domain of the anaerobic sensor kinase ArcB has been determined. The domain consists of six alpha helices containing a four-helix bundle-folding. The pattern of sequence similarity of the HPt domains of ArcB and components in other signaling systems can be interpreted in light of the three-dimensional structure and supports the conclusion that the HPt domains have a common structural motif both in prokaryotes and eukaryotes. In S. cerevisiae ypd1p this domain has been shown to contain a binding surface for Ssk1p (response regulator receiver domain containing protein pfam00072).


Pssm-ID: 426352 [Multi-domain]  Cd Length: 84  Bit Score: 37.33  E-value: 3.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3KYJ_A         11 EIWALYADDGAQALDAMEASLlalqAGEDAAAhvgpLFRAVHTFKGNSRVLGLSVVESRAHLCEDLIglvRDAGVPMDGE 90
Cdd:pfam01627   1 ELLELFLEEAPELLEQLEQAL----DAEDLEA----LFRAAHTLKGSAGSLGLPALAELAHELEDLL---REGELPLDPE 69


                  ....*
3KYJ_A         91 IVEIL 95
Cdd:pfam01627  70 LLEAL 74
 
Name Accession Description Interval E-value
CheA COG0643
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
7-130 7.78e-24

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 95.63  E-value: 7.78e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3KYJ_A        7 DEMDEIWALYADDGAQALDAMEASLLALQAGEDAAAHVGPLFRAVHTFKGNSRVLGLSVVESRAHLCEDLIGLVRDAGVP 86
Cdd:COG0643   1 MDMDELLEIFLEEARELLEQLEEGLLALEQDPDDPELLNAIFRAAHTLKGSAGMLGLDALAELAHALEDLLDALRNGELA 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
3KYJ_A       87 MDGEIVEILLFASDTLRAMLEETAASRAdvEGTGSEALMDQLRS 130
Cdd:COG0643  81 LTPELIDLLLEALDALRALLDALEAGGE--PPADISALLARLDA 122
HPT cd00088
Histidine Phosphotransfer domain, involved in signalling through a two part component systems ...
 9-107 1.75e-10

Histidine Phosphotransfer domain, involved in signalling through a two part component systems in which an autophosphorylating histidine protein kinase serves as a phosphoryl donor to a response regulator protein; the response regulator protein is modulated by phosphorylation and dephosphorylation of a conserved aspartic acid residue; two-component proteins are abundant in most eubacteria; In E. coli there are 62 two-component proteins involved in a variety of processes such as chemotaxis, osmoregulation, metabolism and transport 1; also present in both Gram positive and Gram negative pathogenic bacteria where they regulate basic housekeeping functions and control expression of toxins and other proteins important for pathogenesis; in archaea and eukaryotes, two-component pathways constitute a very small number of all signaling systems; in fungi they mediate environmental stress responses and, in pathogenic yeast, hyphal development. In Dictyostelium and in plants, they are involved in important processes such as osmoregulation, cell growth, and differentiation; to date two-component proteins have not been identified in animals; in most prokaryotic systems, the output response is effected directly by the RR, which functions as a transcription factor while in eukaryotic systems, two-component proteins are found at the beginning of signaling pathways where they interface with more conventional eukaryotic signaling strategies such as MAP kinase and cyclic nucleotide cascades


Pssm-ID: 238041 [Multi-domain]  Cd Length: 94  Bit Score: 53.92  E-value: 1.75e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3KYJ_A        9 MDEIWALYADDGAQALDAMEASLLALQAGEDaaahVGPLFRAVHTFKGNSRVLGLSVVESRAHLCEDLIGLVRDaGVPMD 88
Cdd:cd00088   1 MEELLELFLEEAEELLEELERALLELEDAED----LNEIFRAAHTLKGSAASLGLQRLAQLAHQLEDLLDALRD-GLEVT 75

                        90
                ....*....|....*....
3KYJ_A       89 GEIVEILLFASDTLRAMLE 107
Cdd:cd00088  76 PELIDLLLDALDALKAELE 94
PRK10547 PRK10547
chemotaxis protein CheA; Provisional
 6-107 8.76e-07

chemotaxis protein CheA; Provisional


Pssm-ID: 236712 [Multi-domain]  Cd Length: 670  Bit Score: 47.03  E-value: 8.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3KYJ_A         6 FDEMDEiwaLYADdgaqaldaMEASLLALQAGEDAAAHVGPLFRAVHTFKGNSRVLGLSVVESRAHLCEDLIGLVRDAGV 85
Cdd:PRK10547  11 FDEADE---LLAD--------MEQHLLVLDPEAPDAEQLNAIFRAAHSIKGGAGTFGFTVLQETTHLMENLLDEARRGEM 79

                         90       100
                 ....*....|....*....|..
3KYJ_A        86 PMDGEIVEILLFASDTLRAMLE 107
Cdd:PRK10547  80 QLNTDIINLFLETKDIMQEQLD 101
HPT smart00073
Histidine Phosphotransfer domain; Contains an active histidine residue that mediates ...
 15-103 4.72e-06

Histidine Phosphotransfer domain; Contains an active histidine residue that mediates phosphotransfer reactions. Domain detected only in eubacteria. This alignment is an extension to that shown in the Cell structure paper.


Pssm-ID: 197502 [Multi-domain]  Cd Length: 92  Bit Score: 42.24  E-value: 4.72e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3KYJ_A          15 LYADDGAQALDAMEASLLALQAGEDAAAhVGPLFRAVHTFKGNSRVLGLSVVESRAHLCEDLIGLVRDAGVPMDGEIVEI 94
Cdd:smart00073   5 LFREELAEFLQSLEEGLLELEKALDAQD-VNEIFRAAHTLKGSAGSLGLQQLAQLCHQLENLLDALRSGEVELTPDLLDL 83


                   ....*....
3KYJ_A          95 LLFASDTLR 103
Cdd:smart00073  84 LLELVDVLK 92
Hpt pfam01627
Hpt domain; The histidine-containing phosphotransfer (HPt) domain is a novel protein module ...
 11-95 3.69e-04

Hpt domain; The histidine-containing phosphotransfer (HPt) domain is a novel protein module with an active histidine residue that mediates phosphotransfer reactions in the two-component signaling systems. A multistep phosphorelay involving the HPt domain has been suggested for these signaling pathways. The crystal structure of the HPt domain of the anaerobic sensor kinase ArcB has been determined. The domain consists of six alpha helices containing a four-helix bundle-folding. The pattern of sequence similarity of the HPt domains of ArcB and components in other signaling systems can be interpreted in light of the three-dimensional structure and supports the conclusion that the HPt domains have a common structural motif both in prokaryotes and eukaryotes. In S. cerevisiae ypd1p this domain has been shown to contain a binding surface for Ssk1p (response regulator receiver domain containing protein pfam00072).


Pssm-ID: 426352 [Multi-domain]  Cd Length: 84  Bit Score: 37.33  E-value: 3.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3KYJ_A         11 EIWALYADDGAQALDAMEASLlalqAGEDAAAhvgpLFRAVHTFKGNSRVLGLSVVESRAHLCEDLIglvRDAGVPMDGE 90
Cdd:pfam01627   1 ELLELFLEEAPELLEQLEQAL----DAEDLEA----LFRAAHTLKGSAGSLGLPALAELAHELEDLL---REGELPLDPE 69


                  ....*
3KYJ_A         91 IVEIL 95
Cdd:pfam01627  70 LLEAL 74
 
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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