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Conserved domains on  [gi|691053726|ref|WP_031999676|]
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cache domain-containing protein [Acinetobacter baumannii]

Protein Classification

cache domain-containing protein( domain architecture ID 12982725)

cache domain-containing protein adopts a structure with one or two PAS-like subdomains, and may bind ligands; similar to the ligand binding domain of Pseudomonas putida methyl-accepting chemotaxis protein McpU

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PDC1_MCP_like cd12913
first PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; ...
 30-171 2.91e-16

first PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; Members of this subfamily display varying domain architectures but all contain double PDC (PhoQ/DcuS/CitA) sensor domains. This model represents the first PDC domain of Methyl-accepting chemotaxis proteins (MCPs), Histidine kinases (HKs), and other similar domains. Many members contain both HAMP (HK, Adenylyl cyclase, MCP, and Phosphatase) and MCP domains, which are signalling domains that interact with protein partners to relay a signal. MCPs are part of a transmembrane protein complex that controls bacterial chemotaxis. HK receptors are part of two-component systems (TCS) in bacteria that play a critical role for sensing and adapting to environmental changes. Typically, HK receptors contain an extracellular sensing domain flanked by two transmembrane helices, an intracellular dimerization histidine phosphorylation domain (DHp), and a C-terminal kinase domain, with many variations on this theme. In the case of HKs, signals detected by the sensor domain are transmitted through DHp to the kinase domain, resulting in the phosphorylation of a conserved histidine residue in DHp; phosphotransfer to a conserved aspartate in its cognate response regulator (RR) follows, which leads to the activation of genes for downstream cellular responses.


:

Pssm-ID: 350338  Cd Length: 139  Bit Score: 72.95  E-value: 2.91e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691053726  30 NKASKILSKHASEKNADIKLSTSERAALQKEIKKALSQSHYSQGTGFASYSPATQDEQDYWTLeWWYKKEDQLQQAKLEN 109
Cdd:cd12913    3 EEAESIAEQLASTLESLVSSGSLDRELLENLLKQVLESNPDILGVYVAFEPNAFSDETGRFAP-YWYRDDGGIIDLDEPP 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 691053726 110 YqnaqrfLDFRSFEWFHKPAQNKSPCIHGPYVDYICNGAYTITIAHPVMIHDHFIGVIATDI 171
Cdd:cd12913   82 D------YDYRTRDWYKLAKETGKPVWTEPYIDEVGTGVLMITISVPIYDNGKFIGVVGVDI 137
 
Name Accession Description Interval E-value
PDC1_MCP_like cd12913
first PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; ...
 30-171 2.91e-16

first PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; Members of this subfamily display varying domain architectures but all contain double PDC (PhoQ/DcuS/CitA) sensor domains. This model represents the first PDC domain of Methyl-accepting chemotaxis proteins (MCPs), Histidine kinases (HKs), and other similar domains. Many members contain both HAMP (HK, Adenylyl cyclase, MCP, and Phosphatase) and MCP domains, which are signalling domains that interact with protein partners to relay a signal. MCPs are part of a transmembrane protein complex that controls bacterial chemotaxis. HK receptors are part of two-component systems (TCS) in bacteria that play a critical role for sensing and adapting to environmental changes. Typically, HK receptors contain an extracellular sensing domain flanked by two transmembrane helices, an intracellular dimerization histidine phosphorylation domain (DHp), and a C-terminal kinase domain, with many variations on this theme. In the case of HKs, signals detected by the sensor domain are transmitted through DHp to the kinase domain, resulting in the phosphorylation of a conserved histidine residue in DHp; phosphotransfer to a conserved aspartate in its cognate response regulator (RR) follows, which leads to the activation of genes for downstream cellular responses.


Pssm-ID: 350338  Cd Length: 139  Bit Score: 72.95  E-value: 2.91e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691053726  30 NKASKILSKHASEKNADIKLSTSERAALQKEIKKALSQSHYSQGTGFASYSPATQDEQDYWTLeWWYKKEDQLQQAKLEN 109
Cdd:cd12913    3 EEAESIAEQLASTLESLVSSGSLDRELLENLLKQVLESNPDILGVYVAFEPNAFSDETGRFAP-YWYRDDGGIIDLDEPP 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 691053726 110 YqnaqrfLDFRSFEWFHKPAQNKSPCIHGPYVDYICNGAYTITIAHPVMIHDHFIGVIATDI 171
Cdd:cd12913   82 D------YDYRTRDWYKLAKETGKPVWTEPYIDEVGTGVLMITISVPIYDNGKFIGVVGVDI 137
dCache_1 pfam02743
Cache domain; Double cache domain 1 covers the last three strands from the membrane distal ...
 7-204 3.06e-05

Cache domain; Double cache domain 1 covers the last three strands from the membrane distal PAS-like domain, the first two strands of the membrane proximal domain, and the connecting elements between the two domains. This domain when present in chemoreceptors recognize several signals such as proteinogenic amino acids, GABA, Histamine and polyamines, decanoic acid, Autoinducer-2, purine derivatives, quaternary amines, citrate and taurine, among others. When associated with histidine kinases, it recognizes C3/C4-dicarboxylic acids, Spermine, guanosine and Autoinducer-2 (Mantilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1 https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 460673 [Multi-domain]  Cd Length: 237  Bit Score: 43.86  E-value: 3.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691053726    7 VEELQNLLKTVVDETTSITETLANKASKILSKHASekNADIKLSTSEraalQKEIKKALSQSHYSQGTGFASYSpatqde 86
Cdd:pfam02743   4 KEQAEEQLLSLAKQLAENIESYLDSLEEILELLAS--NPDLQDLLSA----PAEEELAKLESLLRSNPGISSIY------ 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691053726   87 qdywtlewWYKKEDQLQQAKLENYQNAqrFLDFRSFEWFHKPAQNKSP--CIHGPYVDYICNGAYTITIAHPVMIHDH-F 163
Cdd:pfam02743  72 --------LVDADGRVLASSDESPSYP--GLDVSERPWYKEALKGGGGiiWVFSSPYPSSESGEPVLTIARPIYDDDGeV 141

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 691053726  164 IGVIATDILVSALEKLLMPKLKNIKQKAVIMNDSSRVITSN 204
Cdd:pfam02743 142 IGVLVADLDLDTLQELLSQIKLGEGGYVFIVDSDGRILAHP 182
 
Name Accession Description Interval E-value
PDC1_MCP_like cd12913
first PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; ...
 30-171 2.91e-16

first PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; Members of this subfamily display varying domain architectures but all contain double PDC (PhoQ/DcuS/CitA) sensor domains. This model represents the first PDC domain of Methyl-accepting chemotaxis proteins (MCPs), Histidine kinases (HKs), and other similar domains. Many members contain both HAMP (HK, Adenylyl cyclase, MCP, and Phosphatase) and MCP domains, which are signalling domains that interact with protein partners to relay a signal. MCPs are part of a transmembrane protein complex that controls bacterial chemotaxis. HK receptors are part of two-component systems (TCS) in bacteria that play a critical role for sensing and adapting to environmental changes. Typically, HK receptors contain an extracellular sensing domain flanked by two transmembrane helices, an intracellular dimerization histidine phosphorylation domain (DHp), and a C-terminal kinase domain, with many variations on this theme. In the case of HKs, signals detected by the sensor domain are transmitted through DHp to the kinase domain, resulting in the phosphorylation of a conserved histidine residue in DHp; phosphotransfer to a conserved aspartate in its cognate response regulator (RR) follows, which leads to the activation of genes for downstream cellular responses.


Pssm-ID: 350338  Cd Length: 139  Bit Score: 72.95  E-value: 2.91e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691053726  30 NKASKILSKHASEKNADIKLSTSERAALQKEIKKALSQSHYSQGTGFASYSPATQDEQDYWTLeWWYKKEDQLQQAKLEN 109
Cdd:cd12913    3 EEAESIAEQLASTLESLVSSGSLDRELLENLLKQVLESNPDILGVYVAFEPNAFSDETGRFAP-YWYRDDGGIIDLDEPP 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 691053726 110 YqnaqrfLDFRSFEWFHKPAQNKSPCIHGPYVDYICNGAYTITIAHPVMIHDHFIGVIATDI 171
Cdd:cd12913   82 D------YDYRTRDWYKLAKETGKPVWTEPYIDEVGTGVLMITISVPIYDNGKFIGVVGVDI 137
PDC1_HK_sensor cd18773
first PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins, diguanylate-cyclase ...
 112-171 4.11e-08

first PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins, diguanylate-cyclase and similar domains; Histidine kinase (HK) receptors are part of two-component systems (TCS) in bacteria that play a critical role for sensing and adapting to environmental changes. Typically, HK receptors contain an extracellular sensing domain flanked by two transmembrane helices, an intracellular dimerization histidine phosphorylation domain (DHp), and a C-terminal kinase domain, with many variations on this theme. HK receptors in this family contain double PDC (PhoQ/DcuS/CitA) sensor domains. Signals detected by the sensor domain are transmitted through DHp to the kinase domain, resulting in the phosphorylation of a conserved histidine residue in DHp; phosphotransfer to a conserved aspartate in its cognate response regulator (RR) follows, which leads to the activation of genes for downstream cellular responses. The HK family includes not just histidine kinase receptors but also sensors for chemotaxis proteins and diguanylate cyclase receptors, implying a combinatorial molecular evolution.


Pssm-ID: 350341 [Multi-domain]  Cd Length: 125  Bit Score: 50.25  E-value: 4.11e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 691053726 112 NAQRFLDFRSFEWFHKPAQNKSPCIHGPYVDYIcNGAYTITIAHPVMIHD-HFIGVIATDI 171
Cdd:cd18773   64 GGGDDDDDRDRFWYQAAKATGKLVISEPYISRV-TGKPVITLSRPIRDADgRFIGVVGADI 123
dCache_1 pfam02743
Cache domain; Double cache domain 1 covers the last three strands from the membrane distal ...
 7-204 3.06e-05

Cache domain; Double cache domain 1 covers the last three strands from the membrane distal PAS-like domain, the first two strands of the membrane proximal domain, and the connecting elements between the two domains. This domain when present in chemoreceptors recognize several signals such as proteinogenic amino acids, GABA, Histamine and polyamines, decanoic acid, Autoinducer-2, purine derivatives, quaternary amines, citrate and taurine, among others. When associated with histidine kinases, it recognizes C3/C4-dicarboxylic acids, Spermine, guanosine and Autoinducer-2 (Mantilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1 https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 460673 [Multi-domain]  Cd Length: 237  Bit Score: 43.86  E-value: 3.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691053726    7 VEELQNLLKTVVDETTSITETLANKASKILSKHASekNADIKLSTSEraalQKEIKKALSQSHYSQGTGFASYSpatqde 86
Cdd:pfam02743   4 KEQAEEQLLSLAKQLAENIESYLDSLEEILELLAS--NPDLQDLLSA----PAEEELAKLESLLRSNPGISSIY------ 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691053726   87 qdywtlewWYKKEDQLQQAKLENYQNAqrFLDFRSFEWFHKPAQNKSP--CIHGPYVDYICNGAYTITIAHPVMIHDH-F 163
Cdd:pfam02743  72 --------LVDADGRVLASSDESPSYP--GLDVSERPWYKEALKGGGGiiWVFSSPYPSSESGEPVLTIARPIYDDDGeV 141

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 691053726  164 IGVIATDILVSALEKLLMPKLKNIKQKAVIMNDSSRVITSN 204
Cdd:pfam02743 142 IGVLVADLDLDTLQELLSQIKLGEGGYVFIVDSDGRILAHP 182
 
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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