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Conserved domains on  [gi|10434037|dbj|BAB14105|]
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unnamed protein product [Homo sapiens]

Protein Classification

cache domain-containing protein( domain architecture ID 10499564)

cache domain-containing protein adopts a structure with one or two PAS-like subdomains, and may bind ligands

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
dCache_1 pfam02743
Cache domain; Double cache domain 1 covers the last three strands from the membrane distal ...
19-213 4.21e-08

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: 54.27  E-value: 4.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10434037    19 TKRMVEHYTAYLSDNTRLIA-NPGLKFSVRNEVMATShvtdewMTQMEMSSLNTYIVRRYIATPNGVLRIYPG-SLMDKA 96
Cdd:pfam02743  18 LAENIESYLDSLEEILELLAsNPDLQDLLSAPAEEEL------AKLESLLRSNPGISSIYLVDADGRVLASSDeSPSYPG 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10434037    97 FDPTRRQWYLHAVAN--PGLISLTGPYLDVGGAGYVVTISHTIHSSStqlssGHTVAVMGIDFTLRYFYKVLMDLLPvcn 174
Cdd:pfam02743  92 LDVSERPWYKEALKGggGIIWVFSSPYPSSESGEPVLTIARPIYDDD-----GEVIGVLVADLDLDTLQELLSQIKL--- 163
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 10434037   175 qdgGNKIRCFIMEDRGYLVAHPTLIDPKGHAPVEQQHIT 213
Cdd:pfam02743 164 ---GEGGYVFIVDSDGRILAHPLGKNLRSLLAPFLGKSL 199
 
Name Accession Description Interval E-value
dCache_1 pfam02743
Cache domain; Double cache domain 1 covers the last three strands from the membrane distal ...
19-213 4.21e-08

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: 54.27  E-value: 4.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10434037    19 TKRMVEHYTAYLSDNTRLIA-NPGLKFSVRNEVMATShvtdewMTQMEMSSLNTYIVRRYIATPNGVLRIYPG-SLMDKA 96
Cdd:pfam02743  18 LAENIESYLDSLEEILELLAsNPDLQDLLSAPAEEEL------AKLESLLRSNPGISSIYLVDADGRVLASSDeSPSYPG 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10434037    97 FDPTRRQWYLHAVAN--PGLISLTGPYLDVGGAGYVVTISHTIHSSStqlssGHTVAVMGIDFTLRYFYKVLMDLLPvcn 174
Cdd:pfam02743  92 LDVSERPWYKEALKGggGIIWVFSSPYPSSESGEPVLTIARPIYDDD-----GEVIGVLVADLDLDTLQELLSQIKL--- 163
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 10434037   175 qdgGNKIRCFIMEDRGYLVAHPTLIDPKGHAPVEQQHIT 213
Cdd:pfam02743 164 ---GEGGYVFIVDSDGRILAHPLGKNLRSLLAPFLGKSL 199
PDC1_MCP_like cd12913
first PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; ...
97-159 2.68e-06

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: 47.14  E-value: 2.68e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 10434037  97 FDPTRRQWYLHAVANpGLISLTGPYLDVGGAG-YVVTISHTIHssstqlSSGHTVAVMGIDFTL 159
Cdd:cd12913  83 YDYRTRDWYKLAKET-GKPVWTEPYIDEVGTGvLMITISVPIY------DNGKFIGVVGVDISL 139
 
Name Accession Description Interval E-value
dCache_1 pfam02743
Cache domain; Double cache domain 1 covers the last three strands from the membrane distal ...
19-213 4.21e-08

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: 54.27  E-value: 4.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10434037    19 TKRMVEHYTAYLSDNTRLIA-NPGLKFSVRNEVMATShvtdewMTQMEMSSLNTYIVRRYIATPNGVLRIYPG-SLMDKA 96
Cdd:pfam02743  18 LAENIESYLDSLEEILELLAsNPDLQDLLSAPAEEEL------AKLESLLRSNPGISSIYLVDADGRVLASSDeSPSYPG 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10434037    97 FDPTRRQWYLHAVAN--PGLISLTGPYLDVGGAGYVVTISHTIHSSStqlssGHTVAVMGIDFTLRYFYKVLMDLLPvcn 174
Cdd:pfam02743  92 LDVSERPWYKEALKGggGIIWVFSSPYPSSESGEPVLTIARPIYDDD-----GEVIGVLVADLDLDTLQELLSQIKL--- 163
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 10434037   175 qdgGNKIRCFIMEDRGYLVAHPTLIDPKGHAPVEQQHIT 213
Cdd:pfam02743 164 ---GEGGYVFIVDSDGRILAHPLGKNLRSLLAPFLGKSL 199
PDC1_MCP_like cd12913
first PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; ...
97-159 2.68e-06

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: 47.14  E-value: 2.68e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 10434037  97 FDPTRRQWYLHAVANpGLISLTGPYLDVGGAG-YVVTISHTIHssstqlSSGHTVAVMGIDFTL 159
Cdd:cd12913  83 YDYRTRDWYKLAKET-GKPVWTEPYIDEVGTGvLMITISVPIY------DNGKFIGVVGVDISL 139
PDC1_HK_sensor cd18773
first PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins, diguanylate-cyclase ...
77-159 2.40e-04

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: 41.39  E-value: 2.40e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10434037  77 YIATPNGVLRIY--PGSLMDKAFDPTRRQWYLHAVANPGLIsLTGPYLDVGGAGYVVTISHTIHSsstqlSSGHTVAVMG 154
Cdd:cd18773  47 YVVDADGRVVASsdRDPGGGDDDDDRDRFWYQAAKATGKLV-ISEPYISRVTGKPVITLSRPIRD-----ADGRFIGVVG 120

                ....*
gi 10434037 155 IDFTL 159
Cdd:cd18773 121 ADIDL 125
 
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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