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Conserved domains on  [gi|1820318287|gb|QIJ40220|]
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PilZ domain-containing protein [Rhizobium leguminosarum]

Protein Classification

PilZ domain-containing protein( domain architecture ID 10537801)

PilZ domain-containing protein is involved in binding bis-(3'-5')-cyclic dimeric GMP (c-di-GMP), a ubiquitous second messenger that regulates cell surface-associated traits in bacteria

CATH:  2.40.10.220
Gene Ontology:  GO:0035438
PubMed:  30710060|29146598
SCOP:  3000480

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PilZ pfam07238
PilZ domain; PilZ is a c-di-GMP binding domain found in widespread cytoplasmic receptors, ...
10-97 1.03e-05

PilZ domain; PilZ is a c-di-GMP binding domain found in widespread cytoplasmic receptors, which is involved in regulation of motility, biofilm formation and virulence of many bacterial pathogens. This domain binds c-di-GMP through RXXXR and [D/N]hSXXG motifs, however, some PilZ domains lack these motifs and do not bind c-di-GMP. Proteins which contain PilZ are known to interact with the flagellar switch-complex proteins FliG and FliM. This interaction results in a reduction of torque generation and induces CCW motor bias. This is the canonical PilZ domain whose structure consists of six beta-strands that form a beta barrel, followed by a long C-terminal alpha-helix.


:

Pssm-ID: 399904  Cd Length: 102  Bit Score: 41.72  E-value: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820318287  10 RKADRKNCRVFGHVKYLNSQVDARILNLSPTGAALEMKGPLhAASGSKVRIEAENLGL-----LEGVIRWKHNG----RV 80
Cdd:pfam07238   3 RRFPRVPVSLPVTLRDGGGEYKGRLIDISLGGAAIRLPDEP-LALGDRVELSLDLLDDgqelaLPGRVVRIRPDedgaRV 81
                          90
                  ....*....|....*...
gi 1820318287  81 GIQF-DVNSNARAQISSY 97
Cdd:pfam07238  82 GVQFlDLDEEQRRLLVRL 99
 
Name Accession Description Interval E-value
PilZ pfam07238
PilZ domain; PilZ is a c-di-GMP binding domain found in widespread cytoplasmic receptors, ...
10-97 1.03e-05

PilZ domain; PilZ is a c-di-GMP binding domain found in widespread cytoplasmic receptors, which is involved in regulation of motility, biofilm formation and virulence of many bacterial pathogens. This domain binds c-di-GMP through RXXXR and [D/N]hSXXG motifs, however, some PilZ domains lack these motifs and do not bind c-di-GMP. Proteins which contain PilZ are known to interact with the flagellar switch-complex proteins FliG and FliM. This interaction results in a reduction of torque generation and induces CCW motor bias. This is the canonical PilZ domain whose structure consists of six beta-strands that form a beta barrel, followed by a long C-terminal alpha-helix.


Pssm-ID: 399904  Cd Length: 102  Bit Score: 41.72  E-value: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820318287  10 RKADRKNCRVFGHVKYLNSQVDARILNLSPTGAALEMKGPLhAASGSKVRIEAENLGL-----LEGVIRWKHNG----RV 80
Cdd:pfam07238   3 RRFPRVPVSLPVTLRDGGGEYKGRLIDISLGGAAIRLPDEP-LALGDRVELSLDLLDDgqelaLPGRVVRIRPDedgaRV 81
                          90
                  ....*....|....*...
gi 1820318287  81 GIQF-DVNSNARAQISSY 97
Cdd:pfam07238  82 GVQFlDLDEEQRRLLVRL 99
 
Name Accession Description Interval E-value
PilZ pfam07238
PilZ domain; PilZ is a c-di-GMP binding domain found in widespread cytoplasmic receptors, ...
10-97 1.03e-05

PilZ domain; PilZ is a c-di-GMP binding domain found in widespread cytoplasmic receptors, which is involved in regulation of motility, biofilm formation and virulence of many bacterial pathogens. This domain binds c-di-GMP through RXXXR and [D/N]hSXXG motifs, however, some PilZ domains lack these motifs and do not bind c-di-GMP. Proteins which contain PilZ are known to interact with the flagellar switch-complex proteins FliG and FliM. This interaction results in a reduction of torque generation and induces CCW motor bias. This is the canonical PilZ domain whose structure consists of six beta-strands that form a beta barrel, followed by a long C-terminal alpha-helix.


Pssm-ID: 399904  Cd Length: 102  Bit Score: 41.72  E-value: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820318287  10 RKADRKNCRVFGHVKYLNSQVDARILNLSPTGAALEMKGPLhAASGSKVRIEAENLGL-----LEGVIRWKHNG----RV 80
Cdd:pfam07238   3 RRFPRVPVSLPVTLRDGGGEYKGRLIDISLGGAAIRLPDEP-LALGDRVELSLDLLDDgqelaLPGRVVRIRPDedgaRV 81
                          90
                  ....*....|....*...
gi 1820318287  81 GIQF-DVNSNARAQISSY 97
Cdd:pfam07238  82 GVQFlDLDEEQRRLLVRL 99
 
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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