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Conserved domains on  [gi|446575878|ref|WP_000653224|]
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MULTISPECIES: diguanylate cyclase [Bacillaceae]

Protein Classification

nucleotidyl cyclase domain-containing protein( domain architecture ID 34085)

nucleotidyl cyclase domain-containing protein may function as a mononucleotidyl cyclase (MNC) or a diguanylate cyclase (DGC)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GGDEF super family cl43640
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 30-239 4.58e-06

GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants [Signal transduction mechanisms];


The actual alignment was detected with superfamily member COG2199:

Pssm-ID: 441801 [Multi-domain]  Cd Length: 275  Bit Score: 46.51  E-value: 4.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446575878  30 HALIFTLIYVIVNVLFLFLADKTAFIFFILGTIISVFYLFYQAWLHLWSTSDQWQYMITHFLMAANFFIVYITTHLLKKV 109
Cdd:COG2199   20 LSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLLLLALED 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446575878 110 IHENKALTERVRTLEQYIGESKLLTRQEFERRQALLTTAMNRRNETGIIVYFDFTSFSKYTKE---SVMDRV----ASLL 182
Cdd:COG2199  100 ITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTyghAAGDEVlkevARRL 179

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446575878 183 VETVRNDfDLAAEYDNNTLVILLQNTNEAGADIVMNRLKPKMEQWLAAEAIKDIKIS 239
Cdd:COG2199  180 RASLRES-DLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELEGKELRVT 235
 
Name Accession Description Interval E-value
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 30-239 4.58e-06

GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants [Signal transduction mechanisms];


Pssm-ID: 441801 [Multi-domain]  Cd Length: 275  Bit Score: 46.51  E-value: 4.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446575878  30 HALIFTLIYVIVNVLFLFLADKTAFIFFILGTIISVFYLFYQAWLHLWSTSDQWQYMITHFLMAANFFIVYITTHLLKKV 109
Cdd:COG2199   20 LSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLLLLALED 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446575878 110 IHENKALTERVRTLEQYIGESKLLTRQEFERRQALLTTAMNRRNETGIIVYFDFTSFSKYTKE---SVMDRV----ASLL 182
Cdd:COG2199  100 ITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTyghAAGDEVlkevARRL 179

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446575878 183 VETVRNDfDLAAEYDNNTLVILLQNTNEAGADIVMNRLKPKMEQWLAAEAIKDIKIS 239
Cdd:COG2199  180 RASLRES-DLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELEGKELRVT 235
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 131-239 9.27e-03

Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of non-homologous domains in a variety of bacteria. It has been shown to be homologous to the adenylyl cyclase catalytic domain and has diguanylate cyclase activity. This observation correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. In the WspR protein of Pseudomonas aeruginosa, the GGDEF domain acts as a diguanylate cyclase, PDB:3bre, when the whole molecule appears to form a tetramer consisting of two symmetrically-related dimers representing a biological unit. The active site is the GGD/EF motif, buried in the structure, and the cyclic dimeric guanosine monophosphate (c-di-GMP) bind to the inhibitory-motif RxxD on the surface. The enzyme thus catalyzes the cyclization of two guanosine triphosphate (GTP) molecules to one c-di-GMP molecule.


Pssm-ID: 425976 [Multi-domain]  Cd Length: 160  Bit Score: 35.69  E-value: 9.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446575878  131 KLLTRQEFERRqalLTTAMN---RRNETGIIVYFDFTSFSKY-------TKESVMDRVASLLVETVRNDfDLAAEYDNNT 200
Cdd:pfam00990   8 GLPNRRYFEEQ---LEQELQralREGSPVAVLLIDLDNFKRIndtyghsVGDEVLQEVAQRLSSSLRRS-DLVARLGGDE 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 446575878  201 LVILLQNTNEAGADIVMNRLKPKMEQ----WLAAEAIKDIKIS 239
Cdd:pfam00990  84 FAILLPETSLEGAQELAERIRRLLAKlkipHTVSGLPLYVTIS 126
 
Name Accession Description Interval E-value
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 30-239 4.58e-06

GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants [Signal transduction mechanisms];


Pssm-ID: 441801 [Multi-domain]  Cd Length: 275  Bit Score: 46.51  E-value: 4.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446575878  30 HALIFTLIYVIVNVLFLFLADKTAFIFFILGTIISVFYLFYQAWLHLWSTSDQWQYMITHFLMAANFFIVYITTHLLKKV 109
Cdd:COG2199   20 LSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLLLLALED 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446575878 110 IHENKALTERVRTLEQYIGESKLLTRQEFERRQALLTTAMNRRNETGIIVYFDFTSFSKYTKE---SVMDRV----ASLL 182
Cdd:COG2199  100 ITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTyghAAGDEVlkevARRL 179

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446575878 183 VETVRNDfDLAAEYDNNTLVILLQNTNEAGADIVMNRLKPKMEQWLAAEAIKDIKIS 239
Cdd:COG2199  180 RASLRES-DLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELEGKELRVT 235
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 131-239 9.27e-03

Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of non-homologous domains in a variety of bacteria. It has been shown to be homologous to the adenylyl cyclase catalytic domain and has diguanylate cyclase activity. This observation correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. In the WspR protein of Pseudomonas aeruginosa, the GGDEF domain acts as a diguanylate cyclase, PDB:3bre, when the whole molecule appears to form a tetramer consisting of two symmetrically-related dimers representing a biological unit. The active site is the GGD/EF motif, buried in the structure, and the cyclic dimeric guanosine monophosphate (c-di-GMP) bind to the inhibitory-motif RxxD on the surface. The enzyme thus catalyzes the cyclization of two guanosine triphosphate (GTP) molecules to one c-di-GMP molecule.


Pssm-ID: 425976 [Multi-domain]  Cd Length: 160  Bit Score: 35.69  E-value: 9.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446575878  131 KLLTRQEFERRqalLTTAMN---RRNETGIIVYFDFTSFSKY-------TKESVMDRVASLLVETVRNDfDLAAEYDNNT 200
Cdd:pfam00990   8 GLPNRRYFEEQ---LEQELQralREGSPVAVLLIDLDNFKRIndtyghsVGDEVLQEVAQRLSSSLRRS-DLVARLGGDE 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 446575878  201 LVILLQNTNEAGADIVMNRLKPKMEQ----WLAAEAIKDIKIS 239
Cdd:pfam00990  84 FAILLPETSLEGAQELAERIRRLLAKlkipHTVSGLPLYVTIS 126
 
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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