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Conserved domains on  [gi|916565459|ref|WP_051172550|]
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MULTISPECIES: GGDEF domain-containing protein [Amycolatopsis]

Protein Classification

GGDEF domain-containing protein( domain architecture ID 10005578)

GGDEF domain-containing protein may have diguanylate cyclase (DGC) activity, similar to Escherichia coli DgcT (YcdT) and to E. coli CdgI (YeaI), a c-di-GMP-binding effector with a degenerate GGDEF domain which binds c-di-GMP

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
2-207 1.33e-44

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: 150.13  E-value: 1.33e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916565459   2 AEVRVSADDELGTGETAPDLLTLHESIADLFATRGDWRRAYRHLRSALDIARAGSLRDPLTSSYNRRYLDQRLPEL---- 77
Cdd:COG2199   60 LVLLLLALGLLLLALLLLSLVLELLLLLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERElara 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916565459  78 ---PAAVAVALVDLDRFKSVNDTYGHLLGDRVLCRVADLLQEGLPADAFCARYGGEEFALVLPGIDHRGAVRVADAARRR 154
Cdd:COG2199  140 rreGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREA 219
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 916565459 155 VARHPWSELRPGLRVTISVGLAHGTESGPRQ---LHRADNLLYAAKRAGRNKVAFH 207
Cdd:COG2199  220 LEQLPFELEGKELRVTVSIGVALYPEDGDSAeelLRRADLALYRAKRAGRNRVVVY 275
 
Name Accession Description Interval E-value
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
2-207 1.33e-44

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: 150.13  E-value: 1.33e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916565459   2 AEVRVSADDELGTGETAPDLLTLHESIADLFATRGDWRRAYRHLRSALDIARAGSLRDPLTSSYNRRYLDQRLPEL---- 77
Cdd:COG2199   60 LVLLLLALGLLLLALLLLSLVLELLLLLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERElara 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916565459  78 ---PAAVAVALVDLDRFKSVNDTYGHLLGDRVLCRVADLLQEGLPADAFCARYGGEEFALVLPGIDHRGAVRVADAARRR 154
Cdd:COG2199  140 rreGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREA 219
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 916565459 155 VARHPWSELRPGLRVTISVGLAHGTESGPRQ---LHRADNLLYAAKRAGRNKVAFH 207
Cdd:COG2199  220 LEQLPFELEGKELRVTVSIGVALYPEDGDSAeelLRRADLALYRAKRAGRNRVVVY 275
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
57-205 3.58e-43

Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as a domain of unknown function 1 (DUF1). This domain is widely present in bacteria, linked to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain shows homology to the adenylyl cyclase catalytic domain. This 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. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesion in bacteria.


Pssm-ID: 143635 [Multi-domain]  Cd Length: 158  Bit Score: 142.70  E-value: 3.58e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916565459  57 LRDPLTSSYNRRYLDQRLPELPAA-------VAVALVDLDRFKSVNDTYGHLLGDRVLCRVADLLQEGLPADAFCARYGG 129
Cdd:cd01949    1 YTDPLTGLPNRRAFEERLERLLARarrsgrpLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 916565459 130 EEFALVLPGIDHRGAVRVADAARRRVARHPWSELRPgLRVTISVGLAHGTESG--PRQL-HRADNLLYAAKRAGRNKVA 205
Cdd:cd01949   81 DEFAILLPGTDLEEAEALAERLREAIEEPFFIDGQE-IRVTASIGIATYPEDGedAEELlRRADEALYRAKRSGRNRVV 158
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
56-207 1.30e-40

diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 136.22  E-value: 1.30e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916565459    56 SLRDPLTSSYNRRYLDQRLPELPAA-------VAVALVDLDRFKSVNDTYGHLLGDRVLCRVADLLQEGLPADAFCARYG 128
Cdd:smart00267   3 AFRDPLTGLPNRRYFEEELEQELQRaqrqgspFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARLG 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916565459   129 GEEFALVLPGIDHRGAVRVADAARRRVARHPWSELRPgLRVTISVGLAHGTESGPRQ---LHRADNLLYAAKRAGRNKVA 205
Cdd:smart00267  83 GDEFALLLPETSLEEAIALAERILQQLREPIIIHGIP-LYLTISIGVAAYPNPGEDAedlLKRADTALYQAKKAGRNQVA 161

                   ..
gi 916565459   206 FH 207
Cdd:smart00267 162 VY 163
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
56-203 3.07e-38

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: 130.07  E-value: 3.07e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916565459   56 SLRDPLTSSYNRRYLDQRLPEL-------PAAVAVALVDLDRFKSVNDTYGHLLGDRVLCRVADLLQEGLPADAFCARYG 128
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQElqralreGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916565459  129 GEEFALVLPGIDHRGAVRVADAARRRVARH--PWSELRPGLRVTISVGLAHGTESG--PRQL-HRADNLLYAAKRAGRNK 203
Cdd:pfam00990  81 GDEFAILLPETSLEGAQELAERIRRLLAKLkiPHTVSGLPLYVTISIGIAAYPNDGedPEDLlKRADTALYQAKQAGRNR 160
diguan_SiaD NF038266
biofilm regulation diguanylate cyclase SiaD;
43-204 6.41e-35

biofilm regulation diguanylate cyclase SiaD;


Pssm-ID: 468439 [Multi-domain]  Cd Length: 252  Bit Score: 124.32  E-value: 6.41e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916565459  43 RHLRSALdiaRAGSLRDPLTSSYNRRYLDQRLPELPA-------AVAVALVDLDRFKSVNDTYGHLLGDRVLCRVADLLQ 115
Cdd:NF038266  84 RDLNEAL---REASTRDPLTGLPNRRLLMERLREEVErarrsgrPFTLAMLDVDHFKRINDRYGHEVGDRVLVEIARTLR 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916565459 116 EGLPADAFCARYGGEEFALVLPGIDHRGAVRVADAARRRVARHPWSELRPGLRVTISVGLA---HGTESGPRQLHRADNL 192
Cdd:NF038266 161 AELREYDLCGRWGGEEFLLLLPETGLEEAQVVLERLREAVRALAVRVGDDVLSVTASAGLAehrPPEEGLSATLSRADQA 240
                        170
                 ....*....|..
gi 916565459 193 LYAAKRAGRNKV 204
Cdd:NF038266 241 LYQAKRAGRDRV 252
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
56-204 2.12e-33

diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by many proteins carrying the domain. There is evidence that the domain has diguanylate cyclase activity. Several proteins carrying this domain also carry domains with functions relating to environmental sensing. These include PleD, a response regulator protein involved in the swarmer-to-stalked cell transition in Caulobacter crescentus, and FixL, a heme-containing oxygen sensor protein. [Regulatory functions, Small molecule interactions, Signal transduction, Other]


Pssm-ID: 272984 [Multi-domain]  Cd Length: 165  Bit Score: 117.82  E-value: 2.12e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916565459   56 SLRDPLTSSYNRRYLDQRL-PELPAA------VAVALVDLDRFKSVNDTYGHLLGDRVLCRVADLLQEGLPADAFCARYG 128
Cdd:TIGR00254   2 AVRDPLTGLYNRRYLEEMLdSELKRArrfqrsFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916565459  129 GEEFALVLPGIDHRGAVRVADAARRRVARHPWS-ELRPGLRVTISVGLAHGTESG--PRQL-HRADNLLYAAKRAGRNKV 204
Cdd:TIGR00254  82 GEEFVVILPGTPLEDALSKAERLRDAINSKPIEvAGSETLTVTVSIGVACYPGHGltLEELlKRADEALYQAKKAGRNRV 161
pleD PRK09581
response regulator PleD; Reviewed
39-204 3.13e-29

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 113.07  E-value: 3.13e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916565459  39 RRAYR-HLRSALDIARAGSLRDPLTSSYNRRYLDQRLPELPA-------AVAVALVDLDRFKSVNDTYGHLLGDRVL--- 107
Cdd:PRK09581 274 RKRYQdALRNNLEQSIEMAVTDGLTGLHNRRYFDMHLKNLIEranergkPLSLMMIDIDHFKKVNDTYGHDAGDEVLref 353
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916565459 108 -------CRVADLLqeglpadafcARYGGEEFALVLPGIDHRGAVRVADAARRRVARHPW--SELRPGLRVTISVGLAHG 178
Cdd:PRK09581 354 akrlrnnIRGTDLI----------ARYGGEEFVVVMPDTDIEDAIAVAERIRRKIAEEPFiiSDGKERLNVTVSIGVAEL 423
                        170       180
                 ....*....|....*....|....*....
gi 916565459 179 TESG--PRQL-HRADNLLYAAKRAGRNKV 204
Cdd:PRK09581 424 RPSGdtIEALiKRADKALYEAKNTGRNRV 452
 
Name Accession Description Interval E-value
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
2-207 1.33e-44

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: 150.13  E-value: 1.33e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916565459   2 AEVRVSADDELGTGETAPDLLTLHESIADLFATRGDWRRAYRHLRSALDIARAGSLRDPLTSSYNRRYLDQRLPEL---- 77
Cdd:COG2199   60 LVLLLLALGLLLLALLLLSLVLELLLLLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERElara 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916565459  78 ---PAAVAVALVDLDRFKSVNDTYGHLLGDRVLCRVADLLQEGLPADAFCARYGGEEFALVLPGIDHRGAVRVADAARRR 154
Cdd:COG2199  140 rreGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREA 219
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 916565459 155 VARHPWSELRPGLRVTISVGLAHGTESGPRQ---LHRADNLLYAAKRAGRNKVAFH 207
Cdd:COG2199  220 LEQLPFELEGKELRVTVSIGVALYPEDGDSAeelLRRADLALYRAKRAGRNRVVVY 275
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
57-205 3.58e-43

Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as a domain of unknown function 1 (DUF1). This domain is widely present in bacteria, linked to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain shows homology to the adenylyl cyclase catalytic domain. This 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. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesion in bacteria.


Pssm-ID: 143635 [Multi-domain]  Cd Length: 158  Bit Score: 142.70  E-value: 3.58e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916565459  57 LRDPLTSSYNRRYLDQRLPELPAA-------VAVALVDLDRFKSVNDTYGHLLGDRVLCRVADLLQEGLPADAFCARYGG 129
Cdd:cd01949    1 YTDPLTGLPNRRAFEERLERLLARarrsgrpLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 916565459 130 EEFALVLPGIDHRGAVRVADAARRRVARHPWSELRPgLRVTISVGLAHGTESG--PRQL-HRADNLLYAAKRAGRNKVA 205
Cdd:cd01949   81 DEFAILLPGTDLEEAEALAERLREAIEEPFFIDGQE-IRVTASIGIATYPEDGedAEELlRRADEALYRAKRSGRNRVV 158
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
56-207 1.30e-40

diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 136.22  E-value: 1.30e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916565459    56 SLRDPLTSSYNRRYLDQRLPELPAA-------VAVALVDLDRFKSVNDTYGHLLGDRVLCRVADLLQEGLPADAFCARYG 128
Cdd:smart00267   3 AFRDPLTGLPNRRYFEEELEQELQRaqrqgspFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARLG 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916565459   129 GEEFALVLPGIDHRGAVRVADAARRRVARHPWSELRPgLRVTISVGLAHGTESGPRQ---LHRADNLLYAAKRAGRNKVA 205
Cdd:smart00267  83 GDEFALLLPETSLEEAIALAERILQQLREPIIIHGIP-LYLTISIGVAAYPNPGEDAedlLKRADTALYQAKKAGRNQVA 161

                   ..
gi 916565459   206 FH 207
Cdd:smart00267 162 VY 163
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
56-203 3.07e-38

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: 130.07  E-value: 3.07e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916565459   56 SLRDPLTSSYNRRYLDQRLPEL-------PAAVAVALVDLDRFKSVNDTYGHLLGDRVLCRVADLLQEGLPADAFCARYG 128
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQElqralreGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916565459  129 GEEFALVLPGIDHRGAVRVADAARRRVARH--PWSELRPGLRVTISVGLAHGTESG--PRQL-HRADNLLYAAKRAGRNK 203
Cdd:pfam00990  81 GDEFAILLPETSLEGAQELAERIRRLLAKLkiPHTVSGLPLYVTISIGIAAYPNDGedPEDLlKRADTALYQAKQAGRNR 160
diguan_SiaD NF038266
biofilm regulation diguanylate cyclase SiaD;
43-204 6.41e-35

biofilm regulation diguanylate cyclase SiaD;


Pssm-ID: 468439 [Multi-domain]  Cd Length: 252  Bit Score: 124.32  E-value: 6.41e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916565459  43 RHLRSALdiaRAGSLRDPLTSSYNRRYLDQRLPELPA-------AVAVALVDLDRFKSVNDTYGHLLGDRVLCRVADLLQ 115
Cdd:NF038266  84 RDLNEAL---REASTRDPLTGLPNRRLLMERLREEVErarrsgrPFTLAMLDVDHFKRINDRYGHEVGDRVLVEIARTLR 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916565459 116 EGLPADAFCARYGGEEFALVLPGIDHRGAVRVADAARRRVARHPWSELRPGLRVTISVGLA---HGTESGPRQLHRADNL 192
Cdd:NF038266 161 AELREYDLCGRWGGEEFLLLLPETGLEEAQVVLERLREAVRALAVRVGDDVLSVTASAGLAehrPPEEGLSATLSRADQA 240
                        170
                 ....*....|..
gi 916565459 193 LYAAKRAGRNKV 204
Cdd:NF038266 241 LYQAKRAGRDRV 252
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
56-204 2.12e-33

diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by many proteins carrying the domain. There is evidence that the domain has diguanylate cyclase activity. Several proteins carrying this domain also carry domains with functions relating to environmental sensing. These include PleD, a response regulator protein involved in the swarmer-to-stalked cell transition in Caulobacter crescentus, and FixL, a heme-containing oxygen sensor protein. [Regulatory functions, Small molecule interactions, Signal transduction, Other]


Pssm-ID: 272984 [Multi-domain]  Cd Length: 165  Bit Score: 117.82  E-value: 2.12e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916565459   56 SLRDPLTSSYNRRYLDQRL-PELPAA------VAVALVDLDRFKSVNDTYGHLLGDRVLCRVADLLQEGLPADAFCARYG 128
Cdd:TIGR00254   2 AVRDPLTGLYNRRYLEEMLdSELKRArrfqrsFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916565459  129 GEEFALVLPGIDHRGAVRVADAARRRVARHPWS-ELRPGLRVTISVGLAHGTESG--PRQL-HRADNLLYAAKRAGRNKV 204
Cdd:TIGR00254  82 GEEFVVILPGTPLEDALSKAERLRDAINSKPIEvAGSETLTVTVSIGVACYPGHGltLEELlKRADEALYQAKKAGRNRV 161
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
56-210 2.71e-29

Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain [Signal transduction mechanisms];


Pssm-ID: 444025 [Multi-domain]  Cd Length: 678  Bit Score: 114.49  E-value: 2.71e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916565459  56 SLRDPLTSSYNRRYLDQRLPEL-------PAAVAVALVDLDRFKSVNDTYGHLLGDRVLCRVADLLQEGLPADAFCARYG 128
Cdd:COG5001  251 AYHDPLTGLPNRRLFLDRLEQAlararrsGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLG 330
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916565459 129 GEEFALVLPGIDHRGAVRVADAARRRVARHPWSELRPGLRVTISVGLAHGTESG--PRQL-HRADNLLYAAKRAGRNKVA 205
Cdd:COG5001  331 GDEFAVLLPDLDDPEDAEAVAERILAALAEPFELDGHELYVSASIGIALYPDDGadAEELlRNADLAMYRAKAAGRNRYR 410

                 ....*
gi 916565459 206 FHDRE 210
Cdd:COG5001  411 FFDPE 415
pleD PRK09581
response regulator PleD; Reviewed
39-204 3.13e-29

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 113.07  E-value: 3.13e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916565459  39 RRAYR-HLRSALDIARAGSLRDPLTSSYNRRYLDQRLPELPA-------AVAVALVDLDRFKSVNDTYGHLLGDRVL--- 107
Cdd:PRK09581 274 RKRYQdALRNNLEQSIEMAVTDGLTGLHNRRYFDMHLKNLIEranergkPLSLMMIDIDHFKKVNDTYGHDAGDEVLref 353
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916565459 108 -------CRVADLLqeglpadafcARYGGEEFALVLPGIDHRGAVRVADAARRRVARHPW--SELRPGLRVTISVGLAHG 178
Cdd:PRK09581 354 akrlrnnIRGTDLI----------ARYGGEEFVVVMPDTDIEDAIAVAERIRRKIAEEPFiiSDGKERLNVTVSIGVAEL 423
                        170       180
                 ....*....|....*....|....*....
gi 916565459 179 TESG--PRQL-HRADNLLYAAKRAGRNKV 204
Cdd:PRK09581 424 RPSGdtIEALiKRADKALYEAKNTGRNRV 452
PRK15426 PRK15426
cellulose biosynthesis regulator YedQ;
39-209 1.53e-26

cellulose biosynthesis regulator YedQ;


Pssm-ID: 237964 [Multi-domain]  Cd Length: 570  Bit Score: 106.25  E-value: 1.53e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916565459  39 RRAYRHLrsaldIARAGSLR-----DPLTSSYNRRYLDQRLPELPAA-------VAVALVDLDRFKSVNDTYGHLLGDRV 106
Cdd:PRK15426 381 RRMVSNM-----FVLQSSLQwqawhDPLTRLYNRGALFEKARALAKRcqrdqqpFSVIQLDLDHFKSINDRFGHQAGDRV 455
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916565459 107 LCRVADLLQEGLPADAFCARYGGEEFALVLPGIDHRGAVRVADAARRRVARHPwSELRPG--LRVTISVGLAHGTESGPR 184
Cdd:PRK15426 456 LSHAAGLISSSLRAQDVAGRVGGEEFCVVLPGASLAEAAQVAERIRLRINEKE-ILVAKSttIRISASLGVSSAEEDGDY 534
                        170       180
                 ....*....|....*....|....*....
gi 916565459 185 QLHR----ADNLLYAAKRAGRNKVAFHDR 209
Cdd:PRK15426 535 DFEQlqslADRRLYLAKQAGRNRVCASDN 563
PRK09894 PRK09894
diguanylate cyclase; Provisional
39-217 3.09e-26

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 102.45  E-value: 3.09e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916565459  39 RRAYRHLRSALdiARAGSLRDPLTSSYNRRYLD-----QRLPELPAAVAVALVDLDRFKSVNDTYGHLLGDRVLCRVADL 113
Cdd:PRK09894 114 TAALTDYKIYL--LTIRSNMDVLTGLPGRRVLDesfdhQLRNREPQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATY 191
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916565459 114 LQEGLPADAFCARYGGEEFALVLPGIDHRGAVRVADAARRRVARHPWSELRPGLRVTISVGL--AHGTESGPRQLHRADN 191
Cdd:PRK09894 192 LASWTRDYETVYRYGGEEFIICLKAATDEEACRAGERIRQLIANHAITHSDGRINITATFGVsrAFPEETLDVVIGRADR 271
                        170       180
                 ....*....|....*....|....*.
gi 916565459 192 LLYAAKRAGRNKVAFHDREtaQVITH 217
Cdd:PRK09894 272 AMYEGKQTGRNRVMFIDEQ--NVINR 295
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
59-219 2.27e-18

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 83.18  E-value: 2.27e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916565459   59 DPLTSSYNRRYLDQRLPELPAAV-------AVALVDLDRFKSVNDTYGHLLGDRVLCRVADLLQEGLPADAFCARYGGEE 131
Cdd:PRK09776  668 DALTHLANRASFEKQLRRLLQTVnsthqrhALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSDVLARLGGDE 747
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916565459  132 FALVLP--GIDHRGAVRVADAARRRVARHPWsELRPgLRVTISVGLAHGTESGPRQ---LHRADNLLYAAKRAGRNKVAF 206
Cdd:PRK09776  748 FGLLLPdcNVESARFIATRIISAINDYHFPW-EGRV-YRVGASAGITLIDANNHQAsevMSQADIACYAAKNAGRGRVTV 825
                         170
                  ....*....|...
gi 916565459  207 HDRETAQVITHSE 219
Cdd:PRK09776  826 YEPQQAAAHSEHR 838
adrA PRK10245
diguanylate cyclase AdrA; Provisional
56-203 5.66e-15

diguanylate cyclase AdrA; Provisional


Pssm-ID: 182329 [Multi-domain]  Cd Length: 366  Bit Score: 72.55  E-value: 5.66e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916565459  56 SLRDPLTSSYNRRYLDQRL-PELPAA------VAVALVDLDRFKSVNDTYGHLLGDRVLCRVADLLQEGLPADAFCARYG 128
Cdd:PRK10245 205 STRDGMTGVYNRRHWETLLrNEFDNCrrhhrdATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSDVIGRFG 284
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916565459 129 GEEFALVLPGIDHRGAVRVADAARRRVarhpwSELR----PGLRVTISVGLAH-GTESGPRQ--LHRADNLLYAAKRAGR 201
Cdd:PRK10245 285 GDEFAVIMSGTPAESAITAMSRVHEGL-----NTLRlpnaPQVTLRISVGVAPlNPQMSHYRewLKSADLALYKAKNAGR 359

                 ..
gi 916565459 202 NK 203
Cdd:PRK10245 360 NR 361
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
59-203 3.87e-14

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 70.48  E-value: 3.87e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916565459  59 DPLTSSYNRRYLDQRLPEL-----PAAVAVALVDLDRFKSVNDTYGHLLGDRVLCRVADLLQEGLPADAFCARYGGEEFa 133
Cdd:PRK10060 240 DSITGLPNRNAIQELIDHAinaadNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQTLARLGGDEF- 318
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 916565459 134 LVLPGIDHRGAVRVADAARRRVARHPWS----ELRPGLRVTISVGLAHGTESgpRQLHR-ADNLLYAAKRAGRNK 203
Cdd:PRK10060 319 LVLASHTSQAALEAMASRILTRLRLPFRigliEVYTGCSIGIALAPEHGDDS--ESLIRsADTAMYTAKEGGRGQ 391
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
23-140 6.24e-14

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 70.18  E-value: 6.24e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916565459  23 TLHESIADlfatrgdwrrAYRHLrSALDIARAGSLR--------DPLTSSYNRRYLDQRLPEL---PAAVAVALVDLDRF 91
Cdd:PRK11359 346 AFIERVAD----------ISQHL-AALALEQEKSRQhieqliqfDPLTGLPNRNNLHNYLDDLvdkAVSPVVYLIGVDHF 414
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 916565459  92 KSVNDTYGHLLGDRVLCRVADLLQEGLPADAFCARYGGEEFALVLPGID 140
Cdd:PRK11359 415 QDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGTQFVLVSLEND 463
PRK09966 PRK09966
diguanylate cyclase DgcN;
56-201 3.17e-12

diguanylate cyclase DgcN;


Pssm-ID: 182171 [Multi-domain]  Cd Length: 407  Bit Score: 64.64  E-value: 3.17e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916565459  56 SLRDPLTSSYNRRYLDQRLPEL------PAAVAVALVDLDRFKSVNDTYGHLLGDRVLCRVADLLQE--GLPADAFcaRY 127
Cdd:PRK09966 248 ALHDPLTGLANRAAFRSGINTLmnnsdaRKTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEfgGLRHKAY--RL 325
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916565459 128 GGEEFALVLPGIDHRGAVRVADAARRRVARHPWsELRPGLRV--TISVGLA----HGTESGPRQLhrADNLLYAAK--RA 199
Cdd:PRK09966 326 GGDEFAMVLYDVQSESEVQQICSALTQIFNLPF-DLHNGHQTtmTLSIGYAmtieHASAEKLQEL--ADHNMYQAKhqRA 402

                 ..
gi 916565459 200 GR 201
Cdd:PRK09966 403 EK 404
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
81-197 4.35e-08

Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse group of nucleotidyl cyclases (NC's) containing prokaryotic and eukaryotic proteins. They can be divided into two major groups; the mononucleotidyl cyclases (MNC's) and the diguanylate cyclases (DGC's). The MNC's, which include the adenylate cyclases (AC's) and the guanylate cyclases (GC's), have a conserved cyclase homology domain (CHD), while the DGC's have a conserved GGDEF domain, named after a conserved motif within this subgroup. Their products, cyclic guanylyl and adenylyl nucleotides, are second messengers that play important roles in eukaryotic signal transduction and prokaryotic sensory pathways.


Pssm-ID: 143637 [Multi-domain]  Cd Length: 133  Bit Score: 50.05  E-value: 4.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916565459  81 VAVALVDLDRFKSVNDTYGHLLGDRVLCRVADLLQEGL--PADAFCaRYGGEEFALVLPGIDHRGAVRVADAARRRVARH 158
Cdd:cd07556    2 VTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIrrSGDLKI-KTIGDEFMVVSGLDHPAAAVAFAEDMREAVSAL 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 916565459 159 PWSELRPglrVTISVGLAHG------TESGPR------QLHRADNLLYAAK 197
Cdd:cd07556   81 NQSEGNP---VRVRIGIHTGpvvvgvIGSRPQydvwgaLVNLASRMESQAK 128
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
123-196 6.66e-06

Two-component response regulator, PleD family, consists of two REC domains and a diguanylate cyclase (GGDEF) domain [Signal transduction mechanisms, Transcription];


Pssm-ID: 442920 [Multi-domain]  Cd Length: 179  Bit Score: 44.90  E-value: 6.66e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 916565459 123 FCARYGGEEFALVLPGIDHRGAVRVADAARRRVARHpwselrPGLRVTISVGLAhgtesGPRQLHRADNLLYAA 196
Cdd:COG3706  117 LVARYGGEEFAILLPGTDLEGALAVAERIREAVAEL------PSLRVTVSIGVA-----GDSLLKRADALYQAR 179
 
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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