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Conserved domains on  [gi|1397890671|gb|PXW91516|]
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diguanylate cyclase (GGDEF)-like protein [Streptohalobacillus salinus]

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

CATH:  3.30.70.270
EC:  2.7.7.65
Gene Ontology:  GO:0005525|GO:0046872|GO:0052621|GO:0005886
PubMed:  11119645|15063857|15289546|15306016|16530465|16045609

Graphical summary

 Zoom to residue level

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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 ...
 135-295 3.36e-42

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: 147.05  E-value: 3.36e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890671 135 ELKQKIHELKIASITDPLTKLYNRQYFYEYLFEYL--TKDSWSALSIIMIDFNDFKQVNDNYGHKAGDELLIQFAEMIHQ 212
Cdd:COG2199   102 ELRRLEERLRRLATHDPLTGLPNRRAFEERLERELarARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRA 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890671 213 HCHMG---FRFGGDEFVIISVDHDQSYIKEKLDTISRSF-------NTQTSIVTLSYGMTFIDQEQRktinskaDIDYLL 282
Cdd:COG2199   182 SLRESdlvARLGGDEFAVLLPGTDLEEAEALAERLREALeqlpfelEGKELRVTVSIGVALYPEDGD-------SAEELL 254

                         170
                  ....*....|...
gi 1397890671 283 KVADEQMYRNKRQ 295
Cdd:COG2199   255 RRADLALYRAKRA 267
 
Name Accession Description Interval E-value
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 135-295 3.36e-42

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: 147.05  E-value: 3.36e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890671 135 ELKQKIHELKIASITDPLTKLYNRQYFYEYLFEYL--TKDSWSALSIIMIDFNDFKQVNDNYGHKAGDELLIQFAEMIHQ 212
Cdd:COG2199   102 ELRRLEERLRRLATHDPLTGLPNRRAFEERLERELarARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRA 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890671 213 HCHMG---FRFGGDEFVIISVDHDQSYIKEKLDTISRSF-------NTQTSIVTLSYGMTFIDQEQRktinskaDIDYLL 282
Cdd:COG2199   182 SLRESdlvARLGGDEFAVLLPGTDLEEAEALAERLREALeqlpfelEGKELRVTVSIGVALYPEDGD-------SAEELL 254

                         170
                  ....*....|...
gi 1397890671 283 KVADEQMYRNKRQ 295
Cdd:COG2199   255 RRADLALYRAKRA 267
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 149-295 1.61e-39

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: 136.15  E-value: 1.61e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890671 149 TDPLTKLYNRQYFYEYLFEYL--TKDSWSALSIIMIDFNDFKQVNDNYGHKAGDELLIQFAEMIHQHCHMG---FRFGGD 223
Cdd:cd01949     2 TDPLTGLPNRRAFEERLERLLarARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESdlvARLGGD 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1397890671 224 EFVIISVDHDQSYIKEKLDTISRSFNTQTSI------VTLSYGMTFIDQEQRktinskaDIDYLLKVADEQMYRNKRQ 295
Cdd:cd01949    82 EFAILLPGTDLEEAEALAERLREAIEEPFFIdgqeirVTASIGIATYPEDGE-------DAEELLRRADEALYRAKRS 152
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 147-295 1.65e-33

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: 120.82  E-value: 1.65e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890671 147 SITDPLTKLYNRQYFYEYL---FEYLTKDSwSALSIIMIDFNDFKQVNDNYGHKAGDELLIQFAEMIHQHCHMG---FRF 220
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLeqeLQRALREG-SPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSdlvARL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890671 221 GGDEFVII--SVDHDQSY-----IKEKLDTISRSF--NTQTSIVTLSYGMTFIDQEQRktinskaDIDYLLKVADEQMYR 291
Cdd:pfam00990  80 GGDEFAILlpETSLEGAQelaerIRRLLAKLKIPHtvSGLPLYVTISIGIAAYPNDGE-------DPEDLLKRADTALYQ 152


                  ....
gi 1397890671 292 NKRQ 295
Cdd:pfam00990 153 AKQA 156
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 147-295 1.24e-31

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 115.81  E-value: 1.24e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890671  147 SITDPLTKLYNRQYFYEYLFEYLTK--DSWSALSIIMIDFNDFKQVNDNYGHKAGDELLIQFAEMIHQHCHMG---FRFG 221
Cdd:smart00267   3 AFRDPLTGLPNRRYFEEELEQELQRaqRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGdllARLG 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890671  222 GDEFVIISVDHDQSYIKEKLDTISRSFNTQTSI------VTLSYGMTFIDQEQRktinskaDIDYLLKVADEQMYRNKRQ 295
Cdd:smart00267  83 GDEFALLLPETSLEEAIALAERILQQLREPIIIhgiplyLTISIGVAAYPNPGE-------DAEDLLKRADTALYQAKKA 155
pleD PRK09581
response regulator PleD; Reviewed
 102-293 1.01e-24

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 103.44  E-value: 1.01e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890671 102 IPYPSDYNEMVENVLgTNAELARLFDeklNLEMELKQKIhELkiaSITDPLTKLYNRQYFYEYLFEYLTK--DSWSALSI 179
Cdd:PRK09581  255 LMRPIDKNELLARVR-TQIRRKRYQD---ALRNNLEQSI-EM---AVTDGLTGLHNRRYFDMHLKNLIERanERGKPLSL 326

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890671 180 IMIDFNDFKQVNDNYGHKAGDELLIQFAEMIHQH-------ChmgfRFGGDEFVIISVDHDQS---YIKEKLDTI--SRS 247
Cdd:PRK09581  327 MMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNirgtdliA----RYGGEEFVVVMPDTDIEdaiAVAERIRRKiaEEP 402

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1397890671 248 FNTQTSI----VTLSYGMTFIDQEQrktinskADIDYLLKVADEQMYRNK 293
Cdd:PRK09581  403 FIISDGKerlnVTVSIGVAELRPSG-------DTIEALIKRADKALYEAK 445
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 147-294 7.99e-21

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: 87.39  E-value: 7.99e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890671 147 SITDPLTKLYNRQYFYE---YLFEYLTKDSWSaLSIIMIDFNDFKQVNDNYGHKAGDELLIQFAEMIHQHCH---MGFRF 220
Cdd:TIGR00254   2 AVRDPLTGLYNRRYLEEmldSELKRARRFQRS-FSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRgsdVVGRY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890671 221 GGDEFVIISVDHDQS-------YIKEKLDTISRSFNTQTSI-VTLSYGMTFIDQEQRktinskaDIDYLLKVADEQMYRN 292
Cdd:TIGR00254  81 GGEEFVVILPGTPLEdalskaeRLRDAINSKPIEVAGSETLtVTVSIGVACYPGHGL-------TLEELLKRADEALYQA 153


                  ..
gi 1397890671 293 KR 294
Cdd:TIGR00254 154 KK 155
 
Name Accession Description Interval E-value
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 135-295 3.36e-42

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: 147.05  E-value: 3.36e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890671 135 ELKQKIHELKIASITDPLTKLYNRQYFYEYLFEYL--TKDSWSALSIIMIDFNDFKQVNDNYGHKAGDELLIQFAEMIHQ 212
Cdd:COG2199   102 ELRRLEERLRRLATHDPLTGLPNRRAFEERLERELarARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRA 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890671 213 HCHMG---FRFGGDEFVIISVDHDQSYIKEKLDTISRSF-------NTQTSIVTLSYGMTFIDQEQRktinskaDIDYLL 282
Cdd:COG2199   182 SLRESdlvARLGGDEFAVLLPGTDLEEAEALAERLREALeqlpfelEGKELRVTVSIGVALYPEDGD-------SAEELL 254

                         170
                  ....*....|...
gi 1397890671 283 KVADEQMYRNKRQ 295
Cdd:COG2199   255 RRADLALYRAKRA 267
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 149-295 1.61e-39

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: 136.15  E-value: 1.61e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890671 149 TDPLTKLYNRQYFYEYLFEYL--TKDSWSALSIIMIDFNDFKQVNDNYGHKAGDELLIQFAEMIHQHCHMG---FRFGGD 223
Cdd:cd01949     2 TDPLTGLPNRRAFEERLERLLarARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESdlvARLGGD 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1397890671 224 EFVIISVDHDQSYIKEKLDTISRSFNTQTSI------VTLSYGMTFIDQEQRktinskaDIDYLLKVADEQMYRNKRQ 295
Cdd:cd01949    82 EFAILLPGTDLEEAEALAERLREAIEEPFFIdgqeirVTASIGIATYPEDGE-------DAEELLRRADEALYRAKRS 152
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 147-295 1.65e-33

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: 120.82  E-value: 1.65e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890671 147 SITDPLTKLYNRQYFYEYL---FEYLTKDSwSALSIIMIDFNDFKQVNDNYGHKAGDELLIQFAEMIHQHCHMG---FRF 220
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLeqeLQRALREG-SPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSdlvARL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890671 221 GGDEFVII--SVDHDQSY-----IKEKLDTISRSF--NTQTSIVTLSYGMTFIDQEQRktinskaDIDYLLKVADEQMYR 291
Cdd:pfam00990  80 GGDEFAILlpETSLEGAQelaerIRRLLAKLKIPHtvSGLPLYVTISIGIAAYPNDGE-------DPEDLLKRADTALYQ 152


                  ....
gi 1397890671 292 NKRQ 295
Cdd:pfam00990 153 AKQA 156
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 147-295 1.24e-31

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 115.81  E-value: 1.24e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890671  147 SITDPLTKLYNRQYFYEYLFEYLTK--DSWSALSIIMIDFNDFKQVNDNYGHKAGDELLIQFAEMIHQHCHMG---FRFG 221
Cdd:smart00267   3 AFRDPLTGLPNRRYFEEELEQELQRaqRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGdllARLG 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890671  222 GDEFVIISVDHDQSYIKEKLDTISRSFNTQTSI------VTLSYGMTFIDQEQRktinskaDIDYLLKVADEQMYRNKRQ 295
Cdd:smart00267  83 GDEFALLLPETSLEEAIALAERILQQLREPIIIhgiplyLTISIGVAAYPNPGE-------DAEDLLKRADTALYQAKKA 155
pleD PRK09581
response regulator PleD; Reviewed
 102-293 1.01e-24

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 103.44  E-value: 1.01e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890671 102 IPYPSDYNEMVENVLgTNAELARLFDeklNLEMELKQKIhELkiaSITDPLTKLYNRQYFYEYLFEYLTK--DSWSALSI 179
Cdd:PRK09581  255 LMRPIDKNELLARVR-TQIRRKRYQD---ALRNNLEQSI-EM---AVTDGLTGLHNRRYFDMHLKNLIERanERGKPLSL 326

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890671 180 IMIDFNDFKQVNDNYGHKAGDELLIQFAEMIHQH-------ChmgfRFGGDEFVIISVDHDQS---YIKEKLDTI--SRS 247
Cdd:PRK09581  327 MMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNirgtdliA----RYGGEEFVVVMPDTDIEdaiAVAERIRRKiaEEP 402

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1397890671 248 FNTQTSI----VTLSYGMTFIDQEQrktinskADIDYLLKVADEQMYRNK 293
Cdd:PRK09581  403 FIISDGKerlnVTVSIGVAELRPSG-------DTIEALIKRADKALYEAK 445
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 135-295 3.31e-24

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: 102.93  E-value: 3.31e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890671 135 ELKQKIHELKIASITDPLTKLYNRQYFYEYLFEYLT--KDSWSALSIIMIDFNDFKQVNDNYGHKAGDELLIQFAEMIHQ 212
Cdd:COG5001   239 ERKRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALAraRRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRA 318

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890671 213 HCHMG---FRFGGDEFVII--SVDHDQSYIK--EK-LDTISRSF--NTQTSIVTLSYGMTFIDQEQRktinskaDIDYLL 282
Cdd:COG5001   319 CLREGdtvARLGGDEFAVLlpDLDDPEDAEAvaERiLAALAEPFelDGHELYVSASIGIALYPDDGA-------DAEELL 391

                         170
                  ....*....|...
gi 1397890671 283 KVADEQMYRNKRQ 295
Cdd:COG5001   392 RNADLAMYRAKAA 404
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 147-294 7.99e-21

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: 87.39  E-value: 7.99e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890671 147 SITDPLTKLYNRQYFYE---YLFEYLTKDSWSaLSIIMIDFNDFKQVNDNYGHKAGDELLIQFAEMIHQHCH---MGFRF 220
Cdd:TIGR00254   2 AVRDPLTGLYNRRYLEEmldSELKRARRFQRS-FSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRgsdVVGRY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890671 221 GGDEFVIISVDHDQS-------YIKEKLDTISRSFNTQTSI-VTLSYGMTFIDQEQRktinskaDIDYLLKVADEQMYRN 292
Cdd:TIGR00254  81 GGEEFVVILPGTPLEdalskaeRLRDAINSKPIEVAGSETLtVTVSIGVACYPGHGL-------TLEELLKRADEALYQA 153


                  ..
gi 1397890671 293 KR 294
Cdd:TIGR00254 154 KK 155
PRK09966 PRK09966
diguanylate cyclase DgcN;
125-295 2.76e-17

diguanylate cyclase DgcN;


Pssm-ID: 182171 [Multi-domain]  Cd Length: 407  Bit Score: 81.59  E-value: 2.76e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890671 125 LFDEKLNLEMELKQKIHELKIASITDPLTKLYNRQYFYEYLFEYLTKDSW-SALSIIMIDFNDFKQVNDNYGHKAGDELL 203
Cdd:PRK09966  226 LLDEMEEWQLRLQAKNAQLLRTALHDPLTGLANRAAFRSGINTLMNNSDArKTSALLFLDGDNFKYINDTWGHATGDRVL 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890671 204 IQFAEMIHQHC---HMGFRFGGDEFVIISVD-HDQSYIKEKLDTISRSF-------NTQTSIVTLS--YGMTFidqeqrk 270
Cdd:PRK09966  306 IEIAKRLAEFGglrHKAYRLGGDEFAMVLYDvQSESEVQQICSALTQIFnlpfdlhNGHQTTMTLSigYAMTI------- 378

                         170       180
                  ....*....|....*....|....*
gi 1397890671 271 tinSKADIDYLLKVADEQMYRNKRQ 295
Cdd:PRK09966  379 ---EHASAEKLQELADHNMYQAKHQ 400
PRK09894 PRK09894
diguanylate cyclase; Provisional
 106-294 2.83e-15

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 74.72  E-value: 2.83e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890671 106 SDYNEMVENVLGTNAELARLfdeklnlemelkqKIHELKIASITDPLTKLYNRQYFYEYLFEYLTKDSWSALSIIMIDFN 185
Cdd:PRK09894  101 AHFDAFQEGLLSFTAALTDY-------------KIYLLTIRSNMDVLTGLPGRRVLDESFDHQLRNREPQNLYLALLDID 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890671 186 DFKQVNDNYGHKAGDELLIQFAEMIHQHCH---MGFRFGGDEFVII---SVDHDQSYIKEKL-DTISRS---FNTQTSIV 255
Cdd:PRK09894  168 RFKLVNDTYGHLIGDVVLRTLATYLASWTRdyeTVYRYGGEEFIIClkaATDEEACRAGERIrQLIANHaitHSDGRINI 247

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1397890671 256 TLSYGMTFIDQEQrktinskaDIDYLLKVADEQMYRNKR 294
Cdd:PRK09894  248 TATFGVSRAFPEE--------TLDVVIGRADRAMYEGKQ 278
PRK15426 PRK15426
cellulose biosynthesis regulator YedQ;
149-228 4.29e-13

cellulose biosynthesis regulator YedQ;


Pssm-ID: 237964 [Multi-domain]  Cd Length: 570  Bit Score: 69.66  E-value: 4.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890671 149 TDPLTKLYNRQYFYEyLFEYLTKD---SWSALSIIMIDFNDFKQVNDNYGHKAGDELLIQFAEMIHQHCHMG---FRFGG 222
Cdd:PRK15426  400 HDPLTRLYNRGALFE-KARALAKRcqrDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQdvaGRVGG 478


                  ....*.
gi 1397890671 223 DEFVII 228
Cdd:PRK15426  479 EEFCVV 484
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 150-299 2.58e-12

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 67.49  E-value: 2.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890671 150 DPLTKLYNRQYFYEYLFEYLTKDSwsALSIIMIDFNDFKQVNDNYGHKAGDELLIQFAEMIHQHCHMG---FRFGGDEFV 226
Cdd:PRK11359  379 DPLTGLPNRNNLHNYLDDLVDKAV--SPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDqylCRIEGTQFV 456

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1397890671 227 IISVD---HDQSYIKEKLDTISR---SFNTQTSIVTLSYGmtfIDQEQRKtinskaDIDYLLKVADEQMyrnkRQVKKN 299
Cdd:PRK11359  457 LVSLEndvSNITQIADELRNVVSkpiMIDDKPFPLTLSIG---ISYDVGK------NRDYLLSTAHNAM----DYIRKN 522
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 142-278 1.02e-10

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 62.77  E-value: 1.02e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890671  142 ELKIASITDPLTKLYNRQYFYEYLFEYLTK----DSWSALsiIMIDFNDFKQVNDNYGHKAGDELLIQFAEMIHQHCH-- 215
Cdd:PRK09776   660 QLSYSASHDALTHLANRASFEKQLRRLLQTvnstHQRHAL--VFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRss 737

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1397890671  216 -MGFRFGGDEFVII----SVDHDQsYIKEKL-DTI-SRSFNTQTSI--VTLSYGMTFIDQE--QRKTINSKADI 278
Cdd:PRK09776   738 dVLARLGGDEFGLLlpdcNVESAR-FIATRIiSAInDYHFPWEGRVyrVGASAGITLIDANnhQASEVMSQADI 810
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
143-235 1.47e-10

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 62.01  E-value: 1.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890671 143 LKIASITDPLTKLYNRQYFYEYLFEYLTKDSWSALSIIMIDFNDFKQVNDNYGHKAGDELLIQFAEMIH---QHCHMGFR 219
Cdd:PRK10060  233 LRILANTDSITGLPNRNAIQELIDHAINAADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILsclEEDQTLAR 312

                          90
                  ....*....|....*.
gi 1397890671 220 FGGDEFVIISVDHDQS 235
Cdd:PRK10060  313 LGGDEFLVLASHTSQA 328
adrA PRK10245
diguanylate cyclase AdrA; Provisional
 143-228 2.48e-09

diguanylate cyclase AdrA; Provisional


Pssm-ID: 182329 [Multi-domain]  Cd Length: 366  Bit Score: 57.53  E-value: 2.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890671 143 LKIASITDPLTKLYNRQYFYEYL---FEYLTKDSWSAlSIIMIDFNDFKQVNDNYGHKAGDELLIQFAEMIHQHCHMG-- 217
Cdd:PRK10245  201 LQVMSTRDGMTGVYNRRHWETLLrneFDNCRRHHRDA-TLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSdv 279

                          90
                  ....*....|..
gi 1397890671 218 -FRFGGDEFVII 228
Cdd:PRK10245  280 iGRFGGDEFAVI 291
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
 177-232 1.20e-06

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: 46.97  E-value: 1.20e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1397890671 177 LSIIMIDFNDFKQVNDNYGHKAGDELLIQFAEMIHQHC--HMGF--RFGGDEFVIIS-VDH 232
Cdd:cd07556     2 VTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIrrSGDLkiKTIGDEFMVVSgLDH 62
 
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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