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Conserved domains on  [gi|2571039743|ref|WP_307766418|]
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diguanylate cyclase domain-containing protein [Aeromonas rivipollensis]

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

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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 ...
 316-474 5.46e-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: 151.28  E-value: 5.46e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2571039743 316 RSLVTRLRTLAQTDHLTRLPRR----DILDEALLREHDY-----LMILDIDNFKAVNDTHGHGVGDLALVAFATHLKANI 386
Cdd:COG2199   104 RRLEERLRRLATHDPLTGLPNRrafeERLERELARARREgrplaLLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASL 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2571039743 387 RKGDAAIRWGGEEFIVLFKGVENDEMMRLfATRLLER----PLRIPELPAPITFSAGVIRLR-DYLSVTEAVQLADELLY 461
Cdd:COG2199   184 RESDLVARLGGDEFAVLLPGTDLEEAEAL-AERLREAleqlPFELEGKELRVTVSIGVALYPeDGDSAEELLRRADLALY 262

                         170
                  ....*....|...
gi 2571039743 462 HVKQHGKHNIAYY 474
Cdd:COG2199   263 RAKRAGRNRVVVY 275
 
Name Accession Description Interval E-value
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 316-474 5.46e-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: 151.28  E-value: 5.46e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2571039743 316 RSLVTRLRTLAQTDHLTRLPRR----DILDEALLREHDY-----LMILDIDNFKAVNDTHGHGVGDLALVAFATHLKANI 386
Cdd:COG2199   104 RRLEERLRRLATHDPLTGLPNRrafeERLERELARARREgrplaLLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASL 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2571039743 387 RKGDAAIRWGGEEFIVLFKGVENDEMMRLfATRLLER----PLRIPELPAPITFSAGVIRLR-DYLSVTEAVQLADELLY 461
Cdd:COG2199   184 RESDLVARLGGDEFAVLLPGTDLEEAEAL-AERLREAleqlPFELEGKELRVTVSIGVALYPeDGDSAEELLRRADLALY 262

                         170
                  ....*....|...
gi 2571039743 462 HVKQHGKHNIAYY 474
Cdd:COG2199   263 RAKRAGRNRVVVY 275
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 327-472 2.69e-41

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: 145.39  E-value: 2.69e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2571039743 327 QTDHLTRLPRRDILDEALLREHD---------YLMILDIDNFKAVNDTHGHGVGDLALVAFATHLKANIRKGDAAIRWGG 397
Cdd:cd01949     1 YTDPLTGLPNRRAFEERLERLLArarrsgrplALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2571039743 398 EEFIVLFKGVENDEMMRLfATRL---LERPLRIPELPAPITFSAGV-IRLRDYLSVTEAVQLADELLYHVKQHGKHNIA 472
Cdd:cd01949    81 DEFAILLPGTDLEEAEAL-AERLreaIEEPFFIDGQEIRVTASIGIaTYPEDGEDAEELLRRADEALYRAKRSGRNRVV 158
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 325-474 3.80e-37

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 134.30  E-value: 3.80e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2571039743  325 LAQTDHLTRLPRRDILDEALLREHD---------YLMILDIDNFKAVNDTHGHGVGDLALVAFATHLKANIRKGDAAIRW 395
Cdd:smart00267   2 LAFRDPLTGLPNRRYFEEELEQELQraqrqgspfALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2571039743  396 GGEEFIVLFKGVENDEMMRLfATRLLERpLRIPELPAPITF----SAGVIRL-RDYLSVTEAVQLADELLYHVKQHGKHN 470
Cdd:smart00267  82 GGDEFALLLPETSLEEAIAL-AERILQQ-LREPIIIHGIPLyltiSIGVAAYpNPGEDAEDLLKRADTALYQAKKAGRNQ 159


                   ....
gi 2571039743  471 IAYY 474
Cdd:smart00267 160 VAVY 163
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 326-468 6.25e-35

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: 128.14  E-value: 6.25e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2571039743 326 AQTDHLTRLPRRDILDEALLREHDY---------LMILDIDNFKAVNDTHGHGVGDLALVAFATHLKANIRKGDAAIRWG 396
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELQRalregspvaVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2571039743 397 GEEFIVLFKGVENDEMMRL--FATRLLERpLRIP----ELPAPITFSAGVIRL-RDYLSVTEAVQLADELLYHVKQHGK 468
Cdd:pfam00990  81 GDEFAILLPETSLEGAQELaeRIRRLLAK-LKIPhtvsGLPLYVTISIGIAAYpNDGEDPEDLLKRADTALYQAKQAGR 158
PRK09894 PRK09894
diguanylate cyclase; Provisional
 322-481 2.08e-30

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 120.17  E-value: 2.08e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2571039743 322 LRTLAQTDHLTRLPRRDILDEALlrEHD---------YLMILDIDNFKAVNDTHGHGVGDLALVAFATHLKANIRKGDAA 392
Cdd:PRK09894  125 LTIRSNMDVLTGLPGRRVLDESF--DHQlrnrepqnlYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETV 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2571039743 393 IRWGGEEFIVLFKGVENDEmmrlfATRLLER--------PLRIPELPAPITFSAGVIRLRDYLSVTEAVQLADELLYHVK 464
Cdd:PRK09894  203 YRYGGEEFIICLKAATDEE-----ACRAGERirqlianhAITHSDGRINITATFGVSRAFPEETLDVVIGRADRAMYEGK 277

                         170
                  ....*....|....*....
gi 2571039743 465 QHGKHNIAYY--QGQEIRV 481
Cdd:PRK09894  278 QTGRNRVMFIdeQNVINRV 296
diguan_SiaD NF038266
biofilm regulation diguanylate cyclase SiaD;
316-468 4.84e-30

biofilm regulation diguanylate cyclase SiaD;


Pssm-ID: 468439 [Multi-domain]  Cd Length: 252  Bit Score: 117.78  E-value: 4.84e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2571039743 316 RSLVTRLRTLAQTDHLTRLPRRDILDEALLREHDY---------LMILDIDNFKAVNDTHGHGVGDLALVAFATHLKANI 386
Cdd:NF038266   84 RDLNEALREASTRDPLTGLPNRRLLMERLREEVERarrsgrpftLAMLDVDHFKRINDRYGHEVGDRVLVEIARTLRAEL 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2571039743 387 RKGDAAIRWGGEEFIVLFKGVENDEMMRLfATRLLER----PLRIPELPAPITFSAGVIRLR-DYLSVTEAVQLADELLY 461
Cdd:NF038266  164 REYDLCGRWGGEEFLLLLPETGLEEAQVV-LERLREAvralAVRVGDDVLSVTASAGLAEHRpPEEGLSATLSRADQALY 242


                  ....*..
gi 2571039743 462 HVKQHGK 468
Cdd:NF038266  243 QAKRAGR 249
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 325-468 5.96e-27

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: 106.65  E-value: 5.96e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2571039743 325 LAQTDHLTRLPRRDILDEALLRE--------HDY-LMILDIDNFKAVNDTHGHGVGDLALVAFATHLKANIRKGDAAIRW 395
Cdd:TIGR00254   1 QAVRDPLTGLYNRRYLEEMLDSElkrarrfqRSFsVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2571039743 396 GGEEFIVLFKGVE-NDEM--MRLFATRLLERPLRIPELPA-PITFSAGVIRLR-DYLSVTEAVQLADELLYHVKQHGK 468
Cdd:TIGR00254  81 GGEEFVVILPGTPlEDALskAERLRDAINSKPIEVAGSETlTVTVSIGVACYPgHGLTLEELLKRADEALYQAKKAGR 158
 
Name Accession Description Interval E-value
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 316-474 5.46e-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: 151.28  E-value: 5.46e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2571039743 316 RSLVTRLRTLAQTDHLTRLPRR----DILDEALLREHDY-----LMILDIDNFKAVNDTHGHGVGDLALVAFATHLKANI 386
Cdd:COG2199   104 RRLEERLRRLATHDPLTGLPNRrafeERLERELARARREgrplaLLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASL 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2571039743 387 RKGDAAIRWGGEEFIVLFKGVENDEMMRLfATRLLER----PLRIPELPAPITFSAGVIRLR-DYLSVTEAVQLADELLY 461
Cdd:COG2199   184 RESDLVARLGGDEFAVLLPGTDLEEAEAL-AERLREAleqlPFELEGKELRVTVSIGVALYPeDGDSAEELLRRADLALY 262

                         170
                  ....*....|...
gi 2571039743 462 HVKQHGKHNIAYY 474
Cdd:COG2199   263 RAKRAGRNRVVVY 275
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 327-472 2.69e-41

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: 145.39  E-value: 2.69e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2571039743 327 QTDHLTRLPRRDILDEALLREHD---------YLMILDIDNFKAVNDTHGHGVGDLALVAFATHLKANIRKGDAAIRWGG 397
Cdd:cd01949     1 YTDPLTGLPNRRAFEERLERLLArarrsgrplALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2571039743 398 EEFIVLFKGVENDEMMRLfATRL---LERPLRIPELPAPITFSAGV-IRLRDYLSVTEAVQLADELLYHVKQHGKHNIA 472
Cdd:cd01949    81 DEFAILLPGTDLEEAEAL-AERLreaIEEPFFIDGQEIRVTASIGIaTYPEDGEDAEELLRRADEALYRAKRSGRNRVV 158
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 325-474 3.80e-37

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 134.30  E-value: 3.80e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2571039743  325 LAQTDHLTRLPRRDILDEALLREHD---------YLMILDIDNFKAVNDTHGHGVGDLALVAFATHLKANIRKGDAAIRW 395
Cdd:smart00267   2 LAFRDPLTGLPNRRYFEEELEQELQraqrqgspfALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2571039743  396 GGEEFIVLFKGVENDEMMRLfATRLLERpLRIPELPAPITF----SAGVIRL-RDYLSVTEAVQLADELLYHVKQHGKHN 470
Cdd:smart00267  82 GGDEFALLLPETSLEEAIAL-AERILQQ-LREPIIIHGIPLyltiSIGVAAYpNPGEDAEDLLKRADTALYQAKKAGRNQ 159


                   ....
gi 2571039743  471 IAYY 474
Cdd:smart00267 160 VAVY 163
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 326-468 6.25e-35

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: 128.14  E-value: 6.25e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2571039743 326 AQTDHLTRLPRRDILDEALLREHDY---------LMILDIDNFKAVNDTHGHGVGDLALVAFATHLKANIRKGDAAIRWG 396
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELQRalregspvaVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2571039743 397 GEEFIVLFKGVENDEMMRL--FATRLLERpLRIP----ELPAPITFSAGVIRL-RDYLSVTEAVQLADELLYHVKQHGK 468
Cdd:pfam00990  81 GDEFAILLPETSLEGAQELaeRIRRLLAK-LKIPhtvsGLPLYVTISIGIAAYpNDGEDPEDLLKRADTALYQAKQAGR 158
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 321-474 1.83e-34

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: 137.21  E-value: 1.83e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2571039743 321 RLRTLAQTDHLTRLPRR----DILDEALLREHDY-----LMILDIDNFKAVNDTHGHGVGDLALVAFATHLKANIRKGDA 391
Cdd:COG5001   246 RLRHLAYHDPLTGLPNRrlflDRLEQALARARRSgrrlaLLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDT 325

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2571039743 392 AIRWGGEEFIVLFKGVENDEMMRLFATRLLE---RPLRIPELPAPITFSAGV-IRLRDYLSVTEAVQLADELLYHVKQHG 467
Cdd:COG5001   326 VARLGGDEFAVLLPDLDDPEDAEAVAERILAalaEPFELDGHELYVSASIGIaLYPDDGADAEELLRNADLAMYRAKAAG 405


                  ....*..
gi 2571039743 468 KHNIAYY 474
Cdd:COG5001   406 RNRYRFF 412
PRK09894 PRK09894
diguanylate cyclase; Provisional
 322-481 2.08e-30

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 120.17  E-value: 2.08e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2571039743 322 LRTLAQTDHLTRLPRRDILDEALlrEHD---------YLMILDIDNFKAVNDTHGHGVGDLALVAFATHLKANIRKGDAA 392
Cdd:PRK09894  125 LTIRSNMDVLTGLPGRRVLDESF--DHQlrnrepqnlYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETV 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2571039743 393 IRWGGEEFIVLFKGVENDEmmrlfATRLLER--------PLRIPELPAPITFSAGVIRLRDYLSVTEAVQLADELLYHVK 464
Cdd:PRK09894  203 YRYGGEEFIICLKAATDEE-----ACRAGERirqlianhAITHSDGRINITATFGVSRAFPEETLDVVIGRADRAMYEGK 277

                         170
                  ....*....|....*....
gi 2571039743 465 QHGKHNIAYY--QGQEIRV 481
Cdd:PRK09894  278 QTGRNRVMFIdeQNVINRV 296
diguan_SiaD NF038266
biofilm regulation diguanylate cyclase SiaD;
316-468 4.84e-30

biofilm regulation diguanylate cyclase SiaD;


Pssm-ID: 468439 [Multi-domain]  Cd Length: 252  Bit Score: 117.78  E-value: 4.84e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2571039743 316 RSLVTRLRTLAQTDHLTRLPRRDILDEALLREHDY---------LMILDIDNFKAVNDTHGHGVGDLALVAFATHLKANI 386
Cdd:NF038266   84 RDLNEALREASTRDPLTGLPNRRLLMERLREEVERarrsgrpftLAMLDVDHFKRINDRYGHEVGDRVLVEIARTLRAEL 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2571039743 387 RKGDAAIRWGGEEFIVLFKGVENDEMMRLfATRLLER----PLRIPELPAPITFSAGVIRLR-DYLSVTEAVQLADELLY 461
Cdd:NF038266  164 REYDLCGRWGGEEFLLLLPETGLEEAQVV-LERLREAvralAVRVGDDVLSVTASAGLAEHRpPEEGLSATLSRADQALY 242


                  ....*..
gi 2571039743 462 HVKQHGK 468
Cdd:NF038266  243 QAKRAGR 249
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 325-468 5.96e-27

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: 106.65  E-value: 5.96e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2571039743 325 LAQTDHLTRLPRRDILDEALLRE--------HDY-LMILDIDNFKAVNDTHGHGVGDLALVAFATHLKANIRKGDAAIRW 395
Cdd:TIGR00254   1 QAVRDPLTGLYNRRYLEEMLDSElkrarrfqRSFsVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2571039743 396 GGEEFIVLFKGVE-NDEM--MRLFATRLLERPLRIPELPA-PITFSAGVIRLR-DYLSVTEAVQLADELLYHVKQHGK 468
Cdd:TIGR00254  81 GGEEFVVILPGTPlEDALskAERLRDAINSKPIEVAGSETlTVTVSIGVACYPgHGLTLEELLKRADEALYQAKKAGR 158
pleD PRK09581
response regulator PleD; Reviewed
 324-468 1.32e-22

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 100.36  E-value: 1.32e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2571039743 324 TLAQTDHLTRLPRR--------DILDEALLREHD-YLMILDIDNFKAVNDTHGHGVGDLALVAFATHLKANIRKGDAAIR 394
Cdd:PRK09581  290 EMAVTDGLTGLHNRryfdmhlkNLIERANERGKPlSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIAR 369

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2571039743 395 WGGEEFIVLFkgVEND-EMMRLFATRLL----ERPLRIP--ELPAPITFSAGVIRLRDYLSVTEAV-QLADELLYHVKQH 466
Cdd:PRK09581  370 YGGEEFVVVM--PDTDiEDAIAVAERIRrkiaEEPFIISdgKERLNVTVSIGVAELRPSGDTIEALiKRADKALYEAKNT 447


                  ..
gi 2571039743 467 GK 468
Cdd:PRK09581  448 GR 449
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
321-469 1.95e-17

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 85.50  E-value: 1.95e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2571039743 321 RLRTLAQTDHLTRLPRR----DILDEALLREHDY---LMILDIDNFKAVNDTHGHGVGDLALVAFATHLKANIRKGDAAI 393
Cdd:PRK10060  232 RLRILANTDSITGLPNRnaiqELIDHAINAADNNqvgIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQTLA 311

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2571039743 394 RWGGEEFIVLFKGVENDEMMRLfATRLLERpLRIPelpapitFSAGVIRLRDYLSVTEA------------VQLADELLY 461
Cdd:PRK10060  312 RLGGDEFLVLASHTSQAALEAM-ASRILTR-LRLP-------FRIGLIEVYTGCSIGIAlapehgddseslIRSADTAMY 382


                  ....*...
gi 2571039743 462 HVKQHGKH 469
Cdd:PRK10060  383 TAKEGGRG 390
PRK15426 PRK15426
cellulose biosynthesis regulator YedQ;
322-468 8.01e-17

cellulose biosynthesis regulator YedQ;


Pssm-ID: 237964 [Multi-domain]  Cd Length: 570  Bit Score: 83.14  E-value: 8.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2571039743 322 LRTLAQTDHLTRLPRRDIL-----DEALLREHD----YLMILDIDNFKAVNDTHGHGVGDLALVAFATHLKANIRKGDAA 392
Cdd:PRK15426  394 LQWQAWHDPLTRLYNRGALfekarALAKRCQRDqqpfSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVA 473

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2571039743 393 IRWGGEEFIVLFKGVENDEmmrlfATRLLER-PLRIPELP------APITFSA--GVIRLRDYLSVT-EAVQ-LADELLY 461
Cdd:PRK15426  474 GRVGGEEFCVVLPGASLAE-----AAQVAERiRLRINEKEilvaksTTIRISAslGVSSAEEDGDYDfEQLQsLADRRLY 548


                  ....*..
gi 2571039743 462 HVKQHGK 468
Cdd:PRK15426  549 LAKQAGR 555
adrA PRK10245
diguanylate cyclase AdrA; Provisional
 321-468 1.03e-13

diguanylate cyclase AdrA; Provisional


Pssm-ID: 182329 [Multi-domain]  Cd Length: 366  Bit Score: 72.55  E-value: 1.03e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2571039743 321 RLRTLAQTDHLTRLPRRDILDEALLREHDY---------LMILDIDNFKAVNDTHGHGVGDLALVAFATHLKANIRKGDA 391
Cdd:PRK10245  200 RLQVMSTRDGMTGVYNRRHWETLLRNEFDNcrrhhrdatLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSDV 279

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2571039743 392 AIRWGGEEFIVLFKGVENDEMM--------RLFATRLLERP---LRIPELPAPITFSAGVIRlrdylsvtEAVQLADELL 460
Cdd:PRK10245  280 IGRFGGDEFAVIMSGTPAESAItamsrvheGLNTLRLPNAPqvtLRISVGVAPLNPQMSHYR--------EWLKSADLAL 351


                  ....*...
gi 2571039743 461 YHVKQHGK 468
Cdd:PRK10245  352 YKAKNAGR 359
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 314-504 5.65e-11

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 65.46  E-value: 5.65e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2571039743  314 TGRSLVTRLRTLAQTDHLTRLPRR--------DILDEALLREHDY-LMILDIDNFKAVNDTHGHGVGDLALVAFATHLKA 384
Cdd:PRK09776   653 ESRKMLRQLSYSASHDALTHLANRasfekqlrRLLQTVNSTHQRHaLVFIDLDRFKAVNDSAGHAAGDALLRELASLMLS 732

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2571039743  385 NIRKGDAAIRWGGEEFIVLFKGVENDEmMRLFATRLLE--RPLRIPELPA--PITFSAGVIRL-RDYLSVTEAVQLADEL 459
Cdd:PRK09776   733 MLRSSDVLARLGGDEFGLLLPDCNVES-ARFIATRIISaiNDYHFPWEGRvyRVGASAGITLIdANNHQASEVMSQADIA 811

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2571039743  460 LYHVKQHGKHNIAYYQGQEIRVIREtplptdpagaRVSLQVAEGL 504
Cdd:PRK09776   812 CYAAKNAGRGRVTVYEPQQAAAHSE----------HRALSLAEQW 846
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 321-447 1.09e-09

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 60.94  E-value: 1.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2571039743 321 RLRTLAQTDHLTRLPRRDIL----DEALLREHD-YLMILDIDNFKAVNDTHGHGVGDLALVAFATHLKANIRKGDAAIRW 395
Cdd:PRK11359  371 HIEQLIQFDPLTGLPNRNNLhnylDDLVDKAVSpVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRI 450

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2571039743 396 GGEEFIVLFKGVENDEMMrLFATRLLE---RPLRIPELPAPITFSAGVI----RLRDYL 447
Cdd:PRK11359  451 EGTQFVLVSLENDVSNIT-QIADELRNvvsKPIMIDDKPFPLTLSIGISydvgKNRDYL 508
PRK09966 PRK09966
diguanylate cyclase DgcN;
322-465 1.35e-09

diguanylate cyclase DgcN;


Pssm-ID: 182171 [Multi-domain]  Cd Length: 407  Bit Score: 60.02  E-value: 1.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2571039743 322 LRTlAQTDHLTRLPRR--------DILDEALLREHDYLMILDIDNFKAVNDTHGHGVGDLALVAFATHLKANIRKGDAAI 393
Cdd:PRK09966  245 LRT-ALHDPLTGLANRaafrsginTLMNNSDARKTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHKAY 323

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2571039743 394 RWGGEEFIVLFKGVEND-EMMRLFA--TRLLERPLRIPE-LPAPITFSAGVIRLRDYLSVTEAVQLADELLYHVKQ 465
Cdd:PRK09966  324 RLGGDEFAMVLYDVQSEsEVQQICSalTQIFNLPFDLHNgHQTTMTLSIGYAMTIEHASAEKLQELADHNMYQAKH 399
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
 351-464 1.14e-07

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: 50.82  E-value: 1.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2571039743 351 LMILDIDNFKAVNDTHGHGVGDLALVAFATHLKANIRK-GDAAIRWGGEEFIVLFKGVENDEmMRLFATRLLERPLRIPE 429
Cdd:cd07556     4 ILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRsGDLKIKTIGDEFMVVSGLDHPAA-AVAFAEDMREAVSALNQ 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2571039743 430 LPA-PITFSAGV----------IRLRDYLSVTEAVQLADELLYHVK 464
Cdd:cd07556    83 SEGnPVRVRIGIhtgpvvvgviGSRPQYDVWGALVNLASRMESQAK 128
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 390-459 2.12e-04

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: 42.20  E-value: 2.12e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2571039743 390 DAAIRWGGEEFIVLFKGVENDEMMRLfATRLLERPLRIPELpaPITFSAGVirlrdylSVTEAVQLADEL 459
Cdd:COG3706   116 DLVARYGGEEFAILLPGTDLEGALAV-AERIREAVAELPSL--RVTVSIGV-------AGDSLLKRADAL 175
 
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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