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Conserved domains on  [gi|221236330|ref|YP_002518767|]
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GGDEF diguanylate cyclase DgcA [Caulobacter vibrioides NA1000]

Protein Classification

GGDEF domain-containing protein( domain architecture ID 10112692)

GGDEF domain-containing protein may function as a diguanylate cyclase and be involved in regulating cell surface adhesion in bacteria

CATH:  3.30.70.1230
Gene Ontology:  GO:0005525|GO:0005886|GO:0007165|GO:0046872|GO:0052621
PubMed:  16166544|17208514|11119645|15569936

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 86-217 1.74e-47

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: 154.25  E-value: 1.74e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221236330  86 DVLTPVLNRRAFLRELKRVAAFAQRYGSPASVVFFDLDGFKSVNDRFGHAAGDEALKAVAKRLQANVRESDIVGRMGGDE 165
Cdd:cd01949    3 DPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGDE 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 221236330 166 FAVLLAQADKETALAKAQSLAEAVRAEPVEFGEwSAPLHISFGVREIEPGAD 217
Cdd:cd01949   83 FAILLPGTDLEEAEALAERLREAIEEPFFIDGQ-EIRVTASIGIATYPEDGE 133
 
Name Accession Description Interval E-value
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 86-217 1.74e-47

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: 154.25  E-value: 1.74e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221236330  86 DVLTPVLNRRAFLRELKRVAAFAQRYGSPASVVFFDLDGFKSVNDRFGHAAGDEALKAVAKRLQANVRESDIVGRMGGDE 165
Cdd:cd01949    3 DPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGDE 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 221236330 166 FAVLLAQADKETALAKAQSLAEAVRAEPVEFGEwSAPLHISFGVREIEPGAD 217
Cdd:cd01949   83 FAILLPGTDLEEAEALAERLREAIEEPFFIDGQ-EIRVTASIGIATYPEDGE 133
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 11-209 4.11e-47

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: 157.06  E-value: 4.11e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221236330  11 FAAIRKRALARAGAQVAAREVSAPDSAAFLGLTEADLTPKVVEALQTLMGEIEDLRNEVSVLKLRLNEAQGLADMDVLTP 90
Cdd:COG2199   42 LLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLLLLALEDITELRRLEERLRRLATHDPLTG 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221236330  91 VLNRRAFLRELKRVAAFAQRYGSPASVVFFDLDGFKSVNDRFGHAAGDEALKAVAKRLQANVRESDIVGRMGGDEFAVLL 170
Cdd:COG2199  122 LPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLL 201

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 221236330 171 AQADKETALAKAQSLAEAVRAEPVEFGEWSAPLHISFGV 209
Cdd:COG2199  202 PGTDLEEAEALAERLREALEQLPFELEGKELRVTVSIGV 240
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 82-217 1.15e-41

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 139.30  E-value: 1.15e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221236330    82 LADMDVLTPVLNRRAFLRELKRVAAFAQRYGSPASVVFFDLDGFKSVNDRFGHAAGDEALKAVAKRLQANVRESDIVGRM 161
Cdd:smart00267   2 LAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARL 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 221236330   162 GGDEFAVLLAQADKETALAKAQSLAEAVRaEPVEFGEWSAPLHISFGVREIEPGAD 217
Cdd:smart00267  82 GGDEFALLLPETSLEEAIALAERILQQLR-EPIIIHGIPLYLTISIGVAAYPNPGE 136
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 83-209 4.90e-41

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: 137.77  E-value: 4.90e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221236330   83 ADMDVLTPVLNRRAFLRELKRVAAFAQRYGSPASVVFFDLDGFKSVNDRFGHAAGDEALKAVAKRLQANVRESDIVGRMG 162
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 221236330  163 GDEFAVLLaqadKETALAKAQSLAEAVR------AEPVEFGEWSAPLHISFGV 209
Cdd:pfam00990  81 GDEFAILL----PETSLEGAQELAERIRrllaklKIPHTVSGLPLYVTISIGI 129
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 82-217 7.65e-39

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: 132.46  E-value: 7.65e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221236330   82 LADMDVLTPVLNRRAFLRELKRVAAFAQRYGSPASVVFFDLDGFKSVNDRFGHAAGDEALKAVAKRLQANVRESDIVGRM 161
Cdd:TIGR00254   1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 221236330  162 GGDEFAVLLAQADKETALAKAQSLAEAVRAEPVEFgEWSAPLH--ISFGVREIEPGAD 217
Cdd:TIGR00254  81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPIEV-AGSETLTvtVSIGVACYPGHGL 137
PRK15426 PRK15426
cellulose biosynthesis regulator YedQ;
80-217 2.96e-31

cellulose biosynthesis regulator YedQ;


Pssm-ID: 237964 [Multi-domain]  Cd Length: 570  Bit Score: 120.50  E-value: 2.96e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221236330  80 QGLADMDVLTPVLNRRAFLRELKRVAAFAQRYGSPASVVFFDLDGFKSVNDRFGHAAGDEALKAVAKRLQANVRESDIVG 159
Cdd:PRK15426 395 QWQAWHDPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVAG 474

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 221236330 160 RMGGDEFAVLLAQADKETALAKAQSLAEAVRAEPVEFGEwSAPLHI--SFGVREIEPGAD 217
Cdd:PRK15426 475 RVGGEEFCVVLPGASLAEAAQVAERIRLRINEKEILVAK-STTIRIsaSLGVSSAEEDGD 533
 
Name Accession Description Interval E-value
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 86-217 1.74e-47

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: 154.25  E-value: 1.74e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221236330  86 DVLTPVLNRRAFLRELKRVAAFAQRYGSPASVVFFDLDGFKSVNDRFGHAAGDEALKAVAKRLQANVRESDIVGRMGGDE 165
Cdd:cd01949    3 DPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGDE 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 221236330 166 FAVLLAQADKETALAKAQSLAEAVRAEPVEFGEwSAPLHISFGVREIEPGAD 217
Cdd:cd01949   83 FAILLPGTDLEEAEALAERLREAIEEPFFIDGQ-EIRVTASIGIATYPEDGE 133
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 11-209 4.11e-47

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: 157.06  E-value: 4.11e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221236330  11 FAAIRKRALARAGAQVAAREVSAPDSAAFLGLTEADLTPKVVEALQTLMGEIEDLRNEVSVLKLRLNEAQGLADMDVLTP 90
Cdd:COG2199   42 LLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLLLLALEDITELRRLEERLRRLATHDPLTG 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221236330  91 VLNRRAFLRELKRVAAFAQRYGSPASVVFFDLDGFKSVNDRFGHAAGDEALKAVAKRLQANVRESDIVGRMGGDEFAVLL 170
Cdd:COG2199  122 LPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLL 201

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 221236330 171 AQADKETALAKAQSLAEAVRAEPVEFGEWSAPLHISFGV 209
Cdd:COG2199  202 PGTDLEEAEALAERLREALEQLPFELEGKELRVTVSIGV 240
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 82-217 1.15e-41

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 139.30  E-value: 1.15e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221236330    82 LADMDVLTPVLNRRAFLRELKRVAAFAQRYGSPASVVFFDLDGFKSVNDRFGHAAGDEALKAVAKRLQANVRESDIVGRM 161
Cdd:smart00267   2 LAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARL 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 221236330   162 GGDEFAVLLAQADKETALAKAQSLAEAVRaEPVEFGEWSAPLHISFGVREIEPGAD 217
Cdd:smart00267  82 GGDEFALLLPETSLEEAIALAERILQQLR-EPIIIHGIPLYLTISIGVAAYPNPGE 136
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 83-209 4.90e-41

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: 137.77  E-value: 4.90e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221236330   83 ADMDVLTPVLNRRAFLRELKRVAAFAQRYGSPASVVFFDLDGFKSVNDRFGHAAGDEALKAVAKRLQANVRESDIVGRMG 162
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 221236330  163 GDEFAVLLaqadKETALAKAQSLAEAVR------AEPVEFGEWSAPLHISFGV 209
Cdd:pfam00990  81 GDEFAILL----PETSLEGAQELAERIRrllaklKIPHTVSGLPLYVTISIGI 129
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 82-217 7.65e-39

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: 132.46  E-value: 7.65e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221236330   82 LADMDVLTPVLNRRAFLRELKRVAAFAQRYGSPASVVFFDLDGFKSVNDRFGHAAGDEALKAVAKRLQANVRESDIVGRM 161
Cdd:TIGR00254   1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 221236330  162 GGDEFAVLLAQADKETALAKAQSLAEAVRAEPVEFgEWSAPLH--ISFGVREIEPGAD 217
Cdd:TIGR00254  81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPIEV-AGSETLTvtVSIGVACYPGHGL 137
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 3-209 6.59e-37

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: 136.83  E-value: 6.59e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221236330   3 ISGARTEPFAAIRKRALARAGAQVAAREVSAPDSAAFLGLTEADLTPKVVEALQTLMGEIEDLRNEVSVLKLRLNEAQGL 82
Cdd:COG5001  171 ALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEERLRHL 250

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221236330  83 ADMDVLTPVLNRRAFLRELKRVAAFAQRYGSPASVVFFDLDGFKSVNDRFGHAAGDEALKAVAKRLQANVRESDIVGRMG 162
Cdd:COG5001  251 AYHDPLTGLPNRRLFLDRLEQALARARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLG 330

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 221236330 163 GDEFAVLLAQ-ADKETALAKAQSLAEAVrAEPVEFGEWSAPLHISFGV 209
Cdd:COG5001  331 GDEFAVLLPDlDDPEDAEAVAERILAAL-AEPFELDGHELYVSASIGI 377
PRK15426 PRK15426
cellulose biosynthesis regulator YedQ;
80-217 2.96e-31

cellulose biosynthesis regulator YedQ;


Pssm-ID: 237964 [Multi-domain]  Cd Length: 570  Bit Score: 120.50  E-value: 2.96e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221236330  80 QGLADMDVLTPVLNRRAFLRELKRVAAFAQRYGSPASVVFFDLDGFKSVNDRFGHAAGDEALKAVAKRLQANVRESDIVG 159
Cdd:PRK15426 395 QWQAWHDPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVAG 474

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 221236330 160 RMGGDEFAVLLAQADKETALAKAQSLAEAVRAEPVEFGEwSAPLHI--SFGVREIEPGAD 217
Cdd:PRK15426 475 RVGGEEFCVVLPGASLAEAAQVAERIRLRINEKEILVAK-STTIRIsaSLGVSSAEEDGD 533
pleD PRK09581
response regulator PleD; Reviewed
 82-218 1.28e-24

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 100.75  E-value: 1.28e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221236330  82 LADMDVLTPVLNRRAFLRELKRVAAFAQRYGSPASVVFFDLDGFKSVNDRFGHAAGDEALKAVAKRLQANVRESDIVGRM 161
Cdd:PRK09581 291 MAVTDGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARY 370

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 221236330 162 GGDEFAVLLAQADKETALAKAQSLAEAVRAEP--VEFGEWSAPLHISFGVREIEPGADP 218
Cdd:PRK09581 371 GGEEFVVVMPDTDIEDAIAVAERIRRKIAEEPfiISDGKERLNVTVSIGVAELRPSGDT 429
PRK09894 PRK09894
diguanylate cyclase; Provisional
 59-215 9.65e-24

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 96.29  E-value: 9.65e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221236330  59 MGEIEDLRNEVSVLKLRLneAQGLADMDVLTPVLNRRAFLRELKRvaAFAQRYGSPASVVFFDLDGFKSVNDRFGHAAGD 138
Cdd:PRK09894 107 QEGLLSFTAALTDYKIYL--LTIRSNMDVLTGLPGRRVLDESFDH--QLRNREPQNLYLALLDIDRFKLVNDTYGHLIGD 182

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221236330 139 EALKAVAKRLQANVRESDIVGRMGGDEFAVLLAQADKETALAKAQSLAEAVRAEPVEFGEWSAPLHISFGVREIEPG 215
Cdd:PRK09894 183 VVLRTLATYLASWTRDYETVYRYGGEEFIICLKAATDEEACRAGERIRQLIANHAITHSDGRINITATFGVSRAFPE 259
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 83-190 1.59e-21

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 92.81  E-value: 1.59e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221236330   83 ADMDVLTPVLNRRAFLRELKRVAAFAQRYGSPASVVFFDLDGFKSVNDRFGHAAGDEALKAVAKRLQANVRESDIVGRMG 162
Cdd:PRK09776  665 ASHDALTHLANRASFEKQLRRLLQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSDVLARLG 744

                          90       100
                  ....*....|....*....|....*...
gi 221236330  163 GDEFAVLLAQADKETALAKAQSLAEAVR 190
Cdd:PRK09776  745 GDEFGLLLPDCNVESARFIATRIISAIN 772
adrA PRK10245
diguanylate cyclase AdrA; Provisional
 73-214 5.62e-21

diguanylate cyclase AdrA; Provisional


Pssm-ID: 182329 [Multi-domain]  Cd Length: 366  Bit Score: 89.89  E-value: 5.62e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221236330  73 KLRLneaQGLADMDVLTPVLNRRAFLRELKRVAAFAQRYGSPASVVFFDLDGFKSVNDRFGHAAGDEALKAVAKRLQANV 152
Cdd:PRK10245 198 KRRL---QVMSTRDGMTGVYNRRHWETLLRNEFDNCRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITL 274

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221236330 153 RESDIVGRMGGDEFAVLLAQADKETALAKAQSLAEAVRAEPVEfgewSAP---LHISFGVREIEP 214
Cdd:PRK10245 275 RGSDVIGRFGGDEFAVIMSGTPAESAITAMSRVHEGLNTLRLP----NAPqvtLRISVGVAPLNP 335
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
75-190 1.64e-17

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 80.88  E-value: 1.64e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221236330  75 RLNEaqgLADMDVLTPVLNRRAfLRELKRvAAFAQRYGSPASVVFFDLDGFKSVNDRFGHAAGDEALKAVAKRLQANVRE 154
Cdd:PRK10060 232 RLRI---LANTDSITGLPNRNA-IQELID-HAINAADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEE 306

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 221236330 155 SDIVGRMGGDEFAVLLAQADKETALAKAQSLAEAVR 190
Cdd:PRK10060 307 DQTLARLGGDEFLVLASHTSQAALEAMASRILTRLR 342
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
 114-217 6.33e-13

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: 63.53  E-value: 6.33e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221236330 114 PASVVFFDLDGFKSVNDRFGHAAGDEALKAVAKRLQANVRES-DIVGRMGGDEFAVLLAQADKETALAKAQSLAEAVRAE 192
Cdd:cd07556    1 PVTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSgDLKIKTIGDEFMVVSGLDHPAAAVAFAEDMREAVSAL 80

                         90       100
                 ....*....|....*....|....*
gi 221236330 193 PVEFGEwsaPLHISFGVREIEPGAD 217
Cdd:cd07556   81 NQSEGN---PVRVRIGIHTGPVVVG 102
PRK09966 PRK09966
diguanylate cyclase DgcN;
57-176 2.52e-11

diguanylate cyclase DgcN;


Pssm-ID: 182171 [Multi-domain]  Cd Length: 407  Bit Score: 62.72  E-value: 2.52e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221236330  57 TLMGEIEDLRnevsvLKLRLNEAQGL--ADMDVLTPVLNRRAFLRELKRVAAFAQRYGSPAsVVFFDLDGFKSVNDRFGH 134
Cdd:PRK09966 225 SLLDEMEEWQ-----LRLQAKNAQLLrtALHDPLTGLANRAAFRSGINTLMNNSDARKTSA-LLFLDGDNFKYINDTWGH 298

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 221236330 135 AAGDEALKAVAKRLQANVRESDIVGRMGGDEFAVLLAQADKE 176
Cdd:PRK09966 299 ATGDRVLIEIAKRLAEFGGLRHKAYRLGGDEFAMVLYDVQSE 340
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 82-209 8.07e-11

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 61.32  E-value: 8.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221236330  82 LADMDVLTPVLNRRAFLRELKRVAAFAQrygsPASVVFFDLDGFKSVNDRFGHAAGDEALKAVAKRLQANVRESDIVGRM 161
Cdd:PRK11359 375 LIQFDPLTGLPNRNNLHNYLDDLVDKAV----SPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRI 450

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 221236330 162 GGDEFAVLLAQADKETALAKAQSLAEAVrAEPVEFGEWSAPLHISFGV 209
Cdd:PRK11359 451 EGTQFVLVSLENDVSNITQIADELRNVV-SKPIMIDDKPFPLTLSIGI 497
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 156-209 6.68e-05

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: 6.68e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 221236330 156 DIVGRMGGDEFAVLLAQADKETALAKAQSLAEAVRAEPVEFgewsapLHISFGV 209
Cdd:COG3706  116 DLVARYGGEEFAILLPGTDLEGALAVAERIREAVAELPSLR------VTVSIGV 163
 
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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