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Conserved domains on  [gi|2792448071|ref|WP_371882447|]
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GGDEF domain-containing protein [Caballeronia sp. S22]

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 ...
 72-239 1.49e-50

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: 165.92  E-value: 1.49e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792448071  72 REMQALATQLEHRASHDALTGVLNRSAVIERTGKMLRT-----NSAVMIVLDIDEFKRINDDFGHPTGDAVILGVVDCLR 146
Cdd:COG2199   101 TELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARarregRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLR 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792448071 147 RIVGERGFIGRVGGEEFTVLLPGHDPSSAAILAERMREAISD-SLIVPPVDRRITASFGISN-NEAGAGFDTAYASADAA 224
Cdd:COG2199   181 ASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQlPFELEGKELRVTVSIGVALyPEDGDSAEELLRRADLA 260

                         170
                  ....*....|....*
gi 2792448071 225 LYRAKRGGRNRVEFA 239
Cdd:COG2199   261 LYRAKRAGRNRVVVY 275
 
Name Accession Description Interval E-value
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 72-239 1.49e-50

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: 165.92  E-value: 1.49e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792448071  72 REMQALATQLEHRASHDALTGVLNRSAVIERTGKMLRT-----NSAVMIVLDIDEFKRINDDFGHPTGDAVILGVVDCLR 146
Cdd:COG2199   101 TELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARarregRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLR 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792448071 147 RIVGERGFIGRVGGEEFTVLLPGHDPSSAAILAERMREAISD-SLIVPPVDRRITASFGISN-NEAGAGFDTAYASADAA 224
Cdd:COG2199   181 ASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQlPFELEGKELRVTVSIGVALyPEDGDSAEELLRRADLA 260

                         170
                  ....*....|....*
gi 2792448071 225 LYRAKRGGRNRVEFA 239
Cdd:COG2199   261 LYRAKRAGRNRVVVY 275
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 87-236 1.69e-50

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: 161.96  E-value: 1.69e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792448071  87 HDALTGVLNRSAVIERTGKMLRT-----NSAVMIVLDIDEFKRINDDFGHPTGDAVILGVVDCLRRIVGERGFIGRVGGE 161
Cdd:cd01949     2 TDPLTGLPNRRAFEERLERLLARarrsgRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGD 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2792448071 162 EFTVLLPGHDPSSAAILAERMREAISDSLIVPPVDRRITASFGIS-NNEAGAGFDTAYASADAALYRAKRGGRNRV 236
Cdd:cd01949    82 EFAILLPGTDLEEAEALAERLREAIEEPFFIDGQEIRVTASIGIAtYPEDGEDAEELLRRADEALYRAKRSGRNRV 157
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 83-239 1.77e-40

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 136.61  E-value: 1.77e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792448071   83 HRASHDALTGVLNRSAVIERTGKMLRT-----NSAVMIVLDIDEFKRINDDFGHPTGDAVILGVVDCLRRIVGERGFIGR 157
Cdd:smart00267   1 RLAFRDPLTGLPNRRYFEEELEQELQRaqrqgSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792448071  158 VGGEEFTVLLPGHDPSSAAILAERMREAISDSLIVPPVDRRITASFGIS-NNEAGAGFDTAYASADAALYRAKRGGRNRV 236
Cdd:smart00267  81 LGGDEFALLLPETSLEEAIALAERILQQLREPIIIHGIPLYLTISIGVAaYPNPGEDAEDLLKRADTALYQAKKAGRNQV 160


                   ...
gi 2792448071  237 EFA 239
Cdd:smart00267 161 AVY 163
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 85-235 8.13e-38

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


Pssm-ID: 425976 [Multi-domain]  Cd Length: 160  Bit Score: 129.68  E-value: 8.13e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792448071  85 ASHDALTGVLNRSAVIERTGKML----RTNSAVMIVL-DIDEFKRINDDFGHPTGDAVILGVVDCLRRIVGERGFIGRVG 159
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELqralREGSPVAVLLiDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792448071 160 GEEFTVLLPGHDPSSAAILAERMREAISDSLI---VPPVDRRITASFGIS-NNEAGAGFDTAYASADAALYRAKRGGRNR 235
Cdd:pfam00990  81 GDEFAILLPETSLEGAQELAERIRRLLAKLKIphtVSGLPLYVTISIGIAaYPNDGEDPEDLLKRADTALYQAKQAGRNR 160
PRK15426 PRK15426
cellulose biosynthesis regulator YedQ;
72-241 1.13e-36

cellulose biosynthesis regulator YedQ;


Pssm-ID: 237964 [Multi-domain]  Cd Length: 570  Bit Score: 135.53  E-value: 1.13e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792448071  72 REMQALATQLEHRASHDALTGVLNRSAVIERTGKMLRTNSA-----VMIVLDIDEFKRINDDFGHPTGDAVILGVVDCLR 146
Cdd:PRK15426  385 SNMFVLQSSLQWQAWHDPLTRLYNRGALFEKARALAKRCQRdqqpfSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLIS 464

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792448071 147 RIVGERGFIGRVGGEEFTVLLPGHDPSSAAILAERMREAISDS--LIVPPVDRRITASFGISNNEAGA--GFDTAYASAD 222
Cdd:PRK15426  465 SSLRAQDVAGRVGGEEFCVVLPGASLAEAAQVAERIRLRINEKeiLVAKSTTIRISASLGVSSAEEDGdyDFEQLQSLAD 544

                         170
                  ....*....|....*....
gi 2792448071 223 AALYRAKRGGRNRVEFADR 241
Cdd:PRK15426  545 RRLYLAKQAGRNRVCASDN 563
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 84-240 2.99e-31

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: 112.82  E-value: 2.99e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792448071  84 RASHDALTGVLNRSAVIERTGKMLR-----TNSAVMIVLDIDEFKRINDDFGHPTGDAVILGVVDCLRRIVGERGFIGRV 158
Cdd:TIGR00254   1 QAVRDPLTGLYNRRYLEEMLDSELKrarrfQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792448071 159 GGEEFTVLLPGHDPSSAAILAERMREAISDSLIVPPVDR--RITASFGISN-NEAGAGFDTAYASADAALYRAKRGGRNR 235
Cdd:TIGR00254  81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSEtlTVTVSIGVACyPGHGLTLEELLKRADEALYQAKKAGRNR 160


                  ....*
gi 2792448071 236 VEFAD 240
Cdd:TIGR00254 161 VVVAD 165
 
Name Accession Description Interval E-value
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 72-239 1.49e-50

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: 165.92  E-value: 1.49e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792448071  72 REMQALATQLEHRASHDALTGVLNRSAVIERTGKMLRT-----NSAVMIVLDIDEFKRINDDFGHPTGDAVILGVVDCLR 146
Cdd:COG2199   101 TELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARarregRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLR 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792448071 147 RIVGERGFIGRVGGEEFTVLLPGHDPSSAAILAERMREAISD-SLIVPPVDRRITASFGISN-NEAGAGFDTAYASADAA 224
Cdd:COG2199   181 ASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQlPFELEGKELRVTVSIGVALyPEDGDSAEELLRRADLA 260

                         170
                  ....*....|....*
gi 2792448071 225 LYRAKRGGRNRVEFA 239
Cdd:COG2199   261 LYRAKRAGRNRVVVY 275
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 87-236 1.69e-50

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: 161.96  E-value: 1.69e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792448071  87 HDALTGVLNRSAVIERTGKMLRT-----NSAVMIVLDIDEFKRINDDFGHPTGDAVILGVVDCLRRIVGERGFIGRVGGE 161
Cdd:cd01949     2 TDPLTGLPNRRAFEERLERLLARarrsgRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGD 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2792448071 162 EFTVLLPGHDPSSAAILAERMREAISDSLIVPPVDRRITASFGIS-NNEAGAGFDTAYASADAALYRAKRGGRNRV 236
Cdd:cd01949    82 EFAILLPGTDLEEAEALAERLREAIEEPFFIDGQEIRVTASIGIAtYPEDGEDAEELLRRADEALYRAKRSGRNRV 157
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 6-240 4.75e-42

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: 151.47  E-value: 4.75e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792448071   6 SPDLPPDAAPDLFQKESAALVKARAVHAAADADAHVYRESLGELIDHFERLMRDTRRLIGRSDRAEREMQALATQLEHRA 85
Cdd:COG5001   172 LLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEERLRHLA 251

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792448071  86 SHDALTGVLNRSAVIERTGKML----RTNSAV-MIVLDIDEFKRINDDFGHPTGDAVILGVVDCLRRIVGERGFIGRVGG 160
Cdd:COG5001   252 YHDPLTGLPNRRLFLDRLEQALararRSGRRLaLLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGG 331

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792448071 161 EEFTVLLPG-HDPSSAAILAERMREAISDSLIVPPVDRRITASFGIS-NNEAGAGFDTAYASADAALYRAKRGGRNRVEF 238
Cdd:COG5001   332 DEFAVLLPDlDDPEDAEAVAERILAALAEPFELDGHELYVSASIGIAlYPDDGADAEELLRNADLAMYRAKAAGRNRYRF 411


                  ..
gi 2792448071 239 AD 240
Cdd:COG5001   412 FD 413
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 83-239 1.77e-40

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 136.61  E-value: 1.77e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792448071   83 HRASHDALTGVLNRSAVIERTGKMLRT-----NSAVMIVLDIDEFKRINDDFGHPTGDAVILGVVDCLRRIVGERGFIGR 157
Cdd:smart00267   1 RLAFRDPLTGLPNRRYFEEELEQELQRaqrqgSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792448071  158 VGGEEFTVLLPGHDPSSAAILAERMREAISDSLIVPPVDRRITASFGIS-NNEAGAGFDTAYASADAALYRAKRGGRNRV 236
Cdd:smart00267  81 LGGDEFALLLPETSLEEAIALAERILQQLREPIIIHGIPLYLTISIGVAaYPNPGEDAEDLLKRADTALYQAKKAGRNQV 160


                   ...
gi 2792448071  237 EFA 239
Cdd:smart00267 161 AVY 163
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 85-235 8.13e-38

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


Pssm-ID: 425976 [Multi-domain]  Cd Length: 160  Bit Score: 129.68  E-value: 8.13e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792448071  85 ASHDALTGVLNRSAVIERTGKML----RTNSAVMIVL-DIDEFKRINDDFGHPTGDAVILGVVDCLRRIVGERGFIGRVG 159
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELqralREGSPVAVLLiDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792448071 160 GEEFTVLLPGHDPSSAAILAERMREAISDSLI---VPPVDRRITASFGIS-NNEAGAGFDTAYASADAALYRAKRGGRNR 235
Cdd:pfam00990  81 GDEFAILLPETSLEGAQELAERIRRLLAKLKIphtVSGLPLYVTISIGIAaYPNDGEDPEDLLKRADTALYQAKQAGRNR 160
PRK15426 PRK15426
cellulose biosynthesis regulator YedQ;
72-241 1.13e-36

cellulose biosynthesis regulator YedQ;


Pssm-ID: 237964 [Multi-domain]  Cd Length: 570  Bit Score: 135.53  E-value: 1.13e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792448071  72 REMQALATQLEHRASHDALTGVLNRSAVIERTGKMLRTNSA-----VMIVLDIDEFKRINDDFGHPTGDAVILGVVDCLR 146
Cdd:PRK15426  385 SNMFVLQSSLQWQAWHDPLTRLYNRGALFEKARALAKRCQRdqqpfSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLIS 464

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792448071 147 RIVGERGFIGRVGGEEFTVLLPGHDPSSAAILAERMREAISDS--LIVPPVDRRITASFGISNNEAGA--GFDTAYASAD 222
Cdd:PRK15426  465 SSLRAQDVAGRVGGEEFCVVLPGASLAEAAQVAERIRLRINEKeiLVAKSTTIRISASLGVSSAEEDGdyDFEQLQSLAD 544

                         170
                  ....*....|....*....
gi 2792448071 223 AALYRAKRGGRNRVEFADR 241
Cdd:PRK15426  545 RRLYLAKQAGRNRVCASDN 563
PRK09894 PRK09894
diguanylate cyclase; Provisional
 51-240 3.92e-33

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 121.33  E-value: 3.92e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792448071  51 DHFERLMRDTRRLIGRSDRAEREMqalatqLEHRASHDALTGVLNRS---AVIERTGKMLRTNSAVMIVLDIDEFKRIND 127
Cdd:PRK09894  101 AHFDAFQEGLLSFTAALTDYKIYL------LTIRSNMDVLTGLPGRRvldESFDHQLRNREPQNLYLALLDIDRFKLVND 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792448071 128 DFGHPTGDAVILGVVDCLRRIVGERGFIGRVGGEEFTVLLPGHDPSSAAILAERMREAISDSLIVPPVDR-RITASFGIS 206
Cdd:PRK09894  175 TYGHLIGDVVLRTLATYLASWTRDYETVYRYGGEEFIICLKAATDEEACRAGERIRQLIANHAITHSDGRiNITATFGVS 254

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2792448071 207 NNEAGAGFDTAYASADAALYRAKRGGRNRVEFAD 240
Cdd:PRK09894  255 RAFPEETLDVVIGRADRAMYEGKQTGRNRVMFID 288
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 84-240 2.99e-31

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: 112.82  E-value: 2.99e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792448071  84 RASHDALTGVLNRSAVIERTGKMLR-----TNSAVMIVLDIDEFKRINDDFGHPTGDAVILGVVDCLRRIVGERGFIGRV 158
Cdd:TIGR00254   1 QAVRDPLTGLYNRRYLEEMLDSELKrarrfQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792448071 159 GGEEFTVLLPGHDPSSAAILAERMREAISDSLIVPPVDR--RITASFGISN-NEAGAGFDTAYASADAALYRAKRGGRNR 235
Cdd:TIGR00254  81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSEtlTVTVSIGVACyPGHGLTLEELLKRADEALYQAKKAGRNR 160


                  ....*
gi 2792448071 236 VEFAD 240
Cdd:TIGR00254 161 VVVAD 165
pleD PRK09581
response regulator PleD; Reviewed
 88-236 1.01e-27

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 109.61  E-value: 1.01e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792448071  88 DALTGVLNR-------SAVIERTGKMLRTNSAVMIvlDIDEFKRINDDFGHPTGDAVILGVVDCLRRIVgeRG--FIGRV 158
Cdd:PRK09581  295 DGLTGLHNRryfdmhlKNLIERANERGKPLSLMMI--DIDHFKKVNDTYGHDAGDEVLREFAKRLRNNI--RGtdLIARY 370

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792448071 159 GGEEFTVLLPGHDPSSAAILAERMREAISDS-LIVPPVDRRI--TASFGISnnEAGAGFDTAYA---SADAALYRAKRGG 232
Cdd:PRK09581  371 GGEEFVVVMPDTDIEDAIAVAERIRRKIAEEpFIISDGKERLnvTVSIGVA--ELRPSGDTIEAlikRADKALYEAKNTG 448


                  ....
gi 2792448071 233 RNRV 236
Cdd:PRK09581  449 RNRV 452
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 73-236 4.56e-21

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 91.66  E-value: 4.56e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792448071   73 EMQALATQLEHRASHDALTGVLNRSAVIERTGKMLRT-----NSAVMIVLDIDEFKRINDDFGHPTGDAVILGVVDCLRR 147
Cdd:PRK09776   653 ESRKMLRQLSYSASHDALTHLANRASFEKQLRRLLQTvnsthQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLS 732

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792448071  148 IVGERGFIGRVGGEEFTVLLPGHDPSSAAILAERMREAISDSLIvPPVDR--RITASFGI-----SNNEAGagfdTAYAS 220
Cdd:PRK09776   733 MLRSSDVLARLGGDEFGLLLPDCNVESARFIATRIISAINDYHF-PWEGRvyRVGASAGItlidaNNHQAS----EVMSQ 807

                          170
                   ....*....|....*.
gi 2792448071  221 ADAALYRAKRGGRNRV 236
Cdd:PRK09776   808 ADIACYAAKNAGRGRV 823
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
71-233 3.91e-19

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 85.89  E-value: 3.91e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792448071  71 EREMQALATQLehrASHDALTGVLNRSAVIERTGKML--RTNSAVMIV-LDIDEFKRINDDFGHPTGDAVILGVVDCLRR 147
Cdd:PRK10060  226 ERRAQERLRIL---ANTDSITGLPNRNAIQELIDHAInaADNNQVGIVyLDLDNFKKVNDAYGHMFGDQLLQDVSLAILS 302

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792448071 148 IVGERGFIGRVGGEEFTVLLPGHDPSS----AAILAERMREAISDSLIvppvDRRITASFGIS-NNEAGAGFDTAYASAD 222
Cdd:PRK10060  303 CLEEDQTLARLGGDEFLVLASHTSQAAleamASRILTRLRLPFRIGLI----EVYTGCSIGIAlAPEHGDDSESLIRSAD 378

                         170
                  ....*....|.
gi 2792448071 223 AALYRAKRGGR 233
Cdd:PRK10060  379 TAMYTAKEGGR 389
adrA PRK10245
diguanylate cyclase AdrA; Provisional
 80-239 5.23e-19

diguanylate cyclase AdrA; Provisional


Pssm-ID: 182329 [Multi-domain]  Cd Length: 366  Bit Score: 84.50  E-value: 5.23e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792448071  80 QLEHRASHDALTGVLNRsavieRTGKMLRTNS----------AVMIVLDIDEFKRINDDFGHPTGDAVILGVVDCLRRIV 149
Cdd:PRK10245  200 RLQVMSTRDGMTGVYNR-----RHWETLLRNEfdncrrhhrdATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITL 274

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792448071 150 GERGFIGRVGGEEFTVLLPGhDPSSAAILA-ERMREAISDSLI--VPPVDRRITASFGISNNEAGAgFDTAYASADAALY 226
Cdd:PRK10245  275 RGSDVIGRFGGDEFAVIMSG-TPAESAITAmSRVHEGLNTLRLpnAPQVTLRISVGVAPLNPQMSH-YREWLKSADLALY 352

                         170
                  ....*....|...
gi 2792448071 227 RAKRGGRNRVEFA 239
Cdd:PRK10245  353 KAKNAGRNRTEVA 365
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 80-232 1.48e-17

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 81.35  E-value: 1.48e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792448071  80 QLEHRASHDALTGVLNRSAVIERTGKML-RTNSAVMIVLDIDEFKRINDDFGHPTGDAVILGVVDCLRRIVGERGFIGRV 158
Cdd:PRK11359  371 HIEQLIQFDPLTGLPNRNNLHNYLDDLVdKAVSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRI 450

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2792448071 159 GGEEFTVLLPGHDPSSAAILAERMREAISDSLIVPPVDRRITASFGISnNEAGAGFDTAYASADAAL-YRAKRGG 232
Cdd:PRK11359  451 EGTQFVLVSLENDVSNITQIADELRNVVSKPIMIDDKPFPLTLSIGIS-YDVGKNRDYLLSTAHNAMdYIRKNGG 524
PRK09966 PRK09966
diguanylate cyclase DgcN;
48-169 1.78e-16

diguanylate cyclase DgcN;


Pssm-ID: 182171 [Multi-domain]  Cd Length: 407  Bit Score: 77.74  E-value: 1.78e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792448071  48 ELIDHFERLMRDTRRLIGRSDRAEREMQALATQLEHRASHDALTGVLNRSAVIERTGKMLRTNSA----VMIVLDIDEFK 123
Cdd:PRK09966  211 ERIAEFHRFALDFNSLLDEMEEWQLRLQAKNAQLLRTALHDPLTGLANRAAFRSGINTLMNNSDArktsALLFLDGDNFK 290

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2792448071 124 RINDDFGHPTGDAVILGVVDCLRRIVGERGFIGRVGGEEFTVLLPG 169
Cdd:PRK09966  291 YINDTWGHATGDRVLIEIAKRLAEFGGLRHKAYRLGGDEFAMVLYD 336
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 139-229 5.28e-11

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: 59.54  E-value: 5.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792448071 139 LGVVDCLRRIVGER------GFIGRVGGEEFTVLLPGHDPSSAAILAERMREAISDslivpPVDRRITASFGISnneaga 212
Cdd:COG3706    96 AGADDYLTKPFDPEellarvDLVARYGGEEFAILLPGTDLEGALAVAERIREAVAE-----LPSLRVTVSIGVA------ 164

                          90
                  ....*....|....*..
gi 2792448071 213 gFDTAYASADaALYRAK 229
Cdd:COG3706   165 -GDSLLKRAD-ALYQAR 179
PRK13561 PRK13561
putative diguanylate cyclase; Provisional
 48-240 2.81e-10

putative diguanylate cyclase; Provisional


Pssm-ID: 184143 [Multi-domain]  Cd Length: 651  Bit Score: 59.73  E-value: 2.81e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792448071  48 ELIDH---FERLMRDTRrlIGRSDRA-EREMQALATQLEH---RASHDALTGVLNRS---AVIERTgkMLRTNSAVMIVL 117
Cdd:PRK13561  189 ELVGHqlaLPRLHQDDE--IGMLVRSyNLNQQLLQRQYEEqsrNATRFPVSDLPNKAllmALLEQV--VARKQTTALMII 264

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792448071 118 DIDEFKRINDDFGHPTGDAVILGVVDCLRRIVGERGFIGRVGGEEFTVLLPG-HDPSSAAILAERMREAISDSLIVPPVD 196
Cdd:PRK13561  265 TCETLRDTAGVLKEAQREILLLTLVEKLKSVLSPRMVLAQISGYDFAIIANGvKEPWHAITLGQQVLTIINERLPIQRIQ 344

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2792448071 197 RRITASFGISNNEAGAGFDTAYASADAALYRAKRGGRNRVEFAD 240
Cdd:PRK13561  345 LRPSCSIGIAMFYGDLTAEQLYSRAISAAFTARRKGKNQIQFFD 388
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
 118-241 2.37e-08

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


Pssm-ID: 143637 [Multi-domain]  Cd Length: 133  Bit Score: 51.20  E-value: 2.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792448071 118 DIDEFKRINDDFGHPTGDAVILGVVDCLRRIVGERG-FIGRVGGEEFTVLLPGHDPSSAAILAERMREAISDSLIVPPVD 196
Cdd:cd07556     8 DIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSGdLKIKTIGDEFMVVSGLDHPAAAVAFAEDMREAVSALNQSEGNP 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2792448071 197 rrITASFGISNNEAGAGFDTAYASADAAlyrakrggRNRVEFADR 241
Cdd:cd07556    88 --VRVRIGIHTGPVVVGVIGSRPQYDVW--------GALVNLASR 122
 
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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