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Conserved domains on  [gi|727186661|ref|WP_033648510|]
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MULTISPECIES: GGDEF domain-containing protein [Serratia]

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: ...
 191-347 7.77e-56

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: 179.67  E-value: 7.77e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727186661 191 MLDPLTGLYNRRGLENKINMLLE---PQTGRHYVLLLDIDHFKVYNDSYGHAMGDRALVQVAIAIRDAVRSRDIVVRYGG 267
Cdd:cd01949    1 YTDPLTGLPNRRAFEERLERLLArarRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727186661 268 EEFLVLLTNVHEGYAAQLAERVRQRVAELNIPHGassqHSGTLTLSAGISALEK--LDVESAIGAADAALYLAKHSGRNN 345
Cdd:cd01949   81 DEFAILLPGTDLEEAEALAERLREAIEEPFFIDG----QEIRVTASIGIATYPEdgEDAEELLRRADEALYRAKRSGRNR 156


                 ..
gi 727186661 346 IQ 347
Cdd:cd01949  157 VV 158
 
Name Accession Description Interval E-value
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 191-347 7.77e-56

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: 179.67  E-value: 7.77e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727186661 191 MLDPLTGLYNRRGLENKINMLLE---PQTGRHYVLLLDIDHFKVYNDSYGHAMGDRALVQVAIAIRDAVRSRDIVVRYGG 267
Cdd:cd01949    1 YTDPLTGLPNRRAFEERLERLLArarRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727186661 268 EEFLVLLTNVHEGYAAQLAERVRQRVAELNIPHGassqHSGTLTLSAGISALEK--LDVESAIGAADAALYLAKHSGRNN 345
Cdd:cd01949   81 DEFAILLPGTDLEEAEALAERLREAIEEPFFIDG----QEIRVTASIGIATYPEdgEDAEELLRRADEALYRAKRSGRNR 156


                 ..
gi 727186661 346 IQ 347
Cdd:cd01949  157 VV 158
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 190-345 3.43e-55

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: 178.22  E-value: 3.43e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727186661  190 SMLDPLTGLYNRRGLENKINMLLEPQTGRHY---VLLLDIDHFKVYNDSYGHAMGDRALVQVAIAIRDAVRSRDIVVRYG 266
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSpvaVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727186661  267 GEEFLVLLTNVHEGYAAQLAERVRQRVAELNIPHgASSQHSGTLTLSAGISAL--EKLDVESAIGAADAALYLAKHSGRN 344
Cdd:pfam00990  81 GDEFAILLPETSLEGAQELAERIRRLLAKLKIPH-TVSGLPLYVTISIGIAAYpnDGEDPEDLLKRADTALYQAKQAGRN 159


                  .
gi 727186661  345 N 345
Cdd:pfam00990 160 R 160
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 78-349 1.75e-54

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: 180.17  E-value: 1.75e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727186661  78 VLGLLWAAHIYVKSQYCLPNNQDFLLISLFSIFFISAISLTDNFTAFCLHAVPSAMMILALDGMHNTLRILFTTLLPIIA 157
Cdd:COG2199    2 LLLLLLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727186661 158 FSIHHLMLKRSEIFTHALVANLYNERDKFNNLSMLDPLTGLYNRRGLENKINMLLE---PQTGRHYVLLLDIDHFKVYND 234
Cdd:COG2199   82 ELLLLLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELArarREGRPLALLLIDLDHFKRIND 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727186661 235 SYGHAMGDRALVQVAIAIRDAVRSRDIVVRYGGEEFLVLLTNVHEGYAAQLAERVRQRVAELNIPHGassQHSGTLTLSA 314
Cdd:COG2199  162 TYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELE---GKELRVTVSI 238

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 727186661 315 GISALEK--LDVESAIGAADAALYLAKHSGRNNIQLA 349
Cdd:COG2199  239 GVALYPEdgDSAEELLRRADLALYRAKRAGRNRVVVY 275
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 189-349 3.03e-50

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 165.50  E-value: 3.03e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727186661   189 LSMLDPLTGLYNRRGLENKINMLLE---PQTGRHYVLLLDIDHFKVYNDSYGHAMGDRALVQVAIAIRDAVRSRDIVVRY 265
Cdd:smart00267   2 LAFRDPLTGLPNRRYFEEELEQELQraqRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727186661   266 GGEEFLVLLTNVHEGYAAQLAERVRQRVAELNIPHGassqHSGTLTLSAGISALEKL--DVESAIGAADAALYLAKHSGR 343
Cdd:smart00267  82 GGDEFALLLPETSLEEAIALAERILQQLREPIIIHG----IPLYLTISIGVAAYPNPgeDAEDLLKRADTALYQAKKAGR 157


                   ....*.
gi 727186661   344 NNIQLA 349
Cdd:smart00267 158 NQVAVY 163
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 189-349 4.34e-46

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: 154.80  E-value: 4.34e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727186661  189 LSMLDPLTGLYNRRGLENKINMLLE-PQTGRH--YVLLLDIDHFKVYNDSYGHAMGDRALVQVAIAIRDAVRSRDIVVRY 265
Cdd:TIGR00254   1 QAVRDPLTGLYNRRYLEEMLDSELKrARRFQRsfSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727186661  266 GGEEFLVLLTNVHEGYAAQLAERVRQRVAELNIPHGASSQhsGTLTLSAGISALEK--LDVESAIGAADAALYLAKHSGR 343
Cdd:TIGR00254  81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSET--LTVTVSIGVACYPGhgLTLEELLKRADEALYQAKKAGR 158


                  ....*.
gi 727186661  344 NNIQLA 349
Cdd:TIGR00254 159 NRVVVA 164
diguan_SiaD NF038266
biofilm regulation diguanylate cyclase SiaD;
189-344 2.40e-42

biofilm regulation diguanylate cyclase SiaD;


Pssm-ID: 468439 [Multi-domain]  Cd Length: 252  Bit Score: 147.82  E-value: 2.40e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727186661 189 LSMLDPLTGLYNRRGLENKINMLLE--PQTGRHYVL-LLDIDHFKVYNDSYGHAMGDRALVQVAIAIRDAVRSRDIVVRY 265
Cdd:NF038266  93 ASTRDPLTGLPNRRLLMERLREEVEraRRSGRPFTLaMLDVDHFKRINDRYGHEVGDRVLVEIARTLRAELREYDLCGRW 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727186661 266 GGEEFLVLLTNVHEGYAAQLAERVRQRVAELNIPHGASsqhSGTLTLSAGISAL----EKLDveSAIGAADAALYLAKHS 341
Cdd:NF038266 173 GGEEFLLLLPETGLEEAQVVLERLREAVRALAVRVGDD---VLSVTASAGLAEHrppeEGLS--ATLSRADQALYQAKRA 247


                 ...
gi 727186661 342 GRN 344
Cdd:NF038266 248 GRD 250
pleD PRK09581
response regulator PleD; Reviewed
 188-346 1.84e-40

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 148.13  E-value: 1.84e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727186661 188 NLSMLDPLTGLYNRRGLENKINMLLEPQTGRH---YVLLLDIDHFKVYNDSYGHAMGDRALVQVAIAIRDAVRSRDIVVR 264
Cdd:PRK09581 290 EMAVTDGLTGLHNRRYFDMHLKNLIERANERGkplSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIAR 369

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727186661 265 YGGEEFLVLL--TNVHEgyAAQLAERVRQRVAELN-IPHGASSQHSgtLTLSAGISALEKLD--VESAIGAADAALYLAK 339
Cdd:PRK09581 370 YGGEEFVVVMpdTDIED--AIAVAERIRRKIAEEPfIISDGKERLN--VTVSIGVAELRPSGdtIEALIKRADKALYEAK 445


                 ....*..
gi 727186661 340 HSGRNNI 346
Cdd:PRK09581 446 NTGRNRV 452
dguan_cyc_DgcA NF041606
diguanylate cyclase DgcA;
221-350 3.47e-29

diguanylate cyclase DgcA;


Pssm-ID: 469490 [Multi-domain]  Cd Length: 340  Bit Score: 115.23  E-value: 3.47e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727186661 221 VLLLDIDHFKVYNDSYGHAMGDRALVQVAIAIRDAVRSRDIVVRYGGEEFLVLLTNVHEGYAAQLAERVRQRVAELNIPH 300
Cdd:NF041606 212 ILMLDIDFFKQINDTYGHACGDLVLQMVASIIQSCTRTQDMAARYGGEEFVVMLSNTSSKTAKKIAERIRKSIENLSILY 291

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 727186661 301 gaSSQHSgTLTLSAGISALeKLDVESA---IGAADAALYLAKHSGRNNIQLAQ 350
Cdd:NF041606 292 --DEQHI-RVTISIGVAEY-NFDVESAkslVERADKALYESKQNGRNRVSISK 340
 
Name Accession Description Interval E-value
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 191-347 7.77e-56

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: 179.67  E-value: 7.77e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727186661 191 MLDPLTGLYNRRGLENKINMLLE---PQTGRHYVLLLDIDHFKVYNDSYGHAMGDRALVQVAIAIRDAVRSRDIVVRYGG 267
Cdd:cd01949    1 YTDPLTGLPNRRAFEERLERLLArarRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727186661 268 EEFLVLLTNVHEGYAAQLAERVRQRVAELNIPHGassqHSGTLTLSAGISALEK--LDVESAIGAADAALYLAKHSGRNN 345
Cdd:cd01949   81 DEFAILLPGTDLEEAEALAERLREAIEEPFFIDG----QEIRVTASIGIATYPEdgEDAEELLRRADEALYRAKRSGRNR 156


                 ..
gi 727186661 346 IQ 347
Cdd:cd01949  157 VV 158
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 190-345 3.43e-55

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: 178.22  E-value: 3.43e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727186661  190 SMLDPLTGLYNRRGLENKINMLLEPQTGRHY---VLLLDIDHFKVYNDSYGHAMGDRALVQVAIAIRDAVRSRDIVVRYG 266
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSpvaVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727186661  267 GEEFLVLLTNVHEGYAAQLAERVRQRVAELNIPHgASSQHSGTLTLSAGISAL--EKLDVESAIGAADAALYLAKHSGRN 344
Cdd:pfam00990  81 GDEFAILLPETSLEGAQELAERIRRLLAKLKIPH-TVSGLPLYVTISIGIAAYpnDGEDPEDLLKRADTALYQAKQAGRN 159


                  .
gi 727186661  345 N 345
Cdd:pfam00990 160 R 160
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 78-349 1.75e-54

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: 180.17  E-value: 1.75e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727186661  78 VLGLLWAAHIYVKSQYCLPNNQDFLLISLFSIFFISAISLTDNFTAFCLHAVPSAMMILALDGMHNTLRILFTTLLPIIA 157
Cdd:COG2199    2 LLLLLLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727186661 158 FSIHHLMLKRSEIFTHALVANLYNERDKFNNLSMLDPLTGLYNRRGLENKINMLLE---PQTGRHYVLLLDIDHFKVYND 234
Cdd:COG2199   82 ELLLLLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELArarREGRPLALLLIDLDHFKRIND 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727186661 235 SYGHAMGDRALVQVAIAIRDAVRSRDIVVRYGGEEFLVLLTNVHEGYAAQLAERVRQRVAELNIPHGassQHSGTLTLSA 314
Cdd:COG2199  162 TYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELE---GKELRVTVSI 238

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 727186661 315 GISALEK--LDVESAIGAADAALYLAKHSGRNNIQLA 349
Cdd:COG2199  239 GVALYPEdgDSAEELLRRADLALYRAKRAGRNRVVVY 275
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 189-349 3.03e-50

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 165.50  E-value: 3.03e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727186661   189 LSMLDPLTGLYNRRGLENKINMLLE---PQTGRHYVLLLDIDHFKVYNDSYGHAMGDRALVQVAIAIRDAVRSRDIVVRY 265
Cdd:smart00267   2 LAFRDPLTGLPNRRYFEEELEQELQraqRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727186661   266 GGEEFLVLLTNVHEGYAAQLAERVRQRVAELNIPHGassqHSGTLTLSAGISALEKL--DVESAIGAADAALYLAKHSGR 343
Cdd:smart00267  82 GGDEFALLLPETSLEEAIALAERILQQLREPIIIHG----IPLYLTISIGVAAYPNPgeDAEDLLKRADTALYQAKKAGR 157


                   ....*.
gi 727186661   344 NNIQLA 349
Cdd:smart00267 158 NQVAVY 163
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 189-349 4.34e-46

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: 154.80  E-value: 4.34e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727186661  189 LSMLDPLTGLYNRRGLENKINMLLE-PQTGRH--YVLLLDIDHFKVYNDSYGHAMGDRALVQVAIAIRDAVRSRDIVVRY 265
Cdd:TIGR00254   1 QAVRDPLTGLYNRRYLEEMLDSELKrARRFQRsfSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727186661  266 GGEEFLVLLTNVHEGYAAQLAERVRQRVAELNIPHGASSQhsGTLTLSAGISALEK--LDVESAIGAADAALYLAKHSGR 343
Cdd:TIGR00254  81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSET--LTVTVSIGVACYPGhgLTLEELLKRADEALYQAKKAGR 158


                  ....*.
gi 727186661  344 NNIQLA 349
Cdd:TIGR00254 159 NRVVVA 164
diguan_SiaD NF038266
biofilm regulation diguanylate cyclase SiaD;
189-344 2.40e-42

biofilm regulation diguanylate cyclase SiaD;


Pssm-ID: 468439 [Multi-domain]  Cd Length: 252  Bit Score: 147.82  E-value: 2.40e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727186661 189 LSMLDPLTGLYNRRGLENKINMLLE--PQTGRHYVL-LLDIDHFKVYNDSYGHAMGDRALVQVAIAIRDAVRSRDIVVRY 265
Cdd:NF038266  93 ASTRDPLTGLPNRRLLMERLREEVEraRRSGRPFTLaMLDVDHFKRINDRYGHEVGDRVLVEIARTLRAELREYDLCGRW 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727186661 266 GGEEFLVLLTNVHEGYAAQLAERVRQRVAELNIPHGASsqhSGTLTLSAGISAL----EKLDveSAIGAADAALYLAKHS 341
Cdd:NF038266 173 GGEEFLLLLPETGLEEAQVVLERLREAVRALAVRVGDD---VLSVTASAGLAEHrppeEGLS--ATLSRADQALYQAKRA 247


                 ...
gi 727186661 342 GRN 344
Cdd:NF038266 248 GRD 250
pleD PRK09581
response regulator PleD; Reviewed
 188-346 1.84e-40

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 148.13  E-value: 1.84e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727186661 188 NLSMLDPLTGLYNRRGLENKINMLLEPQTGRH---YVLLLDIDHFKVYNDSYGHAMGDRALVQVAIAIRDAVRSRDIVVR 264
Cdd:PRK09581 290 EMAVTDGLTGLHNRRYFDMHLKNLIERANERGkplSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIAR 369

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727186661 265 YGGEEFLVLL--TNVHEgyAAQLAERVRQRVAELN-IPHGASSQHSgtLTLSAGISALEKLD--VESAIGAADAALYLAK 339
Cdd:PRK09581 370 YGGEEFVVVMpdTDIED--AIAVAERIRRKIAEEPfIISDGKERLN--VTVSIGVAELRPSGdtIEALIKRADKALYEAK 445


                 ....*..
gi 727186661 340 HSGRNNI 346
Cdd:PRK09581 446 NTGRNRV 452
PRK09894 PRK09894
diguanylate cyclase; Provisional
 182-353 6.14e-39

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 140.20  E-value: 6.14e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727186661 182 ERDKFNNLSMLDPLTGLYNRRGLENKINMLLEPQTGRH-YVLLLDIDHFKVYNDSYGHAMGDRALVQVAIAIRDAVRSRD 260
Cdd:PRK09894 121 KIYLLTIRSNMDVLTGLPGRRVLDESFDHQLRNREPQNlYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYE 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727186661 261 IVVRYGGEEFLVLLTNVHEGYAAQLAERVRQRVAELNIphgASSQHSGTLTLSAGIS-ALEKLDVESAIGAADAALYLAK 339
Cdd:PRK09894 201 TVYRYGGEEFIICLKAATDEEACRAGERIRQLIANHAI---THSDGRINITATFGVSrAFPEETLDVVIGRADRAMYEGK 277

                        170
                 ....*....|....
gi 727186661 340 HSGRNNIQLAQNVQ 353
Cdd:PRK09894 278 QTGRNRVMFIDEQN 291
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 134-348 2.13e-36

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: 139.52  E-value: 2.13e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727186661 134 MILALDGMHNTLRILFTTLLPIIAFSIHHLMLKRSEIFTHALVANLYNERDKFNNLSMLDPLTGLYNRRGLENKINMLLE 213
Cdd:COG5001  195 RLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALA 274

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727186661 214 ---PQTGRHYVLLLDIDHFKVYNDSYGHAMGDRALVQVAIAIRDAVRSRDIVVRYGGEEFLVLLTNV-HEGYAAQLAERV 289
Cdd:COG5001  275 rarRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVLLPDLdDPEDAEAVAERI 354

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 727186661 290 RQRVAE-LNIphgasSQHSGTLTLSAGIS--ALEKLDVESAIGAADAALYLAKHSGRNNIQL 348
Cdd:COG5001  355 LAALAEpFEL-----DGHELYVSASIGIAlyPDDGADAEELLRNADLAMYRAKAAGRNRYRF 411
PRK15426 PRK15426
cellulose biosynthesis regulator YedQ;
148-346 1.64e-32

cellulose biosynthesis regulator YedQ;


Pssm-ID: 237964 [Multi-domain]  Cd Length: 570  Bit Score: 127.82  E-value: 1.64e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727186661 148 LFTTLLPIIAFSIHHLmlkrseifthalVANLYNERDKFNNLSMLDPLTGLYNRRGLENKINMLLEP-QTGRH--YVLLL 224
Cdd:PRK15426 368 LFTAMLLISWYVIRRM------------VSNMFVLQSSLQWQAWHDPLTRLYNRGALFEKARALAKRcQRDQQpfSVIQL 435

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727186661 225 DIDHFKVYNDSYGHAMGDRALVQVAIAIRDAVRSRDIVVRYGGEEFLVLLTNVHEGYAAQLAERVRQRVAELNIphgaSS 304
Cdd:PRK15426 436 DLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRVGGEEFCVVLPGASLAEAAQVAERIRLRINEKEI----LV 511

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 727186661 305 QHSGTLTLSA--GISALEK---LDVESAIGAADAALYLAKHSGRNNI 346
Cdd:PRK15426 512 AKSTTIRISAslGVSSAEEdgdYDFEQLQSLADRRLYLAKQAGRNRV 558
dguan_cyc_DgcA NF041606
diguanylate cyclase DgcA;
221-350 3.47e-29

diguanylate cyclase DgcA;


Pssm-ID: 469490 [Multi-domain]  Cd Length: 340  Bit Score: 115.23  E-value: 3.47e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727186661 221 VLLLDIDHFKVYNDSYGHAMGDRALVQVAIAIRDAVRSRDIVVRYGGEEFLVLLTNVHEGYAAQLAERVRQRVAELNIPH 300
Cdd:NF041606 212 ILMLDIDFFKQINDTYGHACGDLVLQMVASIIQSCTRTQDMAARYGGEEFVVMLSNTSSKTAKKIAERIRKSIENLSILY 291

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 727186661 301 gaSSQHSgTLTLSAGISALeKLDVESA---IGAADAALYLAKHSGRNNIQLAQ 350
Cdd:NF041606 292 --DEQHI-RVTISIGVAEY-NFDVESAkslVERADKALYESKQNGRNRVSISK 340
adrA PRK10245
diguanylate cyclase AdrA; Provisional
 121-349 5.02e-22

diguanylate cyclase AdrA; Provisional


Pssm-ID: 182329 [Multi-domain]  Cd Length: 366  Bit Score: 95.67  E-value: 5.02e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727186661 121 FTAFCLHAVPSAMMILALDGMHNTLR---ILFTTLLPIIAfsIHHLMLKRseiFTHALVANLYNERDKFNNLSMLDPLTG 197
Cdd:PRK10245 138 FVAGLVLMVVSCLVTLELTGITVSFNsapLEWWLSLPVIV--IYPLLFAW---VSYQTATKLAEHKRRLQVMSTRDGMTG 212

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727186661 198 LYNRRGLENKINMLLEpQTGRHY----VLLLDIDHFKVYNDSYGHAMGDRALVQVAIAIRDAVRSRDIVVRYGGEEFLVL 273
Cdd:PRK10245 213 VYNRRHWETLLRNEFD-NCRRHHrdatLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSDVIGRFGGDEFAVI 291

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 727186661 274 LTNVHEGYAAQLAERVRQRVAELNIPHGASSqhsgTLTLSAGISAL--EKLDVESAIGAADAALYLAKHSGRNNIQLA 349
Cdd:PRK10245 292 MSGTPAESAITAMSRVHEGLNTLRLPNAPQV----TLRISVGVAPLnpQMSHYREWLKSADLALYKAKNAGRNRTEVA 365
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
193-343 3.91e-21

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 94.75  E-value: 3.91e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727186661 193 DPLTGLYNRRGLENKINMLLEPQTGRHY-VLLLDIDHFKVYNDSYGHAMGDRALVQVAIAIRDAVRSRDIVVRYGGEEFL 271
Cdd:PRK10060 240 DSITGLPNRNAIQELIDHAINAADNNQVgIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQTLARLGGDEFL 319

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727186661 272 VLLTNVH----EGYAAQLAERVRQ--RVAELNIPHGAssqhsgtltlSAGIsALEKL---DVESAIGAADAALYLAKHSG 342
Cdd:PRK10060 320 VLASHTSqaalEAMASRILTRLRLpfRIGLIEVYTGC----------SIGI-ALAPEhgdDSESLIRSADTAMYTAKEGG 388


                 .
gi 727186661 343 R 343
Cdd:PRK10060 389 R 389
PRK09966 PRK09966
diguanylate cyclase DgcN;
193-340 6.92e-21

diguanylate cyclase DgcN;


Pssm-ID: 182171 [Multi-domain]  Cd Length: 407  Bit Score: 93.15  E-value: 6.92e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727186661 193 DPLTGLYNRRGLENKINMLLEPQTGRH--YVLLLDIDHFKVYNDSYGHAMGDRALVQVAIAIRDAVRSRDIVVRYGGEEF 270
Cdd:PRK09966 251 DPLTGLANRAAFRSGINTLMNNSDARKtsALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHKAYRLGGDEF 330

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 727186661 271 LVLLTNVHEGYAAQ-LAERVRQrvaELNIPHGASSQHSGTLTLSAGIS-ALEKLDVESAIGAADAALYLAKH 340
Cdd:PRK09966 331 AMVLYDVQSESEVQqICSALTQ---IFNLPFDLHNGHQTTMTLSIGYAmTIEHASAEKLQELADHNMYQAKH 399
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 191-357 8.48e-19

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 88.19  E-value: 8.48e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727186661  191 MLDPLTGLYNRRGLENKINMLLEP---QTGRHYVLLLDIDHFKVYNDSYGHAMGDRALVQVAIAIRDAVRSRDIVVRYGG 267
Cdd:PRK09776  666 SHDALTHLANRASFEKQLRRLLQTvnsTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSDVLARLGG 745

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727186661  268 EEFLVLLTNVHEGYAAQLAERVRQRVAELNIPHGASSQHSGTltlSAGISALEkLDVESA---IGAADAALYLAKHSGRN 344
Cdd:PRK09776  746 DEFGLLLPDCNVESARFIATRIISAINDYHFPWEGRVYRVGA---SAGITLID-ANNHQAsevMSQADIACYAAKNAGRG 821

                         170
                  ....*....|...
gi 727186661  345 NIQLAQNVQPALL 357
Cdd:PRK09776  822 RVTVYEPQQAAAH 834
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 183-347 4.46e-17

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 82.51  E-value: 4.46e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727186661 183 RDKFNNLSMLDPLTGLYNRRGLENKINMLLEPQTgRHYVLLLDIDHFKVYNDSYGHAMGDRALVQVAIAIRDAVRSRDIV 262
Cdd:PRK11359 369 RQHIEQLIQFDPLTGLPNRNNLHNYLDDLVDKAV-SPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDQYL 447

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727186661 263 VRYGGEEFLVLLTNVHEGYAAQLAERVRQRV-AELNIphgasSQHSGTLTLSAGISALEKLDVESAIGAADAALYLAKHS 341
Cdd:PRK11359 448 CRIEGTQFVLVSLENDVSNITQIADELRNVVsKPIMI-----DDKPFPLTLSIGISYDVGKNRDYLLSTAHNAMDYIRKN 522


                 ....*.
gi 727186661 342 GRNNIQ 347
Cdd:PRK11359 523 GGNGWQ 528
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
 221-320 3.07e-16

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: 74.31  E-value: 3.07e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727186661 221 VLLLDIDHFKVYNDSYGHAMGDRALVQVAIAIRDAV-RSRDIVVRYGGEEFLVLLTNVHEGYAAQLAERVRQRVAELNIP 299
Cdd:cd07556    4 ILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIrRSGDLKIKTIGDEFMVVSGLDHPAAAVAFAEDMREAVSALNQS 83

                         90       100
                 ....*....|....*....|.
gi 727186661 300 HGASsqhsgtLTLSAGISALE 320
Cdd:cd07556   84 EGNP------VRVRIGIHTGP 98
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 260-339 6.32e-13

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: 66.47  E-value: 6.32e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727186661 260 DIVVRYGGEEFLVLLTNVHEGYAAQLAERVRQRVAELNIPHgassqhsgtLTLSAGISAlekldvESAIGAADaALYLAK 339
Cdd:COG3706  116 DLVARYGGEEFAILLPGTDLEGALAVAERIREAVAELPSLR---------VTVSIGVAG------DSLLKRAD-ALYQAR 179
PRK11059 PRK11059
regulatory protein CsrD; Provisional
 182-286 9.46e-04

regulatory protein CsrD; Provisional


Pssm-ID: 236833 [Multi-domain]  Cd Length: 640  Bit Score: 41.00  E-value: 9.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727186661 182 ERDKFNNL----SMLDPLTGLYNRRGLENKINMLLEPQ--TGRH-YVLLLDIDHFKVYNDSYGHAMGDRALVQVAIAIRD 254
Cdd:PRK11059 216 ERSRFDTFirsnAFQDAKTGLGNRLFFDNQLATLLEDQemVGAHgVVMLIRLPDFDLLQEEWGESQVEELLFELINLLST 295

                         90       100       110
                 ....*....|....*....|....*....|....
gi 727186661 255 AVRSRD--IVVRYGGEEFLVLLTNVHEGYAAQLA 286
Cdd:PRK11059 296 FVMRYPgaLLARYSRSDFAVLLPHRSLKEADSLA 329
 
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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