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Conserved domains on  [gi|296925963|gb|ADH86773|]
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diguanylate cyclase [Desulfurivibrio alkaliphilus AHT 2]

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 ...
 4-277 2.51e-62

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: 197.89  E-value: 2.51e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296925963   4 ALNILVLIGAAMHLASIYLVSKLVRELPQDNLRQGWKILGIFIFFFFVSYLVYVFLQQSRTGELSGVDLIAPFILFFGAI 83
Cdd:COG2199    8 LLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296925963  84 FVLLVNLLSLKTTLELKRICT-LEQENITDPLLGIYNRRYLEEMLELEFRLSRRDGLPLSILLLDIDHFKEVNDKHGHLA 162
Cdd:COG2199   88 LALLLLLLALEDITELRRLEErLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTYGHAA 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296925963 163 GDRTLLNLVQEIKGNLRETDQLARYGGEEILIMLPHTPEDGAKLVAEKIRRGIAGGIMVAAGEredegwpDISITVSIGV 242
Cdd:COG2199  168 GDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELEGK-------ELRVTVSIGV 240

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 296925963 243 AGLRDEFSSGKELFAKADQALYRAKKTGRNRCVAA 277
Cdd:COG2199  241 ALYPEDGDSAEELLRRADLALYRAKRAGRNRVVVY 275
 
Name Accession Description Interval E-value
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 4-277 2.51e-62

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: 197.89  E-value: 2.51e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296925963   4 ALNILVLIGAAMHLASIYLVSKLVRELPQDNLRQGWKILGIFIFFFFVSYLVYVFLQQSRTGELSGVDLIAPFILFFGAI 83
Cdd:COG2199    8 LLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296925963  84 FVLLVNLLSLKTTLELKRICT-LEQENITDPLLGIYNRRYLEEMLELEFRLSRRDGLPLSILLLDIDHFKEVNDKHGHLA 162
Cdd:COG2199   88 LALLLLLLALEDITELRRLEErLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTYGHAA 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296925963 163 GDRTLLNLVQEIKGNLRETDQLARYGGEEILIMLPHTPEDGAKLVAEKIRRGIAGGIMVAAGEredegwpDISITVSIGV 242
Cdd:COG2199  168 GDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELEGK-------ELRVTVSIGV 240

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 296925963 243 AGLRDEFSSGKELFAKADQALYRAKKTGRNRCVAA 277
Cdd:COG2199  241 ALYPEDGDSAEELLRRADLALYRAKRAGRNRVVVY 275
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 111-275 3.72e-60

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: 188.15  E-value: 3.72e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296925963 111 TDPLLGIYNRRYLEEMLELEFRLSRRDGLPLSILLLDIDHFKEVNDKHGHLAGDRTLLNLVQEIKGNLRETDQLARYGGE 190
Cdd:cd01949    2 TDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296925963 191 EILIMLPHTPEDGAKLVAEKIRRGIAGGIMVAAGEredegwpdISITVSIGVAGLRDEFSSGKELFAKADQALYRAKKTG 270
Cdd:cd01949   82 EFAILLPGTDLEEAEALAERLREAIEEPFFIDGQE--------IRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSG 153


                 ....*
gi 296925963 271 RNRCV 275
Cdd:cd01949  154 RNRVV 158
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 110-277 1.27e-52

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: 169.44  E-value: 1.27e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296925963  110 ITDPLLGIYNRRYLEEMLELEFRLSRRDGLPLSILLLDIDHFKEVNDKHGHLAGDRTLLNLVQEIKGNLRETDQLARYGG 189
Cdd:TIGR00254   3 VRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYGG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296925963  190 EEILIMLPHTPEDGAKLVAEKIRRGIaggimvAAGEREDEGWPDISITVSIGVAGLRDEFSSGKELFAKADQALYRAKKT 269
Cdd:TIGR00254  83 EEFVVILPGTPLEDALSKAERLRDAI------NSKPIEVAGSETLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKA 156


                  ....*...
gi 296925963  270 GRNRCVAA 277
Cdd:TIGR00254 157 GRNRVVVA 164
pleD PRK09581
response regulator PleD; Reviewed
 92-277 2.10e-52

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 177.40  E-value: 2.10e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296925963  92 SLKTTLELKrictleqenITDPLLGIYNRRYLEEMLELEFRLSRRDGLPLSILLLDIDHFKEVNDKHGHLAGDRTLLNLV 171
Cdd:PRK09581 284 NLEQSIEMA---------VTDGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFA 354

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296925963 172 QEIKGNLRETDQLARYGGEEILIMLPHTPEDGAKLVAEKIRRGIAGG-IMVAAGEREdegwpdISITVSIGVAGLRDEFS 250
Cdd:PRK09581 355 KRLRNNIRGTDLIARYGGEEFVVVMPDTDIEDAIAVAERIRRKIAEEpFIISDGKER------LNVTVSIGVAELRPSGD 428

                        170       180
                 ....*....|....*....|....*..
gi 296925963 251 SGKELFAKADQALYRAKKTGRNRCVAA 277
Cdd:PRK09581 429 TIEALIKRADKALYEAKNTGRNRVVAL 455
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 110-273 2.68e-52

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: 168.20  E-value: 2.68e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296925963  110 ITDPLLGIYNRRYLEEMLELEFRLSRRDGLPLSILLLDIDHFKEVNDKHGHLAGDRTLLNLVQEIKGNLRETDQLARYGG 189
Cdd:pfam00990   2 AHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLGG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296925963  190 EEILIMLPHTPEDGAKLVAEKIRRGIAG-GIMVAAGEREdegwpdISITVSIGVAGLRDEFSSGKELFAKADQALYRAKK 268
Cdd:pfam00990  82 DEFAILLPETSLEGAQELAERIRRLLAKlKIPHTVSGLP------LYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQ 155


                  ....*
gi 296925963  269 TGRNR 273
Cdd:pfam00990 156 AGRNR 160
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 107-277 9.90e-48

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 156.64  E-value: 9.90e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296925963   107 QENITDPLLGIYNRRYLEEMLELEFRLSRRDGLPLSILLLDIDHFKEVNDKHGHLAGDRTLLNLVQEIKGNLRETDQLAR 186
Cdd:smart00267   1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296925963   187 YGGEEILIMLPHTPEDGAKLVAEKIRRGIAGGIMVAAGEredegwpdISITVSIGVAGLRDEFSSGKELFAKADQALYRA 266
Cdd:smart00267  81 LGGDEFALLLPETSLEEAIALAERILQQLREPIIIHGIP--------LYLTISIGVAAYPNPGEDAEDLLKRADTALYQA 152

                          170
                   ....*....|.
gi 296925963   267 KKTGRNRCVAA 277
Cdd:smart00267 153 KKAGRNQVAVY 163
diguan_SiaD NF038266
biofilm regulation diguanylate cyclase SiaD;
104-274 1.05e-46

biofilm regulation diguanylate cyclase SiaD;


Pssm-ID: 468439 [Multi-domain]  Cd Length: 252  Bit Score: 157.07  E-value: 1.05e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296925963 104 TLEQENITDPLLGIYNRRYLEEMLELEFRLSRRDGLPLSILLLDIDHFKEVNDKHGHLAGDRTLLNLVQEIKGNLRETDQ 183
Cdd:NF038266  89 ALREASTRDPLTGLPNRRLLMERLREEVERARRSGRPFTLAMLDVDHFKRINDRYGHEVGDRVLVEIARTLRAELREYDL 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296925963 184 LARYGGEEILIMLPHTPEDGAKLVAEKIRRGIAGgimVAAGEREDegwpDISITVSIGVAGLRDEFSSGKELFAKADQAL 263
Cdd:NF038266 169 CGRWGGEEFLLLLPETGLEEAQVVLERLREAVRA---LAVRVGDD----VLSVTASAGLAEHRPPEEGLSATLSRADQAL 241

                        170
                 ....*....|.
gi 296925963 264 YRAKKTGRNRC 274
Cdd:NF038266 242 YQAKRAGRDRV 252
 
Name Accession Description Interval E-value
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 4-277 2.51e-62

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: 197.89  E-value: 2.51e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296925963   4 ALNILVLIGAAMHLASIYLVSKLVRELPQDNLRQGWKILGIFIFFFFVSYLVYVFLQQSRTGELSGVDLIAPFILFFGAI 83
Cdd:COG2199    8 LLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296925963  84 FVLLVNLLSLKTTLELKRICT-LEQENITDPLLGIYNRRYLEEMLELEFRLSRRDGLPLSILLLDIDHFKEVNDKHGHLA 162
Cdd:COG2199   88 LALLLLLLALEDITELRRLEErLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTYGHAA 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296925963 163 GDRTLLNLVQEIKGNLRETDQLARYGGEEILIMLPHTPEDGAKLVAEKIRRGIAGGIMVAAGEredegwpDISITVSIGV 242
Cdd:COG2199  168 GDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELEGK-------ELRVTVSIGV 240

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 296925963 243 AGLRDEFSSGKELFAKADQALYRAKKTGRNRCVAA 277
Cdd:COG2199  241 ALYPEDGDSAEELLRRADLALYRAKRAGRNRVVVY 275
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 111-275 3.72e-60

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: 188.15  E-value: 3.72e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296925963 111 TDPLLGIYNRRYLEEMLELEFRLSRRDGLPLSILLLDIDHFKEVNDKHGHLAGDRTLLNLVQEIKGNLRETDQLARYGGE 190
Cdd:cd01949    2 TDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296925963 191 EILIMLPHTPEDGAKLVAEKIRRGIAGGIMVAAGEredegwpdISITVSIGVAGLRDEFSSGKELFAKADQALYRAKKTG 270
Cdd:cd01949   82 EFAILLPGTDLEEAEALAERLREAIEEPFFIDGQE--------IRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSG 153


                 ....*
gi 296925963 271 RNRCV 275
Cdd:cd01949  154 RNRVV 158
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 110-277 1.27e-52

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: 169.44  E-value: 1.27e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296925963  110 ITDPLLGIYNRRYLEEMLELEFRLSRRDGLPLSILLLDIDHFKEVNDKHGHLAGDRTLLNLVQEIKGNLRETDQLARYGG 189
Cdd:TIGR00254   3 VRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYGG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296925963  190 EEILIMLPHTPEDGAKLVAEKIRRGIaggimvAAGEREDEGWPDISITVSIGVAGLRDEFSSGKELFAKADQALYRAKKT 269
Cdd:TIGR00254  83 EEFVVILPGTPLEDALSKAERLRDAI------NSKPIEVAGSETLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKA 156


                  ....*...
gi 296925963  270 GRNRCVAA 277
Cdd:TIGR00254 157 GRNRVVVA 164
pleD PRK09581
response regulator PleD; Reviewed
 92-277 2.10e-52

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 177.40  E-value: 2.10e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296925963  92 SLKTTLELKrictleqenITDPLLGIYNRRYLEEMLELEFRLSRRDGLPLSILLLDIDHFKEVNDKHGHLAGDRTLLNLV 171
Cdd:PRK09581 284 NLEQSIEMA---------VTDGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFA 354

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296925963 172 QEIKGNLRETDQLARYGGEEILIMLPHTPEDGAKLVAEKIRRGIAGG-IMVAAGEREdegwpdISITVSIGVAGLRDEFS 250
Cdd:PRK09581 355 KRLRNNIRGTDLIARYGGEEFVVVMPDTDIEDAIAVAERIRRKIAEEpFIISDGKER------LNVTVSIGVAELRPSGD 428

                        170       180
                 ....*....|....*....|....*..
gi 296925963 251 SGKELFAKADQALYRAKKTGRNRCVAA 277
Cdd:PRK09581 429 TIEALIKRADKALYEAKNTGRNRVVAL 455
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 110-273 2.68e-52

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: 168.20  E-value: 2.68e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296925963  110 ITDPLLGIYNRRYLEEMLELEFRLSRRDGLPLSILLLDIDHFKEVNDKHGHLAGDRTLLNLVQEIKGNLRETDQLARYGG 189
Cdd:pfam00990   2 AHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLGG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296925963  190 EEILIMLPHTPEDGAKLVAEKIRRGIAG-GIMVAAGEREdegwpdISITVSIGVAGLRDEFSSGKELFAKADQALYRAKK 268
Cdd:pfam00990  82 DEFAILLPETSLEGAQELAERIRRLLAKlKIPHTVSGLP------LYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQ 155


                  ....*
gi 296925963  269 TGRNR 273
Cdd:pfam00990 156 AGRNR 160
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 107-277 9.90e-48

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 156.64  E-value: 9.90e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296925963   107 QENITDPLLGIYNRRYLEEMLELEFRLSRRDGLPLSILLLDIDHFKEVNDKHGHLAGDRTLLNLVQEIKGNLRETDQLAR 186
Cdd:smart00267   1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296925963   187 YGGEEILIMLPHTPEDGAKLVAEKIRRGIAGGIMVAAGEredegwpdISITVSIGVAGLRDEFSSGKELFAKADQALYRA 266
Cdd:smart00267  81 LGGDEFALLLPETSLEEAIALAERILQQLREPIIIHGIP--------LYLTISIGVAAYPNPGEDAEDLLKRADTALYQA 152

                          170
                   ....*....|.
gi 296925963   267 KKTGRNRCVAA 277
Cdd:smart00267 153 KKAGRNQVAVY 163
diguan_SiaD NF038266
biofilm regulation diguanylate cyclase SiaD;
104-274 1.05e-46

biofilm regulation diguanylate cyclase SiaD;


Pssm-ID: 468439 [Multi-domain]  Cd Length: 252  Bit Score: 157.07  E-value: 1.05e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296925963 104 TLEQENITDPLLGIYNRRYLEEMLELEFRLSRRDGLPLSILLLDIDHFKEVNDKHGHLAGDRTLLNLVQEIKGNLRETDQ 183
Cdd:NF038266  89 ALREASTRDPLTGLPNRRLLMERLREEVERARRSGRPFTLAMLDVDHFKRINDRYGHEVGDRVLVEIARTLRAELREYDL 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296925963 184 LARYGGEEILIMLPHTPEDGAKLVAEKIRRGIAGgimVAAGEREDegwpDISITVSIGVAGLRDEFSSGKELFAKADQAL 263
Cdd:NF038266 169 CGRWGGEEFLLLLPETGLEEAQVVLERLREAVRA---LAVRVGDD----VLSVTASAGLAEHRPPEEGLSATLSRADQAL 241

                        170
                 ....*....|.
gi 296925963 264 YRAKKTGRNRC 274
Cdd:NF038266 242 YQAKRAGRDRV 252
PRK09894 PRK09894
diguanylate cyclase; Provisional
 112-282 1.69e-44

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 152.53  E-value: 1.69e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296925963 112 DPLLGIYNRRYLEEmlELEFRLSRRDGLPLSILLLDIDHFKEVNDKHGHLAGDRTLLNLVQEIKGNLRETDQLARYGGEE 191
Cdd:PRK09894 132 DVLTGLPGRRVLDE--SFDHQLRNREPQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGGEE 209

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296925963 192 ILIMLP-HTPEDGAKlVAEKIRRGIAGGIMVAAGERedegwpdISITVSIGVAGLRDEFSSgKELFAKADQALYRAKKTG 270
Cdd:PRK09894 210 FIICLKaATDEEACR-AGERIRQLIANHAITHSDGR-------INITATFGVSRAFPEETL-DVVIGRADRAMYEGKQTG 280

                        170
                 ....*....|..
gi 296925963 271 RNRCVAASELEQ 282
Cdd:PRK09894 281 RNRVMFIDEQNV 292
PRK15426 PRK15426
cellulose biosynthesis regulator YedQ;
105-276 1.68e-40

cellulose biosynthesis regulator YedQ;


Pssm-ID: 237964 [Multi-domain]  Cd Length: 570  Bit Score: 147.47  E-value: 1.68e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296925963 105 LEQENITDPLLGIYNRRYLEEMLELEFRLSRRDGLPLSILLLDIDHFKEVNDKHGHLAGDRTLLNLVQEIKGNLRETDQL 184
Cdd:PRK15426 394 LQWQAWHDPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVA 473

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296925963 185 ARYGGEEILIMLPHTPEDGAKLVAEKIRRGIAGGIMVAAGEREdegwpdISITVSIGVAG-LRDEFSSGKELFAKADQAL 263
Cdd:PRK15426 474 GRVGGEEFCVVLPGASLAEAAQVAERIRLRINEKEILVAKSTT------IRISASLGVSSaEEDGDYDFEQLQSLADRRL 547

                        170
                 ....*....|...
gi 296925963 264 YRAKKTGRNRCVA 276
Cdd:PRK15426 548 YLAKQAGRNRVCA 560
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 111-275 6.19e-40

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: 147.23  E-value: 6.19e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296925963 111 TDPLLGIYNRRYLEEMLELEFRLSRRDGLPLSILLLDIDHFKEVNDKHGHLAGDRTLLNLVQEIKGNLRETDQLARYGGE 190
Cdd:COG5001  253 HDPLTGLPNRRLFLDRLEQALARARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGD 332

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296925963 191 EILIMLPHTP-EDGAKLVAEKIRRGIAGGIMVaaGEREdegwpdISITVSIGVAGLRDEFSSGKELFAKADQALYRAKKT 269
Cdd:COG5001  333 EFAVLLPDLDdPEDAEAVAERILAALAEPFEL--DGHE------LYVSASIGIALYPDDGADAEELLRNADLAMYRAKAA 404


                 ....*.
gi 296925963 270 GRNRCV 275
Cdd:COG5001  405 GRNRYR 410
adrA PRK10245
diguanylate cyclase AdrA; Provisional
 83-277 1.61e-33

diguanylate cyclase AdrA; Provisional


Pssm-ID: 182329 [Multi-domain]  Cd Length: 366  Bit Score: 125.33  E-value: 1.61e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296925963  83 IFVLLVNLLSLKTTLEL---KRicTLEQENITDPLLGIYNRRYLEEMLELEFRLSRRDGLPLSILLLDIDHFKEVNDKHG 159
Cdd:PRK10245 178 IYPLLFAWVSYQTATKLaehKR--RLQVMSTRDGMTGVYNRRHWETLLRNEFDNCRRHHRDATLLIIDIDHFKSINDTWG 255

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296925963 160 HLAGDRTLLNLVQEIKGNLRETDQLARYGGEEILIMLPHTPEDGAKLVAEKIRRGIAGGIMVAAgeredegwPDISITVS 239
Cdd:PRK10245 256 HDVGDEAIVALTRQLQITLRGSDVIGRFGGDEFAVIMSGTPAESAITAMSRVHEGLNTLRLPNA--------PQVTLRIS 327

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 296925963 240 IGVAGLRDEFSSGKELFAKADQALYRAKKTGRNRC-VAA 277
Cdd:PRK10245 328 VGVAPLNPQMSHYREWLKSADLALYKAKNAGRNRTeVAA 366
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
111-283 4.98e-19

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 86.66  E-value: 4.98e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296925963 111 TDPLLGIYNRRYLEEMLELEfrLSRRDGLPLSILLLDIDHFKEVNDKHGHLAGDRTLLNLVQEIKGNLRETDQLARYGGE 190
Cdd:PRK10060 239 TDSITGLPNRNAIQELIDHA--INAADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQTLARLGGD 316

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296925963 191 EILIMLPHTP----EDGAKLVAEKIRRGIAGGIMvaageredegwpDISITVSIGVAGLRDEFSSGKELFAKADQALYRA 266
Cdd:PRK10060 317 EFLVLASHTSqaalEAMASRILTRLRLPFRIGLI------------EVYTGCSIGIALAPEHGDDSESLIRSADTAMYTA 384

                        170
                 ....*....|....*...
gi 296925963 267 KKTGRNR-CVAASELEQK 283
Cdd:PRK10060 385 KEGGRGQfCVFSPEMNQR 402
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 112-273 2.44e-18

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 85.11  E-value: 2.44e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296925963  112 DPLLGIYNRRYLEEMLELEFRLSRRDGLPLSILLLDIDHFKEVNDKHGHLAGDRTLLNLVQEIKGNLRETDQLARYGGEE 191
Cdd:PRK09776  668 DALTHLANRASFEKQLRRLLQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSDVLARLGGDE 747

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296925963  192 ILIMLPHTPEDGAKLVAEKIRRGIAGGIMVAAGEREDEGwpdisitVSIGVAGLRDEFSSGKELFAKADQALYRAKKTGR 271
Cdd:PRK09776  748 FGLLLPDCNVESARFIATRIISAINDYHFPWEGRVYRVG-------ASAGITLIDANNHQASEVMSQADIACYAAKNAGR 820


                  ..
gi 296925963  272 NR 273
Cdd:PRK09776  821 GR 822
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 112-272 3.18e-15

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 75.58  E-value: 3.18e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296925963 112 DPLLGIYNR----RYLEEMLELEfrlsrrdgLPLSILLLDIDHFKEVNDKHGHLAGDRTLLNLVQEIKGNLRETDQLARY 187
Cdd:PRK11359 379 DPLTGLPNRnnlhNYLDDLVDKA--------VSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRI 450

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296925963 188 GGEEILIMLPHTPEDGAKLVAEKIRRgIAGGIMVAAGERedegwpdISITVSIGVAglrdeFSSGKE---LFAKADQALY 264
Cdd:PRK11359 451 EGTQFVLVSLENDVSNITQIADELRN-VVSKPIMIDDKP-------FPLTLSIGIS-----YDVGKNrdyLLSTAHNAMD 517


                 ....*...
gi 296925963 265 RAKKTGRN 272
Cdd:PRK11359 518 YIRKNGGN 525
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 182-267 7.68e-14

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: 68.01  E-value: 7.68e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296925963 182 DQLARYGGEEILIMLPHTPEDGAKLVAEKIRRGIAggimvaageredeGWPDISITVSIGVAglrdefssGKELFAKADq 261
Cdd:COG3706  116 DLVARYGGEEFAILLPGTDLEGALAVAERIREAVA-------------ELPSLRVTVSIGVA--------GDSLLKRAD- 173


                 ....*.
gi 296925963 262 ALYRAK 267
Cdd:COG3706  174 ALYQAR 179
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
 140-243 6.17e-11

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: 58.91  E-value: 6.17e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296925963 140 PLSILLLDIDHFKEVNDKHGHLAGDRTLLNLVQEIKGNLRET-DQLARYGGEEILIMLPHTPEDGAKLVAEKIRrgiagg 218
Cdd:cd07556    1 PVTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSgDLKIKTIGDEFMVVSGLDHPAAAVAFAEDMR------ 74

                         90       100
                 ....*....|....*....|....*
gi 296925963 219 iMVAAGEREDEGWPdisITVSIGVA 243
Cdd:cd07556   75 -EAVSALNQSEGNP---VRVRIGIH 95
PRK09966 PRK09966
diguanylate cyclase DgcN;
73-275 2.14e-08

diguanylate cyclase DgcN;


Pssm-ID: 182171 [Multi-domain]  Cd Length: 407  Bit Score: 54.63  E-value: 2.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296925963  73 IAPFILFFGAIFVLLVNLLSLKTTLELKRiCTLEQENITDPLLGIYNRRYLEEML-ELEFRLSRRDGLPLsiLLLDIDHF 151
Cdd:PRK09966 213 IAEFHRFALDFNSLLDEMEEWQLRLQAKN-AQLLRTALHDPLTGLANRAAFRSGInTLMNNSDARKTSAL--LFLDGDNF 289

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296925963 152 KEVNDKHGHLAGDRTLLNLVQEIK--GNLREtdQLARYGGEEILIMLPHT-PEDGAKLVAEKIRRGIAGGIMVAAGERed 228
Cdd:PRK09966 290 KYINDTWGHATGDRVLIEIAKRLAefGGLRH--KAYRLGGDEFAMVLYDVqSESEVQQICSALTQIFNLPFDLHNGHQ-- 365

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 296925963 229 egwpdISITVSIGVAgLRDEFSSGKELFAKADQALYRAKKTGRNRCV 275
Cdd:PRK09966 366 -----TTMTLSIGYA-MTIEHASAEKLQELADHNMYQAKHQRAEKLV 406
 
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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