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Conserved domains on  [gi|1889614195|ref|WP_182716867|]
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MULTISPECIES: GGDEF domain-containing protein [unclassified Pseudoalteromonas]

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 ...
 67-332 9.90e-42

GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants [Signal transduction mechanisms];


:

Pssm-ID: 441801 [Multi-domain]  Cd Length: 275  Bit Score: 146.66  E-value: 9.90e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614195  67 LQFWQSVVMCALITFIVILGTSLSSPRNGVYVWSFALPILYYLLLGKQYGVIFSANLLVIQVFILGSQSTLAPFETFNLS 146
Cdd:COG2199     3 LLLLLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614195 147 LNLLCAYLSIWAISHVFEGSRSHFSRRLKNLALLDPLTGAGNRLSMNHYFEVELQDKSQLYLFLLDLD----FFKQINDE 222
Cdd:COG2199    83 LLLLLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLidldHFKRINDT 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614195 223 HGHGVGDQVLIEVATLLRVVLGRG-YVFRVGGEEFALFSSFANEETALNTAEQIRARFENTTFDIDGLAINVTTSIGVAK 301
Cdd:COG2199   163 YGHAAGDEVLKEVARRLRASLRESdLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELEGKELRVTVSIGVAL 242

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1889614195 302 FKSTN-SLESFVNQADKQLYKAKQFGRNKVYC 332
Cdd:COG2199   243 YPEDGdSAEELLRRADLALYRAKRAGRNRVVV 274
 
Name Accession Description Interval E-value
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 67-332 9.90e-42

GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants [Signal transduction mechanisms];


Pssm-ID: 441801 [Multi-domain]  Cd Length: 275  Bit Score: 146.66  E-value: 9.90e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614195  67 LQFWQSVVMCALITFIVILGTSLSSPRNGVYVWSFALPILYYLLLGKQYGVIFSANLLVIQVFILGSQSTLAPFETFNLS 146
Cdd:COG2199     3 LLLLLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614195 147 LNLLCAYLSIWAISHVFEGSRSHFSRRLKNLALLDPLTGAGNRLSMNHYFEVELQDKSQLYLFLLDLD----FFKQINDE 222
Cdd:COG2199    83 LLLLLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLidldHFKRINDT 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614195 223 HGHGVGDQVLIEVATLLRVVLGRG-YVFRVGGEEFALFSSFANEETALNTAEQIRARFENTTFDIDGLAINVTTSIGVAK 301
Cdd:COG2199   163 YGHAAGDEVLKEVARRLRASLRESdLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELEGKELRVTVSIGVAL 242

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1889614195 302 FKSTN-SLESFVNQADKQLYKAKQFGRNKVYC 332
Cdd:COG2199   243 YPEDGdSAEELLRRADLALYRAKRAGRNRVVV 274
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 181-330 2.66e-38

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: 133.84  E-value: 2.66e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614195 181 DPLTGAGNRlsmnHYFEVELQDKSQLYLFLLDLDFF--------KQINDEHGHGVGDQVLIEVATLLRVVLGRG-YVFRV 251
Cdd:cd01949     3 DPLTGLPNR----RAFEERLERLLARARRSGRPLALllididhfKQINDTYGHAAGDEVLKEVAERLRSSLRESdLVARL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614195 252 GGEEFALFSSFANEETALNTAEQIRARFENTTFdIDGLAINVTTSIGVAKFKS-TNSLESFVNQADKQLYKAKQFGRNKV 330
Cdd:cd01949    79 GGDEFAILLPGTDLEEAEALAERLREAIEEPFF-IDGQEIRVTASIGIATYPEdGEDAEELLRRADEALYRAKRSGRNRV 157
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 177-330 1.84e-33

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 121.59  E-value: 1.84e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614195  177 LALLDPLTGAGNRLSMNHYFEVELQDKSQLYLFLLDLD----FFKQINDEHGHGVGDQVLIEVATLLRVVLGRG-YVFRV 251
Cdd:smart00267   2 LAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLidldNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGdLLARL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614195  252 GGEEFALFSSFANEETALNTAEQIRARFEnTTFDIDGLAINVTTSIGVAKF-KSTNSLESFVNQADKQLYKAKQFGRNKV 330
Cdd:smart00267  82 GGDEFALLLPETSLEEAIALAERILQQLR-EPIIIHGIPLYLTISIGVAAYpNPGEDAEDLLKRADTALYQAKKAGRNQV 160
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 178-329 2.99e-32

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: 118.12  E-value: 2.99e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614195 178 ALLDPLTGAGNRLSMNHYFEVELQ----DKSQLYLFLLDLDFFKQINDEHGHGVGDQVLIEVATLLRVVLGRG-YVFRVG 252
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELQralrEGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSdLVARLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614195 253 GEEFALFSSFANEETALNTAEQIRARFE--NTTFDIDGLAINVTTSIGVAKF-KSTNSLESFVNQADKQLYKAKQFGRNK 329
Cdd:pfam00990  81 GDEFAILLPETSLEGAQELAERIRRLLAklKIPHTVSGLPLYVTISIGIAAYpNDGEDPEDLLKRADTALYQAKQAGRNR 160
pleD PRK09581
response regulator PleD; Reviewed
 176-331 1.29e-27

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 112.30  E-value: 1.29e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614195 176 NLALLDPLTGAGNRlsmnHYFEVELQ---DKSQLYLFLLDLDFF-----KQINDEHGHGVGDQVLIEVATLLRVVLgRG- 246
Cdd:PRK09581  290 EMAVTDGLTGLHNR----RYFDMHLKnliERANERGKPLSLMMIdidhfKKVNDTYGHDAGDEVLREFAKRLRNNI-RGt 364

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614195 247 -YVFRVGGEEFALFSSFANEETALNTAEQIRARFENTTFDIDGLA--INVTTSIGVAKF-KSTNSLESFVNQADKQLYKA 322
Cdd:PRK09581  365 dLIARYGGEEFVVVMPDTDIEDAIAVAERIRRKIAEEPFIISDGKerLNVTVSIGVAELrPSGDTIEALIKRADKALYEA 444


                  ....*....
gi 1889614195 323 KQFGRNKVY 331
Cdd:PRK09581  445 KNTGRNRVV 453
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 177-331 2.77e-27

diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by many proteins carrying the domain. There is evidence that the domain has diguanylate cyclase activity. Several proteins carrying this domain also carry domains with functions relating to environmental sensing. These include PleD, a response regulator protein involved in the swarmer-to-stalked cell transition in Caulobacter crescentus, and FixL, a heme-containing oxygen sensor protein. [Regulatory functions, Small molecule interactions, Signal transduction, Other]


Pssm-ID: 272984 [Multi-domain]  Cd Length: 165  Bit Score: 105.11  E-value: 2.77e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614195 177 LALLDPLTGAGNRLSMNHYFEVELQ----DKSQLYLFLLDLDFFKQINDEHGHGVGDQVLIEVATLLRV-VLGRGYVFRV 251
Cdd:TIGR00254   1 QAVRDPLTGLYNRRYLEEMLDSELKrarrFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSsVRGSDVVGRY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614195 252 GGEEFALFSSFANEETALNTAEQIRARFENTTFDIDGLA-INVTTSIGVAKFKS-TNSLESFVNQADKQLYKAKQFGRNK 329
Cdd:TIGR00254  81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSEtLTVTVSIGVACYPGhGLTLEELLKRADEALYQAKKAGRNR 160


                  ..
gi 1889614195 330 VY 331
Cdd:TIGR00254 161 VV 162
 
Name Accession Description Interval E-value
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 67-332 9.90e-42

GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants [Signal transduction mechanisms];


Pssm-ID: 441801 [Multi-domain]  Cd Length: 275  Bit Score: 146.66  E-value: 9.90e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614195  67 LQFWQSVVMCALITFIVILGTSLSSPRNGVYVWSFALPILYYLLLGKQYGVIFSANLLVIQVFILGSQSTLAPFETFNLS 146
Cdd:COG2199     3 LLLLLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614195 147 LNLLCAYLSIWAISHVFEGSRSHFSRRLKNLALLDPLTGAGNRLSMNHYFEVELQDKSQLYLFLLDLD----FFKQINDE 222
Cdd:COG2199    83 LLLLLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLidldHFKRINDT 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614195 223 HGHGVGDQVLIEVATLLRVVLGRG-YVFRVGGEEFALFSSFANEETALNTAEQIRARFENTTFDIDGLAINVTTSIGVAK 301
Cdd:COG2199   163 YGHAAGDEVLKEVARRLRASLRESdLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELEGKELRVTVSIGVAL 242

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1889614195 302 FKSTN-SLESFVNQADKQLYKAKQFGRNKVYC 332
Cdd:COG2199   243 YPEDGdSAEELLRRADLALYRAKRAGRNRVVV 274
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 181-330 2.66e-38

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: 133.84  E-value: 2.66e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614195 181 DPLTGAGNRlsmnHYFEVELQDKSQLYLFLLDLDFF--------KQINDEHGHGVGDQVLIEVATLLRVVLGRG-YVFRV 251
Cdd:cd01949     3 DPLTGLPNR----RAFEERLERLLARARRSGRPLALllididhfKQINDTYGHAAGDEVLKEVAERLRSSLRESdLVARL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614195 252 GGEEFALFSSFANEETALNTAEQIRARFENTTFdIDGLAINVTTSIGVAKFKS-TNSLESFVNQADKQLYKAKQFGRNKV 330
Cdd:cd01949    79 GGDEFAILLPGTDLEEAEALAERLREAIEEPFF-IDGQEIRVTASIGIATYPEdGEDAEELLRRADEALYRAKRSGRNRV 157
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 177-330 1.84e-33

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 121.59  E-value: 1.84e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614195  177 LALLDPLTGAGNRLSMNHYFEVELQDKSQLYLFLLDLD----FFKQINDEHGHGVGDQVLIEVATLLRVVLGRG-YVFRV 251
Cdd:smart00267   2 LAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLidldNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGdLLARL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614195  252 GGEEFALFSSFANEETALNTAEQIRARFEnTTFDIDGLAINVTTSIGVAKF-KSTNSLESFVNQADKQLYKAKQFGRNKV 330
Cdd:smart00267  82 GGDEFALLLPETSLEEAIALAERILQQLR-EPIIIHGIPLYLTISIGVAAYpNPGEDAEDLLKRADTALYQAKKAGRNQV 160
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 178-329 2.99e-32

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: 118.12  E-value: 2.99e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614195 178 ALLDPLTGAGNRLSMNHYFEVELQ----DKSQLYLFLLDLDFFKQINDEHGHGVGDQVLIEVATLLRVVLGRG-YVFRVG 252
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELQralrEGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSdLVARLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614195 253 GEEFALFSSFANEETALNTAEQIRARFE--NTTFDIDGLAINVTTSIGVAKF-KSTNSLESFVNQADKQLYKAKQFGRNK 329
Cdd:pfam00990  81 GDEFAILLPETSLEGAQELAERIRRLLAklKIPHTVSGLPLYVTISIGIAAYpNDGEDPEDLLKRADTALYQAKQAGRNR 160
pleD PRK09581
response regulator PleD; Reviewed
 176-331 1.29e-27

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 112.30  E-value: 1.29e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614195 176 NLALLDPLTGAGNRlsmnHYFEVELQ---DKSQLYLFLLDLDFF-----KQINDEHGHGVGDQVLIEVATLLRVVLgRG- 246
Cdd:PRK09581  290 EMAVTDGLTGLHNR----RYFDMHLKnliERANERGKPLSLMMIdidhfKKVNDTYGHDAGDEVLREFAKRLRNNI-RGt 364

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614195 247 -YVFRVGGEEFALFSSFANEETALNTAEQIRARFENTTFDIDGLA--INVTTSIGVAKF-KSTNSLESFVNQADKQLYKA 322
Cdd:PRK09581  365 dLIARYGGEEFVVVMPDTDIEDAIAVAERIRRKIAEEPFIISDGKerLNVTVSIGVAELrPSGDTIEALIKRADKALYEA 444


                  ....*....
gi 1889614195 323 KQFGRNKVY 331
Cdd:PRK09581  445 KNTGRNRVV 453
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 172-328 2.18e-27

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: 112.95  E-value: 2.18e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614195 172 RRLKNLALLDPLTGAGNRLSMNHYFEVELQ----------------DKsqlylflldldfFKQINDEHGHGVGDQVLIEV 235
Cdd:COG5001   245 ERLRHLAYHDPLTGLPNRRLFLDRLEQALArarrsgrrlallfidlDR------------FKEINDTLGHAAGDELLREV 312

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614195 236 ATLLRVVLGRG-YVFRVGGEEFA-LFSSFANEETALNTAEQIRARFeNTTFDIDGLAINVTTSIGVAKF-KSTNSLESFV 312
Cdd:COG5001   313 ARRLRACLREGdTVARLGGDEFAvLLPDLDDPEDAEAVAERILAAL-AEPFELDGHELYVSASIGIALYpDDGADAEELL 391

                         170
                  ....*....|....*.
gi 1889614195 313 NQADKQLYKAKQFGRN 328
Cdd:COG5001   392 RNADLAMYRAKAAGRN 407
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 177-331 2.77e-27

diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by many proteins carrying the domain. There is evidence that the domain has diguanylate cyclase activity. Several proteins carrying this domain also carry domains with functions relating to environmental sensing. These include PleD, a response regulator protein involved in the swarmer-to-stalked cell transition in Caulobacter crescentus, and FixL, a heme-containing oxygen sensor protein. [Regulatory functions, Small molecule interactions, Signal transduction, Other]


Pssm-ID: 272984 [Multi-domain]  Cd Length: 165  Bit Score: 105.11  E-value: 2.77e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614195 177 LALLDPLTGAGNRLSMNHYFEVELQ----DKSQLYLFLLDLDFFKQINDEHGHGVGDQVLIEVATLLRV-VLGRGYVFRV 251
Cdd:TIGR00254   1 QAVRDPLTGLYNRRYLEEMLDSELKrarrFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSsVRGSDVVGRY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614195 252 GGEEFALFSSFANEETALNTAEQIRARFENTTFDIDGLA-INVTTSIGVAKFKS-TNSLESFVNQADKQLYKAKQFGRNK 329
Cdd:TIGR00254  81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSEtLTVTVSIGVACYPGhGLTLEELLKRADEALYQAKKAGRNR 160


                  ..
gi 1889614195 330 VY 331
Cdd:TIGR00254 161 VV 162
PRK09894 PRK09894
diguanylate cyclase; Provisional
 130-330 3.42e-24

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 100.14  E-value: 3.42e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614195 130 ILGSQSTLAPFETFNlslNLLCAY-LSIWAISHvfegsrsHFSRRLKNLallDPLTGAGNRLSMNHYFEVELQDKSQLYL 208
Cdd:PRK09894   93 IVEGHWQDAHFDAFQ---EGLLSFtAALTDYKI-------YLLTIRSNM---DVLTGLPGRRVLDESFDHQLRNREPQNL 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614195 209 FLLDLDF--FKQINDEHGHGVGDQVLIEVATLLRVVLgRGY--VFRVGGEEFALFSSFANEETALNTAEQIRARFENTTF 284
Cdd:PRK09894  160 YLALLDIdrFKLVNDTYGHLIGDVVLRTLATYLASWT-RDYetVYRYGGEEFIICLKAATDEEACRAGERIRQLIANHAI 238

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1889614195 285 DIDGLAINVTTSIGVAKFKSTNSLESFVNQADKQLYKAKQFGRNKV 330
Cdd:PRK09894  239 THSDGRINITATFGVSRAFPEETLDVVIGRADRAMYEGKQTGRNRV 284
PRK15426 PRK15426
cellulose biosynthesis regulator YedQ;
133-330 8.07e-19

cellulose biosynthesis regulator YedQ;


Pssm-ID: 237964 [Multi-domain]  Cd Length: 570  Bit Score: 87.38  E-value: 8.07e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614195 133 SQSTLAPFETFNLSLNLLCAYLSI-----WAI-----SHVFEGSRShfsrrLKNLALLDPLTGAGNRLSMNHYFEVELQ- 201
Cdd:PRK15426  348 REGVRGDFGSISIALTLLWALFTAmllisWYVirrmvSNMFVLQSS-----LQWQAWHDPLTRLYNRGALFEKARALAKr 422

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614195 202 ---DKSQLYLFLLDLDFFKQINDEHGHGVGDQVLIEVATLLRVVLGRGYVF-RVGGEEFALFSSFANEETALNTAEQIRA 277
Cdd:PRK15426  423 cqrDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVAgRVGGEEFCVVLPGASLAEAAQVAERIRL 502

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1889614195 278 RFENTTFDI-DGLAINVTTSIGVAKFKSTN--SLESFVNQADKQLYKAKQFGRNKV 330
Cdd:PRK15426  503 RINEKEILVaKSTTIRISASLGVSSAEEDGdyDFEQLQSLADRRLYLAKQAGRNRV 558
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
173-337 2.77e-14

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 73.95  E-value: 2.77e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614195 173 RLKNLALLDPLTGAGNRLSMNHYFEVELQ--DKSQLYLFLLDLDFFKQINDEHGHGVGDQVLIEVATLLRVVLGRGYVF- 249
Cdd:PRK10060  232 RLRILANTDSITGLPNRNAIQELIDHAINaaDNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQTLa 311

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614195 250 RVGGEEFALFSSFANEETALNTAEQIRARFEnTTFDIdGLaINVTT--SIGVAKF-KSTNSLESFVNQADKQLYKAKQFG 326
Cdd:PRK10060  312 RLGGDEFLVLASHTSQAALEAMASRILTRLR-LPFRI-GL-IEVYTgcSIGIALApEHGDDSESLIRSADTAMYTAKEGG 388

                         170
                  ....*....|.
gi 1889614195 327 RNKvYCKFKKE 337
Cdd:PRK10060  389 RGQ-FCVFSPE 398
PRK09966 PRK09966
diguanylate cyclase DgcN;
133-324 1.05e-13

diguanylate cyclase DgcN;


Pssm-ID: 182171 [Multi-domain]  Cd Length: 407  Bit Score: 71.58  E-value: 1.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614195 133 SQSTLAPFETFNLSLNLLCAYLSIWAIShvFEGSRSHFSRRlknlALLDPLTGAGNRLSMNHYFEVELQD---KSQLYLF 209
Cdd:PRK09966  209 SEERIAEFHRFALDFNSLLDEMEEWQLR--LQAKNAQLLRT----ALHDPLTGLANRAAFRSGINTLMNNsdaRKTSALL 282

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614195 210 LLDLDFFKQINDEHGHGVGDQVLIEVATLLRVVLGRGY-VFRVGGEEFALFSSFANEETALNTAEQIRARFENTTFDI-D 287
Cdd:PRK09966  283 FLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHkAYRLGGDEFAMVLYDVQSESEVQQICSALTQIFNLPFDLhN 362

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1889614195 288 GLAINVTTSIGVAKFKSTNSLESFVNQADKQLYKAKQ 324
Cdd:PRK09966  363 GHQTTMTLSIGYAMTIEHASAEKLQELADHNMYQAKH 399
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 151-300 5.02e-12

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 67.10  E-value: 5.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614195 151 CAYLSIWAISHvfEGSRSHFSRrlknLALLDPLTGAGNRLSMNHYFEVELQDKSQLYLFLLDLDFFKQINDEHGHGVGDQ 230
Cdd:PRK11359  355 SQHLAALALEQ--EKSRQHIEQ----LIQFDPLTGLPNRNNLHNYLDDLVDKAVSPVVYLIGVDHFQDVIDSLGYAWADQ 428

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1889614195 231 VLIEVATLLRVVLGRG-YVFRVGGEEFALFSSFANEETALNTAEQIRaRFENTTFDIDGLAINVTTSIGVA 300
Cdd:PRK11359  429 ALLEVVNRFREKLKPDqYLCRIEGTQFVLVSLENDVSNITQIADELR-NVVSKPIMIDDKPFPLTLSIGIS 498
adrA PRK10245
diguanylate cyclase AdrA; Provisional
 136-329 1.15e-11

diguanylate cyclase AdrA; Provisional


Pssm-ID: 182329 [Multi-domain]  Cd Length: 366  Bit Score: 65.24  E-value: 1.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614195 136 TLAPFETFnLSLNLLCAYLSIWA-ISHVFEGSRSHFSRRLKNLALLDPLTGAGNR----LSMNHYFEVELQDKSQLYLFL 210
Cdd:PRK10245  163 NSAPLEWW-LSLPVIVIYPLLFAwVSYQTATKLAEHKRRLQVMSTRDGMTGVYNRrhweTLLRNEFDNCRRHHRDATLLI 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614195 211 LDLDFFKQINDEHGHGVGDQVLIEVATLLRVVL-GRGYVFRVGGEEFALFSSFANEETALNTAEQIRARFENTTFDIdgl 289
Cdd:PRK10245  242 IDIDHFKSINDTWGHDVGDEAIVALTRQLQITLrGSDVIGRFGGDEFAVIMSGTPAESAITAMSRVHEGLNTLRLPN--- 318

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1889614195 290 AINVT--TSIGVAKFKSTNS-LESFVNQADKQLYKAKQFGRNK 329
Cdd:PRK10245  319 APQVTlrISVGVAPLNPQMShYREWLKSADLALYKAKNAGRNR 361
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 172-331 1.29e-11

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 65.85  E-value: 1.29e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614195  172 RRLKNLALLDPLTGAGNRLSmnhyFEVELQDKSQLYLFLLDLDFF--------KQINDEHGHGVGDQVLIEVATLLRVVL 243
Cdd:PRK09776   659 RQLSYSASHDALTHLANRAS----FEKQLRRLLQTVNSTHQRHALvfidldrfKAVNDSAGHAAGDALLRELASLMLSML 734

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614195  244 -GRGYVFRVGGEEFALFSSFANEETALNTAEQIRARFENTTFDIDGLAINVTTSIGVAKFKSTNSLESFV-NQADKQLYK 321
Cdd:PRK09776   735 rSSDVLARLGGDEFGLLLPDCNVESARFIATRIISAINDYHFPWEGRVYRVGASAGITLIDANNHQASEVmSQADIACYA 814

                          170
                   ....*....|
gi 1889614195  322 AKQFGRNKVY 331
Cdd:PRK09776   815 AKNAGRGRVT 824
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 248-323 9.45e-10

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: 57.23  E-value: 9.45e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1889614195 248 VFRVGGEEFALFSSFANEETALNTAEQIRARFENTTfdidglAINVTTSIGVAKfkstnslESFVNQADKqLYKAK 323
Cdd:COG3706   118 VARYGGEEFAILLPGTDLEGALAVAERIREAVAELP------SLRVTVSIGVAG-------DSLLKRADA-LYQAR 179
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
 217-300 2.60e-04

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: 40.42  E-value: 2.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889614195 217 KQINDEHGHGVGDQVLIEVATLLRVVLGR--GYVFRVGGEEFALFSSFANEETALNTAEQIRARFENTTFdidGLAINVT 294
Cdd:cd07556    13 TSLADALGPDEGDELLNELAGRFDSLIRRsgDLKIKTIGDEFMVVSGLDHPAAAVAFAEDMREAVSALNQ---SEGNPVR 89


                  ....*.
gi 1889614195 295 TSIGVA 300
Cdd:cd07556    90 VRIGIH 95
 
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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