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Conserved domains on  [gi|639331124|ref|WP_024598550|]
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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 1.39e-41

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: 146.28  E-value: 1.39e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639331124  67 LQFWQSLIMCALVTLIIILGTYLASPRNGVFVWSFALPILYYLLLGKQYGVIFSANLLVIQVLILGSKSTLTPFETFNLS 146
Cdd:COG2199    3 LLLLLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639331124 147 LNLICAYFSIWAISHVFEGSRSHFSKRLKNLALLDPLTGAGNRLSMNHYFEVELKDKSQLYLFLLDLD----FFKQVNDE 222
Cdd:COG2199   83 LLLLLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLidldHFKRINDT 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639331124 223 HGHGVGDQVLVEVATLLRVVLGRG-YVFRVGGEEFALFSSFANEEAALNTAEQIRARFENTTFDIDGLAINVTTSIGVAK 301
Cdd:COG2199  163 YGHAAGDEVLKEVARRLRASLRESdLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELEGKELRVTVSIGVAL 242

                        250       260       270
                 ....*....|....*....|....*....|..
gi 639331124 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 1.39e-41

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: 146.28  E-value: 1.39e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639331124  67 LQFWQSLIMCALVTLIIILGTYLASPRNGVFVWSFALPILYYLLLGKQYGVIFSANLLVIQVLILGSKSTLTPFETFNLS 146
Cdd:COG2199    3 LLLLLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639331124 147 LNLICAYFSIWAISHVFEGSRSHFSKRLKNLALLDPLTGAGNRLSMNHYFEVELKDKSQLYLFLLDLD----FFKQVNDE 222
Cdd:COG2199   83 LLLLLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLidldHFKRINDT 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639331124 223 HGHGVGDQVLVEVATLLRVVLGRG-YVFRVGGEEFALFSSFANEEAALNTAEQIRARFENTTFDIDGLAINVTTSIGVAK 301
Cdd:COG2199  163 YGHAAGDEVLKEVARRLRASLRESdLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELEGKELRVTVSIGVAL 242

                        250       260       270
                 ....*....|....*....|....*....|..
gi 639331124 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 3.69e-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: 133.45  E-value: 3.69e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639331124 181 DPLTGAGNRlsmnHYFEVELKDKSQLYLFLLDLDFF--------KQVNDEHGHGVGDQVLVEVATLLRVVLGRG-YVFRV 251
Cdd:cd01949    3 DPLTGLPNR----RAFEERLERLLARARRSGRPLALllididhfKQINDTYGHAAGDEVLKEVAERLRSSLRESdLVARL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639331124 252 GGEEFALFSSFANEEAALNTAEQIRARFENTTFdIDGLAINVTTSIGVAKFKS-TNSLESFVNQADKQLYKAKQFGRNKV 330
Cdd:cd01949   79 GGDEFAILLPGTDLEEAEALAERLREAIEEPFF-IDGQEIRVTASIGIATYPEdGEDAEELLRRADEALYRAKRSGRNRV 157
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 177-330 3.50e-33

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 120.82  E-value: 3.50e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639331124   177 LALLDPLTGAGNRLSMNHYFEVELKDKSQLYLFLLDLD----FFKQVNDEHGHGVGDQVLVEVATLLRVVLGRG-YVFRV 251
Cdd:smart00267   2 LAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLidldNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGdLLARL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639331124   252 GGEEFALFSSFANEEAALNTAEQIRARFEnTTFDIDGLAINVTTSIGVAKF-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 4.52e-31

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: 115.04  E-value: 4.52e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639331124  178 ALLDPLTGAGNRLSMNHYFEVEL----KDKSQLYLFLLDLDFFKQVNDEHGHGVGDQVLVEVATLLRVVLGRG-YVFRVG 252
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELqralREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSdLVARLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639331124  253 GEEFALFSSFANEEAALNTAEQIRARFE--NTTFDIDGLAINVTTSIGVAKF-KSTNSLESFVNQADKQLYKAKQFGRNK 329
Cdd:pfam00990  81 GDEFAILLPETSLEGAQELAERIRRLLAklKIPHTVSGLPLYVTISIGIAAYpNDGEDPEDLLKRADTALYQAKQAGRNR 160
pleD PRK09581
response regulator PleD; Reviewed
 176-331 2.09e-27

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 111.53  E-value: 2.09e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639331124 176 NLALLDPLTGAGNRlsmnHYFEVELK---DKSQLYLFLLDLDFF-----KQVNDEHGHGVGDQVLVEVATLLRVVLgRG- 246
Cdd:PRK09581 290 EMAVTDGLTGLHNR----RYFDMHLKnliERANERGKPLSLMMIdidhfKKVNDTYGHDAGDEVLREFAKRLRNNI-RGt 364

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639331124 247 -YVFRVGGEEFALFSSFANEEAALNTAEQIRARFENTTFDIDGLA--INVTTSIGVAKF-KSTNSLESFVNQADKQLYKA 322
Cdd:PRK09581 365 dLIARYGGEEFVVVMPDTDIEDAIAVAERIRRKIAEEPFIISDGKerLNVTVSIGVAELrPSGDTIEALIKRADKALYEA 444


                 ....*....
gi 639331124 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 8.01e-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: 103.96  E-value: 8.01e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639331124  177 LALLDPLTGAGNRLSMNHYFEVELK----DKSQLYLFLLDLDFFKQVNDEHGHGVGDQVLVEVATLLRV-VLGRGYVFRV 251
Cdd:TIGR00254   1 QAVRDPLTGLYNRRYLEEMLDSELKrarrFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSsVRGSDVVGRY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639331124  252 GGEEFALFSSFANEEAALNTAEQIRARFENTTFDIDGLA-INVTTSIGVAKFKS-TNSLESFVNQADKQLYKAKQFGRNK 329
Cdd:TIGR00254  81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSEtLTVTVSIGVACYPGhGLTLEELLKRADEALYQAKKAGRNR 160


                  ..
gi 639331124  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 1.39e-41

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: 146.28  E-value: 1.39e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639331124  67 LQFWQSLIMCALVTLIIILGTYLASPRNGVFVWSFALPILYYLLLGKQYGVIFSANLLVIQVLILGSKSTLTPFETFNLS 146
Cdd:COG2199    3 LLLLLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639331124 147 LNLICAYFSIWAISHVFEGSRSHFSKRLKNLALLDPLTGAGNRLSMNHYFEVELKDKSQLYLFLLDLD----FFKQVNDE 222
Cdd:COG2199   83 LLLLLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLidldHFKRINDT 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639331124 223 HGHGVGDQVLVEVATLLRVVLGRG-YVFRVGGEEFALFSSFANEEAALNTAEQIRARFENTTFDIDGLAINVTTSIGVAK 301
Cdd:COG2199  163 YGHAAGDEVLKEVARRLRASLRESdLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELEGKELRVTVSIGVAL 242

                        250       260       270
                 ....*....|....*....|....*....|..
gi 639331124 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 3.69e-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: 133.45  E-value: 3.69e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639331124 181 DPLTGAGNRlsmnHYFEVELKDKSQLYLFLLDLDFF--------KQVNDEHGHGVGDQVLVEVATLLRVVLGRG-YVFRV 251
Cdd:cd01949    3 DPLTGLPNR----RAFEERLERLLARARRSGRPLALllididhfKQINDTYGHAAGDEVLKEVAERLRSSLRESdLVARL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639331124 252 GGEEFALFSSFANEEAALNTAEQIRARFENTTFdIDGLAINVTTSIGVAKFKS-TNSLESFVNQADKQLYKAKQFGRNKV 330
Cdd:cd01949   79 GGDEFAILLPGTDLEEAEALAERLREAIEEPFF-IDGQEIRVTASIGIATYPEdGEDAEELLRRADEALYRAKRSGRNRV 157
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 177-330 3.50e-33

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 120.82  E-value: 3.50e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639331124   177 LALLDPLTGAGNRLSMNHYFEVELKDKSQLYLFLLDLD----FFKQVNDEHGHGVGDQVLVEVATLLRVVLGRG-YVFRV 251
Cdd:smart00267   2 LAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLidldNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGdLLARL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639331124   252 GGEEFALFSSFANEEAALNTAEQIRARFEnTTFDIDGLAINVTTSIGVAKF-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 4.52e-31

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: 115.04  E-value: 4.52e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639331124  178 ALLDPLTGAGNRLSMNHYFEVEL----KDKSQLYLFLLDLDFFKQVNDEHGHGVGDQVLVEVATLLRVVLGRG-YVFRVG 252
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELqralREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSdLVARLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639331124  253 GEEFALFSSFANEEAALNTAEQIRARFE--NTTFDIDGLAINVTTSIGVAKF-KSTNSLESFVNQADKQLYKAKQFGRNK 329
Cdd:pfam00990  81 GDEFAILLPETSLEGAQELAERIRRLLAklKIPHTVSGLPLYVTISIGIAAYpNDGEDPEDLLKRADTALYQAKQAGRNR 160
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 173-339 4.90e-28

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: 114.87  E-value: 4.90e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639331124 173 RLKNLALLDPLTGAGNRLSMNHYFEVELK----------------DKsqlylflldldfFKQVNDEHGHGVGDQVLVEVA 236
Cdd:COG5001  246 RLRHLAYHDPLTGLPNRRLFLDRLEQALArarrsgrrlallfidlDR------------FKEINDTLGHAAGDELLREVA 313

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639331124 237 TLLRVVLGRG-YVFRVGGEEFA-LFSSFANEEAALNTAEQIRARFeNTTFDIDGLAINVTTSIGVAKF-KSTNSLESFVN 313
Cdd:COG5001  314 RRLRACLREGdTVARLGGDEFAvLLPDLDDPEDAEAVAERILAAL-AEPFELDGHELYVSASIGIALYpDDGADAEELLR 392

                        170       180
                 ....*....|....*....|....*.
gi 639331124 314 QADKQLYKAKQFGRNKvYCKFKKEHD 339
Cdd:COG5001  393 NADLAMYRAKAAGRNR-YRFFDPEMD 417
pleD PRK09581
response regulator PleD; Reviewed
 176-331 2.09e-27

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 111.53  E-value: 2.09e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639331124 176 NLALLDPLTGAGNRlsmnHYFEVELK---DKSQLYLFLLDLDFF-----KQVNDEHGHGVGDQVLVEVATLLRVVLgRG- 246
Cdd:PRK09581 290 EMAVTDGLTGLHNR----RYFDMHLKnliERANERGKPLSLMMIdidhfKKVNDTYGHDAGDEVLREFAKRLRNNI-RGt 364

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639331124 247 -YVFRVGGEEFALFSSFANEEAALNTAEQIRARFENTTFDIDGLA--INVTTSIGVAKF-KSTNSLESFVNQADKQLYKA 322
Cdd:PRK09581 365 dLIARYGGEEFVVVMPDTDIEDAIAVAERIRRKIAEEPFIISDGKerLNVTVSIGVAELrPSGDTIEALIKRADKALYEA 444


                 ....*....
gi 639331124 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 8.01e-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: 103.96  E-value: 8.01e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639331124  177 LALLDPLTGAGNRLSMNHYFEVELK----DKSQLYLFLLDLDFFKQVNDEHGHGVGDQVLVEVATLLRV-VLGRGYVFRV 251
Cdd:TIGR00254   1 QAVRDPLTGLYNRRYLEEMLDSELKrarrFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSsVRGSDVVGRY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639331124  252 GGEEFALFSSFANEEAALNTAEQIRARFENTTFDIDGLA-INVTTSIGVAKFKS-TNSLESFVNQADKQLYKAKQFGRNK 329
Cdd:TIGR00254  81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSEtLTVTVSIGVACYPGhGLTLEELLKRADEALYQAKKAGRNR 160


                  ..
gi 639331124  330 VY 331
Cdd:TIGR00254 161 VV 162
PRK09894 PRK09894
diguanylate cyclase; Provisional
 167-330 3.63e-25

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 102.84  E-value: 3.63e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639331124 167 RSHFSKRLKNLallDPLTGAGNRLSMNHYFEVELKDKSQLYLFLLDLDF--FKQVNDEHGHGVGDQVLVEVATLLRVVLg 244
Cdd:PRK09894 121 KIYLLTIRSNM---DVLTGLPGRRVLDESFDHQLRNREPQNLYLALLDIdrFKLVNDTYGHLIGDVVLRTLATYLASWT- 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639331124 245 RGY--VFRVGGEEFALFSSFANEEAALNTAEQIRARFENTTFDIDGLAINVTTSIGVAKFKSTNSLESFVNQADKQLYKA 322
Cdd:PRK09894 197 RDYetVYRYGGEEFIICLKAATDEEACRAGERIRQLIANHAITHSDGRINITATFGVSRAFPEETLDVVIGRADRAMYEG 276


                 ....*...
gi 639331124 323 KQFGRNKV 330
Cdd:PRK09894 277 KQTGRNRV 284
PRK15426 PRK15426
cellulose biosynthesis regulator YedQ;
140-330 1.33e-18

cellulose biosynthesis regulator YedQ;


Pssm-ID: 237964 [Multi-domain]  Cd Length: 570  Bit Score: 86.61  E-value: 1.33e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639331124 140 FETFNLSLNLICAYFSI-----WAI-----SHVFEGSRShfskrLKNLALLDPLTGAGNRLSMNHYFEVELK----DKSQ 205
Cdd:PRK15426 355 FGSISIALTLLWALFTAmllisWYVirrmvSNMFVLQSS-----LQWQAWHDPLTRLYNRGALFEKARALAKrcqrDQQP 429

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639331124 206 LYLFLLDLDFFKQVNDEHGHGVGDQVLVEVATLLRVVLGRGYVF-RVGGEEFALFSSFANEEAALNTAEQIRARFENTTF 284
Cdd:PRK15426 430 FSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVAgRVGGEEFCVVLPGASLAEAAQVAERIRLRINEKEI 509

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 639331124 285 DI-DGLAINVTTSIGVAKFKSTN--SLESFVNQADKQLYKAKQFGRNKV 330
Cdd:PRK15426 510 LVaKSTTIRISASLGVSSAEEDGdyDFEQLQSLADRRLYLAKQAGRNRV 558
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
173-337 3.26e-15

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 76.64  E-value: 3.26e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639331124 173 RLKNLALLDPLTGAGNRLSMNHYFE--VELKDKSQLYLFLLDLDFFKQVNDEHGHGVGDQVLVEVATLLRVVLGRGYVF- 249
Cdd:PRK10060 232 RLRILANTDSITGLPNRNAIQELIDhaINAADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQTLa 311

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639331124 250 RVGGEEFALFSSFANEEAALNTAEQIRARFEnTTFDIdGLaINVTT--SIGVAKF-KSTNSLESFVNQADKQLYKAKQFG 326
Cdd:PRK10060 312 RLGGDEFLVLASHTSQAALEAMASRILTRLR-LPFRI-GL-IEVYTgcSIGIALApEHGDDSESLIRSADTAMYTAKEGG 388

                        170
                 ....*....|.
gi 639331124 327 RNKvYCKFKKE 337
Cdd:PRK10060 389 RGQ-FCVFSPE 398
PRK09966 PRK09966
diguanylate cyclase DgcN;
173-324 7.16e-13

diguanylate cyclase DgcN;


Pssm-ID: 182171 [Multi-domain]  Cd Length: 407  Bit Score: 68.88  E-value: 7.16e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639331124 173 RLKNLALLDPLTGAGNRLSMNHYFEVELKD---KSQLYLFLLDLDFFKQVNDEHGHGVGDQVLVEVATLLRVVLGRGY-V 248
Cdd:PRK09966 243 QLLRTALHDPLTGLANRAAFRSGINTLMNNsdaRKTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHkA 322

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 639331124 249 FRVGGEEFALFSSFANEEAALNTAEQIRARFENTTFDI-DGLAINVTTSIGVAKFKSTNSLESFVNQADKQLYKAKQ 324
Cdd:PRK09966 323 YRLGGDEFAMVLYDVQSESEVQQICSALTQIFNLPFDLhNGHQTTMTLSIGYAMTIEHASAEKLQELADHNMYQAKH 399
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 172-331 3.97e-12

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 67.39  E-value: 3.97e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639331124  172 KRLKNLALLDPLTGAGNRLSmnhyFEVELKDKSQLYLFLLDLDFF--------KQVNDEHGHGVGDQVLVEVATLLRVVL 243
Cdd:PRK09776  659 RQLSYSASHDALTHLANRAS----FEKQLRRLLQTVNSTHQRHALvfidldrfKAVNDSAGHAAGDALLRELASLMLSML 734

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639331124  244 -GRGYVFRVGGEEFALFSsfanEEAALNTAEQIRARFENTT----FDIDGLAINVTTSIGVAKFKSTNSLESFV-NQADK 317
Cdd:PRK09776  735 rSSDVLARLGGDEFGLLL----PDCNVESARFIATRIISAIndyhFPWEGRVYRVGASAGITLIDANNHQASEVmSQADI 810

                         170
                  ....*....|....
gi 639331124  318 QLYKAKQFGRNKVY 331
Cdd:PRK09776  811 ACYAAKNAGRGRVT 824
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 172-300 4.92e-11

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 64.02  E-value: 4.92e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639331124 172 KRLKNLALLDPLTGAGNRLSMNHYFEVELKDKSQLYLFLLDLDFFKQVNDEHGHGVGDQVLVEVATLLRVVLGRG-YVFR 250
Cdd:PRK11359 370 QHIEQLIQFDPLTGLPNRNNLHNYLDDLVDKAVSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDqYLCR 449

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 639331124 251 VGGEEFALFSSFANEEAALNTAEQIRaRFENTTFDIDGLAINVTTSIGVA 300
Cdd:PRK11359 450 IEGTQFVLVSLENDVSNITQIADELR-NVVSKPIMIDDKPFPLTLSIGIS 498
adrA PRK10245
diguanylate cyclase AdrA; Provisional
 136-329 2.12e-10

diguanylate cyclase AdrA; Provisional


Pssm-ID: 182329 [Multi-domain]  Cd Length: 366  Bit Score: 61.38  E-value: 2.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639331124 136 TLTPFETFnLSLNLICAYFSIWA-ISHVFEGSRSHFSKRLKNLALLDPLTGAGNR----LSMNHYFEVELKDKSQLYLFL 210
Cdd:PRK10245 163 NSAPLEWW-LSLPVIVIYPLLFAwVSYQTATKLAEHKRRLQVMSTRDGMTGVYNRrhweTLLRNEFDNCRRHHRDATLLI 241

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639331124 211 LDLDFFKQVNDEHGHGVGDQVLVEVATLLRVVL-GRGYVFRVGGEEFALFSSFANEEAALNTAEQIRARFENTTFDIdgl 289
Cdd:PRK10245 242 IDIDHFKSINDTWGHDVGDEAIVALTRQLQITLrGSDVIGRFGGDEFAVIMSGTPAESAITAMSRVHEGLNTLRLPN--- 318

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 639331124 290 AINVT--TSIGVAKFKSTNS-LESFVNQADKQLYKAKQFGRNK 329
Cdd:PRK10245 319 APQVTlrISVGVAPLNPQMShYREWLKSADLALYKAKNAGRNR 361
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 248-323 4.56e-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: 58.00  E-value: 4.56e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 639331124 248 VFRVGGEEFALFSSFANEEAALNTAEQIRARFENTTfdidglAINVTTSIGVAKfkstnslESFVNQADKqLYKAK 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 2.17e-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: 40.80  E-value: 2.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639331124 217 KQVNDEHGHGVGDQVLVEVATLLRVVLGR--GYVFRVGGEEFALFSSFANEEAALNTAEQIRARFENTTFdidGLAINVT 294
Cdd:cd07556   13 TSLADALGPDEGDELLNELAGRFDSLIRRsgDLKIKTIGDEFMVVSGLDHPAAAVAFAEDMREAVSALNQ---SEGNPVR 89


                 ....*.
gi 639331124 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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