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Conserved domains on  [gi|1577374649|ref|WP_130145597|]
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MULTISPECIES: GGDEF domain-containing protein [Acinetobacter]

Protein Classification

GGDEF domain-containing protein( domain architecture ID 10112692)

GGDEF domain-containing protein may function as a diguanylate cyclase and be involved in regulating cell surface adhesion in bacteria

CATH:  3.30.70.1230
Gene Ontology:  GO:0005525|GO:0005886|GO:0007165|GO:0046872|GO:0052621
PubMed:  16166544|17208514|11119645|15569936

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 229-380 1.31e-59

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: 190.08  E-value: 1.31e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577374649 229 RDPLTGLYNRIGFFEKSKALFIDPCA--GHIYVVMCDIDFFKSINDTWGHTAGDQILCRVAALLRESIRQKDIVARFGGE 306
Cdd:cd01949     2 TDPLTGLPNRRAFEERLERLLARARRsgRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGD 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1577374649 307 EFIILFQSTDEASSYYLVERLRSKIEKQLFMNN--IKVTASFGVACM-ANEEDLMNALEMADKRLYSAKNNGRNQIC 380
Cdd:cd01949    82 EFAILLPGTDLEEAEALAERLREAIEEPFFIDGqeIRVTASIGIATYpEDGEDAEELLRRADEALYRAKRSGRNRVV 158
 
Name Accession Description Interval E-value
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 229-380 1.31e-59

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: 190.08  E-value: 1.31e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577374649 229 RDPLTGLYNRIGFFEKSKALFIDPCA--GHIYVVMCDIDFFKSINDTWGHTAGDQILCRVAALLRESIRQKDIVARFGGE 306
Cdd:cd01949     2 TDPLTGLPNRRAFEERLERLLARARRsgRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGD 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1577374649 307 EFIILFQSTDEASSYYLVERLRSKIEKQLFMNN--IKVTASFGVACM-ANEEDLMNALEMADKRLYSAKNNGRNQIC 380
Cdd:cd01949    82 EFAILLPGTDLEEAEALAERLREAIEEPFFIDGqeIRVTASIGIATYpEDGEDAEELLRRADEALYRAKRSGRNRVV 158
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 114-381 4.31e-58

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: 190.19  E-value: 4.31e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577374649 114 FAYVDEQLWFRMITINLIILCLEALALPAVYALYKKSSGLLKLLSFSYFLLFSYALLRTLAVVFFLQNVDRIMLSASSWW 193
Cdd:COG2199     1 VLLLLLLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577374649 194 MLMLAINIVLSLWFTIIVSASTIKEFFTVLNEERIRDPLTGLYNRIGFFEKSKALFIDPCA--GHIYVVMCDIDFFKSIN 271
Cdd:COG2199    81 LELLLLLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARRegRPLALLLIDLDHFKRIN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577374649 272 DTWGHTAGDQILCRVAALLRESIRQKDIVARFGGEEFIILFQSTDEASSYYLVERLRSKIEKQLFM---NNIKVTASFGV 348
Cdd:COG2199   161 DTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFElegKELRVTVSIGV 240

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1577374649 349 ACM-ANEEDLMNALEMADKRLYSAKNNGRNQICF 381
Cdd:COG2199   241 ALYpEDGDSAEELLRRADLALYRAKRAGRNRVVV 274
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 228-378 5.11e-50

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: 165.50  E-value: 5.11e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577374649 228 IRDPLTGLYNRIGFFEK-SKALFIDPCAGH-IYVVMCDIDFFKSINDTWGHTAGDQILCRVAALLRESIRQKDIVARFGG 305
Cdd:pfam00990   2 AHDPLTGLPNRRYFEEQlEQELQRALREGSpVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLGG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577374649 306 EEFIILFQSTDEASSYYLVERLRSKIEKQLF-----MNNIKVTASFGVACMANE----EDLMNAlemADKRLYSAKNNGR 376
Cdd:pfam00990  82 DEFAILLPETSLEGAQELAERIRRLLAKLKIphtvsGLPLYVTISIGIAAYPNDgedpEDLLKR---ADTALYQAKQAGR 158


                  ..
gi 1577374649 377 NQ 378
Cdd:pfam00990 159 NR 160
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 229-381 1.02e-47

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 159.72  E-value: 1.02e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577374649  229 RDPLTGLYNRIGFFEK-SKALFIDPCAGH-IYVVMCDIDFFKSINDTWGHTAGDQILCRVAALLRESIRQKDIVARFGGE 306
Cdd:smart00267   5 RDPLTGLPNRRYFEEElEQELQRAQRQGSpFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARLGGD 84

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1577374649  307 EFIILFQSTDEASSYYLVERLRSKIEKQLFMNNIK--VTASFGVACMANE-EDLMNALEMADKRLYSAKNNGRNQICF 381
Cdd:smart00267  85 EFALLLPETSLEEAIALAERILQQLREPIIIHGIPlyLTISIGVAAYPNPgEDAEDLLKRADTALYQAKKAGRNQVAV 162
PRK15426 PRK15426
cellulose biosynthesis regulator YedQ;
194-382 1.16e-44

cellulose biosynthesis regulator YedQ;


Pssm-ID: 237964 [Multi-domain]  Cd Length: 570  Bit Score: 162.11  E-value: 1.16e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577374649 194 MLMLAINIVLSLWFTIIVSASTIKEFFTV---LNEERIRDPLTGLYNRIGFFEKSKALFIDpCAGH---IYVVMCDIDFF 267
Cdd:PRK15426  362 LTLLWALFTAMLLISWYVIRRMVSNMFVLqssLQWQAWHDPLTRLYNRGALFEKARALAKR-CQRDqqpFSVIQLDLDHF 440

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577374649 268 KSINDTWGHTAGDQILCRVAALLRESIRQKDIVARFGGEEFIILFQSTDEASSYYLVERLRSKIE-KQLFMNN---IKVT 343
Cdd:PRK15426  441 KSINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRVGGEEFCVVLPGASLAEAAQVAERIRLRINeKEILVAKsttIRIS 520

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1577374649 344 ASFGVACMANEEDL-MNALEM-ADKRLYSAKNNGRNQICFE 382
Cdd:PRK15426  521 ASLGVSSAEEDGDYdFEQLQSlADRRLYLAKQAGRNRVCAS 561
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 228-379 9.97e-44

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: 149.41  E-value: 9.97e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577374649 228 IRDPLTGLYNRIGFFEKSKALFiDPCAGH---IYVVMCDIDFFKSINDTWGHTAGDQILCRVAALLRESIRQKDIVARFG 304
Cdd:TIGR00254   3 VRDPLTGLYNRRYLEEMLDSEL-KRARRFqrsFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577374649 305 GEEFIILFQSTDEASSYYLVERLRSKIEKQLFMN----NIKVTASFGVACMANE-EDLMNALEMADKRLYSAKNNGRNQI 379
Cdd:TIGR00254  82 GEEFVVILPGTPLEDALSKAERLRDAINSKPIEVagseTLTVTVSIGVACYPGHgLTLEELLKRADEALYQAKKAGRNRV 161
diguan_SiaD NF038266
biofilm regulation diguanylate cyclase SiaD;
223-379 2.90e-39

biofilm regulation diguanylate cyclase SiaD;


Pssm-ID: 468439 [Multi-domain]  Cd Length: 252  Bit Score: 140.50  E-value: 2.90e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577374649 223 LNEERIRDPLTGLYNR----------IGFFEKSKALFIdpcaghiyVVMCDIDFFKSINDTWGHTAGDQILCRVAALLRE 292
Cdd:NF038266   90 LREASTRDPLTGLPNRrllmerlreeVERARRSGRPFT--------LAMLDVDHFKRINDRYGHEVGDRVLVEIARTLRA 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577374649 293 SIRQKDIVARFGGEEFIILFQSTDEASSYYLVERLRSKIEKQLF---MNNIKVTASFGVACM-ANEEDLMNALEMADKRL 368
Cdd:NF038266  162 ELREYDLCGRWGGEEFLLLLPETGLEEAQVVLERLREAVRALAVrvgDDVLSVTASAGLAEHrPPEEGLSATLSRADQAL 241

                         170
                  ....*....|.
gi 1577374649 369 YSAKNNGRNQI 379
Cdd:NF038266  242 YQAKRAGRDRV 252
diguan_DgcJ NF040885
diguanylate cyclase DgcJ;
223-376 6.91e-17

diguanylate cyclase DgcJ;


Pssm-ID: 468821 [Multi-domain]  Cd Length: 490  Bit Score: 81.93  E-value: 6.91e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577374649 223 LNEERIRDPLTGLYNRI-----------GFFEKSKAlfidpcaghIYVVMCDIDFFKSINDTWGHTAGDQILCRVAALLR 291
Cdd:NF040885  337 VSRENISDSMTGLYNRKiltptleqrlqRLTEKGIP---------VTFIALDCDKLKHINDTLGHHEGDRAITLLAQAIS 407

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577374649 292 ESIRQKDIVARFGGEEFIILFQSTDEASSYYLVERLRSKIekQLFMNNIKVTASFGVACMANEEDLMNALEMADKRLYSA 371
Cdd:NF040885  408 ASIRKSDYGIRLGGDEFCIILIDYEEAEAQNLIERIRQHL--RTIDPDKRVSFSWGAYQMQPGDTLDDAYKAADERLYLN 485


                  ....*
gi 1577374649 372 KNNGR 376
Cdd:NF040885  486 KKQKH 490
 
Name Accession Description Interval E-value
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 229-380 1.31e-59

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: 190.08  E-value: 1.31e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577374649 229 RDPLTGLYNRIGFFEKSKALFIDPCA--GHIYVVMCDIDFFKSINDTWGHTAGDQILCRVAALLRESIRQKDIVARFGGE 306
Cdd:cd01949     2 TDPLTGLPNRRAFEERLERLLARARRsgRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGD 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1577374649 307 EFIILFQSTDEASSYYLVERLRSKIEKQLFMNN--IKVTASFGVACM-ANEEDLMNALEMADKRLYSAKNNGRNQIC 380
Cdd:cd01949    82 EFAILLPGTDLEEAEALAERLREAIEEPFFIDGqeIRVTASIGIATYpEDGEDAEELLRRADEALYRAKRSGRNRVV 158
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 114-381 4.31e-58

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: 190.19  E-value: 4.31e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577374649 114 FAYVDEQLWFRMITINLIILCLEALALPAVYALYKKSSGLLKLLSFSYFLLFSYALLRTLAVVFFLQNVDRIMLSASSWW 193
Cdd:COG2199     1 VLLLLLLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577374649 194 MLMLAINIVLSLWFTIIVSASTIKEFFTVLNEERIRDPLTGLYNRIGFFEKSKALFIDPCA--GHIYVVMCDIDFFKSIN 271
Cdd:COG2199    81 LELLLLLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARRegRPLALLLIDLDHFKRIN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577374649 272 DTWGHTAGDQILCRVAALLRESIRQKDIVARFGGEEFIILFQSTDEASSYYLVERLRSKIEKQLFM---NNIKVTASFGV 348
Cdd:COG2199   161 DTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFElegKELRVTVSIGV 240

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1577374649 349 ACM-ANEEDLMNALEMADKRLYSAKNNGRNQICF 381
Cdd:COG2199   241 ALYpEDGDSAEELLRRADLALYRAKRAGRNRVVV 274
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 228-378 5.11e-50

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: 165.50  E-value: 5.11e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577374649 228 IRDPLTGLYNRIGFFEK-SKALFIDPCAGH-IYVVMCDIDFFKSINDTWGHTAGDQILCRVAALLRESIRQKDIVARFGG 305
Cdd:pfam00990   2 AHDPLTGLPNRRYFEEQlEQELQRALREGSpVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLGG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577374649 306 EEFIILFQSTDEASSYYLVERLRSKIEKQLF-----MNNIKVTASFGVACMANE----EDLMNAlemADKRLYSAKNNGR 376
Cdd:pfam00990  82 DEFAILLPETSLEGAQELAERIRRLLAKLKIphtvsGLPLYVTISIGIAAYPNDgedpEDLLKR---ADTALYQAKQAGR 158


                  ..
gi 1577374649 377 NQ 378
Cdd:pfam00990 159 NR 160
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 229-381 1.02e-47

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 159.72  E-value: 1.02e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577374649  229 RDPLTGLYNRIGFFEK-SKALFIDPCAGH-IYVVMCDIDFFKSINDTWGHTAGDQILCRVAALLRESIRQKDIVARFGGE 306
Cdd:smart00267   5 RDPLTGLPNRRYFEEElEQELQRAQRQGSpFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARLGGD 84

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1577374649  307 EFIILFQSTDEASSYYLVERLRSKIEKQLFMNNIK--VTASFGVACMANE-EDLMNALEMADKRLYSAKNNGRNQICF 381
Cdd:smart00267  85 EFALLLPETSLEEAIALAERILQQLREPIIIHGIPlyLTISIGVAAYPNPgEDAEDLLKRADTALYQAKKAGRNQVAV 162
PRK15426 PRK15426
cellulose biosynthesis regulator YedQ;
194-382 1.16e-44

cellulose biosynthesis regulator YedQ;


Pssm-ID: 237964 [Multi-domain]  Cd Length: 570  Bit Score: 162.11  E-value: 1.16e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577374649 194 MLMLAINIVLSLWFTIIVSASTIKEFFTV---LNEERIRDPLTGLYNRIGFFEKSKALFIDpCAGH---IYVVMCDIDFF 267
Cdd:PRK15426  362 LTLLWALFTAMLLISWYVIRRMVSNMFVLqssLQWQAWHDPLTRLYNRGALFEKARALAKR-CQRDqqpFSVIQLDLDHF 440

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577374649 268 KSINDTWGHTAGDQILCRVAALLRESIRQKDIVARFGGEEFIILFQSTDEASSYYLVERLRSKIE-KQLFMNN---IKVT 343
Cdd:PRK15426  441 KSINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRVGGEEFCVVLPGASLAEAAQVAERIRLRINeKEILVAKsttIRIS 520

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1577374649 344 ASFGVACMANEEDL-MNALEM-ADKRLYSAKNNGRNQICFE 382
Cdd:PRK15426  521 ASLGVSSAEEDGDYdFEQLQSlADRRLYLAKQAGRNRVCAS 561
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 228-379 9.97e-44

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: 149.41  E-value: 9.97e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577374649 228 IRDPLTGLYNRIGFFEKSKALFiDPCAGH---IYVVMCDIDFFKSINDTWGHTAGDQILCRVAALLRESIRQKDIVARFG 304
Cdd:TIGR00254   3 VRDPLTGLYNRRYLEEMLDSEL-KRARRFqrsFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577374649 305 GEEFIILFQSTDEASSYYLVERLRSKIEKQLFMN----NIKVTASFGVACMANE-EDLMNALEMADKRLYSAKNNGRNQI 379
Cdd:TIGR00254  82 GEEFVVILPGTPLEDALSKAERLRDAINSKPIEVagseTLTVTVSIGVACYPGHgLTLEELLKRADEALYQAKKAGRNRV 161
pleD PRK09581
response regulator PleD; Reviewed
 228-380 7.05e-43

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 155.06  E-value: 7.05e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577374649 228 IRDPLTGLYNRiGFFEKSKALFIDPCAGH---IYVVMCDIDFFKSINDTWGHTAGDQILCRVAALLRESIRQKDIVARFG 304
Cdd:PRK09581  293 VTDGLTGLHNR-RYFDMHLKNLIERANERgkpLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARYG 371

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577374649 305 GEEFIILFQSTDEASSYYLVERLRSKIEKQLFM-----NNIKVTASFGVACMANEEDLMNAL-EMADKRLYSAKNNGRNQ 378
Cdd:PRK09581  372 GEEFVVVMPDTDIEDAIAVAERIRRKIAEEPFIisdgkERLNVTVSIGVAELRPSGDTIEALiKRADKALYEAKNTGRNR 451


                  ..
gi 1577374649 379 IC 380
Cdd:PRK09581  452 VV 453
diguan_SiaD NF038266
biofilm regulation diguanylate cyclase SiaD;
223-379 2.90e-39

biofilm regulation diguanylate cyclase SiaD;


Pssm-ID: 468439 [Multi-domain]  Cd Length: 252  Bit Score: 140.50  E-value: 2.90e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577374649 223 LNEERIRDPLTGLYNR----------IGFFEKSKALFIdpcaghiyVVMCDIDFFKSINDTWGHTAGDQILCRVAALLRE 292
Cdd:NF038266   90 LREASTRDPLTGLPNRrllmerlreeVERARRSGRPFT--------LAMLDVDHFKRINDRYGHEVGDRVLVEIARTLRA 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577374649 293 SIRQKDIVARFGGEEFIILFQSTDEASSYYLVERLRSKIEKQLF---MNNIKVTASFGVACM-ANEEDLMNALEMADKRL 368
Cdd:NF038266  162 ELREYDLCGRWGGEEFLLLLPETGLEEAQVVLERLREAVRALAVrvgDDVLSVTASAGLAEHrPPEEGLSATLSRADQAL 241

                         170
                  ....*....|.
gi 1577374649 369 YSAKNNGRNQI 379
Cdd:NF038266  242 YQAKRAGRDRV 252
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 98-381 1.58e-37

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: 143.38  E-value: 1.58e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577374649  98 ILSAAVVALGLMFLFYFAYVDEQLWFRMITINLIILCLEALALPAVYALYKKSSGLLKLLSFSYFLLFSYALLRTLAVVF 177
Cdd:COG5001   115 LLAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARALLALLLLLLLALLLLLLLLLLLALLLLLLLALLL 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577374649 178 FLQNVDRIMLSASSWWMLMLAINIVLSLWFTIIVSASTIKEFFTVL--NEERIR-----DPLTGLYNRIGFFEKSKALFI 250
Cdd:COG5001   195 RLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERkrAEERLRhlayhDPLTGLPNRRLFLDRLEQALA 274

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577374649 251 DPCA--GHIYVVMCDIDFFKSINDTWGHTAGDQILCRVAALLRESIRQKDIVARFGGEEFIILF---QSTDEASSyyLVE 325
Cdd:COG5001   275 RARRsgRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVLLpdlDDPEDAEA--VAE 352

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1577374649 326 RLRSKIEKQLFMNN--IKVTASFGVACM----ANEEDLMNALEMAdkrLYSAKNNGRNQICF 381
Cdd:COG5001   353 RILAALAEPFELDGheLYVSASIGIALYpddgADAEELLRNADLA---MYRAKAAGRNRYRF 411
PRK09894 PRK09894
diguanylate cyclase; Provisional
 229-381 1.04e-35

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 132.11  E-value: 1.04e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577374649 229 RDPLTGLYNRIGFFEKSKALFIDPCAGHIYVVMCDIDFFKSINDTWGHTAGDQILCRVAALLRESIRQKDIVARFGGEEF 308
Cdd:PRK09894  131 MDVLTGLPGRRVLDESFDHQLRNREPQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGGEEF 210

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1577374649 309 IILFQSTDEASSYYLVERLRSKIEKQLFM---NNIKVTASFGVACMANEEDLMNALEMADKRLYSAKNNGRNQICF 381
Cdd:PRK09894  211 IICLKAATDEEACRAGERIRQLIANHAIThsdGRINITATFGVSRAFPEETLDVVIGRADRAMYEGKQTGRNRVMF 286
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
225-380 2.45e-21

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 95.90  E-value: 2.45e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577374649 225 EERIR-----DPLTGLYNRIGFFEKSKALFIDPCAGHIYVVMCDIDFFKSINDTWGHTAGDQILCRVAALLRESIRQKDI 299
Cdd:PRK10060  230 QERLRilantDSITGLPNRNAIQELIDHAINAADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQT 309

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577374649 300 VARFGGEEFIILFQSTD----EASSYYLVERLRSKIEKQLfmnnIKV--TASFGVAcMANE--EDLMNALEMADKRLYSA 371
Cdd:PRK10060  310 LARLGGDEFLVLASHTSqaalEAMASRILTRLRLPFRIGL----IEVytGCSIGIA-LAPEhgDDSESLIRSADTAMYTA 384


                  ....*....
gi 1577374649 372 KNNGRNQIC 380
Cdd:PRK10060  385 KEGGRGQFC 393
adrA PRK10245
diguanylate cyclase AdrA; Provisional
 185-378 6.33e-19

diguanylate cyclase AdrA; Provisional


Pssm-ID: 182329 [Multi-domain]  Cd Length: 366  Bit Score: 87.19  E-value: 6.33e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577374649 185 IMLSASSWWMLMLAINIVLSLWFTIIVSASTIK--EFFTVLNEERIRDPLTGLYNRiGFFEKSKALFIDPCAGH---IYV 259
Cdd:PRK10245  161 SFNSAPLEWWLSLPVIVIYPLLFAWVSYQTATKlaEHKRRLQVMSTRDGMTGVYNR-RHWETLLRNEFDNCRRHhrdATL 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577374649 260 VMCDIDFFKSINDTWGHTAGDQILCRVAALLRESIRQKDIVARFGGEEFIILFQSTDEASSYYLVERLRSKIEKQLFMN- 338
Cdd:PRK10245  240 LIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSDVIGRFGGDEFAVIMSGTPAESAITAMSRVHEGLNTLRLPNa 319

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1577374649 339 -NIKVTASFGVACMANE-EDLMNALEMADKRLYSAKNNGRNQ 378
Cdd:PRK10245  320 pQVTLRISVGVAPLNPQmSHYREWLKSADLALYKAKNAGRNR 361
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 230-379 1.66e-18

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 87.42  E-value: 1.66e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577374649  230 DPLTGLYNRIGFFEKSKALFIDPCAGHIYVVMC--DIDFFKSINDTWGHTAGDQILCRVAALLRESIRQKDIVARFGGEE 307
Cdd:PRK09776   668 DALTHLANRASFEKQLRRLLQTVNSTHQRHALVfiDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSDVLARLGGDE 747

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1577374649  308 FIILFQSTDEASSYYLVERLRSKIEKQLFM---NNIKVTASFGVACMANE----EDLMNaleMADKRLYSAKNNGRNQI 379
Cdd:PRK09776   748 FGLLLPDCNVESARFIATRIISAINDYHFPwegRVYRVGASAGITLIDANnhqaSEVMS---QADIACYAAKNAGRGRV 823
diguan_DgcJ NF040885
diguanylate cyclase DgcJ;
223-376 6.91e-17

diguanylate cyclase DgcJ;


Pssm-ID: 468821 [Multi-domain]  Cd Length: 490  Bit Score: 81.93  E-value: 6.91e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577374649 223 LNEERIRDPLTGLYNRI-----------GFFEKSKAlfidpcaghIYVVMCDIDFFKSINDTWGHTAGDQILCRVAALLR 291
Cdd:NF040885  337 VSRENISDSMTGLYNRKiltptleqrlqRLTEKGIP---------VTFIALDCDKLKHINDTLGHHEGDRAITLLAQAIS 407

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577374649 292 ESIRQKDIVARFGGEEFIILFQSTDEASSYYLVERLRSKIekQLFMNNIKVTASFGVACMANEEDLMNALEMADKRLYSA 371
Cdd:NF040885  408 ASIRKSDYGIRLGGDEFCIILIDYEEAEAQNLIERIRQHL--RTIDPDKRVSFSWGAYQMQPGDTLDDAYKAADERLYLN 485


                  ....*
gi 1577374649 372 KNNGR 376
Cdd:NF040885  486 KKQKH 490
PRK09966 PRK09966
diguanylate cyclase DgcN;
228-373 4.74e-15

diguanylate cyclase DgcN;


Pssm-ID: 182171 [Multi-domain]  Cd Length: 407  Bit Score: 76.20  E-value: 4.74e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577374649 228 IRDPLTGLYNRIGFFEKSKALFIDPCAGHIYVVM-CDIDFFKSINDTWGHTAGDQILCRVAALLRESIRQKDIVARFGGE 306
Cdd:PRK09966  249 LHDPLTGLANRAAFRSGINTLMNNSDARKTSALLfLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHKAYRLGGD 328

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1577374649 307 EF-IILFQSTDEASSYYLVERLRSKIEKQLFMNN---IKVTASFGVACM---ANEEDLMnalEMADKRLYSAKN 373
Cdd:PRK09966  329 EFaMVLYDVQSESEVQQICSALTQIFNLPFDLHNghqTTMTLSIGYAMTiehASAEKLQ---ELADHNMYQAKH 399
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
 259-374 5.56e-12

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: 62.76  E-value: 5.56e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577374649 259 VVMCDIDFFKSINDTWGHTAGDQILCRVAALLRESIRQK-DIVARFGGEEFIILFQSTDEASSYYLVERLRSKIEKQLFM 337
Cdd:cd07556     4 ILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSgDLKIKTIGDEFMVVSGLDHPAAAVAFAEDMREAVSALNQS 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1577374649 338 NNIKVTASFGVACMANEEDLM----------NALEMADKRLYSAKNN 374
Cdd:cd07556    84 EGNPVRVRIGIHTGPVVVGVIgsrpqydvwgALVNLASRMESQAKAG 130
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 298-372 4.19e-11

Two-component response regulator, PleD family, consists of two REC domains and a diguanylate cyclase (GGDEF) domain [Signal transduction mechanisms, Transcription];


Pssm-ID: 442920 [Multi-domain]  Cd Length: 179  Bit Score: 61.08  E-value: 4.19e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1577374649 298 DIVARFGGEEFIILFQSTDEASSYYLVERLRSKIEKqlfMNNIKVTASFGVAcmanEEDLMNAlemADkRLYSAK 372
Cdd:COG3706   116 DLVARYGGEEFAILLPGTDLEGALAVAERIREAVAE---LPSLRVTVSIGVA----GDSLLKR---AD-ALYQAR 179
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 230-375 5.55e-10

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 60.94  E-value: 5.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577374649 230 DPLTGLYNRiGFFEKSKALFIDPcAGHIYVVMCDIDFFKSINDTWGHTAGDQILCRVAALLRESIRQKDIVARFGGEEFI 309
Cdd:PRK11359  379 DPLTGLPNR-NNLHNYLDDLVDK-AVSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGTQFV 456

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577374649 310 ILFQSTDEASSYYLVERLRSKIEKQLFMNN--IKVTASFGVACMA--NEEDLMNALEMADKRLYSAKNNG 375
Cdd:PRK11359  457 LVSLENDVSNITQIADELRNVVSKPIMIDDkpFPLTLSIGISYDVgkNRDYLLSTAHNAMDYIRKNGGNG 526
PRK11829 PRK11829
biofilm formation regulator HmsP; Provisional
 256-381 5.50e-05

biofilm formation regulator HmsP; Provisional


Pssm-ID: 183329 [Multi-domain]  Cd Length: 660  Bit Score: 45.32  E-value: 5.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577374649 256 HIYVVMCDIDFFKSINDTWGHTAGDQILCRVAALLRESIRQKDIVARFGGEEFIILFQSTDEAS-SYYLVERLRSKIEKQ 334
Cdd:PRK11829  262 HFHLLVIGIETLQEVSGAMSEAQHQQLLLTIVQRIEQCIDDSDLLAQLSKTEFAVLARGTRRSFpAMQLARRIMSQVTQP 341

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1577374649 335 LFMNNIKV--TASFGVA-CMANEEDLMNALEMADKRLYSAKNNGRNQICF 381
Cdd:PRK11829  342 LFFDEITLrpSASIGITrYQAQQDTAESMMRNASTAMMAAHHEGRNQIMV 391
 
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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