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Conserved domains on  [gi|654156648|ref|WP_027726765|]
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GGDEF domain-containing protein [Vibrio owensii]

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: ...
 239-409 3.51e-48

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: 161.57  E-value: 3.51e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654156648 239 FTDSLTLIPSRRALDLELKHM-------GRKFTIAMLDVDHFKKFNDTYGHDTGDDVLKMVASRLMKT-QGGAKVYRFGG 310
Cdd:cd01949    1 YTDPLTGLPNRRAFEERLERLlararrsGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSlRESDLVARLGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654156648 311 EEFTIVFKGKYTEDCEAHLEEVRELIAQYEMILrdqdtrpddnkqgrkkrgsadskKKTVSVTASFGVADSRS-ARNPAD 389
Cdd:cd01949   81 DEFAILLPGTDLEEAEALAERLREAIEEPFFID-----------------------GQEIRVTASIGIATYPEdGEDAEE 137

                        170       180
                 ....*....|....*....|
gi 654156648 390 VIKLADEALYKAKKAGRNCV 409
Cdd:cd01949  138 LLRRADEALYRAKRSGRNRV 157
 
Name Accession Description Interval E-value
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 239-409 3.51e-48

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: 161.57  E-value: 3.51e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654156648 239 FTDSLTLIPSRRALDLELKHM-------GRKFTIAMLDVDHFKKFNDTYGHDTGDDVLKMVASRLMKT-QGGAKVYRFGG 310
Cdd:cd01949    1 YTDPLTGLPNRRAFEERLERLlararrsGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSlRESDLVARLGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654156648 311 EEFTIVFKGKYTEDCEAHLEEVRELIAQYEMILrdqdtrpddnkqgrkkrgsadskKKTVSVTASFGVADSRS-ARNPAD 389
Cdd:cd01949   81 DEFAILLPGTDLEEAEALAERLREAIEEPFFID-----------------------GQEIRVTASIGIATYPEdGEDAEE 137

                        170       180
                 ....*....|....*....|
gi 654156648 390 VIKLADEALYKAKKAGRNCV 409
Cdd:cd01949  138 LLRRADEALYRAKRSGRNRV 157
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 129-409 6.15e-48

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: 164.77  E-value: 6.15e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654156648 129 LIMFVFWSYVTLTYYVEGGFDEWTNGILFIVPTLSKLPLVLVLYCIGIVCFLGILVLKKNKIIHAMTYSAMVLASATFIF 208
Cdd:COG2199    5 LLLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654156648 209 FDVQYISSTMFTLTGLLIIIYSTSASHQLAFTDSLTLIPSRRALDLELKHM-------GRKFTIAMLDVDHFKKFNDTYG 281
Cdd:COG2199   85 LLLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERElararreGRPLALLLIDLDHFKRINDTYG 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654156648 282 HDTGDDVLKMVASRLMKT-QGGAKVYRFGGEEFTIVFKGKYTEDCEAHLEEVRELIAQYEMILRDQdtrpddnkqgrkkr 360
Cdd:COG2199  165 HAAGDEVLKEVARRLRASlRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELEGK-------------- 230

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 654156648 361 gsadskkkTVSVTASFGVAD-SRSARNPADVIKLADEALYKAKKAGRNCV 409
Cdd:COG2199  231 --------ELRVTVSIGVALyPEDGDSAEELLRRADLALYRAKRAGRNRV 272
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 238-408 4.29e-43

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: 148.17  E-value: 4.29e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654156648  238 AFTDSLTLIPSRRALDLELKHM-------GRKFTIAMLDVDHFKKFNDTYGHDTGDDVLKMVASRLMKT-QGGAKVYRFG 309
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQElqralreGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSlRRSDLVARLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654156648  310 GEEFTIVFKGKYTEDCEAHLEEVRELIAQYEMILRDQDTrpddnkqgrkkrgsadskkkTVSVTASFGVADS-RSARNPA 388
Cdd:pfam00990  81 GDEFAILLPETSLEGAQELAERIRRLLAKLKIPHTVSGL--------------------PLYVTISIGIAAYpNDGEDPE 140

                         170       180
                  ....*....|....*....|
gi 654156648  389 DVIKLADEALYKAKKAGRNC 408
Cdd:pfam00990 141 DLLKRADTALYQAKQAGRNR 160
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 236-409 3.67e-41

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 143.16  E-value: 3.67e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654156648   236 QLAFTDSLTLIPSRRALDLELKH-------MGRKFTIAMLDVDHFKKFNDTYGHDTGDDVLKMVASRLMKT-QGGAKVYR 307
Cdd:smart00267   1 RLAFRDPLTGLPNRRYFEEELEQelqraqrQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSClRPGDLLAR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654156648   308 FGGEEFTIVFKGKYTEDCEAHLEEVRELIAQYEMILRdqdtrpddnkqgrkkrgsadskkKTVSVTASFGVA-DSRSARN 386
Cdd:smart00267  81 LGGDEFALLLPETSLEEAIALAERILQQLREPIIIHG-----------------------IPLYLTISIGVAaYPNPGED 137

                          170       180
                   ....*....|....*....|...
gi 654156648   387 PADVIKLADEALYKAKKAGRNCV 409
Cdd:smart00267 138 AEDLLKRADTALYQAKKAGRNQV 160
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 237-411 1.82e-38

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: 136.31  E-value: 1.82e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654156648  237 LAFTDSLTLIPSRRA----LDLELKHM---GRKFTIAMLDVDHFKKFNDTYGHDTGDDVLKMVASRLMKTQGGAKVY-RF 308
Cdd:TIGR00254   1 QAVRDPLTGLYNRRYleemLDSELKRArrfQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVgRY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654156648  309 GGEEFTIVFKGKYTEDCEAHLEEVRELIAQYEMILrdqdtrpddnkqgrkkrgsadSKKKTVSVTASFGVADSRS-ARNP 387
Cdd:TIGR00254  81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPIEV---------------------AGSETLTVTVSIGVACYPGhGLTL 139

                         170       180
                  ....*....|....*....|....
gi 654156648  388 ADVIKLADEALYKAKKAGRNCVKY 411
Cdd:TIGR00254 140 EELLKRADEALYQAKKAGRNRVVV 163
PRK09894 PRK09894
diguanylate cyclase; Provisional
 241-409 4.52e-37

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 136.74  E-value: 4.52e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654156648 241 DSLTLIPSRRALDLELKHM-----GRKFTIAMLDVDHFKKFNDTYGHDTGDDVLKMVASRLMK-TQGGAKVYRFGGEEFT 314
Cdd:PRK09894 132 DVLTGLPGRRVLDESFDHQlrnrePQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASwTRDYETVYRYGGEEFI 211

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654156648 315 IVFKGKYTEDCEAHLEEVRELIAQYEMILRDqdtrpddnkqGRkkrgsadskkktVSVTASFGVADSRSARNPADVIKLA 394
Cdd:PRK09894 212 ICLKAATDEEACRAGERIRQLIANHAITHSD----------GR------------INITATFGVSRAFPEETLDVVIGRA 269

                        170
                 ....*....|....*
gi 654156648 395 DEALYKAKKAGRNCV 409
Cdd:PRK09894 270 DRAMYEGKQTGRNRV 284
diguan_SiaD NF038266
biofilm regulation diguanylate cyclase SiaD;
235-409 9.12e-35

biofilm regulation diguanylate cyclase SiaD;


Pssm-ID: 468439 [Multi-domain]  Cd Length: 252  Bit Score: 129.33  E-value: 9.12e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654156648 235 HQLAFTDSLTLIPSRRALDLELK-------HMGRKFTIAMLDVDHFKKFNDTYGHDTGDDVLKMVASRLmktQGGAKVY- 306
Cdd:NF038266  91 REASTRDPLTGLPNRRLLMERLReeverarRSGRPFTLAMLDVDHFKRINDRYGHEVGDRVLVEIARTL---RAELREYd 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654156648 307 ---RFGGEEFTIVFKGKYTEDCEAHLEEVRELIaqyemilRDQDTRPDDnkqgrkkrgsadskkKTVSVTASFGVADSR- 382
Cdd:NF038266 168 lcgRWGGEEFLLLLPETGLEEAQVVLERLREAV-------RALAVRVGD---------------DVLSVTASAGLAEHRp 225

                        170       180
                 ....*....|....*....|....*..
gi 654156648 383 SARNPADVIKLADEALYKAKKAGRNCV 409
Cdd:NF038266 226 PEEGLSATLSRADQALYQAKRAGRDRV 252
 
Name Accession Description Interval E-value
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 239-409 3.51e-48

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: 161.57  E-value: 3.51e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654156648 239 FTDSLTLIPSRRALDLELKHM-------GRKFTIAMLDVDHFKKFNDTYGHDTGDDVLKMVASRLMKT-QGGAKVYRFGG 310
Cdd:cd01949    1 YTDPLTGLPNRRAFEERLERLlararrsGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSlRESDLVARLGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654156648 311 EEFTIVFKGKYTEDCEAHLEEVRELIAQYEMILrdqdtrpddnkqgrkkrgsadskKKTVSVTASFGVADSRS-ARNPAD 389
Cdd:cd01949   81 DEFAILLPGTDLEEAEALAERLREAIEEPFFID-----------------------GQEIRVTASIGIATYPEdGEDAEE 137

                        170       180
                 ....*....|....*....|
gi 654156648 390 VIKLADEALYKAKKAGRNCV 409
Cdd:cd01949  138 LLRRADEALYRAKRSGRNRV 157
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 129-409 6.15e-48

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: 164.77  E-value: 6.15e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654156648 129 LIMFVFWSYVTLTYYVEGGFDEWTNGILFIVPTLSKLPLVLVLYCIGIVCFLGILVLKKNKIIHAMTYSAMVLASATFIF 208
Cdd:COG2199    5 LLLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654156648 209 FDVQYISSTMFTLTGLLIIIYSTSASHQLAFTDSLTLIPSRRALDLELKHM-------GRKFTIAMLDVDHFKKFNDTYG 281
Cdd:COG2199   85 LLLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERElararreGRPLALLLIDLDHFKRINDTYG 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654156648 282 HDTGDDVLKMVASRLMKT-QGGAKVYRFGGEEFTIVFKGKYTEDCEAHLEEVRELIAQYEMILRDQdtrpddnkqgrkkr 360
Cdd:COG2199  165 HAAGDEVLKEVARRLRASlRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELEGK-------------- 230

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 654156648 361 gsadskkkTVSVTASFGVAD-SRSARNPADVIKLADEALYKAKKAGRNCV 409
Cdd:COG2199  231 --------ELRVTVSIGVALyPEDGDSAEELLRRADLALYRAKRAGRNRV 272
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 238-408 4.29e-43

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: 148.17  E-value: 4.29e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654156648  238 AFTDSLTLIPSRRALDLELKHM-------GRKFTIAMLDVDHFKKFNDTYGHDTGDDVLKMVASRLMKT-QGGAKVYRFG 309
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQElqralreGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSlRRSDLVARLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654156648  310 GEEFTIVFKGKYTEDCEAHLEEVRELIAQYEMILRDQDTrpddnkqgrkkrgsadskkkTVSVTASFGVADS-RSARNPA 388
Cdd:pfam00990  81 GDEFAILLPETSLEGAQELAERIRRLLAKLKIPHTVSGL--------------------PLYVTISIGIAAYpNDGEDPE 140

                         170       180
                  ....*....|....*....|
gi 654156648  389 DVIKLADEALYKAKKAGRNC 408
Cdd:pfam00990 141 DLLKRADTALYQAKQAGRNR 160
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 236-409 3.67e-41

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 143.16  E-value: 3.67e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654156648   236 QLAFTDSLTLIPSRRALDLELKH-------MGRKFTIAMLDVDHFKKFNDTYGHDTGDDVLKMVASRLMKT-QGGAKVYR 307
Cdd:smart00267   1 RLAFRDPLTGLPNRRYFEEELEQelqraqrQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSClRPGDLLAR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654156648   308 FGGEEFTIVFKGKYTEDCEAHLEEVRELIAQYEMILRdqdtrpddnkqgrkkrgsadskkKTVSVTASFGVA-DSRSARN 386
Cdd:smart00267  81 LGGDEFALLLPETSLEEAIALAERILQQLREPIIIHG-----------------------IPLYLTISIGVAaYPNPGED 137

                          170       180
                   ....*....|....*....|...
gi 654156648   387 PADVIKLADEALYKAKKAGRNCV 409
Cdd:smart00267 138 AEDLLKRADTALYQAKKAGRNQV 160
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 237-411 1.82e-38

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: 136.31  E-value: 1.82e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654156648  237 LAFTDSLTLIPSRRA----LDLELKHM---GRKFTIAMLDVDHFKKFNDTYGHDTGDDVLKMVASRLMKTQGGAKVY-RF 308
Cdd:TIGR00254   1 QAVRDPLTGLYNRRYleemLDSELKRArrfQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVgRY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654156648  309 GGEEFTIVFKGKYTEDCEAHLEEVRELIAQYEMILrdqdtrpddnkqgrkkrgsadSKKKTVSVTASFGVADSRS-ARNP 387
Cdd:TIGR00254  81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPIEV---------------------AGSETLTVTVSIGVACYPGhGLTL 139

                         170       180
                  ....*....|....*....|....
gi 654156648  388 ADVIKLADEALYKAKKAGRNCVKY 411
Cdd:TIGR00254 140 EELLKRADEALYQAKKAGRNRVVV 163
PRK09894 PRK09894
diguanylate cyclase; Provisional
 241-409 4.52e-37

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 136.74  E-value: 4.52e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654156648 241 DSLTLIPSRRALDLELKHM-----GRKFTIAMLDVDHFKKFNDTYGHDTGDDVLKMVASRLMK-TQGGAKVYRFGGEEFT 314
Cdd:PRK09894 132 DVLTGLPGRRVLDESFDHQlrnrePQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASwTRDYETVYRYGGEEFI 211

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654156648 315 IVFKGKYTEDCEAHLEEVRELIAQYEMILRDqdtrpddnkqGRkkrgsadskkktVSVTASFGVADSRSARNPADVIKLA 394
Cdd:PRK09894 212 ICLKAATDEEACRAGERIRQLIANHAITHSD----------GR------------INITATFGVSRAFPEETLDVVIGRA 269

                        170
                 ....*....|....*
gi 654156648 395 DEALYKAKKAGRNCV 409
Cdd:PRK09894 270 DRAMYEGKQTGRNRV 284
pleD PRK09581
response regulator PleD; Reviewed
 237-409 8.61e-36

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 136.57  E-value: 8.61e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654156648 237 LAFTDSLTLIPSRRALDLELKHM-------GRKFTIAMLDVDHFKKFNDTYGHDTGDDVLKMVASRLMKTQGGAK-VYRF 308
Cdd:PRK09581 291 MAVTDGLTGLHNRRYFDMHLKNLieranerGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDlIARY 370

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654156648 309 GGEEFTIVFKGKYTEDCEAHLEEVRELIAQYEMILRDQDTRpddnkqgrkkrgsadskkktVSVTASFGVADSR-SARNP 387
Cdd:PRK09581 371 GGEEFVVVMPDTDIEDAIAVAERIRRKIAEEPFIISDGKER--------------------LNVTVSIGVAELRpSGDTI 430

                        170       180
                 ....*....|....*....|..
gi 654156648 388 ADVIKLADEALYKAKKAGRNCV 409
Cdd:PRK09581 431 EALIKRADKALYEAKNTGRNRV 452
diguan_SiaD NF038266
biofilm regulation diguanylate cyclase SiaD;
235-409 9.12e-35

biofilm regulation diguanylate cyclase SiaD;


Pssm-ID: 468439 [Multi-domain]  Cd Length: 252  Bit Score: 129.33  E-value: 9.12e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654156648 235 HQLAFTDSLTLIPSRRALDLELK-------HMGRKFTIAMLDVDHFKKFNDTYGHDTGDDVLKMVASRLmktQGGAKVY- 306
Cdd:NF038266  91 REASTRDPLTGLPNRRLLMERLReeverarRSGRPFTLAMLDVDHFKRINDRYGHEVGDRVLVEIARTL---RAELREYd 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654156648 307 ---RFGGEEFTIVFKGKYTEDCEAHLEEVRELIaqyemilRDQDTRPDDnkqgrkkrgsadskkKTVSVTASFGVADSR- 382
Cdd:NF038266 168 lcgRWGGEEFLLLLPETGLEEAQVVLERLREAV-------RALAVRVGD---------------DVLSVTASAGLAEHRp 225

                        170       180
                 ....*....|....*....|....*..
gi 654156648 383 SARNPADVIKLADEALYKAKKAGRNCV 409
Cdd:NF038266 226 PEEGLSATLSRADQALYQAKRAGRDRV 252
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 235-409 1.98e-33

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: 132.21  E-value: 1.98e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654156648 235 HQLAFTDSLTLIPSRRALDLELKHM-------GRKFTIAMLDVDHFKKFNDTYGHDTGDDVLKMVASRLMKT-QGGAKVY 306
Cdd:COG5001  248 RHLAYHDPLTGLPNRRLFLDRLEQAlararrsGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRAClREGDTVA 327

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654156648 307 RFGGEEFTIVFKG-KYTEDCEAHLEEVRELIAQyEMILRDQdtrpddnkqgrkkrgsadskkkTVSVTASFGVA-DSRSA 384
Cdd:COG5001  328 RLGGDEFAVLLPDlDDPEDAEAVAERILAALAE-PFELDGH----------------------ELYVSASIGIAlYPDDG 384

                        170       180
                 ....*....|....*....|....*
gi 654156648 385 RNPADVIKLADEALYKAKKAGRNCV 409
Cdd:COG5001  385 ADAEELLRNADLAMYRAKAAGRNRY 409
PRK15426 PRK15426
cellulose biosynthesis regulator YedQ;
236-409 1.83e-21

cellulose biosynthesis regulator YedQ;


Pssm-ID: 237964 [Multi-domain]  Cd Length: 570  Bit Score: 96.62  E-value: 1.83e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654156648 236 QLAFTDSLTLIPSRRALDLELKHM-------GRKFTIAMLDVDHFKKFNDTYGHDTGDDVLKMVASRLMKT-----QGGa 303
Cdd:PRK15426 396 WQAWHDPLTRLYNRGALFEKARALakrcqrdQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSlraqdVAG- 474

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654156648 304 kvyRFGGEEFTIVFKGKYTEDCEAHLEEVRELIAQYEMILRdqdtrpddnkqgrkkrgsadsKKKTVSVTASFGVAdsrS 383
Cdd:PRK15426 475 ---RVGGEEFCVVLPGASLAEAAQVAERIRLRINEKEILVA---------------------KSTTIRISASLGVS---S 527

                        170       180       190
                 ....*....|....*....|....*....|.
gi 654156648 384 ARNPAD-----VIKLADEALYKAKKAGRNCV 409
Cdd:PRK15426 528 AEEDGDydfeqLQSLADRRLYLAKQAGRNRV 558
adrA PRK10245
diguanylate cyclase AdrA; Provisional
 261-407 3.00e-15

diguanylate cyclase AdrA; Provisional


Pssm-ID: 182329 [Multi-domain]  Cd Length: 366  Bit Score: 76.41  E-value: 3.00e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654156648 261 RKFTIAMLDVDHFKKFNDTYGHDTGDDVLKMVASRL-MKTQGGAKVYRFGGEEFTIVFKGKYTEDCEAHLEEVRELIAQY 339
Cdd:PRK10245 235 RDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLqITLRGSDVIGRFGGDEFAVIMSGTPAESAITAMSRVHEGLNTL 314

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 654156648 340 EMILRDQdtrpddnkqgrkkrgsadskkktVSVTASFGVAD-SRSARNPADVIKLADEALYKAKKAGRN 407
Cdd:PRK10245 315 RLPNAPQ-----------------------VTLRISVGVAPlNPQMSHYREWLKSADLALYKAKNAGRN 360
PRK09966 PRK09966
diguanylate cyclase DgcN;
268-402 1.91e-11

diguanylate cyclase DgcN;


Pssm-ID: 182171 [Multi-domain]  Cd Length: 407  Bit Score: 65.41  E-value: 1.91e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654156648 268 LDVDHFKKFNDTYGHDTGDDVLKMVASRLMKTQGGA-KVYRFGGEEFTIVFKGKYTEdceahlEEVRELIAQYEMILrdq 346
Cdd:PRK09966 284 LDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRhKAYRLGGDEFAMVLYDVQSE------SEVQQICSALTQIF--- 354

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 654156648 347 dTRPDDNKQGRKkrgsadskkktVSVTASFGVADSRSARNPADVIKLADEALYKAK 402
Cdd:PRK09966 355 -NLPFDLHNGHQ-----------TTMTLSIGYAMTIEHASAEKLQELADHNMYQAK 398
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 200-410 8.45e-11

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 63.92  E-value: 8.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654156648  200 VLASATFIFFDVQYISSTMFTLTG-----LLIII-----------YSTSASHqlaftDSLTLIPSRRALDLELKHM---- 259
Cdd:PRK09776  616 VLHCRSGGSYDVHYSITPLSTLDGenigsVLVIQdvtesrkmlrqLSYSASH-----DALTHLANRASFEKQLRRLlqtv 690

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654156648  260 ---GRKFTIAMLDVDHFKKFNDTYGHDTGDDVLKMVaSRLMK--TQGGAKVYRFGGEEFTIVFKGKYTEDCEAHLEEVRE 334
Cdd:PRK09776  691 nstHQRHALVFIDLDRFKAVNDSAGHAAGDALLREL-ASLMLsmLRSSDVLARLGGDEFGLLLPDCNVESARFIATRIIS 769

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654156648  335 LIAQYEMILrdqdtrpddnkQGRKKRgsadskkktvsVTASFGV----ADSRSArnpADVIKLADEALYKAKKAGRNCVK 410
Cdd:PRK09776  770 AINDYHFPW-----------EGRVYR-----------VGASAGItlidANNHQA---SEVMSQADIACYAAKNAGRGRVT 824
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
236-317 1.83e-10

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 62.78  E-value: 1.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654156648 236 QLAFTDSLTLIPSRRALDLELKH-----MGRKFTIAMLDVDHFKKFNDTYGHDTGDDVLKMVASRLMKT-QGGAKVYRFG 309
Cdd:PRK10060 235 ILANTDSITGLPNRNAIQELIDHainaaDNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSClEEDQTLARLG 314


                 ....*...
gi 654156648 310 GEEFTIVF 317
Cdd:PRK10060 315 GDEFLVLA 322
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 236-407 5.34e-08

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 55.16  E-value: 5.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654156648 236 QLAFTDSLTLIPSR----RALDlELKHMGRKFTIAMLDVDHFKKFNDTYGHDTGDDVLKMVASRLM-KTQGGAKVYRFGG 310
Cdd:PRK11359 374 QLIQFDPLTGLPNRnnlhNYLD-DLVDKAVSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFReKLKPDQYLCRIEG 452

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654156648 311 EEFTIVfkgkyTEDCEAH-----LEEVRELIAQYEMIlrdqdtrpDDnkqgrkkrgsadskkKTVSVTASFGVADSrSAR 385
Cdd:PRK11359 453 TQFVLV-----SLENDVSnitqiADELRNVVSKPIMI--------DD---------------KPFPLTLSIGISYD-VGK 503

                        170       180
                 ....*....|....*....|..
gi 654156648 386 NPADVIKLADEALYKAKKAGRN 407
Cdd:PRK11359 504 NRDYLLSTAHNAMDYIRKNGGN 525
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
 264-338 7.64e-08

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: 50.82  E-value: 7.64e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 654156648 264 TIAMLDVDHFKKFNDTYGHDTGDDVLKMVASRLMK--TQGGAKVYRFGGEEFTIVFKGKYTEDCEAHLEEVRELIAQ 338
Cdd:cd07556    3 TILFADIVGFTSLADALGPDEGDELLNELAGRFDSliRRSGDLKIKTIGDEFMVVSGLDHPAAAVAFAEDMREAVSA 79
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 305-402 7.40e-07

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: 49.14  E-value: 7.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654156648 305 VYRFGGEEFTIVFKGKYTEDCEAHLEEVRELIAQYEmilrdqdtrpddnkqgrkkrgsadskkkTVSVTASFGVADSrsa 384
Cdd:COG3706  118 VARYGGEEFAILLPGTDLEGALAVAERIREAVAELP----------------------------SLRVTVSIGVAGD--- 166

                         90
                 ....*....|....*...
gi 654156648 385 rnpaDVIKLADeALYKAK 402
Cdd:COG3706  167 ----SLLKRAD-ALYQAR 179
 
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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