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Conserved domains on  [gi|1237404204|ref|WP_095213247.1|]
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GGDEF domain-containing protein

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 COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 187-377 1.01e-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: 166.31  E-value: 1.01e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237404204 187 LLSVLVILPLYVLQRSMLIKRLEELATTDQKTQLLNATTWQDGAQREISRAERENGSFGALMIDLDHFKRINDTFGHLAG 266
Cdd:COG2199    89 ALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTYGHAAG 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237404204 267 DAVLKAVAAVVKQETRAHDLVGRFGGEEFVALLPSTSKEDAIVTAERIRQRISELVIPTqtnEGESVSIenrTASIGVAA 346
Cdd:COG2199   169 DEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFEL---EGKELRV---TVSIGVAL 242

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1237404204 347 FPLDGTSIEEVMAAADAAVYAAKDSGRNRVV 377
Cdd:COG2199   243 YPEDGDSAEELLRRADLALYRAKRAGRNRVV 273
COG5001 super family cl34859
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 9-358 5.69e-33

Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain [Signal transduction mechanisms];


The actual alignment was detected with superfamily member COG5001:

Pssm-ID: 444025 [Multi-domain]  Cd Length: 678  Bit Score: 130.28  E-value: 5.69e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237404204   9 LVFPVSLGQIGILGMLAGLAIAQTEVTRQIERQRRMLSQGPHITVTSVWLLPAALLVPPQLVAALGVIIYVYLAFRSWNG 88
Cdd:COG5001    48 ALLLAALLLLALLALLALLLLAAALLALALAALLLAALLAALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALAAL 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237404204  89 TRPGEAHRVAANATTMILSGFGAALAGHLADGHSVTTVVAGALGYFLVNTALTGLGLYLTDPAKATPESCLGTMDDNLLE 168
Cdd:COG5001   128 LLAAASAALLAAALGAALLAALALALLLALARALLALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLR 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237404204 169 LATLCVGGLLVMVLSHEPLLSVLVILPLYVLQRSMLIKRLEELATTDQKTQLLNATTWQDGAQREISRAERENGSFGALM 248
Cdd:COG5001   208 LALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRLALLF 287

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237404204 249 IDLDHFKRINDTFGHLAGDAVLKAVAAVVKQETRAHDLVGRFGGEEFVALLPS-TSKEDAIVTAERIRQRISE-LVIptq 326
Cdd:COG5001   288 IDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVLLPDlDDPEDAEAVAERILAALAEpFEL--- 364

                         330       340       350
                  ....*....|....*....|....*....|..
gi 1237404204 327 tnEGESVSIenrTASIGVAAFPLDGTSIEEVM 358
Cdd:COG5001   365 --DGHELYV---SASIGIALYPDDGADAEELL 391
 
Name Accession Description Interval E-value
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 187-377 1.01e-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: 166.31  E-value: 1.01e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237404204 187 LLSVLVILPLYVLQRSMLIKRLEELATTDQKTQLLNATTWQDGAQREISRAERENGSFGALMIDLDHFKRINDTFGHLAG 266
Cdd:COG2199    89 ALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTYGHAAG 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237404204 267 DAVLKAVAAVVKQETRAHDLVGRFGGEEFVALLPSTSKEDAIVTAERIRQRISELVIPTqtnEGESVSIenrTASIGVAA 346
Cdd:COG2199   169 DEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFEL---EGKELRV---TVSIGVAL 242

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1237404204 347 FPLDGTSIEEVMAAADAAVYAAKDSGRNRVV 377
Cdd:COG2199   243 YPEDGDSAEELLRRADLALYRAKRAGRNRVV 273
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 213-377 7.74e-45

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: 151.94  E-value: 7.74e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237404204 213 TTDQKTQLLNATTWQDGAQREISRAERENGSFGALMIDLDHFKRINDTFGHLAGDAVLKAVAAVVKQETRAHDLVGRFGG 292
Cdd:cd01949     1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237404204 293 EEFVALLPSTSKEDAIVTAERIRQRISELVIPtqtnEGESVSIenrTASIGVAAFPLDGTSIEEVMAAADAAVYAAKDSG 372
Cdd:cd01949    81 DEFAILLPGTDLEEAEALAERLREAIEEPFFI----DGQEIRV---TASIGIATYPEDGEDAEELLRRADEALYRAKRSG 153


                  ....*
gi 1237404204 373 RNRVV 377
Cdd:cd01949   154 RNRVV 158
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 211-379 5.39e-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: 150.18  E-value: 5.39e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237404204 211 LATTDQKTQLLNATTWQDGAQREISRAERENGSFGALMIDLDHFKRINDTFGHLAGDAVLKAVAAVVKQETRAHDLVGRF 290
Cdd:TIGR00254   1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237404204 291 GGEEFVALLPSTSKEDAIVTAERIRQRISELVIPTQTNEGESVsienrTASIGVAAFPLDGTSIEEVMAAADAAVYAAKD 370
Cdd:TIGR00254  81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSETLTV-----TVSIGVACYPGHGLTLEELLKRADEALYQAKK 155


                  ....*....
gi 1237404204 371 SGRNRVVGS 379
Cdd:TIGR00254 156 AGRNRVVVA 164
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 212-375 6.08e-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: 147.40  E-value: 6.08e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237404204 212 ATTDQKTQLLNATTWQDGAQREISRAERENGSFGALMIDLDHFKRINDTFGHLAGDAVLKAVAAVVKQETRAHDLVGRFG 291
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237404204 292 GEEFVALLPSTSKEDAIVTAERIRQRISELVIPTqTNEGESVSIenrTASIGVAAFPLDGTSIEEVMAAADAAVYAAKDS 371
Cdd:pfam00990  81 GDEFAILLPETSLEGAQELAERIRRLLAKLKIPH-TVSGLPLYV---TISIGIAAYPNDGEDPEDLLKRADTALYQAKQA 156


                  ....
gi 1237404204 372 GRNR 375
Cdd:pfam00990 157 GRNR 160
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 210-378 5.09e-39

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 136.99  E-value: 5.09e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237404204  210 ELATTDQKTQLLNATTWQDGAQREISRAERENGSFGALMIDLDHFKRINDTFGHLAGDAVLKAVAAVVKQETRAHDLVGR 289
Cdd:smart00267   1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237404204  290 FGGEEFVALLPSTSKEDAIVTAERIRQRISELVIPtqtnEGESVSIenrTASIGVAAFPLDGTSIEEVMAAADAAVYAAK 369
Cdd:smart00267  81 LGGDEFALLLPETSLEEAIALAERILQQLREPIII----HGIPLYL---TISIGVAAYPNPGEDAEDLLKRADTALYQAK 153


                   ....*....
gi 1237404204  370 DSGRNRVVG 378
Cdd:smart00267 154 KAGRNQVAV 162
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 9-358 5.69e-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: 130.28  E-value: 5.69e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237404204   9 LVFPVSLGQIGILGMLAGLAIAQTEVTRQIERQRRMLSQGPHITVTSVWLLPAALLVPPQLVAALGVIIYVYLAFRSWNG 88
Cdd:COG5001    48 ALLLAALLLLALLALLALLLLAAALLALALAALLLAALLAALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALAAL 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237404204  89 TRPGEAHRVAANATTMILSGFGAALAGHLADGHSVTTVVAGALGYFLVNTALTGLGLYLTDPAKATPESCLGTMDDNLLE 168
Cdd:COG5001   128 LLAAASAALLAAALGAALLAALALALLLALARALLALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLR 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237404204 169 LATLCVGGLLVMVLSHEPLLSVLVILPLYVLQRSMLIKRLEELATTDQKTQLLNATTWQDGAQREISRAERENGSFGALM 248
Cdd:COG5001   208 LALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRLALLF 287

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237404204 249 IDLDHFKRINDTFGHLAGDAVLKAVAAVVKQETRAHDLVGRFGGEEFVALLPS-TSKEDAIVTAERIRQRISE-LVIptq 326
Cdd:COG5001   288 IDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVLLPDlDDPEDAEAVAERILAALAEpFEL--- 364

                         330       340       350
                  ....*....|....*....|....*....|..
gi 1237404204 327 tnEGESVSIenrTASIGVAAFPLDGTSIEEVM 358
Cdd:COG5001   365 --DGHELYV---SASIGIALYPDDGADAEELL 391
pleD PRK09581
response regulator PleD; Reviewed
 199-379 1.40e-32

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 127.32  E-value: 1.40e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237404204 199 LQRSMlikrleELATTDQKTQLLNATTWQDGAQREISRAERENGSFGALMIDLDHFKRINDTFGHLAGDAVLKAVAAVVK 278
Cdd:PRK09581  285 LEQSI------EMAVTDGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLR 358

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237404204 279 QETRAHDLVGRFGGEEFVALLPSTSKEDAIVTAERIRQRISELviPTQTNEGESVSieNRTASIGVAAFPLDGTSIEEVM 358
Cdd:PRK09581  359 NNIRGTDLIARYGGEEFVVVMPDTDIEDAIAVAERIRRKIAEE--PFIISDGKERL--NVTVSIGVAELRPSGDTIEALI 434

                         170       180
                  ....*....|....*....|.
gi 1237404204 359 AAADAAVYAAKDSGRNRVVGS 379
Cdd:PRK09581  435 KRADKALYEAKNTGRNRVVAL 455
 
Name Accession Description Interval E-value
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 187-377 1.01e-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: 166.31  E-value: 1.01e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237404204 187 LLSVLVILPLYVLQRSMLIKRLEELATTDQKTQLLNATTWQDGAQREISRAERENGSFGALMIDLDHFKRINDTFGHLAG 266
Cdd:COG2199    89 ALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTYGHAAG 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237404204 267 DAVLKAVAAVVKQETRAHDLVGRFGGEEFVALLPSTSKEDAIVTAERIRQRISELVIPTqtnEGESVSIenrTASIGVAA 346
Cdd:COG2199   169 DEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFEL---EGKELRV---TVSIGVAL 242

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1237404204 347 FPLDGTSIEEVMAAADAAVYAAKDSGRNRVV 377
Cdd:COG2199   243 YPEDGDSAEELLRRADLALYRAKRAGRNRVV 273
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 213-377 7.74e-45

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: 151.94  E-value: 7.74e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237404204 213 TTDQKTQLLNATTWQDGAQREISRAERENGSFGALMIDLDHFKRINDTFGHLAGDAVLKAVAAVVKQETRAHDLVGRFGG 292
Cdd:cd01949     1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237404204 293 EEFVALLPSTSKEDAIVTAERIRQRISELVIPtqtnEGESVSIenrTASIGVAAFPLDGTSIEEVMAAADAAVYAAKDSG 372
Cdd:cd01949    81 DEFAILLPGTDLEEAEALAERLREAIEEPFFI----DGQEIRV---TASIGIATYPEDGEDAEELLRRADEALYRAKRSG 153


                  ....*
gi 1237404204 373 RNRVV 377
Cdd:cd01949   154 RNRVV 158
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 211-379 5.39e-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: 150.18  E-value: 5.39e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237404204 211 LATTDQKTQLLNATTWQDGAQREISRAERENGSFGALMIDLDHFKRINDTFGHLAGDAVLKAVAAVVKQETRAHDLVGRF 290
Cdd:TIGR00254   1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237404204 291 GGEEFVALLPSTSKEDAIVTAERIRQRISELVIPTQTNEGESVsienrTASIGVAAFPLDGTSIEEVMAAADAAVYAAKD 370
Cdd:TIGR00254  81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSETLTV-----TVSIGVACYPGHGLTLEELLKRADEALYQAKK 155


                  ....*....
gi 1237404204 371 SGRNRVVGS 379
Cdd:TIGR00254 156 AGRNRVVVA 164
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 212-375 6.08e-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: 147.40  E-value: 6.08e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237404204 212 ATTDQKTQLLNATTWQDGAQREISRAERENGSFGALMIDLDHFKRINDTFGHLAGDAVLKAVAAVVKQETRAHDLVGRFG 291
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237404204 292 GEEFVALLPSTSKEDAIVTAERIRQRISELVIPTqTNEGESVSIenrTASIGVAAFPLDGTSIEEVMAAADAAVYAAKDS 371
Cdd:pfam00990  81 GDEFAILLPETSLEGAQELAERIRRLLAKLKIPH-TVSGLPLYV---TISIGIAAYPNDGEDPEDLLKRADTALYQAKQA 156


                  ....
gi 1237404204 372 GRNR 375
Cdd:pfam00990 157 GRNR 160
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 210-378 5.09e-39

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 136.99  E-value: 5.09e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237404204  210 ELATTDQKTQLLNATTWQDGAQREISRAERENGSFGALMIDLDHFKRINDTFGHLAGDAVLKAVAAVVKQETRAHDLVGR 289
Cdd:smart00267   1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237404204  290 FGGEEFVALLPSTSKEDAIVTAERIRQRISELVIPtqtnEGESVSIenrTASIGVAAFPLDGTSIEEVMAAADAAVYAAK 369
Cdd:smart00267  81 LGGDEFALLLPETSLEEAIALAERILQQLREPIII----HGIPLYL---TISIGVAAYPNPGEDAEDLLKRADTALYQAK 153


                   ....*....
gi 1237404204  370 DSGRNRVVG 378
Cdd:smart00267 154 KAGRNQVAV 162
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 9-358 5.69e-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: 130.28  E-value: 5.69e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237404204   9 LVFPVSLGQIGILGMLAGLAIAQTEVTRQIERQRRMLSQGPHITVTSVWLLPAALLVPPQLVAALGVIIYVYLAFRSWNG 88
Cdd:COG5001    48 ALLLAALLLLALLALLALLLLAAALLALALAALLLAALLAALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALAAL 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237404204  89 TRPGEAHRVAANATTMILSGFGAALAGHLADGHSVTTVVAGALGYFLVNTALTGLGLYLTDPAKATPESCLGTMDDNLLE 168
Cdd:COG5001   128 LLAAASAALLAAALGAALLAALALALLLALARALLALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLR 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237404204 169 LATLCVGGLLVMVLSHEPLLSVLVILPLYVLQRSMLIKRLEELATTDQKTQLLNATTWQDGAQREISRAERENGSFGALM 248
Cdd:COG5001   208 LALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRLALLF 287

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237404204 249 IDLDHFKRINDTFGHLAGDAVLKAVAAVVKQETRAHDLVGRFGGEEFVALLPS-TSKEDAIVTAERIRQRISE-LVIptq 326
Cdd:COG5001   288 IDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVLLPDlDDPEDAEAVAERILAALAEpFEL--- 364

                         330       340       350
                  ....*....|....*....|....*....|..
gi 1237404204 327 tnEGESVSIenrTASIGVAAFPLDGTSIEEVM 358
Cdd:COG5001   365 --DGHELYV---SASIGIALYPDDGADAEELL 391
pleD PRK09581
response regulator PleD; Reviewed
 199-379 1.40e-32

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 127.32  E-value: 1.40e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237404204 199 LQRSMlikrleELATTDQKTQLLNATTWQDGAQREISRAERENGSFGALMIDLDHFKRINDTFGHLAGDAVLKAVAAVVK 278
Cdd:PRK09581  285 LEQSI------EMAVTDGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLR 358

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237404204 279 QETRAHDLVGRFGGEEFVALLPSTSKEDAIVTAERIRQRISELviPTQTNEGESVSieNRTASIGVAAFPLDGTSIEEVM 358
Cdd:PRK09581  359 NNIRGTDLIARYGGEEFVVVMPDTDIEDAIAVAERIRRKIAEE--PFIISDGKERL--NVTVSIGVAELRPSGDTIEALI 434

                         170       180
                  ....*....|....*....|.
gi 1237404204 359 AAADAAVYAAKDSGRNRVVGS 379
Cdd:PRK09581  435 KRADKALYEAKNTGRNRVVAL 455
PRK15426 PRK15426
cellulose biosynthesis regulator YedQ;
187-377 2.87e-31

cellulose biosynthesis regulator YedQ;


Pssm-ID: 237964 [Multi-domain]  Cd Length: 570  Bit Score: 124.74  E-value: 2.87e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237404204 187 LLSVLVILPL----YVLQRSmlikrLEELATTDQKTQLLNATTWQDGAQREISRAERENGSFGALMIDLDHFKRINDTFG 262
Cdd:PRK15426  374 LISWYVIRRMvsnmFVLQSS-----LQWQAWHDPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFKSINDRFG 448

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237404204 263 HLAGDAVLKAVAAVVKQETRAHDLVGRFGGEEFVALLPSTSKEDAIVTAERIRQRIselviptqtNEGESVSIENRT--- 339
Cdd:PRK15426  449 HQAGDRVLSHAAGLISSSLRAQDVAGRVGGEEFCVVLPGASLAEAAQVAERIRLRI---------NEKEILVAKSTTiri 519

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1237404204 340 -ASIGVAAFPLDGT-SIEEVMAAADAAVYAAKDSGRNRVV 377
Cdd:PRK15426  520 sASLGVSSAEEDGDyDFEQLQSLADRRLYLAKQAGRNRVC 559
PRK09894 PRK09894
diguanylate cyclase; Provisional
 201-377 1.35e-25

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 104.76  E-value: 1.35e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237404204 201 RSMLIKRLEELATTDQKTQLLNATTWQDGAQREISRAERENgsFGALMIDLDHFKRINDTFGHLAGDAVLKAVAAVVKQE 280
Cdd:PRK09894  118 TDYKIYLLTIRSNMDVLTGLPGRRVLDESFDHQLRNREPQN--LYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASW 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237404204 281 TRAHDLVGRFGGEEFVALLPSTSKEDAIVTAERIRQRISELviPTQTNEGEsVSIenrTASIGVA-AFPldGTSIEEVMA 359
Cdd:PRK09894  196 TRDYETVYRYGGEEFIICLKAATDEEACRAGERIRQLIANH--AITHSDGR-INI---TATFGVSrAFP--EETLDVVIG 267

                         170
                  ....*....|....*...
gi 1237404204 360 AADAAVYAAKDSGRNRVV 377
Cdd:PRK09894  268 RADRAMYEGKQTGRNRVM 285
adrA PRK10245
diguanylate cyclase AdrA; Provisional
 169-375 3.20e-20

diguanylate cyclase AdrA; Provisional


Pssm-ID: 182329 [Multi-domain]  Cd Length: 366  Bit Score: 91.04  E-value: 3.20e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237404204 169 LATLCVGGLLVmVLSHEPL-----LSVLVILPLYVLQRSMLI--------KRLEELATTDQKTQLLNATTWQDGAQREIS 235
Cdd:PRK10245  150 LVTLELTGITV-SFNSAPLewwlsLPVIVIYPLLFAWVSYQTatklaehkRRLQVMSTRDGMTGVYNRRHWETLLRNEFD 228

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237404204 236 RAERENGSFGALMIDLDHFKRINDTFGHLAGDAVLKAVAAVVKQETRAHDLVGRFGGEEFVALLPSTSKEDAIVTAERIR 315
Cdd:PRK10245  229 NCRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSDVIGRFGGDEFAVIMSGTPAESAITAMSRVH 308

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237404204 316 QRISELVIPTQTNEGESVsienrtaSIGVAAFPLDGTSIEEVMAAADAAVYAAKDSGRNR 375
Cdd:PRK10245  309 EGLNTLRLPNAPQVTLRI-------SVGVAPLNPQMSHYREWLKSADLALYKAKNAGRNR 361
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 179-388 6.19e-17

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 82.80  E-value: 6.19e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237404204  179 VMVLSHEPLLSVLVILPLyVLQRSMLiKRLEELATTDQKTQLLNATTWQDGAQREISRAeRENGSFGAL-MIDLDHFKRI 257
Cdd:PRK09776   634 LSTLDGENIGSVLVIQDV-TESRKML-RQLSYSASHDALTHLANRASFEKQLRRLLQTV-NSTHQRHALvFIDLDRFKAV 710

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237404204  258 NDTFGHLAGDAVLKAVAAVVKQETRAHDLVGRFGGEEFVALLPSTSKEDAIVTAERIRQRISELVIPTqtnEGESVSIen 337
Cdd:PRK09776   711 NDSAGHAAGDALLRELASLMLSMLRSSDVLARLGGDEFGLLLPDCNVESARFIATRIISAINDYHFPW---EGRVYRV-- 785

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1237404204  338 rTASIGVAAFPLDGTSIEEVMAAADAAVYAAKDSGRNRVvgSVTPARELAA 388
Cdd:PRK09776   786 -GASAGITLIDANNHQASEVMSQADIACYAAKNAGRGRV--TVYEPQQAAA 833
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
207-373 2.82e-15

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 77.41  E-value: 2.82e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237404204 207 RLEELATTDQKTQLLNATTWQDGAQREIsrAERENGSFGALMIDLDHFKRINDTFGHLAGDAVLKAVAAVVKQETRAHDL 286
Cdd:PRK10060  232 RLRILANTDSITGLPNRNAIQELIDHAI--NAADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQT 309

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237404204 287 VGRFGGEEFVALLPSTSKEDAIVTAERIRQRiseLVIPTQTNegesvSIENRTA-SIGVAAFPLDGTSIEEVMAAADAAV 365
Cdd:PRK10060  310 LARLGGDEFLVLASHTSQAALEAMASRILTR---LRLPFRIG-----LIEVYTGcSIGIALAPEHGDDSESLIRSADTAM 381


                  ....*...
gi 1237404204 366 YAAKDSGR 373
Cdd:PRK10060  382 YTAKEGGR 389
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 285-349 2.14e-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: 62.23  E-value: 2.14e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1237404204 285 DLVGRFGGEEFVALLPSTSKEDAIVTAERIRQRISELviptqtnegESVSIenrTASIGVAAFPL 349
Cdd:COG3706   116 DLVARYGGEEFAILLPGTDLEGALAVAERIREAVAEL---------PSLRV---TVSIGVAGDSL 168
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
 245-351 4.18e-10

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: 57.37  E-value: 4.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237404204 245 GALMIDLDHFKRINDTFGHLAGDAVLKAVAAVVKQE-TRAHDLVGRFGGEEFVALLPSTSKEDAIVTAERIRQRISELVI 323
Cdd:cd07556     3 TILFADIVGFTSLADALGPDEGDELLNELAGRFDSLiRRSGDLKIKTIGDEFMVVSGLDHPAAAVAFAEDMREAVSALNQ 82

                          90       100
                  ....*....|....*....|....*...
gi 1237404204 324 PTqtnegesvsIENRTASIGVAAFPLDG 351
Cdd:cd07556    83 SE---------GNPVRVRIGIHTGPVVV 101
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 249-345 6.78e-06

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 48.23  E-value: 6.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237404204 249 IDLDHFKRINDTFGHLAGDAVLKAVAAVVKQETRAHDLVGRFGGEEFVALLPSTSKEDAIVTAERIRQRISELVIPtqtn 328
Cdd:PRK11359  409 IGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGTQFVLVSLENDVSNITQIADELRNVVSKPIMI---- 484

                          90
                  ....*....|....*..
gi 1237404204 329 EGESVSIenrTASIGVA 345
Cdd:PRK11359  485 DDKPFPL---TLSIGIS 498
PRK09966 PRK09966
diguanylate cyclase DgcN;
247-345 9.64e-05

diguanylate cyclase DgcN;


Pssm-ID: 182171 [Multi-domain]  Cd Length: 407  Bit Score: 44.23  E-value: 9.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237404204 247 LMIDLDHFKRINDTFGHLAGDAVLKAVAAVVKQETRAHDLVGRFGGEEFVALLPSTSKEDAIvtaERIRQRISELV-IPT 325
Cdd:PRK09966  282 LFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHKAYRLGGDEFAMVLYDVQSESEV---QQICSALTQIFnLPF 358

                          90       100
                  ....*....|....*....|
gi 1237404204 326 QTNEGESVSIenrTASIGVA 345
Cdd:PRK09966  359 DLHNGHQTTM---TLSIGYA 375
 
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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