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Conserved domains on  [gi|2088339344|ref|WP_222570055|]
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GGDEF domain-containing protein [Halomonas sp. DP5N14-9]

Protein Classification

GGDEF domain-containing protein( domain architecture ID 10005578)

GGDEF domain-containing protein may have diguanylate cyclase (DGC) activity, similar to Escherichia coli DgcT (YcdT) and to E. coli CdgI (YeaI), a c-di-GMP-binding effector with a degenerate GGDEF domain which binds c-di-GMP

CATH:  3.30.70.270
EC:  2.7.7.65
Gene Ontology:  GO:0005525|GO:0046872|GO:0052621|GO:0005886
PubMed:  11119645|15063857|15289546|15306016|16530465|16045609

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 433-667 3.24e-61

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: 205.98  E-value: 3.24e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339344 433 AYLPLELTLRPDTRLLTRLRSRLPAVTLMLGLLFSQFLYLTLFSQHQMASQHRALARSNGDLRREVRTRHRLQQQLSWLA 512
Cdd:COG2199    35 LLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLLLLALEDITELRRLEERLRRLA 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339344 513 DHDELTGLPNRRHLQATAQTW-----RARLPLSVTLVDIDHFKRINDCLGHAEGDRVLKAVGRLAQETLGDDGLLGRYGG 587
Cdd:COG2199   115 THDPLTGLPNRRAFEERLERElararREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDLVARLGG 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339344 588 EEFLVIIPEGRLAEASAVAERLRRAVRQAPLAHHDGT-PLTISLGVACQDQAPLDLARLIQQADQALYTAKHQGRDRVEL 666
Cdd:COG2199   195 DEFAVLLPGTDLEEAEALAERLREALEQLPFELEGKElRVTVSIGVALYPEDGDSAEELLRRADLALYRAKRAGRNRVVV 274


                  .
gi 2088339344 667 F 667
Cdd:COG2199   275 Y 275
 
Name Accession Description Interval E-value
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 433-667 3.24e-61

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: 205.98  E-value: 3.24e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339344 433 AYLPLELTLRPDTRLLTRLRSRLPAVTLMLGLLFSQFLYLTLFSQHQMASQHRALARSNGDLRREVRTRHRLQQQLSWLA 512
Cdd:COG2199    35 LLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLLLLALEDITELRRLEERLRRLA 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339344 513 DHDELTGLPNRRHLQATAQTW-----RARLPLSVTLVDIDHFKRINDCLGHAEGDRVLKAVGRLAQETLGDDGLLGRYGG 587
Cdd:COG2199   115 THDPLTGLPNRRAFEERLERElararREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDLVARLGG 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339344 588 EEFLVIIPEGRLAEASAVAERLRRAVRQAPLAHHDGT-PLTISLGVACQDQAPLDLARLIQQADQALYTAKHQGRDRVEL 666
Cdd:COG2199   195 DEFAVLLPGTDLEEAEALAERLREALEQLPFELEGKElRVTVSIGVALYPEDGDSAEELLRRADLALYRAKRAGRNRVVV 274


                  .
gi 2088339344 667 F 667
Cdd:COG2199   275 Y 275
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 514-664 1.38e-58

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: 194.70  E-value: 1.38e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339344 514 HDELTGLPNRRHL-----QATAQTWRARLPLSVTLVDIDHFKRINDCLGHAEGDRVLKAVGRLAQETLGDDGLLGRYGGE 588
Cdd:cd01949     2 TDPLTGLPNRRAFeerleRLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGD 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2088339344 589 EFLVIIPEGRLAEASAVAERLRRAVRQAPLAHHDGTPLTISLGVACQDQAPLDLARLIQQADQALYTAKHQGRDRV 664
Cdd:cd01949    82 EFAILLPGTDLEEAEALAERLREAIEEPFFIDGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNRV 157
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 512-663 2.10e-53

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: 180.91  E-value: 2.10e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339344 512 ADHDELTGLPNRRHL-----QATAQTWRARLPLSVTLVDIDHFKRINDCLGHAEGDRVLKAVGRLAQETLGDDGLLGRYG 586
Cdd:pfam00990   1 AAHDPLTGLPNRRYFeeqleQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339344 587 GEEFLVIIPEGRLAEASAVAERLRRAVRQAPLAHHDGT---PLTISLGVACQDQAPLDLARLIQQADQALYTAKHQGRDR 663
Cdd:pfam00990  81 GDEFAILLPETSLEGAQELAERIRRLLAKLKIPHTVSGlplYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGRNR 160
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 510-667 1.14e-51

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 176.28  E-value: 1.14e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339344  510 WLADHDELTGLPNRRHL-QATAQTWRARL----PLSVTLVDIDHFKRINDCLGHAEGDRVLKAVGRLAQETLGDDGLLGR 584
Cdd:smart00267   1 RLAFRDPLTGLPNRRYFeEELEQELQRAQrqgsPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339344  585 YGGEEFLVIIPEGRLAEASAVAERLRRAVRQAPLAHHDGTPLTISLGVACQDQAPLDLARLIQQADQALYTAKHQGRDRV 664
Cdd:smart00267  81 LGGDEFALLLPETSLEEAIALAERILQQLREPIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQV 160


                   ...
gi 2088339344  665 ELF 667
Cdd:smart00267 161 AVY 163
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 511-667 4.19e-48

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: 166.74  E-value: 4.19e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339344 511 LADHDELTGLPNRRHLQATAQTWRAR-----LPLSVTLVDIDHFKRINDCLGHAEGDRVLKAVGRLAQETLGDDGLLGRY 585
Cdd:TIGR00254   1 QAVRDPLTGLYNRRYLEEMLDSELKRarrfqRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339344 586 GGEEFLVIIPEGRLAEASAVAERLRRAVRQAPLAHHDGTP--LTISLGVACQDQAPLDLARLIQQADQALYTAKHQGRDR 663
Cdd:TIGR00254  81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSETltVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRNR 160


                  ....
gi 2088339344 664 VELF 667
Cdd:TIGR00254 161 VVVA 164
pleD PRK09581
response regulator PleD; Reviewed
 487-664 1.42e-42

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 160.07  E-value: 1.42e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339344 487 LARSNGDLRREVRT---RHRLQQQLSwLADHDELTGLPNRR----HLQATAQTWRAR-LPLSVTLVDIDHFKRINDCLGH 558
Cdd:PRK09581  265 LARVRTQIRRKRYQdalRNNLEQSIE-MAVTDGLTGLHNRRyfdmHLKNLIERANERgKPLSLMMIDIDHFKKVNDTYGH 343

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339344 559 AEGDRVLKAV-GRLAQETLGDDgLLGRYGGEEFLVIIPEGRLAEASAVAERLRRAVRQAPLAHHDGT---PLTISLGVAC 634
Cdd:PRK09581  344 DAGDEVLREFaKRLRNNIRGTD-LIARYGGEEFVVVMPDTDIEDAIAVAERIRRKIAEEPFIISDGKerlNVTVSIGVAE 422

                         170       180       190
                  ....*....|....*....|....*....|
gi 2088339344 635 QDQAPLDLARLIQQADQALYTAKHQGRDRV 664
Cdd:PRK09581  423 LRPSGDTIEALIKRADKALYEAKNTGRNRV 452
 
Name Accession Description Interval E-value
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 433-667 3.24e-61

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: 205.98  E-value: 3.24e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339344 433 AYLPLELTLRPDTRLLTRLRSRLPAVTLMLGLLFSQFLYLTLFSQHQMASQHRALARSNGDLRREVRTRHRLQQQLSWLA 512
Cdd:COG2199    35 LLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLLLLALEDITELRRLEERLRRLA 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339344 513 DHDELTGLPNRRHLQATAQTW-----RARLPLSVTLVDIDHFKRINDCLGHAEGDRVLKAVGRLAQETLGDDGLLGRYGG 587
Cdd:COG2199   115 THDPLTGLPNRRAFEERLERElararREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDLVARLGG 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339344 588 EEFLVIIPEGRLAEASAVAERLRRAVRQAPLAHHDGT-PLTISLGVACQDQAPLDLARLIQQADQALYTAKHQGRDRVEL 666
Cdd:COG2199   195 DEFAVLLPGTDLEEAEALAERLREALEQLPFELEGKElRVTVSIGVALYPEDGDSAEELLRRADLALYRAKRAGRNRVVV 274


                  .
gi 2088339344 667 F 667
Cdd:COG2199   275 Y 275
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 514-664 1.38e-58

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: 194.70  E-value: 1.38e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339344 514 HDELTGLPNRRHL-----QATAQTWRARLPLSVTLVDIDHFKRINDCLGHAEGDRVLKAVGRLAQETLGDDGLLGRYGGE 588
Cdd:cd01949     2 TDPLTGLPNRRAFeerleRLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGD 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2088339344 589 EFLVIIPEGRLAEASAVAERLRRAVRQAPLAHHDGTPLTISLGVACQDQAPLDLARLIQQADQALYTAKHQGRDRV 664
Cdd:cd01949    82 EFAILLPGTDLEEAEALAERLREAIEEPFFIDGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNRV 157
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 512-663 2.10e-53

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: 180.91  E-value: 2.10e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339344 512 ADHDELTGLPNRRHL-----QATAQTWRARLPLSVTLVDIDHFKRINDCLGHAEGDRVLKAVGRLAQETLGDDGLLGRYG 586
Cdd:pfam00990   1 AAHDPLTGLPNRRYFeeqleQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339344 587 GEEFLVIIPEGRLAEASAVAERLRRAVRQAPLAHHDGT---PLTISLGVACQDQAPLDLARLIQQADQALYTAKHQGRDR 663
Cdd:pfam00990  81 GDEFAILLPETSLEGAQELAERIRRLLAKLKIPHTVSGlplYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGRNR 160
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 510-667 1.14e-51

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 176.28  E-value: 1.14e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339344  510 WLADHDELTGLPNRRHL-QATAQTWRARL----PLSVTLVDIDHFKRINDCLGHAEGDRVLKAVGRLAQETLGDDGLLGR 584
Cdd:smart00267   1 RLAFRDPLTGLPNRRYFeEELEQELQRAQrqgsPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339344  585 YGGEEFLVIIPEGRLAEASAVAERLRRAVRQAPLAHHDGTPLTISLGVACQDQAPLDLARLIQQADQALYTAKHQGRDRV 664
Cdd:smart00267  81 LGGDEFALLLPETSLEEAIALAERILQQLREPIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQV 160


                   ...
gi 2088339344  665 ELF 667
Cdd:smart00267 161 AVY 163
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 511-667 4.19e-48

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: 166.74  E-value: 4.19e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339344 511 LADHDELTGLPNRRHLQATAQTWRAR-----LPLSVTLVDIDHFKRINDCLGHAEGDRVLKAVGRLAQETLGDDGLLGRY 585
Cdd:TIGR00254   1 QAVRDPLTGLYNRRYLEEMLDSELKRarrfqRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339344 586 GGEEFLVIIPEGRLAEASAVAERLRRAVRQAPLAHHDGTP--LTISLGVACQDQAPLDLARLIQQADQALYTAKHQGRDR 663
Cdd:TIGR00254  81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSETltVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRNR 160


                  ....
gi 2088339344 664 VELF 667
Cdd:TIGR00254 161 VVVA 164
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 435-667 1.10e-44

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: 170.34  E-value: 1.10e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339344 435 LPLELTLRPDTRLLTRLRSRLPAVTLMLGLLFSQFLYLTLFSQHQMASQHRALARSNGDLRREVRTRHRLQQQLSWLADH 514
Cdd:COG5001   174 LLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEERLRHLAYH 253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339344 515 DELTGLPNRRHL-----QATAQTWRARLPLSVTLVDIDHFKRINDCLGHAEGDRVLKAVGRLAQETLGDDGLLGRYGGEE 589
Cdd:COG5001   254 DPLTGLPNRRLFldrleQALARARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDE 333

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339344 590 FLVIIPE-GRLAEASAVAERLRRAVRQaPLaHHDGTPLTI--SLGVACQDQAPLDLARLIQQADQALYTAKHQGRDRVEL 666
Cdd:COG5001   334 FAVLLPDlDDPEDAEAVAERILAALAE-PF-ELDGHELYVsaSIGIALYPDDGADAEELLRNADLAMYRAKAAGRNRYRF 411


                  .
gi 2088339344 667 F 667
Cdd:COG5001   412 F 412
pleD PRK09581
response regulator PleD; Reviewed
 487-664 1.42e-42

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 160.07  E-value: 1.42e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339344 487 LARSNGDLRREVRT---RHRLQQQLSwLADHDELTGLPNRR----HLQATAQTWRAR-LPLSVTLVDIDHFKRINDCLGH 558
Cdd:PRK09581  265 LARVRTQIRRKRYQdalRNNLEQSIE-MAVTDGLTGLHNRRyfdmHLKNLIERANERgKPLSLMMIDIDHFKKVNDTYGH 343

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339344 559 AEGDRVLKAV-GRLAQETLGDDgLLGRYGGEEFLVIIPEGRLAEASAVAERLRRAVRQAPLAHHDGT---PLTISLGVAC 634
Cdd:PRK09581  344 DAGDEVLREFaKRLRNNIRGTD-LIARYGGEEFVVVMPDTDIEDAIAVAERIRRKIAEEPFIISDGKerlNVTVSIGVAE 422

                         170       180       190
                  ....*....|....*....|....*....|
gi 2088339344 635 QDQAPLDLARLIQQADQALYTAKHQGRDRV 664
Cdd:PRK09581  423 LRPSGDTIEALIKRADKALYEAKNTGRNRV 452
PRK15426 PRK15426
cellulose biosynthesis regulator YedQ;
461-664 9.28e-42

cellulose biosynthesis regulator YedQ;


Pssm-ID: 237964 [Multi-domain]  Cd Length: 570  Bit Score: 160.18  E-value: 9.28e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339344 461 MLGLLFSQFLYLTLFSQHQMASQHRALARSngdlrrevrtrhrlqqqLSWLADHDELTGLPNRRHL----QATAQTWRA- 535
Cdd:PRK15426  364 LLWALFTAMLLISWYVIRRMVSNMFVLQSS-----------------LQWQAWHDPLTRLYNRGALfekaRALAKRCQRd 426

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339344 536 RLPLSVTLVDIDHFKRINDCLGHAEGDRVLKAVGRLAQETLGDDGLLGRYGGEEFLVIIPEGRLAEASAVAERLRRAVRQ 615
Cdd:PRK15426  427 QQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRVGGEEFCVVLPGASLAEAAQVAERIRLRINE 506

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2088339344 616 APLAHHDGTPL--TISLGVAC-QDQAPLDLARLIQQADQALYTAKHQGRDRV 664
Cdd:PRK15426  507 KEILVAKSTTIriSASLGVSSaEEDGDYDFEQLQSLADRRLYLAKQAGRNRV 558
PRK09894 PRK09894
diguanylate cyclase; Provisional
 515-670 8.11e-35

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 134.04  E-value: 8.11e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339344 515 DELTGLPNRRHLQATAQTWRAR---LPLSVTLVDIDHFKRINDCLGHAEGDRVLKA-VGRLAQETLGDDGLLgRYGGEEF 590
Cdd:PRK09894  132 DVLTGLPGRRVLDESFDHQLRNrepQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTlATYLASWTRDYETVY-RYGGEEF 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339344 591 LVIIPEGRLAEASAVAERLRRAVRQAPLAHHDGT-PLTISLGVAcQDQAPLDLARLIQQADQALYTAKHQGRDRVELFVD 669
Cdd:PRK09894  211 IICLKAATDEEACRAGERIRQLIANHAITHSDGRiNITATFGVS-RAFPEETLDVVIGRADRAMYEGKQTGRNRVMFIDE 289


                  .
gi 2088339344 670 T 670
Cdd:PRK09894  290 Q 290
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
503-661 4.25e-24

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 107.46  E-value: 4.25e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339344 503 RLQQQLSWLADHDELTGLPNRRHLQ-ATAQTWRARLPLSVTLV--DIDHFKRINDCLGHAEGDRVLKAVGRLAQETLGDD 579
Cdd:PRK10060  228 RAQERLRILANTDSITGLPNRNAIQeLIDHAINAADNNQVGIVylDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEED 307

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339344 580 GLLGRYGGEEFLVIIPEGRLAEASAVA----ERLRRAVRQAPLAHHDGTpltiSLGVACQDQAPLDLARLIQQADQALYT 655
Cdd:PRK10060  308 QTLARLGGDEFLVLASHTSQAALEAMAsrilTRLRLPFRIGLIEVYTGC----SIGIALAPEHGDDSESLIRSADTAMYT 383


                  ....*.
gi 2088339344 656 AKHQGR 661
Cdd:PRK10060  384 AKEGGR 389
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 497-667 5.44e-23

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 104.75  E-value: 5.44e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339344  497 EVRTRHRLQQQLSWLADHDELTGLPNR-------RHLQATAQTWRARLPLsvTLVDIDHFKRINDCLGHAEGDRVLKAVG 569
Cdd:PRK09776   650 DVTESRKMLRQLSYSASHDALTHLANRasfekqlRRLLQTVNSTHQRHAL--VFIDLDRFKAVNDSAGHAAGDALLRELA 727

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339344  570 RLAQETLGDDGLLGRYGGEEFLVIIPEGRLAEASAVAERLRRAVRQAPL-----AHHDGTpltiSLGVACQDQAPLDLAR 644
Cdd:PRK09776   728 SLMLSMLRSSDVLARLGGDEFGLLLPDCNVESARFIATRIISAINDYHFpwegrVYRVGA----SAGITLIDANNHQASE 803

                          170       180
                   ....*....|....*....|...
gi 2088339344  645 LIQQADQALYTAKHQGRDRVELF 667
Cdd:PRK09776   804 VMSQADIACYAAKNAGRGRVTVY 826
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 481-633 5.45e-21

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 97.92  E-value: 5.45e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339344 481 ASQHR-ALArsngdLRREvrtrhRLQQQLSWLADHDELTGLPNRRHLQA-TAQTWRARLPLSVTLVDIDHFKRINDCLGH 558
Cdd:PRK11359  354 ISQHLaALA-----LEQE-----KSRQHIEQLIQFDPLTGLPNRNNLHNyLDDLVDKAVSPVVYLIGVDHFQDVIDSLGY 423

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2088339344 559 AEGDRVLKAVGRLAQETLGDDGLLGRYGGEEFLVIIPEGRLAEASAVAERLRRAVRQAPLAHHDGTPLTISLGVA 633
Cdd:PRK11359  424 AWADQALLEVVNRFREKLKPDQYLCRIEGTQFVLVSLENDVSNITQIADELRNVVSKPIMIDDKPFPLTLSIGIS 498
adrA PRK10245
diguanylate cyclase AdrA; Provisional
 505-666 5.31e-18

diguanylate cyclase AdrA; Provisional


Pssm-ID: 182329 [Multi-domain]  Cd Length: 366  Bit Score: 86.42  E-value: 5.31e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339344 505 QQQLSWLADHDELTGLPNRRHLQATAQT-----WRARLPLSVTLVDIDHFKRINDCLGHAEGDRVLKAVGRLAQETLGDD 579
Cdd:PRK10245  198 KRRLQVMSTRDGMTGVYNRRHWETLLRNefdncRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGS 277

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339344 580 GLLGRYGGEEFLVII----PEGRLAEASAVAERLrRAVRqapLAHHDGTPLTISLGVACQDQAPLDLARLIQQADQALYT 655
Cdd:PRK10245  278 DVIGRFGGDEFAVIMsgtpAESAITAMSRVHEGL-NTLR---LPNAPQVTLRISVGVAPLNPQMSHYREWLKSADLALYK 353

                         170
                  ....*....|.
gi 2088339344 656 AKHQGRDRVEL 666
Cdd:PRK10245  354 AKNAGRNRTEV 364
PRK09966 PRK09966
diguanylate cyclase DgcN;
476-663 2.02e-14

diguanylate cyclase DgcN;


Pssm-ID: 182171 [Multi-domain]  Cd Length: 407  Bit Score: 75.81  E-value: 2.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339344 476 SQHQMASQHRALARSNGDLRREVRTRHRLQ---QQLSWLADHDELTGLPNRRHLQATAQTW----RARLPLSVTLVDIDH 548
Cdd:PRK09966  209 SEERIAEFHRFALDFNSLLDEMEEWQLRLQaknAQLLRTALHDPLTGLANRAAFRSGINTLmnnsDARKTSALLFLDGDN 288

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339344 549 FKRINDCLGHAEGDRVLKAVGRLAQETLGDDGLLGRYGGEEFLVIIPEgrlAEASAVAERLRRAVRQA---PLAHHDG-- 623
Cdd:PRK09966  289 FKYINDTWGHATGDRVLIEIAKRLAEFGGLRHKAYRLGGDEFAMVLYD---VQSESEVQQICSALTQIfnlPFDLHNGhq 365

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2088339344 624 TPLTISLGVACQ-DQAPLDlaRLIQQADQALYTAKHQGRDR 663
Cdd:PRK09966  366 TTMTLSIGYAMTiEHASAE--KLQELADHNMYQAKHQRAEK 404
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 581-657 2.36e-14

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: 71.48  E-value: 2.36e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2088339344 581 LLGRYGGEEFLVIIPEGRLAEASAVAERLRRAVRQAPLAHhdgtpLTISLGVACQDqapldlarLIQQADqALYTAK 657
Cdd:COG3706   117 LVARYGGEEFAILLPGTDLEGALAVAERIREAVAELPSLR-----VTVSIGVAGDS--------LLKRAD-ALYQAR 179
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
 538-633 1.28e-13

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: 68.15  E-value: 1.28e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339344 538 PLSVTLVDIDHFKRINDCLGHAEGDRVLKAV-GRLAQETLGDDGLLGRYGGEEFLVIIPEGRLAEASAVAERLRRAVRQa 616
Cdd:cd07556     1 PVTILFADIVGFTSLADALGPDEGDELLNELaGRFDSLIRRSGDLKIKTIGDEFMVVSGLDHPAAAVAFAEDMREAVSA- 79

                          90
                  ....*....|....*..
gi 2088339344 617 pLAHHDGTPLTISLGVA 633
Cdd:cd07556    80 -LNQSEGNPVRVRIGIH 95
PRK11829 PRK11829
biofilm formation regulator HmsP; Provisional
 498-667 6.69e-03

biofilm formation regulator HmsP; Provisional


Pssm-ID: 183329 [Multi-domain]  Cd Length: 660  Bit Score: 39.54  E-value: 6.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339344 498 VRTRHRLQQQL-------SWLADHDELTGLPNR----RHLQATAQTWRARLPLSVTLVDIDHFKRINDCLGHAEGDRVLK 566
Cdd:PRK11829  211 VRNYNRNQQLLadayadmGRISHRFPVTELPNRslfiSLLEKEIASSTRTDHFHLLVIGIETLQEVSGAMSEAQHQQLLL 290

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339344 567 AVGRLAQETLGDDGLLGRYGGEEFLVIIPE-GRLAEASAVAERLRRAVRQAPLAHHDGTPLTISLGVAcQDQAPLDLAR- 644
Cdd:PRK11829  291 TIVQRIEQCIDDSDLLAQLSKTEFAVLARGtRRSFPAMQLARRIMSQVTQPLFFDEITLRPSASIGIT-RYQAQQDTAEs 369

                         170       180
                  ....*....|....*....|...
gi 2088339344 645 LIQQADQALYTAKHQGRDRVELF 667
Cdd:PRK11829  370 MMRNASTAMMAAHHEGRNQIMVF 392
 
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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