NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|446009065|ref|WP_000086920|]
View 

MULTISPECIES: GGDEF domain-containing protein [Shigella]

Protein Classification

GGDEF domain-containing protein( domain architecture ID 11977858)

GGDEF domain-containing protein similar to E.coli diguanylate cyclases DgcZ (YdeH) and DgcT (YcdT), and to E. coli CdgI (YeaI), a c-di-GMP-binding effector with a degenerate GGDEF domain which binds c-di-GMP

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
GAPES2 super family cl28835
Gammaproteobacterial periplasmic sensor domain; GAPES2 (GAmmaproteobacterial PEriplasmic ...
 26-229 2.65e-149

Gammaproteobacterial periplasmic sensor domain; GAPES2 (GAmmaproteobacterial PEriplasmic Sensor) domain is a periplasmic sensor domain found in diguanylate cyclases, including the diguanylate cyclase DgcI (YliF) of Escherichia coli. It contains three conserved Cys residues that might participate in thiol-disulfide exchange.


The actual alignment was detected with superfamily member pfam17156:

Pssm-ID: 319174  Cd Length: 204  Bit Score: 422.55  E-value: 2.65e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446009065   26 IYTQMVKERVYSLKQSVIDTAFAVANIAEYRRSVAIDLINTLNPTEEQLLVGLRTAYADSVSPSYLYDVGPYLISSDECI 105
Cdd:pfam17156   1 IYTQMVKERVYSLKQSVIDTAFAVANIAEYRRSVAIDLINTLNPTEEQLLVGLRTAYADSVSPSYLYDVGPYLISSDECI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446009065  106 QVKEFEKNYCADIMQVVKYRHVKNTGFISFDGKTFVYYLYPVTHNRSLIFLLGLERFSLLSKSLVMDSENLMFSLFKNGK 185
Cdd:pfam17156  81 QVKEFEKNYCADIMQVVKYRHVKNTGFISFDGKTFVYYLYPVTHNRSLIFLLGLERFSLLSKSLAMDSENLMFSLFKNGK 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 446009065  186 PVTGDEYNAKNAIFTVSEAMEHFAYLPTGLYVFAYKKDVYLRVC 229
Cdd:pfam17156 161 PVTGDEYNAKNAIFTVSEAMEHFAYLPTGLYVFAYKKDVYLRVC 204
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 295-441 7.82e-40

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


:

Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 140.46  E-value: 7.82e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446009065   295 AFLDDLTKAMGRKSFDEDLKALPEKG------GYLCLFDVDKFKNINDTFGHLLGDEVLMKVVKILKSQIPvDKGKVYRF 368
Cdd:smart00267   3 AFRDPLTGLPNRRYFEEELEQELQRAqrqgspFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLR-PGDLLARL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446009065   369 GGDEFAVIYTGGTLEELLSILKEIVH-------FQVGSINLSTSIGVAH-SNECTTVERLKMLADERLYKSKKNGRAQIS 440
Cdd:smart00267  82 GGDEFALLLPETSLEEAIALAERILQqlrepiiIHGIPLYLTISIGVAAyPNPGEDAEDLLKRADTALYQAKKAGRNQVA 161


                   .
gi 446009065   441 W 441
Cdd:smart00267 162 V 162
 
Name Accession Description Interval E-value
GAPES2 pfam17156
Gammaproteobacterial periplasmic sensor domain; GAPES2 (GAmmaproteobacterial PEriplasmic ...
 26-229 2.65e-149

Gammaproteobacterial periplasmic sensor domain; GAPES2 (GAmmaproteobacterial PEriplasmic Sensor) domain is a periplasmic sensor domain found in diguanylate cyclases, including the diguanylate cyclase DgcI (YliF) of Escherichia coli. It contains three conserved Cys residues that might participate in thiol-disulfide exchange.


Pssm-ID: 319174  Cd Length: 204  Bit Score: 422.55  E-value: 2.65e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446009065   26 IYTQMVKERVYSLKQSVIDTAFAVANIAEYRRSVAIDLINTLNPTEEQLLVGLRTAYADSVSPSYLYDVGPYLISSDECI 105
Cdd:pfam17156   1 IYTQMVKERVYSLKQSVIDTAFAVANIAEYRRSVAIDLINTLNPTEEQLLVGLRTAYADSVSPSYLYDVGPYLISSDECI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446009065  106 QVKEFEKNYCADIMQVVKYRHVKNTGFISFDGKTFVYYLYPVTHNRSLIFLLGLERFSLLSKSLVMDSENLMFSLFKNGK 185
Cdd:pfam17156  81 QVKEFEKNYCADIMQVVKYRHVKNTGFISFDGKTFVYYLYPVTHNRSLIFLLGLERFSLLSKSLAMDSENLMFSLFKNGK 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 446009065  186 PVTGDEYNAKNAIFTVSEAMEHFAYLPTGLYVFAYKKDVYLRVC 229
Cdd:pfam17156 161 PVTGDEYNAKNAIFTVSEAMEHFAYLPTGLYVFAYKKDVYLRVC 204
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 295-441 7.82e-40

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 140.46  E-value: 7.82e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446009065   295 AFLDDLTKAMGRKSFDEDLKALPEKG------GYLCLFDVDKFKNINDTFGHLLGDEVLMKVVKILKSQIPvDKGKVYRF 368
Cdd:smart00267   3 AFRDPLTGLPNRRYFEEELEQELQRAqrqgspFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLR-PGDLLARL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446009065   369 GGDEFAVIYTGGTLEELLSILKEIVH-------FQVGSINLSTSIGVAH-SNECTTVERLKMLADERLYKSKKNGRAQIS 440
Cdd:smart00267  82 GGDEFALLLPETSLEEAIALAERILQqlrepiiIHGIPLYLTISIGVAAyPNPGEDAEDLLKRADTALYQAKKAGRNQVA 161


                   .
gi 446009065   441 W 441
Cdd:smart00267 162 V 162
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 298-439 1.01e-38

Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as a domain of unknown function 1 (DUF1). This domain is widely present in bacteria, linked to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain shows homology to the adenylyl cyclase catalytic domain. This correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesion in bacteria.


Pssm-ID: 143635 [Multi-domain]  Cd Length: 158  Bit Score: 137.30  E-value: 1.01e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446009065 298 DDLTKAMGRKSFDEDLKAL------PEKGGYLCLFDVDKFKNINDTFGHLLGDEVLMKVVKILKSQIPvDKGKVYRFGGD 371
Cdd:cd01949    3 DPLTGLPNRRAFEERLERLlararrSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLR-ESDLVARLGGD 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446009065 372 EFAVIYTGGTLEELLSILKEI-------VHFQVGSINLSTSIGVAHSNE-CTTVERLKMLADERLYKSKKNGRAQI 439
Cdd:cd01949   82 EFAILLPGTDLEEAEALAERLreaieepFFIDGQEIRVTASIGIATYPEdGEDAEELLRRADEALYRAKRSGRNRV 157
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 226-440 8.07e-36

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: 133.18  E-value: 8.07e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446009065 226 LRVCTLIIFFAALVAVILGASCLYLVRRVINRGIVEKEAIINNHFERVLDGGLFFSAADVKKLYS----MYNSAFLDDLT 301
Cdd:COG2199   41 LLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLLLLALEDITELRRleerLRRLATHDPLT 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446009065 302 KAMGRKSFDEDLKAL------PEKGGYLCLFDVDKFKNINDTFGHLLGDEVLMKVVKILKSQIPvDKGKVYRFGGDEFAV 375
Cdd:COG2199  121 GLPNRRAFEERLERElararrEGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLR-ESDLVARLGGDEFAV 199

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446009065 376 IYTGGTLEELLSILKEI--------VHFQVGSINLSTSIGVAHSNEC-TTVERLKMLADERLYKSKKNGRAQIS 440
Cdd:COG2199  200 LLPGTDLEEAEALAERLrealeqlpFELEGKELRVTVSIGVALYPEDgDSAEELLRRADLALYRAKRAGRNRVV 273
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 295-436 3.50e-30

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: 114.66  E-value: 3.50e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446009065  295 AFLDDLTKAMGRKSFDEDLKALPEKG------GYLCLFDVDKFKNINDTFGHLLGDEVLMKVVKILKSQIPvDKGKVYRF 368
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELQRAlregspVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLR-RSDLVARL 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446009065  369 GGDEFAVIYTGGTLEE----------LLSILKEIVHFQVGSINLSTSIGVAHS-NECTTVERLKMLADERLYKSKKNGR 436
Cdd:pfam00990  80 GGDEFAILLPETSLEGaqelaerirrLLAKLKIPHTVSGLPLYVTISIGIAAYpNDGEDPEDLLKRADTALYQAKQAGR 158
PRK09894 PRK09894
diguanylate cyclase; Provisional
 253-436 1.40e-24

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 102.84  E-value: 1.40e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446009065 253 RVINRGIVEKEaIINNHFERVLDGGLFFSAAdvkklYSMYNSAFL------DDLTKAMGRK----SFDEDLKALPEKGGY 322
Cdd:PRK09894  87 RELLLAIVEGH-WQDAHFDAFQEGLLSFTAA-----LTDYKIYLLtirsnmDVLTGLPGRRvldeSFDHQLRNREPQNLY 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446009065 323 LCLFDVDKFKNINDTFGHLLGDEVLMKVVKILKSQI-PVDkgKVYRFGGDEFAVIYTGGTLEELLSILKEI--------V 393
Cdd:PRK09894 161 LALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTrDYE--TVYRYGGEEFIICLKAATDEEACRAGERIrqlianhaI 238

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 446009065 394 HFQVGSINLSTSIGVAHSNECTTVERLKMLADERLYKSKKNGR 436
Cdd:PRK09894 239 THSDGRINITATFGVSRAFPEETLDVVIGRADRAMYEGKQTGR 281
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 295-436 2.16e-24

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: 98.95  E-value: 2.16e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446009065  295 AFLDDLTKAMGRKSFDEDLKALPEKG---GY---LCLFDVDKFKNINDTFGHLLGDEVLMKVVKILKSQIpvdKGK--VY 366
Cdd:TIGR00254   2 AVRDPLTGLYNRRYLEEMLDSELKRArrfQRsfsVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSV---RGSdvVG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446009065  367 RFGGDEFAVIYTGGTLEELLSIL---------KEIVHFQVGSINLSTSIGVAHS-NECTTVERLKMLADERLYKSKKNGR 436
Cdd:TIGR00254  79 RYGGEEFVVILPGTPLEDALSKAerlrdainsKPIEVAGSETLTVTVSIGVACYpGHGLTLEELLKRADEALYQAKKAGR 158
 
Name Accession Description Interval E-value
GAPES2 pfam17156
Gammaproteobacterial periplasmic sensor domain; GAPES2 (GAmmaproteobacterial PEriplasmic ...
 26-229 2.65e-149

Gammaproteobacterial periplasmic sensor domain; GAPES2 (GAmmaproteobacterial PEriplasmic Sensor) domain is a periplasmic sensor domain found in diguanylate cyclases, including the diguanylate cyclase DgcI (YliF) of Escherichia coli. It contains three conserved Cys residues that might participate in thiol-disulfide exchange.


Pssm-ID: 319174  Cd Length: 204  Bit Score: 422.55  E-value: 2.65e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446009065   26 IYTQMVKERVYSLKQSVIDTAFAVANIAEYRRSVAIDLINTLNPTEEQLLVGLRTAYADSVSPSYLYDVGPYLISSDECI 105
Cdd:pfam17156   1 IYTQMVKERVYSLKQSVIDTAFAVANIAEYRRSVAIDLINTLNPTEEQLLVGLRTAYADSVSPSYLYDVGPYLISSDECI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446009065  106 QVKEFEKNYCADIMQVVKYRHVKNTGFISFDGKTFVYYLYPVTHNRSLIFLLGLERFSLLSKSLVMDSENLMFSLFKNGK 185
Cdd:pfam17156  81 QVKEFEKNYCADIMQVVKYRHVKNTGFISFDGKTFVYYLYPVTHNRSLIFLLGLERFSLLSKSLAMDSENLMFSLFKNGK 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 446009065  186 PVTGDEYNAKNAIFTVSEAMEHFAYLPTGLYVFAYKKDVYLRVC 229
Cdd:pfam17156 161 PVTGDEYNAKNAIFTVSEAMEHFAYLPTGLYVFAYKKDVYLRVC 204
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 295-441 7.82e-40

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 140.46  E-value: 7.82e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446009065   295 AFLDDLTKAMGRKSFDEDLKALPEKG------GYLCLFDVDKFKNINDTFGHLLGDEVLMKVVKILKSQIPvDKGKVYRF 368
Cdd:smart00267   3 AFRDPLTGLPNRRYFEEELEQELQRAqrqgspFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLR-PGDLLARL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446009065   369 GGDEFAVIYTGGTLEELLSILKEIVH-------FQVGSINLSTSIGVAH-SNECTTVERLKMLADERLYKSKKNGRAQIS 440
Cdd:smart00267  82 GGDEFALLLPETSLEEAIALAERILQqlrepiiIHGIPLYLTISIGVAAyPNPGEDAEDLLKRADTALYQAKKAGRNQVA 161


                   .
gi 446009065   441 W 441
Cdd:smart00267 162 V 162
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 298-439 1.01e-38

Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as a domain of unknown function 1 (DUF1). This domain is widely present in bacteria, linked to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain shows homology to the adenylyl cyclase catalytic domain. This correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesion in bacteria.


Pssm-ID: 143635 [Multi-domain]  Cd Length: 158  Bit Score: 137.30  E-value: 1.01e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446009065 298 DDLTKAMGRKSFDEDLKAL------PEKGGYLCLFDVDKFKNINDTFGHLLGDEVLMKVVKILKSQIPvDKGKVYRFGGD 371
Cdd:cd01949    3 DPLTGLPNRRAFEERLERLlararrSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLR-ESDLVARLGGD 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446009065 372 EFAVIYTGGTLEELLSILKEI-------VHFQVGSINLSTSIGVAHSNE-CTTVERLKMLADERLYKSKKNGRAQI 439
Cdd:cd01949   82 EFAILLPGTDLEEAEALAERLreaieepFFIDGQEIRVTASIGIATYPEdGEDAEELLRRADEALYRAKRSGRNRV 157
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 226-440 8.07e-36

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: 133.18  E-value: 8.07e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446009065 226 LRVCTLIIFFAALVAVILGASCLYLVRRVINRGIVEKEAIINNHFERVLDGGLFFSAADVKKLYS----MYNSAFLDDLT 301
Cdd:COG2199   41 LLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLLLLALEDITELRRleerLRRLATHDPLT 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446009065 302 KAMGRKSFDEDLKAL------PEKGGYLCLFDVDKFKNINDTFGHLLGDEVLMKVVKILKSQIPvDKGKVYRFGGDEFAV 375
Cdd:COG2199  121 GLPNRRAFEERLERElararrEGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLR-ESDLVARLGGDEFAV 199

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446009065 376 IYTGGTLEELLSILKEI--------VHFQVGSINLSTSIGVAHSNEC-TTVERLKMLADERLYKSKKNGRAQIS 440
Cdd:COG2199  200 LLPGTDLEEAEALAERLrealeqlpFELEGKELRVTVSIGVALYPEDgDSAEELLRRADLALYRAKRAGRNRVV 273
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 295-436 3.50e-30

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: 114.66  E-value: 3.50e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446009065  295 AFLDDLTKAMGRKSFDEDLKALPEKG------GYLCLFDVDKFKNINDTFGHLLGDEVLMKVVKILKSQIPvDKGKVYRF 368
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELQRAlregspVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLR-RSDLVARL 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446009065  369 GGDEFAVIYTGGTLEE----------LLSILKEIVHFQVGSINLSTSIGVAHS-NECTTVERLKMLADERLYKSKKNGR 436
Cdd:pfam00990  80 GGDEFAILLPETSLEGaqelaerirrLLAKLKIPHTVSGLPLYVTISIGIAAYpNDGEDPEDLLKRADTALYQAKQAGR 158
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 295-441 9.46e-27

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: 113.33  E-value: 9.46e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446009065 295 AFLDDLTKAMGRKSFDEDLKAL------PEKGGYLCLFDVDKFKNINDTFGHLLGDEVLMKVVKILKSQIPvDKGKVYRF 368
Cdd:COG5001  251 AYHDPLTGLPNRRLFLDRLEQAlararrSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLR-EGDTVARL 329

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446009065 369 GGDEFAVIYTG-GTLEELLSILKEIVH-----FQVG--SINLSTSIGVAHSNE-CTTVERLKMLADERLYKSKKNGRAQI 439
Cdd:COG5001  330 GGDEFAVLLPDlDDPEDAEAVAERILAalaepFELDghELYVSASIGIALYPDdGADAEELLRNADLAMYRAKAAGRNRY 409


                 ..
gi 446009065 440 SW 441
Cdd:COG5001  410 RF 411
PRK09894 PRK09894
diguanylate cyclase; Provisional
 253-436 1.40e-24

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 102.84  E-value: 1.40e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446009065 253 RVINRGIVEKEaIINNHFERVLDGGLFFSAAdvkklYSMYNSAFL------DDLTKAMGRK----SFDEDLKALPEKGGY 322
Cdd:PRK09894  87 RELLLAIVEGH-WQDAHFDAFQEGLLSFTAA-----LTDYKIYLLtirsnmDVLTGLPGRRvldeSFDHQLRNREPQNLY 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446009065 323 LCLFDVDKFKNINDTFGHLLGDEVLMKVVKILKSQI-PVDkgKVYRFGGDEFAVIYTGGTLEELLSILKEI--------V 393
Cdd:PRK09894 161 LALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTrDYE--TVYRYGGEEFIICLKAATDEEACRAGERIrqlianhaI 238

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 446009065 394 HFQVGSINLSTSIGVAHSNECTTVERLKMLADERLYKSKKNGR 436
Cdd:PRK09894 239 THSDGRINITATFGVSRAFPEETLDVVIGRADRAMYEGKQTGR 281
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 295-436 2.16e-24

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: 98.95  E-value: 2.16e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446009065  295 AFLDDLTKAMGRKSFDEDLKALPEKG---GY---LCLFDVDKFKNINDTFGHLLGDEVLMKVVKILKSQIpvdKGK--VY 366
Cdd:TIGR00254   2 AVRDPLTGLYNRRYLEEMLDSELKRArrfQRsfsVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSV---RGSdvVG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446009065  367 RFGGDEFAVIYTGGTLEELLSIL---------KEIVHFQVGSINLSTSIGVAHS-NECTTVERLKMLADERLYKSKKNGR 436
Cdd:TIGR00254  79 RYGGEEFVVILPGTPLEDALSKAerlrdainsKPIEVAGSETLTVTVSIGVACYpGHGLTLEELLKRADEALYQAKKAGR 158
PRK15426 PRK15426
cellulose biosynthesis regulator YedQ;
327-441 1.09e-18

cellulose biosynthesis regulator YedQ;


Pssm-ID: 237964 [Multi-domain]  Cd Length: 570  Bit Score: 88.53  E-value: 1.09e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446009065 327 DVDKFKNINDTFGHLLGDEVLMKVVKILKSQI-PVDKGKvyRFGGDEFAVIYTGGTLEELLSI---------LKEIVHFQ 396
Cdd:PRK15426 436 DLDHFKSINDRFGHQAGDRVLSHAAGLISSSLrAQDVAG--RVGGEEFCVVLPGASLAEAAQVaerirlrinEKEILVAK 513

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 446009065 397 VGSINLSTSIGVAHS--NECTTVERLKMLADERLYKSKKNGRAQISW 441
Cdd:PRK15426 514 STTIRISASLGVSSAeeDGDYDFEQLQSLADRRLYLAKQAGRNRVCA 560
pleD PRK09581
response regulator PleD; Reviewed
 298-439 2.23e-18

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 86.88  E-value: 2.23e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446009065 298 DDLTKAMGRKSFDEDLKALPEKGG------YLCLFDVDKFKNINDTFGHLLGDEVLMKVVKILKSQIPV-DkgKVYRFGG 370
Cdd:PRK09581 295 DGLTGLHNRRYFDMHLKNLIERANergkplSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGtD--LIARYGG 372

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446009065 371 DEFAVIYTGGTLEELLSI---LKEIVH---FQVGS----INLSTSIGVAHSNECT-TVERLKMLADERLYKSKKNGRAQI 439
Cdd:PRK09581 373 EEFVVVMPDTDIEDAIAVaerIRRKIAeepFIISDgkerLNVTVSIGVAELRPSGdTIEALIKRADKALYEAKNTGRNRV 452
PRK09966 PRK09966
diguanylate cyclase DgcN;
182-432 4.27e-15

diguanylate cyclase DgcN;


Pssm-ID: 182171 [Multi-domain]  Cd Length: 407  Bit Score: 76.58  E-value: 4.27e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446009065 182 KNGKPVTGDEYNAKNAIFTVSEAMEHFAY-LPTGLYVFaYKKDVYLRVC-----TLIIFF-----AALVAVILGASCL-Y 249
Cdd:PRK09966  96 KQQNILASWHYTRKDPGDTFSNFISHWLFpAPIIQPIR-HNGETIGEVRltardSSISHFiwfslAVLTGCILLASGIaI 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446009065 250 LVRRVINRGIVEKEAII---------NNHF------ERVLDGGLFfsAADVKKLY---------------SMYNSAFLDD 299
Cdd:PRK09966 175 TLTRHLHNGLVEALKNItdvvhdvrsNRNFsrrvseERIAEFHRF--ALDFNSLLdemeewqlrlqaknaQLLRTALHDP 252

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446009065 300 LTKAMGRKSFDEDLKAL-----PEKGGYLCLFDVDKFKNINDTFGHLLGDEVLMKVVKILkSQIPVDKGKVYRFGGDEFA 374
Cdd:PRK09966 253 LTGLANRAAFRSGINTLmnnsdARKTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRL-AEFGGLRHKAYRLGGDEFA 331

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446009065 375 VIYTG----GTLEELLSILKEIVH--FQVGS---INLSTSIGVAHSNECTTVERLKMLADERLYKSK 432
Cdd:PRK09966 332 MVLYDvqseSEVQQICSALTQIFNlpFDLHNghqTTMTLSIGYAMTIEHASAEKLQELADHNMYQAK 398
adrA PRK10245
diguanylate cyclase AdrA; Provisional
 323-436 2.12e-13

diguanylate cyclase AdrA; Provisional


Pssm-ID: 182329 [Multi-domain]  Cd Length: 366  Bit Score: 71.01  E-value: 2.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446009065 323 LCLFDVDKFKNINDTFGHLLGDEVLMKVVKILksQIPVDKGKVY-RFGGDEFAVIYTGGTLE----------ELLSILK- 390
Cdd:PRK10245 239 LLIIDIDHFKSINDTWGHDVGDEAIVALTRQL--QITLRGSDVIgRFGGDEFAVIMSGTPAEsaitamsrvhEGLNTLRl 316

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446009065 391 -----EIVHFQVGSINLSTSIGvaHSNECttverLKMlADERLYKSKKNGR 436
Cdd:PRK10245 317 pnapqVTLRISVGVAPLNPQMS--HYREW-----LKS-ADLALYKAKNAGR 359
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
327-438 1.10e-11

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 66.63  E-value: 1.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446009065 327 DVDKFKNINDTFGHLLGDEVLMKVVKILKSQIPVDKgKVYRFGGDEFAVIYTGGTLEELLSILKEIVH-----FQVGSIN 401
Cdd:PRK10060 273 DLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQ-TLARLGGDEFLVLASHTSQAALEAMASRILTrlrlpFRIGLIE 351

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 446009065 402 LST--SIGVA----HSNECTTVERlkmLADERLYKSKKNGRAQ 438
Cdd:PRK10060 352 VYTgcSIGIAlapeHGDDSESLIR---SADTAMYTAKEGGRGQ 391
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 294-440 1.10e-11

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 67.00  E-value: 1.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446009065  294 SAFLDDLTKAMGRKSFDEDLKALPEKG------GYLCLFDVDKFKNINDTFGHLLGDEVLMKVVKILKSQI-PVDkgKVY 366
Cdd:PRK09776  664 SASHDALTHLANRASFEKQLRRLLQTVnsthqrHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLrSSD--VLA 741

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446009065  367 RFGGDEFAVIYTGGTLEELLSILKEIVH-------------FQVGSinlstSIGVA--HSNECTTVERLKMlADERLYKS 431
Cdd:PRK09776  742 RLGGDEFGLLLPDCNVESARFIATRIISaindyhfpwegrvYRVGA-----SAGITliDANNHQASEVMSQ-ADIACYAA 815


                  ....*....
gi 446009065  432 KKNGRAQIS 440
Cdd:PRK09776  816 KNAGRGRVT 824
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 325-411 1.07e-06

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 50.92  E-value: 1.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446009065 325 LFDVDKFKNINDTFGHLLGDEVLMKVVKILKSQIPVDKgKVYRFGGDEFAVIYTGGTL-------EELLSILKEIVHFQV 397
Cdd:PRK11359 408 LIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDQ-YLCRIEGTQFVLVSLENDVsnitqiaDELRNVVSKPIMIDD 486

                         90
                 ....*....|....
gi 446009065 398 GSINLSTSIGVAHS 411
Cdd:PRK11359 487 KPFPLTLSIGISYD 500
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
 325-410 7.15e-05

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: 42.34  E-value: 7.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446009065 325 LF-DVDKFKNINDTFGHLLGDEVLMKVVKILKSQIPVDKGKVYRFGGDEFAVIYTGGTLEELLSILKEIV-HF----QVG 398
Cdd:cd07556    5 LFaDIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSGDLKIKTIGDEFMVVSGLDHPAAAVAFAEDMReAVsalnQSE 84

                         90
                 ....*....|..
gi 446009065 399 SINLSTSIGVAH 410
Cdd:cd07556   85 GNPVRVRIGIHT 96
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 365-409 1.17e-03

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: 39.89  E-value: 1.17e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 446009065 365 VYRFGGDEFAVIYTGGTLEELLSILKEIVHF--QVGSINLSTSIGVA 409
Cdd:COG3706  118 VARYGGEEFAILLPGTDLEGALAVAERIREAvaELPSLRVTVSIGVA 164
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH