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Conserved domains on  [gi|1552986886|ref|WP_127454419|]
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MULTISPECIES: GGDEF domain-containing protein [Paenibacillus]

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 ...
 134-377 5.40e-50

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: 169.00  E-value: 5.40e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552986886 134 QVRLLQDIALELYVFVLIFLCFYMIPPYIGQQAKYQWALTVFFLIQTCHLINVYMYGNEQIWLTLAGNLLPIVFYFLLFI 213
Cdd:COG2199    15 LLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLLL 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552986886 214 LLFDRVVELMQA---IYNSSITDGLTRLYNRKFFYNRVSQYVGR----HLPISILFSDIDNFKKLNDTKGHQMGDDVLKQ 286
Cdd:COG2199    95 LALEDITELRRLeerLRRLATHDPLTGLPNRRAFEERLERELARarreGRPLALLLIDLDHFKRINDTYGHAAGDEVLKE 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552986886 287 VAQIMKEEAEECGIAGRYGGEEMVVMVTDPSVK-MDAFAERVRSRIEKETI--------VTASIGYSKY-KNGVSAEELI 356
Cdd:COG2199   175 VARRLRASLRESDLVARLGGDEFAVLLPGTDLEeAEALAERLREALEQLPFelegkelrVTVSIGVALYpEDGDSAEELL 254

                         250       260
                  ....*....|....*....|.
gi 1552986886 357 KQADEAMYRAKTTGKNKVVKY 377
Cdd:COG2199   255 RRADLALYRAKRAGRNRVVVY 275
 
Name Accession Description Interval E-value
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 134-377 5.40e-50

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: 169.00  E-value: 5.40e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552986886 134 QVRLLQDIALELYVFVLIFLCFYMIPPYIGQQAKYQWALTVFFLIQTCHLINVYMYGNEQIWLTLAGNLLPIVFYFLLFI 213
Cdd:COG2199    15 LLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLLL 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552986886 214 LLFDRVVELMQA---IYNSSITDGLTRLYNRKFFYNRVSQYVGR----HLPISILFSDIDNFKKLNDTKGHQMGDDVLKQ 286
Cdd:COG2199    95 LALEDITELRRLeerLRRLATHDPLTGLPNRRAFEERLERELARarreGRPLALLLIDLDHFKRINDTYGHAAGDEVLKE 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552986886 287 VAQIMKEEAEECGIAGRYGGEEMVVMVTDPSVK-MDAFAERVRSRIEKETI--------VTASIGYSKY-KNGVSAEELI 356
Cdd:COG2199   175 VARRLRASLRESDLVARLGGDEFAVLLPGTDLEeAEALAERLREALEQLPFelegkelrVTVSIGVALYpEDGDSAEELL 254

                         250       260
                  ....*....|....*....|.
gi 1552986886 357 KQADEAMYRAKTTGKNKVVKY 377
Cdd:COG2199   255 RRADLALYRAKRAGRNRVVVY 275
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 232-375 1.88e-49

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: 163.88  E-value: 1.88e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552986886 232 TDGLTRLYNRKFFYNRVSQYVGRHL----PISILFSDIDNFKKLNDTKGHQMGDDVLKQVAQIMKEEAEECGIAGRYGGE 307
Cdd:cd01949     2 TDPLTGLPNRRAFEERLERLLARARrsgrPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGD 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1552986886 308 EMVVMVTDPSVK-MDAFAERVRSRIEKETI-------VTASIGYSKYK-NGVSAEELIKQADEAMYRAKTTGKNKVV 375
Cdd:cd01949    82 EFAILLPGTDLEeAEALAERLREAIEEPFFidgqeirVTASIGIATYPeDGEDAEELLRRADEALYRAKRSGRNRVV 158
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 230-373 3.34e-44

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: 150.10  E-value: 3.34e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552986886 230 SITDGLTRLYNRKFFYNRVSQ----YVGRHLPISILFSDIDNFKKLNDTKGHQMGDDVLKQVAQIMKEEAEECGIAGRYG 305
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQelqrALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552986886 306 GEEMVVMVTDPSVKM-DAFAERVRSRIEK----------ETIVTASIGYSKYKN-GVSAEELIKQADEAMYRAKTTGKNK 373
Cdd:pfam00990  81 GDEFAILLPETSLEGaQELAERIRRLLAKlkiphtvsglPLYVTISIGIAAYPNdGEDPEDLLKRADTALYQAKQAGRNR 160
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 230-375 3.94e-43

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: 147.48  E-value: 3.94e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552986886 230 SITDGLTRLYNRKFFYNRVSQYVGR----HLPISILFSDIDNFKKLNDTKGHQMGDDVLKQVAQIMKEEAEECGIAGRYG 305
Cdd:TIGR00254   2 AVRDPLTGLYNRRYLEEMLDSELKRarrfQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552986886 306 GEEMVVMVTDPSVKmDAF--AERVRSRIEKETI---------VTASIGYSKYKN-GVSAEELIKQADEAMYRAKTTGKNK 373
Cdd:TIGR00254  82 GEEFVVILPGTPLE-DALskAERLRDAINSKPIevagsetltVTVSIGVACYPGhGLTLEELLKRADEALYQAKKAGRNR 160


                  ..
gi 1552986886 374 VV 375
Cdd:TIGR00254 161 VV 162
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 230-377 8.25e-42

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 143.93  E-value: 8.25e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552986886  230 SITDGLTRLYNRKFFYNRVSQYVGRHL----PISILFSDIDNFKKLNDTKGHQMGDDVLKQVAQIMKEEAEECGIAGRYG 305
Cdd:smart00267   3 AFRDPLTGLPNRRYFEEELEQELQRAQrqgsPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARLG 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552986886  306 GEEMVVMVTDPSVK-MDAFAERVRSRIEKETI-------VTASIGYSKYKNGV-SAEELIKQADEAMYRAKTTGKNKVVK 376
Cdd:smart00267  83 GDEFALLLPETSLEeAIALAERILQQLREPIIihgiplyLTISIGVAAYPNPGeDAEDLLKRADTALYQAKKAGRNQVAV 162


                   .
gi 1552986886  377 Y 377
Cdd:smart00267 163 Y 163
pleD PRK09581
response regulator PleD; Reviewed
 230-378 6.78e-41

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 149.67  E-value: 6.78e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552986886 230 SITDGLTRLYNRKFFYNRVSQYVGRHL----PISILFSDIDNFKKLNDTKGHQMGDDVLKQVAQIMKEEAEECGIAGRYG 305
Cdd:PRK09581  292 AVTDGLTGLHNRRYFDMHLKNLIERANergkPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARYG 371

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552986886 306 GEEMVVMVTDPSVKmDAF--AERVRSRIEKETI----------VTASIGYSKYKNGV-SAEELIKQADEAMYRAKTTGKN 372
Cdd:PRK09581  372 GEEFVVVMPDTDIE-DAIavAERIRRKIAEEPFiisdgkerlnVTVSIGVAELRPSGdTIEALIKRADKALYEAKNTGRN 450


                  ....*.
gi 1552986886 373 KVVKYA 378
Cdd:PRK09581  451 RVVALA 456
 
Name Accession Description Interval E-value
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 134-377 5.40e-50

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: 169.00  E-value: 5.40e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552986886 134 QVRLLQDIALELYVFVLIFLCFYMIPPYIGQQAKYQWALTVFFLIQTCHLINVYMYGNEQIWLTLAGNLLPIVFYFLLFI 213
Cdd:COG2199    15 LLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLLL 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552986886 214 LLFDRVVELMQA---IYNSSITDGLTRLYNRKFFYNRVSQYVGR----HLPISILFSDIDNFKKLNDTKGHQMGDDVLKQ 286
Cdd:COG2199    95 LALEDITELRRLeerLRRLATHDPLTGLPNRRAFEERLERELARarreGRPLALLLIDLDHFKRINDTYGHAAGDEVLKE 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552986886 287 VAQIMKEEAEECGIAGRYGGEEMVVMVTDPSVK-MDAFAERVRSRIEKETI--------VTASIGYSKY-KNGVSAEELI 356
Cdd:COG2199   175 VARRLRASLRESDLVARLGGDEFAVLLPGTDLEeAEALAERLREALEQLPFelegkelrVTVSIGVALYpEDGDSAEELL 254

                         250       260
                  ....*....|....*....|.
gi 1552986886 357 KQADEAMYRAKTTGKNKVVKY 377
Cdd:COG2199   255 RRADLALYRAKRAGRNRVVVY 275
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 232-375 1.88e-49

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: 163.88  E-value: 1.88e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552986886 232 TDGLTRLYNRKFFYNRVSQYVGRHL----PISILFSDIDNFKKLNDTKGHQMGDDVLKQVAQIMKEEAEECGIAGRYGGE 307
Cdd:cd01949     2 TDPLTGLPNRRAFEERLERLLARARrsgrPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGD 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1552986886 308 EMVVMVTDPSVK-MDAFAERVRSRIEKETI-------VTASIGYSKYK-NGVSAEELIKQADEAMYRAKTTGKNKVV 375
Cdd:cd01949    82 EFAILLPGTDLEeAEALAERLREAIEEPFFidgqeirVTASIGIATYPeDGEDAEELLRRADEALYRAKRSGRNRVV 158
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 230-373 3.34e-44

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: 150.10  E-value: 3.34e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552986886 230 SITDGLTRLYNRKFFYNRVSQ----YVGRHLPISILFSDIDNFKKLNDTKGHQMGDDVLKQVAQIMKEEAEECGIAGRYG 305
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQelqrALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552986886 306 GEEMVVMVTDPSVKM-DAFAERVRSRIEK----------ETIVTASIGYSKYKN-GVSAEELIKQADEAMYRAKTTGKNK 373
Cdd:pfam00990  81 GDEFAILLPETSLEGaQELAERIRRLLAKlkiphtvsglPLYVTISIGIAAYPNdGEDPEDLLKRADTALYQAKQAGRNR 160
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 230-375 3.94e-43

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: 147.48  E-value: 3.94e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552986886 230 SITDGLTRLYNRKFFYNRVSQYVGR----HLPISILFSDIDNFKKLNDTKGHQMGDDVLKQVAQIMKEEAEECGIAGRYG 305
Cdd:TIGR00254   2 AVRDPLTGLYNRRYLEEMLDSELKRarrfQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552986886 306 GEEMVVMVTDPSVKmDAF--AERVRSRIEKETI---------VTASIGYSKYKN-GVSAEELIKQADEAMYRAKTTGKNK 373
Cdd:TIGR00254  82 GEEFVVILPGTPLE-DALskAERLRDAINSKPIevagsetltVTVSIGVACYPGhGLTLEELLKRADEALYQAKKAGRNR 160


                  ..
gi 1552986886 374 VV 375
Cdd:TIGR00254 161 VV 162
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 230-377 8.25e-42

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 143.93  E-value: 8.25e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552986886  230 SITDGLTRLYNRKFFYNRVSQYVGRHL----PISILFSDIDNFKKLNDTKGHQMGDDVLKQVAQIMKEEAEECGIAGRYG 305
Cdd:smart00267   3 AFRDPLTGLPNRRYFEEELEQELQRAQrqgsPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARLG 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552986886  306 GEEMVVMVTDPSVK-MDAFAERVRSRIEKETI-------VTASIGYSKYKNGV-SAEELIKQADEAMYRAKTTGKNKVVK 376
Cdd:smart00267  83 GDEFALLLPETSLEeAIALAERILQQLREPIIihgiplyLTISIGVAAYPNPGeDAEDLLKRADTALYQAKKAGRNQVAV 162


                   .
gi 1552986886  377 Y 377
Cdd:smart00267 163 Y 163
pleD PRK09581
response regulator PleD; Reviewed
 230-378 6.78e-41

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 149.67  E-value: 6.78e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552986886 230 SITDGLTRLYNRKFFYNRVSQYVGRHL----PISILFSDIDNFKKLNDTKGHQMGDDVLKQVAQIMKEEAEECGIAGRYG 305
Cdd:PRK09581  292 AVTDGLTGLHNRRYFDMHLKNLIERANergkPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARYG 371

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552986886 306 GEEMVVMVTDPSVKmDAF--AERVRSRIEKETI----------VTASIGYSKYKNGV-SAEELIKQADEAMYRAKTTGKN 372
Cdd:PRK09581  372 GEEFVVVMPDTDIE-DAIavAERIRRKIAEEPFiisdgkerlnVTVSIGVAELRPSGdTIEALIKRADKALYEAKNTGRN 450


                  ....*.
gi 1552986886 373 KVVKYA 378
Cdd:PRK09581  451 RVVALA 456
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 192-377 6.41e-37

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


Pssm-ID: 444025 [Multi-domain]  Cd Length: 678  Bit Score: 141.45  E-value: 6.41e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552986886 192 EQIWLTLAGNLLPIVFYFLLFILLFDRVVELMQA---IYNSSITDGLTRLYNRKFFYNRVSQYVGR----HLPISILFSD 264
Cdd:COG5001   210 LRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAeerLRHLAYHDPLTGLPNRRLFLDRLEQALARarrsGRRLALLFID 289

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552986886 265 IDNFKKLNDTKGHQMGDDVLKQVAQIMKEEAEECGIAGRYGGEEMVVMVTDPS--VKMDAFAERVRSRIEK-------ET 335
Cdd:COG5001   290 LDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVLLPDLDdpEDAEAVAERILAALAEpfeldghEL 369

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1552986886 336 IVTASIGYSKY-KNGVSAEELIKQADEAMYRAKTTGKNKVVKY 377
Cdd:COG5001   370 YVSASIGIALYpDDGADAEELLRNADLAMYRAKAAGRNRYRFF 412
PRK15426 PRK15426
cellulose biosynthesis regulator YedQ;
232-375 9.13e-25

cellulose biosynthesis regulator YedQ;


Pssm-ID: 237964 [Multi-domain]  Cd Length: 570  Bit Score: 105.87  E-value: 9.13e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552986886 232 TDGLTRLYNRKFFYNRVSQYVGR----HLPISILFSDIDNFKKLNDTKGHQMGDDVLKQVAQIMKEEAEECGIAGRYGGE 307
Cdd:PRK15426  400 HDPLTRLYNRGALFEKARALAKRcqrdQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRVGGE 479

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552986886 308 EM-VVMVTDPSVKMDAFAERVRSRIEKETI---------VTASIGYSKYKNGV--SAEELIKQADEAMYRAKTTGKNKVV 375
Cdd:PRK15426  480 EFcVVLPGASLAEAAQVAERIRLRINEKEIlvaksttirISASLGVSSAEEDGdyDFEQLQSLADRRLYLAKQAGRNRVC 559
PRK09894 PRK09894
diguanylate cyclase; Provisional
 233-377 6.76e-23

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 97.44  E-value: 6.76e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552986886 233 DGLTRLYNRKFFYNRV-SQYVGRH-LPISILFSDIDNFKKLNDTKGHQMGDDVLKQVAQIMKEEAEECGIAGRYGGEEMV 310
Cdd:PRK09894  132 DVLTGLPGRRVLDESFdHQLRNREpQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGGEEFI 211

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1552986886 311 VMVTDPS-VKMDAFAERVRSRIEKETI--------VTASIGYSKYKNGVSAEELIKQADEAMYRAKTTGKNKVVKY 377
Cdd:PRK09894  212 ICLKAATdEEACRAGERIRQLIANHAIthsdgrinITATFGVSRAFPEETLDVVIGRADRAMYEGKQTGRNRVMFI 287
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
232-373 6.73e-20

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 91.28  E-value: 6.73e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552986886 232 TDGLTRLYNRKFFYNRVSQYVGRHLP--ISILFSDIDNFKKLNDTKGHQMGDDVLKQVAQIMKEEAEECGIAGRYGGEEM 309
Cdd:PRK10060  239 TDSITGLPNRNAIQELIDHAINAADNnqVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQTLARLGGDEF 318

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1552986886 310 VVMVTDPSVK-MDAFAERVRSRIEK-------ETIVTASIGYSKY-KNGVSAEELIKQADEAMYRAKTTGKNK 373
Cdd:PRK10060  319 LVLASHTSQAaLEAMASRILTRLRLpfrigliEVYTGCSIGIALApEHGDDSESLIRSADTAMYTAKEGGRGQ 391
adrA PRK10245
diguanylate cyclase AdrA; Provisional
 218-373 1.26e-14

diguanylate cyclase AdrA; Provisional


Pssm-ID: 182329 [Multi-domain]  Cd Length: 366  Bit Score: 74.48  E-value: 1.26e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552986886 218 RVVELMqaiynsSITDGLTRLYNRK----FFYNRVSQYVGRHLPISILFSDIDNFKKLNDTKGHQMGDDVLKQVAQIMKE 293
Cdd:PRK10245  199 RRLQVM------STRDGMTGVYNRRhwetLLRNEFDNCRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQI 272

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552986886 294 EAEECGIAGRYGGEEM-VVMVTDPSVKMDAFAERVRSRIEK-------ETIVTASIGYSKYKNGVSA-EELIKQADEAMY 364
Cdd:PRK10245  273 TLRGSDVIGRFGGDEFaVIMSGTPAESAITAMSRVHEGLNTlrlpnapQVTLRISVGVAPLNPQMSHyREWLKSADLALY 352


                  ....*....
gi 1552986886 365 RAKTTGKNK 373
Cdd:PRK10245  353 KAKNAGRNR 361
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 229-377 6.38e-14

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 73.55  E-value: 6.38e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552986886  229 SSITDGLTRLYNRKFFYNRV----SQYVGRHLPISILFSDIDNFKKLNDTKGHQMGDDVLKQVAQIMKEEAEECGIAGRY 304
Cdd:PRK09776   664 SASHDALTHLANRASFEKQLrrllQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSDVLARL 743

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552986886  305 GGEEMVVMVTDPSVkmdAFAERVRSRIeKETI-------------VTASIGYSKYKNGV-SAEELIKQADEAMYRAKTTG 370
Cdd:PRK09776   744 GGDEFGLLLPDCNV---ESARFIATRI-ISAIndyhfpwegrvyrVGASAGITLIDANNhQASEVMSQADIACYAAKNAG 819


                   ....*..
gi 1552986886  371 KNKVVKY 377
Cdd:PRK09776   820 RGRVTVY 826
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
 257-367 1.52e-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: 67.00  E-value: 1.52e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552986886 257 PISILFSDIDNFKKLNDTKGHQMGDDVLKQVAQIMKEEAEECG-IAGRYGGEE-MVVM-VTDPSVkMDAFAERVRSRIEK 333
Cdd:cd07556     1 PVTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSGdLKIKTIGDEfMVVSgLDHPAA-AVAFAEDMREAVSA 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1552986886 334 ETI-----VTASIG-----------YSKYKNGVsAEELIKQADEAMYRAK 367
Cdd:cd07556    80 LNQsegnpVRVRIGihtgpvvvgviGSRPQYDV-WGALVNLASRMESQAK 128
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 218-370 1.64e-12

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 69.03  E-value: 1.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552986886 218 RVVELMQaiynssiTDGLTRLYNRKFFYNRVSQYVGRHLPISILFSDIDNFKKLNDTKGHQMGDDVLKQVAQIMKEEAEE 297
Cdd:PRK11359  371 HIEQLIQ-------FDPLTGLPNRNNLHNYLDDLVDKAVSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKP 443

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552986886 298 CGIAGRYGGEEMVVMVTDPSV-KMDAFAERVRSRIEKETIV-------TASIGYSkYKNGVSAEELIKQADEAM-YRAKT 368
Cdd:PRK11359  444 DQYLCRIEGTQFVLVSLENDVsNITQIADELRNVVSKPIMIddkpfplTLSIGIS-YDVGKNRDYLLSTAHNAMdYIRKN 522


                  ..
gi 1552986886 369 TG 370
Cdd:PRK11359  523 GG 524
PRK09966 PRK09966
diguanylate cyclase DgcN;
229-376 2.42e-12

diguanylate cyclase DgcN;


Pssm-ID: 182171 [Multi-domain]  Cd Length: 407  Bit Score: 67.72  E-value: 2.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552986886 229 SSITDGLTRLYNRKFFYNRVSQYVGRHLPIS---ILFSDIDNFKKLNDTKGHQMGDDVLKQVAQIMKEEAEECGIAGRYG 305
Cdd:PRK09966  247 TALHDPLTGLANRAAFRSGINTLMNNSDARKtsaLLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHKAYRLG 326

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552986886 306 GEEMVVMVTDpsVKMDAFAERVRSRIEKE------------TIVTASIGYSKYKNGVSAEELIKQADEAMYRAKTTGKNK 373
Cdd:PRK09966  327 GDEFAMVLYD--VQSESEVQQICSALTQIfnlpfdlhnghqTTMTLSIGYAMTIEHASAEKLQELADHNMYQAKHQRAEK 404


                  ...
gi 1552986886 374 VVK 376
Cdd:PRK09966  405 LVR 407
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 300-367 8.69e-09

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: 54.53  E-value: 8.69e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1552986886 300 IAGRYGGEEMVVMVTDPSVK-MDAFAERVRSRIEK--ETIVTASIgyskyknGVSAEELIKQADeAMYRAK 367
Cdd:COG3706   117 LVARYGGEEFAILLPGTDLEgALAVAERIREAVAElpSLRVTVSI-------GVAGDSLLKRAD-ALYQAR 179
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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