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Conserved domains on  [gi|757754641|ref|WP_042975675|]
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diguanylate cyclase [Bacillus subtilis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 425-571 2.56e-54

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: 181.30  E-value: 2.56e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757754641  425 TDQLTELYSRAYLDEK----IQYSMKIHQKGVFILVDIDNFKNVNDTYGHQTGDEILIQVASVIKSNIRKHDVGARWGGE 500
Cdd:pfam00990   3 HDPLTGLPNRRYFEEQleqeLQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLGGD 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 757754641  501 ELAIYLPNVPVAVGKRITERLVYAVRKNTKP--------EVTISCGISCWTTETkKSLKELVHEADEALYSAKRSGKNR 571
Cdd:pfam00990  83 EFAILLPETSLEGAQELAERIRRLLAKLKIPhtvsglplYVTISIGIAAYPNDG-EDPEDLLKRADTALYQAKQAGRNR 160
GAF COG2203
GAF domain [Signal transduction mechanisms];
202-526 1.79e-09

GAF domain [Signal transduction mechanisms];


:

Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 60.59  E-value: 1.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757754641 202 ILRKNESAAYIPIKGQQGTYGVLKAEGTGDSFLADACLDEMSLLANAAGKAFENAQLYEQSKASIAN-LELINETSRRLN 280
Cdd:COG2203  124 ALAARLLDLLLLGLGGRLRGVVLRGLRSAALLLSRVDTDLVGQLAALAGLILDIARLLTQRARLELErLALLNEISQALR 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757754641 281 QRLTLTDTMNDLAVRMAESFQAEEVGFFHIDHfENLTLLPGSTAFFKEAKPSDFYNE---LKEKLYEGE---------KG 348
Cdd:COG2203  204 SALDLEELLQRILELAGELLGADRGAILLVDE-DGGELELVAAPGLPEEELGRLPLGeglAGRALRTGEpvvvndastDP 282

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757754641 349 VFIGNGQSVFGKAGYGSLMAAPMIQNDRLLGFAVLLKQELYAFTFEMYKLFQALIHHATLAVTNS------------MLR 416
Cdd:COG2203  283 RFAPSLRELLLALGIRSLLCVPLLVDGRLIGVLALYSKEPRAFTEEDLELLEALADQAAIAIERArlyealeaalaaLLQ 362

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757754641 417 DRLEHLVKTDQLTELYSRAYLDEKIQYSMKIHQKG----VFILVDIDNFKNVNDTYGHQTGDEILIQVASVIKSNIRKHD 492
Cdd:COG2203  363 ELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLlgaeLLLLLLDAADLSGLLALEGLLLLDLLLLLLLLRRILLLRVL 442

                        330       340       350
                 ....*....|....*....|....*....|....
gi 757754641 493 VGARWGGEELAIYLPNVPVAVGKRITERLVYAVR 526
Cdd:COG2203  443 RRLLLGDEEGLVLLLALAELELLEILELLVLLAV 476
 
Name Accession Description Interval E-value
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 425-571 2.56e-54

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: 181.30  E-value: 2.56e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757754641  425 TDQLTELYSRAYLDEK----IQYSMKIHQKGVFILVDIDNFKNVNDTYGHQTGDEILIQVASVIKSNIRKHDVGARWGGE 500
Cdd:pfam00990   3 HDPLTGLPNRRYFEEQleqeLQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLGGD 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 757754641  501 ELAIYLPNVPVAVGKRITERLVYAVRKNTKP--------EVTISCGISCWTTETkKSLKELVHEADEALYSAKRSGKNR 571
Cdd:pfam00990  83 EFAILLPETSLEGAQELAERIRRLLAKLKIPhtvsglplYVTISIGIAAYPNDG-EDPEDLLKRADTALYQAKQAGRNR 160
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 363-575 3.74e-51

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: 177.09  E-value: 3.74e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757754641 363 YGSLMAAPMIQNDRLLGFAVLLKQELYAFTFEMYKLFQALIHHATLAVTNSMLR---DRLEHLVKTDQLTELYSRAYLDE 439
Cdd:COG2199   51 LLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLLLLALEDITELRrleERLRRLATHDPLTGLPNRRAFEE 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757754641 440 K----IQYSMKIHQKGVFILVDIDNFKNVNDTYGHQTGDEILIQVASVIKSNIRKHDVGARWGGEELAIYLPNVPVAVGK 515
Cdd:COG2199  131 RlereLARARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAE 210

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 757754641 516 RITERLVYAVRK------NTKPEVTISCGISCWtTETKKSLKELVHEADEALYSAKRSGKNRLMVH 575
Cdd:COG2199  211 ALAERLREALEQlpfeleGKELRVTVSIGVALY-PEDGDSAEELLRRADLALYRAKRAGRNRVVVY 275
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 421-575 3.31e-49

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 167.81  E-value: 3.31e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757754641   421 HLVKTDQLTELYSRAYLDE--KIQYSMKIHQKGVF--ILVDIDNFKNVNDTYGHQTGDEILIQVASVIKSNIRKHDVGAR 496
Cdd:smart00267   1 RLAFRDPLTGLPNRRYFEEelEQELQRAQRQGSPFalLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757754641   497 WGGEELAIYLPNVPVAVGKRITERLVYAVRKNTKPE-----VTISCGISCWTTETkKSLKELVHEADEALYSAKRSGKNR 571
Cdd:smart00267  81 LGGDEFALLLPETSLEEAIALAERILQQLREPIIIHgiplyLTISIGVAAYPNPG-EDAEDLLKRADTALYQAKKAGRNQ 159


                   ....
gi 757754641   572 LMVH 575
Cdd:smart00267 160 VAVY 163
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 425-571 7.91e-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: 166.58  E-value: 7.91e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757754641 425 TDQLTELYSRAYLDEKIQYSMKI----HQKGVFILVDIDNFKNVNDTYGHQTGDEILIQVASVIKSNIRKHDVGARWGGE 500
Cdd:cd01949    2 TDPLTGLPNRRAFEERLERLLARarrsGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGD 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 757754641 501 ELAIYLPNVPVAVGKRITERLVYAVRK-----NTKPEVTISCGISCWtTETKKSLKELVHEADEALYSAKRSGKNR 571
Cdd:cd01949   82 EFAILLPGTDLEEAEALAERLREAIEEpffidGQEIRVTASIGIATY-PEDGEDAEELLRRADEALYRAKRSGRNR 156
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 425-576 1.35e-39

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: 142.09  E-value: 1.35e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757754641  425 TDQLTELYSRAYLDEKIQYSMKI---HQKGV-FILVDIDNFKNVNDTYGHQTGDEILIQVASVIKSNIRKHDVGARWGGE 500
Cdd:TIGR00254   4 RDPLTGLYNRRYLEEMLDSELKRarrFQRSFsVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYGGE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757754641  501 ELAIYLPNVPVAVGKRITERLVYA-------VRKNTKPEVTISCGISCwTTETKKSLKELVHEADEALYSAKRSGKNRLM 573
Cdd:TIGR00254  84 EFVVILPGTPLEDALSKAERLRDAinskpieVAGSETLTVTVSIGVAC-YPGHGLTLEELLKRADEALYQAKKAGRNRVV 162


                  ...
gi 757754641  574 VHD 576
Cdd:TIGR00254 163 VAD 165
diguan_SiaD NF038266
biofilm regulation diguanylate cyclase SiaD;
413-572 9.98e-36

biofilm regulation diguanylate cyclase SiaD;


Pssm-ID: 468439 [Multi-domain]  Cd Length: 252  Bit Score: 134.34  E-value: 9.98e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757754641 413 SMLRD---RLEHLVKTDQLTELYSRAYLDEKIQYSMKIHQKG----VFILVDIDNFKNVNDTYGHQTGDEILIQVASVIK 485
Cdd:NF038266  81 RMMRDlneALREASTRDPLTGLPNRRLLMERLREEVERARRSgrpfTLAMLDVDHFKRINDRYGHEVGDRVLVEIARTLR 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757754641 486 SNIRKHDVGARWGGEELAIYLPNVPVAVGKRITERLVYAVR------KNTKPEVTISCGISCWTTETkKSLKELVHEADE 559
Cdd:NF038266 161 AELREYDLCGRWGGEEFLLLLPETGLEEAQVVLERLREAVRalavrvGDDVLSVTASAGLAEHRPPE-EGLSATLSRADQ 239

                        170
                 ....*....|...
gi 757754641 560 ALYSAKRSGKNRL 572
Cdd:NF038266 240 ALYQAKRAGRDRV 252
pleD PRK09581
response regulator PleD; Reviewed
 415-571 2.53e-35

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 138.50  E-value: 2.53e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757754641 415 LRDRLEHLVK---TDQLTELYSRAYLDEKIQY----SMKIHQKGVFILVDIDNFKNVNDTYGHQTGDEILIQVASVIKSN 487
Cdd:PRK09581 281 LRNNLEQSIEmavTDGLTGLHNRRYFDMHLKNlierANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNN 360

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757754641 488 IRKHDVGARWGGEELAIYLPNVPVAVGKRITERLVYAVRK--------NTKPEVTISCGIScwttETKK---SLKELVHE 556
Cdd:PRK09581 361 IRGTDLIARYGGEEFVVVMPDTDIEDAIAVAERIRRKIAEepfiisdgKERLNVTVSIGVA----ELRPsgdTIEALIKR 436

                        170
                 ....*....|....*
gi 757754641 557 ADEALYSAKRSGKNR 571
Cdd:PRK09581 437 ADKALYEAKNTGRNR 451
GAF COG2203
GAF domain [Signal transduction mechanisms];
202-526 1.79e-09

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 60.59  E-value: 1.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757754641 202 ILRKNESAAYIPIKGQQGTYGVLKAEGTGDSFLADACLDEMSLLANAAGKAFENAQLYEQSKASIAN-LELINETSRRLN 280
Cdd:COG2203  124 ALAARLLDLLLLGLGGRLRGVVLRGLRSAALLLSRVDTDLVGQLAALAGLILDIARLLTQRARLELErLALLNEISQALR 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757754641 281 QRLTLTDTMNDLAVRMAESFQAEEVGFFHIDHfENLTLLPGSTAFFKEAKPSDFYNE---LKEKLYEGE---------KG 348
Cdd:COG2203  204 SALDLEELLQRILELAGELLGADRGAILLVDE-DGGELELVAAPGLPEEELGRLPLGeglAGRALRTGEpvvvndastDP 282

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757754641 349 VFIGNGQSVFGKAGYGSLMAAPMIQNDRLLGFAVLLKQELYAFTFEMYKLFQALIHHATLAVTNS------------MLR 416
Cdd:COG2203  283 RFAPSLRELLLALGIRSLLCVPLLVDGRLIGVLALYSKEPRAFTEEDLELLEALADQAAIAIERArlyealeaalaaLLQ 362

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757754641 417 DRLEHLVKTDQLTELYSRAYLDEKIQYSMKIHQKG----VFILVDIDNFKNVNDTYGHQTGDEILIQVASVIKSNIRKHD 492
Cdd:COG2203  363 ELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLlgaeLLLLLLDAADLSGLLALEGLLLLDLLLLLLLLRRILLLRVL 442

                        330       340       350
                 ....*....|....*....|....*....|....
gi 757754641 493 VGARWGGEELAIYLPNVPVAVGKRITERLVYAVR 526
Cdd:COG2203  443 RRLLLGDEEGLVLLLALAELELLEILELLVLLAV 476
GAF_2 pfam13185
GAF domain; The GAF domain is named after some of the proteins it is found in, including ...
 283-410 2.61e-04

GAF domain; The GAF domain is named after some of the proteins it is found in, including cGMP-specific phosphodiesterases, adenylyl cyclases and FhlA. It is also found in guanylyl cyclases and phytochromes. The structure of a GAF domain shows that the domain shares a similar fold with the PAS domain. This domain can bind O2, CO and NO (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 433019 [Multi-domain]  Cd Length: 137  Bit Score: 41.30  E-value: 2.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757754641  283 LTLTDTMnDLAVRMAESFQAEEVGFFHIDHFENLTLLPGSTAFFKEAKPSDFYNE--LKEKLYEGEKgVFIGN------- 353
Cdd:pfam13185   2 ADLEELL-DAVLEAAVELGASAVGFILLVDDDGRLAAWGGAADELSAALDDPPGEglVGEALRTGRP-VIVNDlaadpak 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 757754641  354 GQSVFGKAGYGSLMAAPMIQNDRLLGFAVLLKQELYAFTFEMYKLFQALIHHATLAV 410
Cdd:pfam13185  80 KGLPAGHAGLRSFLSVPLVSGGRVVGVLALGSNRPGAFDEEDLELLELLAEQAAIAI 136
 
Name Accession Description Interval E-value
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 425-571 2.56e-54

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: 181.30  E-value: 2.56e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757754641  425 TDQLTELYSRAYLDEK----IQYSMKIHQKGVFILVDIDNFKNVNDTYGHQTGDEILIQVASVIKSNIRKHDVGARWGGE 500
Cdd:pfam00990   3 HDPLTGLPNRRYFEEQleqeLQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLGGD 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 757754641  501 ELAIYLPNVPVAVGKRITERLVYAVRKNTKP--------EVTISCGISCWTTETkKSLKELVHEADEALYSAKRSGKNR 571
Cdd:pfam00990  83 EFAILLPETSLEGAQELAERIRRLLAKLKIPhtvsglplYVTISIGIAAYPNDG-EDPEDLLKRADTALYQAKQAGRNR 160
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 363-575 3.74e-51

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: 177.09  E-value: 3.74e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757754641 363 YGSLMAAPMIQNDRLLGFAVLLKQELYAFTFEMYKLFQALIHHATLAVTNSMLR---DRLEHLVKTDQLTELYSRAYLDE 439
Cdd:COG2199   51 LLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLLLLALEDITELRrleERLRRLATHDPLTGLPNRRAFEE 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757754641 440 K----IQYSMKIHQKGVFILVDIDNFKNVNDTYGHQTGDEILIQVASVIKSNIRKHDVGARWGGEELAIYLPNVPVAVGK 515
Cdd:COG2199  131 RlereLARARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAE 210

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 757754641 516 RITERLVYAVRK------NTKPEVTISCGISCWtTETKKSLKELVHEADEALYSAKRSGKNRLMVH 575
Cdd:COG2199  211 ALAERLREALEQlpfeleGKELRVTVSIGVALY-PEDGDSAEELLRRADLALYRAKRAGRNRVVVY 275
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 421-575 3.31e-49

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 167.81  E-value: 3.31e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757754641   421 HLVKTDQLTELYSRAYLDE--KIQYSMKIHQKGVF--ILVDIDNFKNVNDTYGHQTGDEILIQVASVIKSNIRKHDVGAR 496
Cdd:smart00267   1 RLAFRDPLTGLPNRRYFEEelEQELQRAQRQGSPFalLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757754641   497 WGGEELAIYLPNVPVAVGKRITERLVYAVRKNTKPE-----VTISCGISCWTTETkKSLKELVHEADEALYSAKRSGKNR 571
Cdd:smart00267  81 LGGDEFALLLPETSLEEAIALAERILQQLREPIIIHgiplyLTISIGVAAYPNPG-EDAEDLLKRADTALYQAKKAGRNQ 159


                   ....
gi 757754641   572 LMVH 575
Cdd:smart00267 160 VAVY 163
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 425-571 7.91e-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: 166.58  E-value: 7.91e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757754641 425 TDQLTELYSRAYLDEKIQYSMKI----HQKGVFILVDIDNFKNVNDTYGHQTGDEILIQVASVIKSNIRKHDVGARWGGE 500
Cdd:cd01949    2 TDPLTGLPNRRAFEERLERLLARarrsGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGD 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 757754641 501 ELAIYLPNVPVAVGKRITERLVYAVRK-----NTKPEVTISCGISCWtTETKKSLKELVHEADEALYSAKRSGKNR 571
Cdd:cd01949   82 EFAILLPGTDLEEAEALAERLREAIEEpffidGQEIRVTASIGIATY-PEDGEDAEELLRRADEALYRAKRSGRNR 156
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 425-576 1.35e-39

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: 142.09  E-value: 1.35e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757754641  425 TDQLTELYSRAYLDEKIQYSMKI---HQKGV-FILVDIDNFKNVNDTYGHQTGDEILIQVASVIKSNIRKHDVGARWGGE 500
Cdd:TIGR00254   4 RDPLTGLYNRRYLEEMLDSELKRarrFQRSFsVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYGGE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757754641  501 ELAIYLPNVPVAVGKRITERLVYA-------VRKNTKPEVTISCGISCwTTETKKSLKELVHEADEALYSAKRSGKNRLM 573
Cdd:TIGR00254  84 EFVVILPGTPLEDALSKAERLRDAinskpieVAGSETLTVTVSIGVAC-YPGHGLTLEELLKRADEALYQAKKAGRNRVV 162


                  ...
gi 757754641  574 VHD 576
Cdd:TIGR00254 163 VAD 165
diguan_SiaD NF038266
biofilm regulation diguanylate cyclase SiaD;
413-572 9.98e-36

biofilm regulation diguanylate cyclase SiaD;


Pssm-ID: 468439 [Multi-domain]  Cd Length: 252  Bit Score: 134.34  E-value: 9.98e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757754641 413 SMLRD---RLEHLVKTDQLTELYSRAYLDEKIQYSMKIHQKG----VFILVDIDNFKNVNDTYGHQTGDEILIQVASVIK 485
Cdd:NF038266  81 RMMRDlneALREASTRDPLTGLPNRRLLMERLREEVERARRSgrpfTLAMLDVDHFKRINDRYGHEVGDRVLVEIARTLR 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757754641 486 SNIRKHDVGARWGGEELAIYLPNVPVAVGKRITERLVYAVR------KNTKPEVTISCGISCWTTETkKSLKELVHEADE 559
Cdd:NF038266 161 AELREYDLCGRWGGEEFLLLLPETGLEEAQVVLERLREAVRalavrvGDDVLSVTASAGLAEHRPPE-EGLSATLSRADQ 239

                        170
                 ....*....|...
gi 757754641 560 ALYSAKRSGKNRL 572
Cdd:NF038266 240 ALYQAKRAGRDRV 252
pleD PRK09581
response regulator PleD; Reviewed
 415-571 2.53e-35

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 138.50  E-value: 2.53e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757754641 415 LRDRLEHLVK---TDQLTELYSRAYLDEKIQY----SMKIHQKGVFILVDIDNFKNVNDTYGHQTGDEILIQVASVIKSN 487
Cdd:PRK09581 281 LRNNLEQSIEmavTDGLTGLHNRRYFDMHLKNlierANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNN 360

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757754641 488 IRKHDVGARWGGEELAIYLPNVPVAVGKRITERLVYAVRK--------NTKPEVTISCGIScwttETKK---SLKELVHE 556
Cdd:PRK09581 361 IRGTDLIARYGGEEFVVVMPDTDIEDAIAVAERIRRKIAEepfiisdgKERLNVTVSIGVA----ELRPsgdTIEALIKR 436

                        170
                 ....*....|....*
gi 757754641 557 ADEALYSAKRSGKNR 571
Cdd:PRK09581 437 ADKALYEAKNTGRNR 451
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 415-577 4.11e-33

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


Pssm-ID: 444025 [Multi-domain]  Cd Length: 678  Bit Score: 134.52  E-value: 4.11e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757754641 415 LRDRLEHLVKTDQLTELYSRAYLDEKIQYSMKI----HQKGVFILVDIDNFKNVNDTYGHQTGDEILIQVASVIKSNIRK 490
Cdd:COG5001  243 AEERLRHLAYHDPLTGLPNRRLFLDRLEQALARarrsGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLRE 322

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757754641 491 HDVGARWGGEELAIYLPNVP-VAVGKRITERLVYAVRkntKP------EVTISC--GISCWTTETkKSLKELVHEADEAL 561
Cdd:COG5001  323 GDTVARLGGDEFAVLLPDLDdPEDAEAVAERILAALA---EPfeldghELYVSAsiGIALYPDDG-ADAEELLRNADLAM 398

                        170
                 ....*....|....*.
gi 757754641 562 YSAKRSGKNRLMVHDS 577
Cdd:COG5001  399 YRAKAAGRNRYRFFDP 414
PRK15426 PRK15426
cellulose biosynthesis regulator YedQ;
395-577 9.24e-31

cellulose biosynthesis regulator YedQ;


Pssm-ID: 237964 [Multi-domain]  Cd Length: 570  Bit Score: 126.67  E-value: 9.24e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757754641 395 MYKLFQALIHhATLAVTNSMLRD------RLEHLVKTDQLTELYSRAYLDEKIQYSMKIHQKG----VFILVDIDNFKNV 464
Cdd:PRK15426 365 LWALFTAMLL-ISWYVIRRMVSNmfvlqsSLQWQAWHDPLTRLYNRGALFEKARALAKRCQRDqqpfSVIQLDLDHFKSI 443

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757754641 465 NDTYGHQTGDEILIQVASVIKSNIRKHDVGARWGGEELAIYLPNVPVAVGKRITERLVYA-------VRKNTKPEVTISC 537
Cdd:PRK15426 444 NDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRVGGEEFCVVLPGASLAEAAQVAERIRLRinekeilVAKSTTIRISASL 523

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 757754641 538 GISCWTTETKKSLKELVHEADEALYSAKRSGKNRLMVHDS 577
Cdd:PRK15426 524 GVSSAEEDGDYDFEQLQSLADRRLYLAKQAGRNRVCASDN 563
PRK09894 PRK09894
diguanylate cyclase; Provisional
 399-576 5.65e-29

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 116.70  E-value: 5.65e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757754641 399 FQALIHHATLAVTnSMLRDRLEHLVKTDQLTELYSRAYLDEKIQYSMKIHQKGVF--ILVDIDNFKNVNDTYGHQTGDEI 476
Cdd:PRK09894 106 FQEGLLSFTAALT-DYKIYLLTIRSNMDVLTGLPGRRVLDESFDHQLRNREPQNLylALLDIDRFKLVNDTYGHLIGDVV 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757754641 477 LIQVASVIKSNIRKHDVGARWGGEELAIYLPNVPVAVGKRITERLVYAVRKN--TKPE----VTISCGISCWTTEtkKSL 550
Cdd:PRK09894 185 LRTLATYLASWTRDYETVYRYGGEEFIICLKAATDEEACRAGERIRQLIANHaiTHSDgrinITATFGVSRAFPE--ETL 262

                        170       180
                 ....*....|....*....|....*.
gi 757754641 551 KELVHEADEALYSAKRSGKNRLMVHD 576
Cdd:PRK09894 263 DVVIGRADRAMYEGKQTGRNRVMFID 288
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 410-575 7.34e-23

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 103.60  E-value: 7.34e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757754641  410 VTNS--MLRdRLEHLVKTDQLTELYSRAY----LDEKIQYSMKIHQKGVFILVDIDNFKNVNDTYGHQTGDEILIQVASV 483
Cdd:PRK09776  651 VTESrkMLR-QLSYSASHDALTHLANRASfekqLRRLLQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASL 729

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757754641  484 IKSNIRKHDVGARWGGEELAIYLPNVPVAVGKRITERLVYAVRKNTKP------EVTISCGISCwTTETKKSLKELVHEA 557
Cdd:PRK09776  730 MLSMLRSSDVLARLGGDEFGLLLPDCNVESARFIATRIISAINDYHFPwegrvyRVGASAGITL-IDANNHQASEVMSQA 808

                         170
                  ....*....|....*...
gi 757754641  558 DEALYSAKRSGKNRLMVH 575
Cdd:PRK09776  809 DIACYAAKNAGRGRVTVY 826
adrA PRK10245
diguanylate cyclase AdrA; Provisional
 395-574 8.37e-23

diguanylate cyclase AdrA; Provisional


Pssm-ID: 182329 [Multi-domain]  Cd Length: 366  Bit Score: 100.29  E-value: 8.37e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757754641 395 MYKLFQALIHHATlAVTNSMLRDRLEHLVKTDQLTELYSRAY----LDEKIQYSMKIHQKGVFILVDIDNFKNVNDTYGH 470
Cdd:PRK10245 178 IYPLLFAWVSYQT-ATKLAEHKRRLQVMSTRDGMTGVYNRRHwetlLRNEFDNCRRHHRDATLLIIDIDHFKSINDTWGH 256

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757754641 471 QTGDEILIQVASVIKSNIRKHDVGARWGGEELAIYLPNVP----VAVGKRITERLvYAVRKNTKPEVT--ISCGISCWTT 544
Cdd:PRK10245 257 DVGDEAIVALTRQLQITLRGSDVIGRFGGDEFAVIMSGTPaesaITAMSRVHEGL-NTLRLPNAPQVTlrISVGVAPLNP 335

                        170       180       190
                 ....*....|....*....|....*....|
gi 757754641 545 ETKKsLKELVHEADEALYSAKRSGKNRLMV 574
Cdd:PRK10245 336 QMSH-YREWLKSADLALYKAKNAGRNRTEV 364
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
417-569 9.01e-20

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 93.21  E-value: 9.01e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757754641 417 DRLEHLVKTDQLTELYSRAYLDEKIQYSMKI---HQKGVFILvDIDNFKNVNDTYGHQTGDEILIQVASVIKSNIRKHDV 493
Cdd:PRK10060 231 ERLRILANTDSITGLPNRNAIQELIDHAINAadnNQVGIVYL-DLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQT 309

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757754641 494 GARWGGEELAIYLPNVPV----AVGKRITERLVYAVRKNTkPEVTISC--GISCWtTETKKSLKELVHEADEALYSAKRS 567
Cdd:PRK10060 310 LARLGGDEFLVLASHTSQaaleAMASRILTRLRLPFRIGL-IEVYTGCsiGIALA-PEHGDDSESLIRSADTAMYTAKEG 387


                 ..
gi 757754641 568 GK 569
Cdd:PRK10060 388 GR 389
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 401-570 1.72e-14

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 76.73  E-value: 1.72e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757754641 401 ALIHHATLAVTNSMLRDRLEHLVKTDQLTELYSRAYLDEKIQYSMKIHQKGVFILVDIDNFKNVNDTYGHQTGDEILIQV 480
Cdd:PRK11359 354 ISQHLAALALEQEKSRQHIEQLIQFDPLTGLPNRNNLHNYLDDLVDKAVSPVVYLIGVDHFQDVIDSLGYAWADQALLEV 433

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757754641 481 ASVIKSNIRKHDVGARWGGEELAIYLPNVPVAVGKRITERLVYAVRK----NTKP-EVTISCGIScwtTETKKSLKELVH 555
Cdd:PRK11359 434 VNRFREKLKPDQYLCRIEGTQFVLVSLENDVSNITQIADELRNVVSKpimiDDKPfPLTLSIGIS---YDVGKNRDYLLS 510

                        170
                 ....*....|....*
gi 757754641 556 EADEALYSAKRSGKN 570
Cdd:PRK11359 511 TAHNAMDYIRKNGGN 525
PRK09966 PRK09966
diguanylate cyclase DgcN;
415-573 2.56e-11

diguanylate cyclase DgcN;


Pssm-ID: 182171 [Multi-domain]  Cd Length: 407  Bit Score: 65.80  E-value: 2.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757754641 415 LRDRLEHLVKT---DQLTELYSRAYLDEKIQYSMK---IHQKGVFILVDIDNFKNVNDTYGHQTGDEILIQVASVIKSNI 488
Cdd:PRK09966 237 LQAKNAQLLRTalhDPLTGLANRAAFRSGINTLMNnsdARKTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFG 316

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757754641 489 RKHDVGARWGGEELAIYLPNVPVAVG-KRITERLVYA------VRKNTKPEVTISCGIS-CWTTETKKSLKELvheADEA 560
Cdd:PRK09966 317 GLRHKAYRLGGDEFAMVLYDVQSESEvQQICSALTQIfnlpfdLHNGHQTTMTLSIGYAmTIEHASAEKLQEL---ADHN 393

                        170
                 ....*....|...
gi 757754641 561 LYSAKRSGKNRLM 573
Cdd:PRK09966 394 MYQAKHQRAEKLV 406
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
 454-540 5.28e-11

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: 60.45  E-value: 5.28e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757754641 454 ILVDIDNFKNVNDTYGHQTGDEILIQVASVIKSNIRKH-DVGARWGGEELAIYLPNVPVAVGKRITERLVYAVRKNTKPE 532
Cdd:cd07556    5 LFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSgDLKIKTIGDEFMVVSGLDHPAAAVAFAEDMREAVSALNQSE 84

                         90
                 ....*....|.
gi 757754641 533 ---VTISCGIS 540
Cdd:cd07556   85 gnpVRVRIGIH 95
GAF COG2203
GAF domain [Signal transduction mechanisms];
202-526 1.79e-09

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 60.59  E-value: 1.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757754641 202 ILRKNESAAYIPIKGQQGTYGVLKAEGTGDSFLADACLDEMSLLANAAGKAFENAQLYEQSKASIAN-LELINETSRRLN 280
Cdd:COG2203  124 ALAARLLDLLLLGLGGRLRGVVLRGLRSAALLLSRVDTDLVGQLAALAGLILDIARLLTQRARLELErLALLNEISQALR 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757754641 281 QRLTLTDTMNDLAVRMAESFQAEEVGFFHIDHfENLTLLPGSTAFFKEAKPSDFYNE---LKEKLYEGE---------KG 348
Cdd:COG2203  204 SALDLEELLQRILELAGELLGADRGAILLVDE-DGGELELVAAPGLPEEELGRLPLGeglAGRALRTGEpvvvndastDP 282

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757754641 349 VFIGNGQSVFGKAGYGSLMAAPMIQNDRLLGFAVLLKQELYAFTFEMYKLFQALIHHATLAVTNS------------MLR 416
Cdd:COG2203  283 RFAPSLRELLLALGIRSLLCVPLLVDGRLIGVLALYSKEPRAFTEEDLELLEALADQAAIAIERArlyealeaalaaLLQ 362

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757754641 417 DRLEHLVKTDQLTELYSRAYLDEKIQYSMKIHQKG----VFILVDIDNFKNVNDTYGHQTGDEILIQVASVIKSNIRKHD 492
Cdd:COG2203  363 ELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLlgaeLLLLLLDAADLSGLLALEGLLLLDLLLLLLLLRRILLLRVL 442

                        330       340       350
                 ....*....|....*....|....*....|....
gi 757754641 493 VGARWGGEELAIYLPNVPVAVGKRITERLVYAVR 526
Cdd:COG2203  443 RRLLLGDEEGLVLLLALAELELLEILELLVLLAV 476
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 492-565 1.82e-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: 57.23  E-value: 1.82e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 757754641 492 DVGARWGGEELAIYLPNVPVAVGKRITERLVYAVRKNTKPEVTISCGIscwttetkkSLKELVHEADeALYSAK 565
Cdd:COG3706  116 DLVARYGGEEFAILLPGTDLEGALAVAERIREAVAELPSLRVTVSIGV---------AGDSLLKRAD-ALYQAR 179
GAF_2 pfam13185
GAF domain; The GAF domain is named after some of the proteins it is found in, including ...
 283-410 2.61e-04

GAF domain; The GAF domain is named after some of the proteins it is found in, including cGMP-specific phosphodiesterases, adenylyl cyclases and FhlA. It is also found in guanylyl cyclases and phytochromes. The structure of a GAF domain shows that the domain shares a similar fold with the PAS domain. This domain can bind O2, CO and NO (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 433019 [Multi-domain]  Cd Length: 137  Bit Score: 41.30  E-value: 2.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757754641  283 LTLTDTMnDLAVRMAESFQAEEVGFFHIDHFENLTLLPGSTAFFKEAKPSDFYNE--LKEKLYEGEKgVFIGN------- 353
Cdd:pfam13185   2 ADLEELL-DAVLEAAVELGASAVGFILLVDDDGRLAAWGGAADELSAALDDPPGEglVGEALRTGRP-VIVNDlaadpak 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 757754641  354 GQSVFGKAGYGSLMAAPMIQNDRLLGFAVLLKQELYAFTFEMYKLFQALIHHATLAV 410
Cdd:pfam13185  80 KGLPAGHAGLRSFLSVPLVSGGRVVGVLALGSNRPGAFDEEDLELLELLAEQAAIAI 136
PtsP COG3605
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];
359-436 4.02e-03

Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];


Pssm-ID: 442824 [Multi-domain]  Cd Length: 188  Bit Score: 38.72  E-value: 4.02e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 757754641 359 GKAGYGSLMAAPMIQNDRLLGFAVLLKQELYAFTFEMYKLFQALIHHATLAVTNSMLRDRLEHLVKTDQLTELYSRAY 436
Cdd:COG3605  104 GEEGFRSFLGVPIIRRGRVLGVLVVQSREPREFTEEEVEFLVTLAAQLAEAIANAELLGELRAALAELSLAREEEREA 181
GAF_3 pfam13492
GAF domain;
207-255 6.84e-03

GAF domain;


Pssm-ID: 433253 [Multi-domain]  Cd Length: 129  Bit Score: 36.96  E-value: 6.84e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 757754641  207 ESAAYIPIKGQQGTYGVLKAEGTGDSFLADACLDEMSLLANAAGKAFEN 255
Cdd:pfam13492  81 GPALVVPLVAGRRVIGVLALASSKPRAFDAEDLRLLESLAAQIATAIEN 129
 
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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