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Conserved domains on  [gi|754753039|ref|WP_042117591|]
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sensor domain-containing diguanylate cyclase [Photobacterium leiognathi]

Protein Classification

sensor domain-containing diguanylate cyclase( domain architecture ID 13404624)

sensor domain-containing diguanylate cyclase similar to Idiomarina sp. phytochrome-activated diguanylyl cyclase (PadC), which is red-light regulated

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 137-288 1.61e-50

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: 164.27  E-value: 1.61e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754753039 137 PLTGLLNQRYLDlikHDYPKLFK-----GQSLGIAFLDLDRFKPVNDQYGHDVGDILLKKIAQRLKRLFPSDDYVFRIGG 211
Cdd:cd01949    4 PLTGLPNRRAFE---ERLERLLArarrsGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 754753039 212 DEFLVIFKlstvDNQHAELEHAAKRIHHDLTQPIYIASLAIHISvgVSVGIAYYPFEDEHLPTLISKADEAMYYAKK 288
Cdd:cd01949   81 DEFAILLP----GTDLEEAEALAERLREAIEEPFFIDGQEIRVT--ASIGIATYPEDGEDAEELLRRADEALYRAKR 151
NtrB super family cl34682
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
10-155 3.60e-12

Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];


The actual alignment was detected with superfamily member COG3852:

Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 66.02  E-value: 3.60e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754753039  10 LLDFLGDAVLIVNETSKIVFSNNACCTLLGYSKNELLDMQLSDLINPSSinTHDENVARFIKHQSAPKvmseRNLITCYK 89
Cdd:COG3852   12 ILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELFPEDS--PLRELLERALAEGQPVT----EREVTLRR 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754753039  90 KNGQPVKLRISISCL-EYQGKPCAIAIIHDFTS---IQASISELEnKLN-------------REPLTGLLNqrYLDLIKH 152
Cdd:COG3852   86 KDGEERPVDVSVSPLrDAEGEGGVLLVLRDITErkrLERELRRAE-KLAavgelaaglaheiRNPLTGIRG--AAQLLER 162


                 ...
gi 754753039 153 DYP 155
Cdd:COG3852  163 ELP 165
 
Name Accession Description Interval E-value
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 137-288 1.61e-50

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: 164.27  E-value: 1.61e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754753039 137 PLTGLLNQRYLDlikHDYPKLFK-----GQSLGIAFLDLDRFKPVNDQYGHDVGDILLKKIAQRLKRLFPSDDYVFRIGG 211
Cdd:cd01949    4 PLTGLPNRRAFE---ERLERLLArarrsGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 754753039 212 DEFLVIFKlstvDNQHAELEHAAKRIHHDLTQPIYIASLAIHISvgVSVGIAYYPFEDEHLPTLISKADEAMYYAKK 288
Cdd:cd01949   81 DEFAILLP----GTDLEEAEALAERLREAIEEPFFIDGQEIRVT--ASIGIATYPEDGEDAEELLRRADEALYRAKR 151
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 112-289 3.33e-49

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: 164.77  E-value: 3.33e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754753039 112 AIAIIHDFTSIQASISELENKLNREPLTGLLNQRYLDlikHDYPKLFK-----GQSLGIAFLDLDRFKPVNDQYGHDVGD 186
Cdd:COG2199   93 LLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFE---ERLERELArarreGRPLALLLIDLDHFKRINDTYGHAAGD 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754753039 187 ILLKKIAQRLKRLFPSDDYVFRIGGDEFLVIFKlstvDNQHAELEHAAKRIHHDLTQ-PIYIASLAIHISvgVSVGIAYY 265
Cdd:COG2199  170 EVLKEVARRLRASLRESDLVARLGGDEFAVLLP----GTDLEEAEALAERLREALEQlPFELEGKELRVT--VSIGVALY 243

                        170       180
                 ....*....|....*....|....
gi 754753039 266 PFEDEHLPTLISKADEAMYYAKKH 289
Cdd:COG2199  244 PEDGDSAEELLRRADLALYRAKRA 267
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 134-288 4.43e-45

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 150.48  E-value: 4.43e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754753039   134 NREPLTGLLNQRYLD-LIKHDYPKLF-KGQSLGIAFLDLDRFKPVNDQYGHDVGDILLKKIAQRLKRLFPSDDYVFRIGG 211
Cdd:smart00267   4 FRDPLTGLPNRRYFEeELEQELQRAQrQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARLGG 83

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 754753039   212 DEFLVIfkLSTVDNQHAelEHAAKRIHHDLTQPIYIASLAIHISvgVSVGIAYYPFEDEHLPTLISKADEAMYYAKK 288
Cdd:smart00267  84 DEFALL--LPETSLEEA--IALAERILQQLREPIIIHGIPLYLT--ISIGVAAYPNPGEDAEDLLKRADTALYQAKK 154
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 134-289 9.01e-43

Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of non-homologous domains in a variety of bacteria. It has been shown to be homologous to the adenylyl cyclase catalytic domain and has diguanylate cyclase activity. This observation correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. In the WspR protein of Pseudomonas aeruginosa, the GGDEF domain acts as a diguanylate cyclase, PDB:3bre, when the whole molecule appears to form a tetramer consisting of two symmetrically-related dimers representing a biological unit. The active site is the GGD/EF motif, buried in the structure, and the cyclic dimeric guanosine monophosphate (c-di-GMP) bind to the inhibitory-motif RxxD on the surface. The enzyme thus catalyzes the cyclization of two guanosine triphosphate (GTP) molecules to one c-di-GMP molecule.


Pssm-ID: 425976 [Multi-domain]  Cd Length: 160  Bit Score: 144.32  E-value: 9.01e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754753039  134 NREPLTGLLNQRYLD-----LIKHDypkLFKGQSLGIAFLDLDRFKPVNDQYGHDVGDILLKKIAQRLKRLFPSDDYVFR 208
Cdd:pfam00990   2 AHDPLTGLPNRRYFEeqleqELQRA---LREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVAR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754753039  209 IGGDEFLVIFKlSTVDNQHAELEHAAKRIHHDLTQPIYIASLAIHISvgVSVGIAYYPFEDEHLPTLISKADEAMYYAKK 288
Cdd:pfam00990  79 LGGDEFAILLP-ETSLEGAQELAERIRRLLAKLKIPHTVSGLPLYVT--ISIGIAAYPNDGEDPEDLLKRADTALYQAKQ 155


                  .
gi 754753039  289 H 289
Cdd:pfam00990 156 A 156
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 135-288 3.70e-37

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: 130.15  E-value: 3.70e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754753039  135 REPLTGLLNQRYLD-LIKHDYPKLFKGQ-SLGIAFLDLDRFKPVNDQYGHDVGDILLKKIAQRLKRLFPSDDYVFRIGGD 212
Cdd:TIGR00254   4 RDPLTGLYNRRYLEeMLDSELKRARRFQrSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYGGE 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 754753039  213 EFLVIFkLSTvdNQHAELEHAAKRIHHDLTQPIYIASLAIhISVGVSVGIAYYPFEDEHLPTLISKADEAMYYAKK 288
Cdd:TIGR00254  84 EFVVIL-PGT--PLEDALSKAERLRDAINSKPIEVAGSET-LTVTVSIGVACYPGHGLTLEELLKRADEALYQAKK 155
PRK09894 PRK09894
diguanylate cyclase; Provisional
 114-287 4.10e-30

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 115.55  E-value: 4.10e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754753039 114 AIIHDFTSIQASISELENKL-----NREPLTGLLNQRYLDL-IKHDYpKLFKGQSLGIAFLDLDRFKPVNDQYGHDVGDI 187
Cdd:PRK09894 105 AFQEGLLSFTAALTDYKIYLltirsNMDVLTGLPGRRVLDEsFDHQL-RNREPQNLYLALLDIDRFKLVNDTYGHLIGDV 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754753039 188 LLKKIAQRLKRLFPSDDYVFRIGGDEFLVIFKLSTVDNQHAELEhaakRIHHDL-TQPIYIASLAIHISVGVSVGIAyyp 266
Cdd:PRK09894 184 VLRTLATYLASWTRDYETVYRYGGEEFIICLKAATDEEACRAGE----RIRQLIaNHAITHSDGRINITATFGVSRA--- 256

                        170       180
                 ....*....|....*....|.
gi 754753039 267 FEDEHLPTLISKADEAMYYAK 287
Cdd:PRK09894 257 FPEETLDVVIGRADRAMYEGK 277
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
10-155 3.60e-12

Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 66.02  E-value: 3.60e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754753039  10 LLDFLGDAVLIVNETSKIVFSNNACCTLLGYSKNELLDMQLSDLINPSSinTHDENVARFIKHQSAPKvmseRNLITCYK 89
Cdd:COG3852   12 ILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELFPEDS--PLRELLERALAEGQPVT----EREVTLRR 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754753039  90 KNGQPVKLRISISCL-EYQGKPCAIAIIHDFTS---IQASISELEnKLN-------------REPLTGLLNqrYLDLIKH 152
Cdd:COG3852   86 KDGEERPVDVSVSPLrDAEGEGGVLLVLRDITErkrLERELRRAE-KLAavgelaaglaheiRNPLTGIRG--AAQLLER 162


                 ...
gi 754753039 153 DYP 155
Cdd:COG3852  163 ELP 165
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 14-118 1.99e-09

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 54.18  E-value: 1.99e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754753039  14 LGDAVLIVNETSKIVFSNNACCTLLGYSKNELLDMQLSDLINPSSINTHDENVArfikhQSAPKVMSERNLITCYKKNGQ 93
Cdd:cd00130    1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLE-----NLLSGGEPVTLEVRLRRKDGS 75

                         90       100
                 ....*....|....*....|....*..
gi 754753039  94 PVKLRISISCL--EYQGKPCAIAIIHD 118
Cdd:cd00130   76 VIWVLVSLTPIrdEGGEVIGLLGVVRD 102
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
 10-133 8.36e-08

PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions]


Pssm-ID: 272971 [Multi-domain]  Cd Length: 124  Bit Score: 49.98  E-value: 8.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754753039   10 LLDFLGDAVLIVNETSKIVFSNNACCTLLGYSKNELLDMQLSDLINPSSINTHDENVARFIKHQSAPKVMsERNLITcyk 89
Cdd:TIGR00229   8 IFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGEPEPVSE-ERRVRR--- 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 754753039   90 KNGQPVKLRISISCL-EYQGKPCAIAIIHDFTSIQasisELENKL 133
Cdd:TIGR00229  84 KDGSEIWVEVSVSPIrTNGGELGVVGIVRDITERK----EAEEAL 124
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
 26-118 3.45e-07

PAS domain; This domain is found in many signalling proteins in which it functions as a sensor domain. It recognizes FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 463873 [Multi-domain]  Cd Length: 93  Bit Score: 47.46  E-value: 3.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754753039   26 KIVFSNNACCTLLGYSKNELLDMQLSDLINPSSINTHDENVARFIKHQsapkvmsERNLITCYKKNGQPVKLRISISCLE 105
Cdd:pfam13426   3 RIIYVNDAALRLLGYTREELLGKSITDLFAEPEDSERLREALREGKAV-------REFEVVLYRKDGEPFPVLVSLAPIR 75

                          90
                  ....*....|....*
gi 754753039  106 YQGKPC--AIAIIHD 118
Cdd:pfam13426  76 DDGGELvgIIAILRD 90
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 14-68 1.51e-06

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.


Pssm-ID: 214512  Cd Length: 67  Bit Score: 45.08  E-value: 1.51e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 754753039    14 LGDAVLIVNETSKIVFSNNACCTLLGYSKNELLDMQLSDLINPSSINTHDENVAR 68
Cdd:smart00091  10 LPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQR 64
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 17-118 5.96e-04

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 41.29  E-value: 5.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754753039  17 AVLIVNETSKIVFSNNACCTLLGYSKNELLDMQLSDLINPSSINTHDENVaRFIKHQSAPKVMSERNLITCYKKNGQPVK 96
Cdd:PRK11359  24 GAVLINENDEVLFFNPAAEKLWGYKREEVIGNNIDMLIPRDLRPAHPEYI-RHNREGGKARVEGMSRELQLEKKDGSKIW 102

                         90       100
                 ....*....|....*....|..
gi 754753039  97 LRISISCLEYQGKPCAIAIIHD 118
Cdd:PRK11359 103 TRFALSKVSAEGKVYYLALVRD 124
 
Name Accession Description Interval E-value
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 137-288 1.61e-50

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: 164.27  E-value: 1.61e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754753039 137 PLTGLLNQRYLDlikHDYPKLFK-----GQSLGIAFLDLDRFKPVNDQYGHDVGDILLKKIAQRLKRLFPSDDYVFRIGG 211
Cdd:cd01949    4 PLTGLPNRRAFE---ERLERLLArarrsGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 754753039 212 DEFLVIFKlstvDNQHAELEHAAKRIHHDLTQPIYIASLAIHISvgVSVGIAYYPFEDEHLPTLISKADEAMYYAKK 288
Cdd:cd01949   81 DEFAILLP----GTDLEEAEALAERLREAIEEPFFIDGQEIRVT--ASIGIATYPEDGEDAEELLRRADEALYRAKR 151
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 112-289 3.33e-49

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: 164.77  E-value: 3.33e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754753039 112 AIAIIHDFTSIQASISELENKLNREPLTGLLNQRYLDlikHDYPKLFK-----GQSLGIAFLDLDRFKPVNDQYGHDVGD 186
Cdd:COG2199   93 LLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFE---ERLERELArarreGRPLALLLIDLDHFKRINDTYGHAAGD 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754753039 187 ILLKKIAQRLKRLFPSDDYVFRIGGDEFLVIFKlstvDNQHAELEHAAKRIHHDLTQ-PIYIASLAIHISvgVSVGIAYY 265
Cdd:COG2199  170 EVLKEVARRLRASLRESDLVARLGGDEFAVLLP----GTDLEEAEALAERLREALEQlPFELEGKELRVT--VSIGVALY 243

                        170       180
                 ....*....|....*....|....
gi 754753039 266 PFEDEHLPTLISKADEAMYYAKKH 289
Cdd:COG2199  244 PEDGDSAEELLRRADLALYRAKRA 267
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 112-289 2.41e-46

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: 165.72  E-value: 2.41e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754753039 112 AIAIIHDFTSIQASISEL---ENKLNRE----PLTGLLNQRYL-----DLIKHDYPKlfkGQSLGIAFLDLDRFKPVNDQ 179
Cdd:COG5001  223 LLLLLVAVLAIARLITERkraEERLRHLayhdPLTGLPNRRLFldrleQALARARRS---GRRLALLFIDLDRFKEINDT 299

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754753039 180 YGHDVGDILLKKIAQRLKRLFPSDDYVFRIGGDEFLVIfkLSTVDNqHAELEHAAKRIHHDLTQPIYIASLAIHISvgVS 259
Cdd:COG5001  300 LGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVL--LPDLDD-PEDAEAVAERILAALAEPFELDGHELYVS--AS 374

                        170       180       190
                 ....*....|....*....|....*....|
gi 754753039 260 VGIAYYPFEDEHLPTLISKADEAMYYAKKH 289
Cdd:COG5001  375 IGIALYPDDGADAEELLRNADLAMYRAKAA 404
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 134-288 4.43e-45

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 150.48  E-value: 4.43e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754753039   134 NREPLTGLLNQRYLD-LIKHDYPKLF-KGQSLGIAFLDLDRFKPVNDQYGHDVGDILLKKIAQRLKRLFPSDDYVFRIGG 211
Cdd:smart00267   4 FRDPLTGLPNRRYFEeELEQELQRAQrQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARLGG 83

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 754753039   212 DEFLVIfkLSTVDNQHAelEHAAKRIHHDLTQPIYIASLAIHISvgVSVGIAYYPFEDEHLPTLISKADEAMYYAKK 288
Cdd:smart00267  84 DEFALL--LPETSLEEA--IALAERILQQLREPIIIHGIPLYLT--ISIGVAAYPNPGEDAEDLLKRADTALYQAKK 154
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 134-289 9.01e-43

Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of non-homologous domains in a variety of bacteria. It has been shown to be homologous to the adenylyl cyclase catalytic domain and has diguanylate cyclase activity. This observation correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. In the WspR protein of Pseudomonas aeruginosa, the GGDEF domain acts as a diguanylate cyclase, PDB:3bre, when the whole molecule appears to form a tetramer consisting of two symmetrically-related dimers representing a biological unit. The active site is the GGD/EF motif, buried in the structure, and the cyclic dimeric guanosine monophosphate (c-di-GMP) bind to the inhibitory-motif RxxD on the surface. The enzyme thus catalyzes the cyclization of two guanosine triphosphate (GTP) molecules to one c-di-GMP molecule.


Pssm-ID: 425976 [Multi-domain]  Cd Length: 160  Bit Score: 144.32  E-value: 9.01e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754753039  134 NREPLTGLLNQRYLD-----LIKHDypkLFKGQSLGIAFLDLDRFKPVNDQYGHDVGDILLKKIAQRLKRLFPSDDYVFR 208
Cdd:pfam00990   2 AHDPLTGLPNRRYFEeqleqELQRA---LREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVAR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754753039  209 IGGDEFLVIFKlSTVDNQHAELEHAAKRIHHDLTQPIYIASLAIHISvgVSVGIAYYPFEDEHLPTLISKADEAMYYAKK 288
Cdd:pfam00990  79 LGGDEFAILLP-ETSLEGAQELAERIRRLLAKLKIPHTVSGLPLYVT--ISIGIAAYPNDGEDPEDLLKRADTALYQAKQ 155


                  .
gi 754753039  289 H 289
Cdd:pfam00990 156 A 156
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 135-288 3.70e-37

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: 130.15  E-value: 3.70e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754753039  135 REPLTGLLNQRYLD-LIKHDYPKLFKGQ-SLGIAFLDLDRFKPVNDQYGHDVGDILLKKIAQRLKRLFPSDDYVFRIGGD 212
Cdd:TIGR00254   4 RDPLTGLYNRRYLEeMLDSELKRARRFQrSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYGGE 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 754753039  213 EFLVIFkLSTvdNQHAELEHAAKRIHHDLTQPIYIASLAIhISVGVSVGIAYYPFEDEHLPTLISKADEAMYYAKK 288
Cdd:TIGR00254  84 EFVVIL-PGT--PLEDALSKAERLRDAINSKPIEVAGSET-LTVTVSIGVACYPGHGLTLEELLKRADEALYQAKK 155
PRK09894 PRK09894
diguanylate cyclase; Provisional
 114-287 4.10e-30

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 115.55  E-value: 4.10e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754753039 114 AIIHDFTSIQASISELENKL-----NREPLTGLLNQRYLDL-IKHDYpKLFKGQSLGIAFLDLDRFKPVNDQYGHDVGDI 187
Cdd:PRK09894 105 AFQEGLLSFTAALTDYKIYLltirsNMDVLTGLPGRRVLDEsFDHQL-RNREPQNLYLALLDIDRFKLVNDTYGHLIGDV 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754753039 188 LLKKIAQRLKRLFPSDDYVFRIGGDEFLVIFKLSTVDNQHAELEhaakRIHHDL-TQPIYIASLAIHISVGVSVGIAyyp 266
Cdd:PRK09894 184 VLRTLATYLASWTRDYETVYRYGGEEFIICLKAATDEEACRAGE----RIRQLIaNHAITHSDGRINITATFGVSRA--- 256

                        170       180
                 ....*....|....*....|.
gi 754753039 267 FEDEHLPTLISKADEAMYYAK 287
Cdd:PRK09894 257 FPEETLDVVIGRADRAMYEGK 277
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
134-289 1.25e-29

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 118.25  E-value: 1.25e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754753039 134 NREPLTGLLNQRYL-DLIKHDYPKLFKGQsLGIAFLDLDRFKPVNDQYGHDVGDILLKKIAQRLKRLFPSDDYVFRIGGD 212
Cdd:PRK10060 238 NTDSITGLPNRNAIqELIDHAINAADNNQ-VGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQTLARLGGD 316

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 754753039 213 EFLVifkLSTVDNQHAeLEHAAKRIHHDLTQPIYIAslAIHISVGVSVGIAYYPFEDEHLPTLISKADEAMYYAKKH 289
Cdd:PRK10060 317 EFLV---LASHTSQAA-LEAMASRILTRLRLPFRIG--LIEVYTGCSIGIALAPEHGDDSESLIRSADTAMYTAKEG 387
pleD PRK09581
response regulator PleD; Reviewed
 129-288 2.13e-27

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 110.76  E-value: 2.13e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754753039 129 LENKLN---REPLTGLLNQRYLDliKHdYPKLF-----KGQSLGIAFLDLDRFKPVNDQYGHDVGDILLKKIAQRLKRLF 200
Cdd:PRK09581 285 LEQSIEmavTDGLTGLHNRRYFD--MH-LKNLIeraneRGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNI 361

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754753039 201 PSDDYVFRIGGDEFLVIfkLSTVDNQHAELehAAKRIHHDL-TQPIYIASLAIHISVGVSVGIAYYPFEDEHLPTLISKA 279
Cdd:PRK09581 362 RGTDLIARYGGEEFVVV--MPDTDIEDAIA--VAERIRRKIaEEPFIISDGKERLNVTVSIGVAELRPSGDTIEALIKRA 437


                 ....*....
gi 754753039 280 DEAMYYAKK 288
Cdd:PRK09581 438 DKALYEAKN 446
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 11-287 6.88e-18

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 83.95  E-value: 6.88e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754753039   11 LDFLGDAVLIVNETSKIVFSNNACCTLLGYSKNELLDMQLSDLINPSSINTHD--ENVARFIKHQSAPKVMSERNLITcy 88
Cdd:PRK09776  542 LDSIGEAVVCTDMAMKVTFMNPVAEKMTGWTQEEALGVPLLTVLHITFGDNGPlmENIYSCLTSRSAAYLEQDVVLHC-- 619

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754753039   89 kKNGQPVKLRISISCL-----EYQGkpcAIAIIHDFTSIQASISELENKLNREPLTGLLN--------QRYLDLIKHdyp 155
Cdd:PRK09776  620 -RSGGSYDVHYSITPLstldgENIG---SVLVIQDVTESRKMLRQLSYSASHDALTHLANrasfekqlRRLLQTVNS--- 692

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754753039  156 klfKGQSLGIAFLDLDRFKPVNDQYGHDVGDILLKKIAQRLKRLFPSDDYVFRIGGDEFLVIFKLSTVDNqhaelehaAK 235
Cdd:PRK09776  693 ---THQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSDVLARLGGDEFGLLLPDCNVES--------AR 761

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 754753039  236 RIHHDLTQPI----YIASLAIHiSVGVSVGIAYYPFEDEHLPTLISKADEAMYYAK 287
Cdd:PRK09776  762 FIATRIISAIndyhFPWEGRVY-RVGASAGITLIDANNHQASEVMSQADIACYAAK 816
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 136-288 2.66e-16

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 79.43  E-value: 2.66e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754753039 136 EPLTGLLNQ----RYLDLIkhdypkLFKGQSLGIAFLDLDRFKPVNDQYGHDVGDILLKKIAQRLKRLFPSDDYVFRIGG 211
Cdd:PRK11359 379 DPLTGLPNRnnlhNYLDDL------VDKAVSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEG 452

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 754753039 212 DEFLVIfklsTVDNQHAELEHAAKRIHHDLTQPIYIASLAIHISvgVSVGIAYYPFEDEHlpTLISKADEAMYYAKK 288
Cdd:PRK11359 453 TQFVLV----SLENDVSNITQIADELRNVVSKPIMIDDKPFPLT--LSIGISYDVGKNRD--YLLSTAHNAMDYIRK 521
adrA PRK10245
diguanylate cyclase AdrA; Provisional
 115-288 9.75e-16

diguanylate cyclase AdrA; Provisional


Pssm-ID: 182329 [Multi-domain]  Cd Length: 366  Bit Score: 76.79  E-value: 9.75e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754753039 115 IIHDFTSIQASISELENKL------NREPLTGLLNQRYLD-LIKHDYPKLFKGQ-SLGIAFLDLDRFKPVNDQYGHDVGD 186
Cdd:PRK10245 181 LLFAWVSYQTATKLAEHKRrlqvmsTRDGMTGVYNRRHWEtLLRNEFDNCRRHHrDATLLIIDIDHFKSINDTWGHDVGD 260

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754753039 187 ILLKKIAQRLKRLFPSDDYVFRIGGDEFLVIFKLSTVDNQHAELEHAAKRIHHdLTQPIyiaslAIHISVGVSVGIAYYP 266
Cdd:PRK10245 261 EAIVALTRQLQITLRGSDVIGRFGGDEFAVIMSGTPAESAITAMSRVHEGLNT-LRLPN-----APQVTLRISVGVAPLN 334

                        170       180
                 ....*....|....*....|..
gi 754753039 267 FEDEHLPTLISKADEAMYYAKK 288
Cdd:PRK10245 335 PQMSHYREWLKSADLALYKAKN 356
PRK15426 PRK15426
cellulose biosynthesis regulator YedQ;
136-287 1.59e-15

cellulose biosynthesis regulator YedQ;


Pssm-ID: 237964 [Multi-domain]  Cd Length: 570  Bit Score: 76.59  E-value: 1.59e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754753039 136 EPLTGLLNQRYL-DLIKHDYPKLFK-GQSLGIAFLDLDRFKPVNDQYGHDVGDILLKKIAQRLKRLFPSDDYVFRIGGDE 213
Cdd:PRK15426 401 DPLTRLYNRGALfEKARALAKRCQRdQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRVGGEE 480

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 754753039 214 FLVIFKLSTVDnqhaELEHAAKRIHHDLT-QPIYIA---SLAIHISVGVSVGIAYYPFEDEHLPTLiskADEAMYYAK 287
Cdd:PRK15426 481 FCVVLPGASLA----EAAQVAERIRLRINeKEILVAkstTIRISASLGVSSAEEDGDYDFEQLQSL---ADRRLYLAK 551
PRK09966 PRK09966
diguanylate cyclase DgcN;
122-290 1.85e-13

diguanylate cyclase DgcN;


Pssm-ID: 182171 [Multi-domain]  Cd Length: 407  Bit Score: 70.04  E-value: 1.85e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754753039 122 IQASISELENKLNREPLTGLLNQRYL-----DLIKHDYPKlfkgQSLGIAFLDLDRFKPVNDQYGHDVGDILLKKIAQRL 196
Cdd:PRK09966 237 LQAKNAQLLRTALHDPLTGLANRAAFrsginTLMNNSDAR----KTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRL 312

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754753039 197 KRLFPSDDYVFRIGGDEFLVIFKlstvdNQHAELEhaAKRIHHDLTQpIYIASLAIH----ISVGVSVGIAyYPFEDEHL 272
Cdd:PRK09966 313 AEFGGLRHKAYRLGGDEFAMVLY-----DVQSESE--VQQICSALTQ-IFNLPFDLHnghqTTMTLSIGYA-MTIEHASA 383

                        170
                 ....*....|....*...
gi 754753039 273 PTLISKADEAMYYAkKHQ 290
Cdd:PRK09966 384 EKLQELADHNMYQA-KHQ 400
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
10-155 3.60e-12

Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 66.02  E-value: 3.60e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754753039  10 LLDFLGDAVLIVNETSKIVFSNNACCTLLGYSKNELLDMQLSDLINPSSinTHDENVARFIKHQSAPKvmseRNLITCYK 89
Cdd:COG3852   12 ILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELFPEDS--PLRELLERALAEGQPVT----EREVTLRR 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754753039  90 KNGQPVKLRISISCL-EYQGKPCAIAIIHDFTS---IQASISELEnKLN-------------REPLTGLLNqrYLDLIKH 152
Cdd:COG3852   86 KDGEERPVDVSVSPLrDAEGEGGVLLVLRDITErkrLERELRRAE-KLAavgelaaglaheiRNPLTGIRG--AAQLLER 162


                 ...
gi 754753039 153 DYP 155
Cdd:COG3852  163 ELP 165
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
 2-146 1.23e-10

RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis domains [Transcription, Signal transduction mechanisms];


Pssm-ID: 443041 [Multi-domain]  Cd Length: 448  Bit Score: 61.71  E-value: 1.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754753039   2 DNNSSINKLLDFLGDAVLIVNETSKIVFSNNACCTLLGYSKNELLDMQLSDLINPSSInthdenvarfikhqsaPKVMSE 81
Cdd:COG3829    8 ELEEELEAILDSLDDGIIVVDADGRITYVNRAAERILGLPREEVIGKNVTELIPNSPL----------------LEVLKT 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 754753039  82 RNLITC--YKKNGQPVKLRISISCLEYQGKPC-AIAIIHDFTSIQasisELENKLNREPLTGLLNQRY 146
Cdd:COG3829   72 GKPVTGviQKTGGKGKTVIVTAIPIFEDGEVIgAVETFRDITELK----RLERKLREEELERGLSAKY 135
PAS COG2202
PAS domain [Signal transduction mechanisms];
10-243 9.14e-10

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 58.11  E-value: 9.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754753039  10 LLDFLGDAVLIVNETSKIVFSNNACCTLLGYSKNELLDMQLSDLINPSSINTHDENVARFIKHQsapkvMSERNLITCYK 89
Cdd:COG2202   16 LVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGG-----GVWRGELRNRR 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754753039  90 KNGQPVKLRISISCLEY-QGKP-CAIAIIHDFTS---IQASISELENKL--------------NREPLTGLLNQRYLDLi 150
Cdd:COG2202   91 KDGSLFWVELSISPVRDeDGEItGFVGIARDITErkrAEEALRESEERLrllvenapdgifvlDLDGRILYVNPAAEEL- 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754753039 151 khdypklfkgqsLGIAFLDLDRfKPVNDQYGHDVGDILLKKIAQRLKRLFPSDDYVFRI-GGDEFLVIFKLSTVDNQHAE 229
Cdd:COG2202  170 ------------LGYSPEELLG-KSLLDLLHPEDRERLLELLRRLLEGGRESYELELRLkDGDGRWVWVEASAVPLRDGG 236

                        250
                 ....*....|....
gi 754753039 230 LEHAAKRIHHDLTQ 243
Cdd:COG2202  237 EVIGVLGIVRDITE 250
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 14-118 1.99e-09

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 54.18  E-value: 1.99e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754753039  14 LGDAVLIVNETSKIVFSNNACCTLLGYSKNELLDMQLSDLINPSSINTHDENVArfikhQSAPKVMSERNLITCYKKNGQ 93
Cdd:cd00130    1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLE-----NLLSGGEPVTLEVRLRRKDGS 75

                         90       100
                 ....*....|....*....|....*..
gi 754753039  94 PVKLRISISCL--EYQGKPCAIAIIHD 118
Cdd:cd00130   76 VIWVLVSLTPIrdEGGEVIGLLGVVRD 102
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
 163-263 2.11e-08

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: 51.97  E-value: 2.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754753039 163 LGIAFLDLDRFKPVNDQYGHDVGDILLKKIAQRLKRL-FPSDDYVFRIGGDEFLVIFklsTVDNQHAELEHAAKRIHHdl 241
Cdd:cd07556    2 VTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLiRRSGDLKIKTIGDEFMVVS---GLDHPAAAVAFAEDMREA-- 76

                         90       100
                 ....*....|....*....|....
gi 754753039 242 tqpiyIASLAIHISVGV--SVGIA 263
Cdd:cd07556   77 -----VSALNQSEGNPVrvRIGIH 95
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
 10-133 8.36e-08

PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions]


Pssm-ID: 272971 [Multi-domain]  Cd Length: 124  Bit Score: 49.98  E-value: 8.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754753039   10 LLDFLGDAVLIVNETSKIVFSNNACCTLLGYSKNELLDMQLSDLINPSSINTHDENVARFIKHQSAPKVMsERNLITcyk 89
Cdd:TIGR00229   8 IFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGEPEPVSE-ERRVRR--- 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 754753039   90 KNGQPVKLRISISCL-EYQGKPCAIAIIHDFTSIQasisELENKL 133
Cdd:TIGR00229  84 KDGSEIWVEVSVSPIrTNGGELGVVGIVRDITERK----EAEEAL 124
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
 26-118 3.45e-07

PAS domain; This domain is found in many signalling proteins in which it functions as a sensor domain. It recognizes FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 463873 [Multi-domain]  Cd Length: 93  Bit Score: 47.46  E-value: 3.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754753039   26 KIVFSNNACCTLLGYSKNELLDMQLSDLINPSSINTHDENVARFIKHQsapkvmsERNLITCYKKNGQPVKLRISISCLE 105
Cdd:pfam13426   3 RIIYVNDAALRLLGYTREELLGKSITDLFAEPEDSERLREALREGKAV-------REFEVVLYRKDGEPFPVLVSLAPIR 75

                          90
                  ....*....|....*
gi 754753039  106 YQGKPC--AIAIIHD 118
Cdd:pfam13426  76 DDGGELvgIIAILRD 90
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 174-287 4.94e-07

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: 49.14  E-value: 4.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754753039 174 KPVNDQyghdvgdILLKKIaqrlkrlfpsdDYVFRIGGDEFLVIFKlstvDNQHAELEHAAKRIHHDLTQPiyiaslaIH 253
Cdd:COG3706  104 KPFDPE-------ELLARV-----------DLVARYGGEEFAILLP----GTDLEGALAVAERIREAVAEL-------PS 154

                         90       100       110
                 ....*....|....*....|....*....|....
gi 754753039 254 ISVGVSVGIAYypfedehlPTLISKADeAMYYAK 287
Cdd:COG3706  155 LRVTVSIGVAG--------DSLLKRAD-ALYQAR 179
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 10-118 1.06e-06

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain can bind gases (O2, CO and NO), FAD, 4-hydroxycinnamic acid and NAD+ (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 395786 [Multi-domain]  Cd Length: 113  Bit Score: 46.64  E-value: 1.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754753039   10 LLDFLGDAVLIVNETSKIVFSNNACCTLLGYSKNELLDMQLSDLINPssiNTHDENVARFIK--HQSAPKVMSERNLITc 87
Cdd:pfam00989   6 ILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPE---EDDAEVAELLRQalLQGEESRGFEVSFRV- 81

                          90       100       110
                  ....*....|....*....|....*....|...
gi 754753039   88 ykKNGQPVKLRISISCL-EYQGKP-CAIAIIHD 118
Cdd:pfam00989  82 --PDGRPRHVEVRASPVrDAGGEIlGFLGVLRD 112
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 14-68 1.51e-06

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.


Pssm-ID: 214512  Cd Length: 67  Bit Score: 45.08  E-value: 1.51e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 754753039    14 LGDAVLIVNETSKIVFSNNACCTLLGYSKNELLDMQLSDLINPSSINTHDENVAR 68
Cdd:smart00091  10 LPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQR 64
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
 16-204 6.79e-05

Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444511 [Multi-domain]  Cd Length: 489  Bit Score: 44.20  E-value: 6.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754753039  16 DAVLIVNETSKIVFSNNACCTLLGYSKNELLDMQLSDLINPSSINTHDENVARFIKHQSAPKVMSERnlitcYKKNGQPV 95
Cdd:COG5809   26 DAILILDLEGKILKVNPAAERIFGYTEDELLGTNILDFLHPDDEKELREILKLLKEGESRDELEFEL-----RHKNGKRL 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754753039  96 KLRISISCLE-YQGKPCAI-AIIHDFTS---IQASISELENKlnrepltgllnqryldlikhdYPKLFKGQSLGIAFLDL 170
Cdd:COG5809  101 EFSSKLSPIFdQNGDIEGMlAISRDITErkrMEEALRESEEK---------------------FRLIFNHSPDGIIVTDL 159

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 754753039 171 D-RFKPVNDQYGHDVGDILLKKIAQRLKRLFPSDD 204
Cdd:COG5809  160 DgRIIYANPAACKLLGISIEELIGKSILELIHSDD 194
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 17-118 5.96e-04

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 41.29  E-value: 5.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754753039  17 AVLIVNETSKIVFSNNACCTLLGYSKNELLDMQLSDLINPSSINTHDENVaRFIKHQSAPKVMSERNLITCYKKNGQPVK 96
Cdd:PRK11359  24 GAVLINENDEVLFFNPAAEKLWGYKREEVIGNNIDMLIPRDLRPAHPEYI-RHNREGGKARVEGMSRELQLEKKDGSKIW 102

                         90       100
                 ....*....|....*....|..
gi 754753039  97 LRISISCLEYQGKPCAIAIIHD 118
Cdd:PRK11359 103 TRFALSKVSAEGKVYYLALVRD 124
PAS_8 pfam13188
PAS domain; PAS domains are involved in many signalling proteins where they are used as a ...
 7-56 5.34e-03

PAS domain; PAS domains are involved in many signalling proteins where they are used as a signal sensor domain. PAS domains appear in archaea, bacteria and eukaryotes. Several PAS-domain proteins are known to detect their signal by way of an associated cofactor. Heme, flavin, and a 4-hydroxycinnamyl chromophore are used in different proteins. This domain recognizes oxygen and CO (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 463802 [Multi-domain]  Cd Length: 65  Bit Score: 34.83  E-value: 5.34e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 754753039    7 INKLLDFLGDAVLIVNETSKIVFSNNACCTLLGYSKNELLDMQLSDLINP 56
Cdd:pfam13188   3 LRALFESSPDGILVLDEGGRIIYVNPAALELLGYELLGELLGELLDLLDP 52
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
 3-120 6.41e-03

Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444507 [Multi-domain]  Cd Length: 496  Bit Score: 38.17  E-value: 6.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754753039   3 NNSSINKLLDFLGDAVLIVNETSKIVFSNNACCTLLGYSKNELLDMQLSDLINPSSinthDENVARFIKHQSAPKVMSE- 81
Cdd:COG5805  155 QEERLQTLIENSPDLICVIDTDGRILFINESIERLFGAPREELIGKNLLELLHPCD----KEEFKERIESITEVWQEFIi 230

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 754753039  82 -RNLITcykKNGQPVKLRISISCL--EYQGKPCAIAIIHDFT 120
Cdd:COG5805  231 eREIIT---KDGRIRYFEAVIVPLidTDGSVKGILVILRDIT 269
 
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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