NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|653594720|ref|WP_027607612|]
View 

MULTISPECIES: diguanylate cyclase domain-containing protein [Pseudomonas]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 179-331 1.03e-58

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


:

Pssm-ID: 143635 [Multi-domain]  Cd Length: 158  Bit Score: 186.22  E-value: 1.03e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720 179 RDALTLVANRYRLEKVLLEECDRAQRFRLPLALIAMDIDDFKPINDQHGHGVGDQTLLQVVECLESCLRPGDLLARWGGD 258
Cdd:cd01949    2 TDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGD 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 653594720 259 EFIAVLPKSALETARELAEKICQKMRKIPMRGG--LHVTLSVGVAERRMD-ESPSALMARADQALYRAKAAGKDGV 331
Cdd:cd01949   82 EFAILLPGTDLEEAEALAERLREAIEEPFFIDGqeIRVTASIGIATYPEDgEDAEELLRRADEALYRAKRSGRNRV 157
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 38-128 1.52e-24

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.


:

Pssm-ID: 430001 [Multi-domain]  Cd Length: 89  Bit Score: 95.10  E-value: 1.52e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720   38 FVYRNPGWYEMLGYPRHSLENSVFTWETVIHPEDYPHVMTLFDDYIHRRAPhYQIEYRCRKKDGSYLWIEDRGYVIaRNP 117
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELLGKGESWLDLVHPDDRERVREALWEALKGGEP-YSGEYRIRRKDGEYRWVEARARPI-RDE 78

                          90
                  ....*....|.
gi 653594720  118 DGSVARMVGAH 128
Cdd:pfam08447  79 NGKPVRVIGVA 89
PAS_8 pfam13188
PAS domain; PAS domains are involved in many signalling proteins where they are used as a ...
 17-51 2.69e-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: 35.99  E-value: 2.69e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 653594720   17 MLHTVLELVSDGIWDWNANTGFVYRNPGWYEMLGY 51
Cdd:pfam13188   2 RLRALFESSPDGILVLDEGGRIIYVNPAALELLGY 36
 
Name Accession Description Interval E-value
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 179-331 1.03e-58

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


Pssm-ID: 143635 [Multi-domain]  Cd Length: 158  Bit Score: 186.22  E-value: 1.03e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720 179 RDALTLVANRYRLEKVLLEECDRAQRFRLPLALIAMDIDDFKPINDQHGHGVGDQTLLQVVECLESCLRPGDLLARWGGD 258
Cdd:cd01949    2 TDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGD 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 653594720 259 EFIAVLPKSALETARELAEKICQKMRKIPMRGG--LHVTLSVGVAERRMD-ESPSALMARADQALYRAKAAGKDGV 331
Cdd:cd01949   82 EFAILLPGTDLEEAEALAERLREAIEEPFFIDGqeIRVTASIGIATYPEDgEDAEELLRRADEALYRAKRSGRNRV 157
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 104-332 5.82e-58

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: 188.26  E-value: 5.82e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720 104 LWIEDRGYVIARNPDGSVARMVGAHRDIHIRKCSVEQLERRNQSLEALVAERTRELSRVNQQLQLQLDENRSLAERDALT 183
Cdd:COG2199   41 LLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLLLLALEDITELRRLEERLRRLATHDPLT 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720 184 LVANRYRLEKVLLEECDRAQRFRLPLALIAMDIDDFKPINDQHGHGVGDQTLLQVVECLESCLRPGDLLARWGGDEFIAV 263
Cdd:COG2199  121 GLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVL 200

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 653594720 264 LPKSALETARELAEKICQKMRKIPMR---GGLHVTLSVGVAERRMD-ESPSALMARADQALYRAKAAGKDGVS 332
Cdd:COG2199  201 LPGTDLEEAEALAERLREALEQLPFElegKELRVTVSIGVALYPEDgDSAEELLRRADLALYRAKRAGRNRVV 273
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 176-332 5.21e-51

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 166.65  E-value: 5.21e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720   176 LAERDALTLVANRYRLEKVLLEECDRAQRFRLPLALIAMDIDDFKPINDQHGHGVGDQTLLQVVECLESCLRPGDLLARW 255
Cdd:smart00267   2 LAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720   256 GGDEFIAVLPKSALETARELAEKICQKMRK--IPMRGGLHVTLSVGVAERRMD-ESPSALMARADQALYRAKAAGKDGVS 332
Cdd:smart00267  82 GGDEFALLLPETSLEEAIALAERILQQLREpiIIHGIPLYLTISIGVAAYPNPgEDAEDLLKRADTALYQAKKAGRNQVA 161
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 177-329 8.56e-50

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: 163.19  E-value: 8.56e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720  177 AERDALTLVANRYRLEKVLLEECDRAQRFRLPLALIAMDIDDFKPINDQHGHGVGDQTLLQVVECLESCLRPGDLLARWG 256
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 653594720  257 GDEFIAVLPKSALETARELAEKICQ--KMRKIPMRGG---LHVTLSVGVAERRMD-ESPSALMARADQALYRAKAAGKD 329
Cdd:pfam00990  81 GDEFAILLPETSLEGAQELAERIRRllAKLKIPHTVSglpLYVTISIGIAAYPNDgEDPEDLLKRADTALYQAKQAGRN 159
diguan_SiaD NF038266
biofilm regulation diguanylate cyclase SiaD;
144-329 1.81e-44

biofilm regulation diguanylate cyclase SiaD;


Pssm-ID: 468439 [Multi-domain]  Cd Length: 252  Bit Score: 152.83  E-value: 1.81e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720 144 RNQSLEALVAERTRELSRVN------QQLQLQLDEN-RSLAERDALTLVANRYRLEKVLLEECDRAQRFRLPLALIAMDI 216
Cdd:NF038266  54 RELSLAERYDRQLRRLEKIVrisdryQRMMRDLNEAlREASTRDPLTGLPNRRLLMERLREEVERARRSGRPFTLAMLDV 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720 217 DDFKPINDQHGHGVGDQTLLQVVECLESCLRPGDLLARWGGDEFIAVLPKSALETARELAEKICQKMRKIPMRGG---LH 293
Cdd:NF038266 134 DHFKRINDRYGHEVGDRVLVEIARTLRAELREYDLCGRWGGEEFLLLLPETGLEEAQVVLERLREAVRALAVRVGddvLS 213

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 653594720 294 VTLSVGVAERRMDESP-SALMARADQALYRAKAAGKD 329
Cdd:NF038266 214 VTASAGLAEHRPPEEGlSATLSRADQALYQAKRAGRD 250
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 176-331 9.84e-41

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: 140.16  E-value: 9.84e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720  176 LAERDALTLVANRYRLEKVLLEECDRAQRFRLPLALIAMDIDDFKPINDQHGHGVGDQTLLQVVECLESCLRPGDLLARW 255
Cdd:TIGR00254   1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720  256 GGDEFIAVLPKSALETARELAEKICQKMRKIPM----RGGLHVTLSVGVAERRMD-ESPSALMARADQALYRAKAAGKDG 330
Cdd:TIGR00254  81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPIevagSETLTVTVSIGVACYPGHgLTLEELLKRADEALYQAKKAGRNR 160


                  .
gi 653594720  331 V 331
Cdd:TIGR00254 161 V 161
pleD PRK09581
response regulator PleD; Reviewed
 161-333 4.99e-40

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 146.20  E-value: 4.99e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720 161 RVNQQLQLQLDENRSLAERDALTLVANRYRLEKVLLEECDRAQRFRLPLALIAMDIDDFKPINDQHGHGVGDQTLLQVVE 240
Cdd:PRK09581 276 RYQDALRNNLEQSIEMAVTDGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAK 355

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720 241 CLESCLRPGDLLARWGGDEFIAVLPKSALETARELAEKICQKMRKIPMR--GG---LHVTLSVGVAE-RRMDESPSALMA 314
Cdd:PRK09581 356 RLRNNIRGTDLIARYGGEEFVVVMPDTDIEDAIAVAERIRRKIAEEPFIisDGkerLNVTVSIGVAElRPSGDTIEALIK 435

                        170
                 ....*....|....*....
gi 653594720 315 RADQALYRAKAAGKDGVSA 333
Cdd:PRK09581 436 RADKALYEAKNTGRNRVVA 454
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 38-128 1.52e-24

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.


Pssm-ID: 430001 [Multi-domain]  Cd Length: 89  Bit Score: 95.10  E-value: 1.52e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720   38 FVYRNPGWYEMLGYPRHSLENSVFTWETVIHPEDYPHVMTLFDDYIHRRAPhYQIEYRCRKKDGSYLWIEDRGYVIaRNP 117
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELLGKGESWLDLVHPDDRERVREALWEALKGGEP-YSGEYRIRRKDGEYRWVEARARPI-RDE 78

                          90
                  ....*....|.
gi 653594720  118 DGSVARMVGAH 128
Cdd:pfam08447  79 NGKPVRVIGVA 89
PAS COG2202
PAS domain [Signal transduction mechanisms];
16-178 6.64e-16

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 76.22  E-value: 6.64e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720  16 DMLHTVLELVSDGIWDWNANTGFVYRNPGWYEMLGYPRHSLENSvfTWETVIHPEDYPHVMTLFDDYIHRRaPHYQIEYR 95
Cdd:COG2202   11 RRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGK--TLRDLLPPEDDDEFLELLRAALAGG-GVWRGELR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720  96 CRKKDGSYLWIEDRGYVIaRNPDGSVARMVGAHRDIHIRKCSVEQLERRNQSLEALVAERTRELSRVNQQLQLqLDENRS 175
Cdd:COG2202   88 NRRKDGSLFWVELSISPV-RDEDGEITGFVGIARDITERKRAEEALRESEERLRLLVENAPDGIFVLDLDGRI-LYVNPA 165


                 ...
gi 653594720 176 LAE 178
Cdd:COG2202  166 AEE 168
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 26-131 2.95e-10

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: 56.49  E-value: 2.95e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720  26 SDGIWDWNANTGFVYRNPGWYEMLGYPRHSLENSvfTWETVIHPEDYPHVMTLFDDYIHRRAPhYQIEYRCRKKDGSYLW 105
Cdd:cd00130    2 PDGVIVLDLDGRILYANPAAEQLLGYSPEELIGK--SLLDLIHPEDREELRERLENLLSGGEP-VTLEVRLRRKDGSVIW 78

                         90       100
                 ....*....|....*....|....*.
gi 653594720 106 IEDRGYVIaRNPDGSVARMVGAHRDI 131
Cdd:cd00130   79 VLVSLTPI-RDEGGEVIGLLGVVRDI 103
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
 16-141 5.73e-09

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: 53.45  E-value: 5.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720   16 DMLHTVLELVSDGIWDWNANTGFVYRNPGWYEMLGYPRHSLENSvfTWETVIHPEDYPHVMTLFDDYIHRRAPHYQIEYR 95
Cdd:TIGR00229   3 ERYRAIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGR--NVLELIPEEDREEVRERIERRLEGEPEPVSEERR 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 653594720   96 CRKKDGSYLWIEDRGYVIARNpdGSVARMVGAHRDIHIRKCSVEQL 141
Cdd:TIGR00229  81 VRRKDGSEIWVEVSVSPIRTN--GGELGVVGIVRDITERKEAEEAL 124
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 16-76 3.94e-07

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: 46.62  E-value: 3.94e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 653594720    16 DMLHTVLELVSDGIWDWNANTGFVYRNPGWYEMLGYPRHSLENSvfTWETVIHPEDYPHVM 76
Cdd:smart00091   1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGK--SLLELIHPEDRERVQ 59
PRK13560 PRK13560
hypothetical protein; Provisional
 43-186 2.28e-05

hypothetical protein; Provisional


Pssm-ID: 106506 [Multi-domain]  Cd Length: 807  Bit Score: 46.20  E-value: 2.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720  43 PGWYEML--------GYPRHSLENSVFTWETVIHPEDYPHVMTLFDDYIHRRAPHYQIEYRCRKKDGSYLWIEDRGYViA 114
Cdd:PRK13560 493 EGWPVELvsknitqfGYEPDEFISGKRMFAAIIHPADLEQVAAEVAEFAAQGVDRFEQEYRILGKGGAVCWIDDQSAA-E 571

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 653594720 115 RNPDGSVARMVGAHRDIHIRKCSVEQLERRNQSLEALVAERTRelsRVNQQLQL---QLD-ENRSLAERDALTLVA 186
Cdd:PRK13560 572 RDEEGQISHFEGIVIDISERKHAEEKIKAALTEKEVLLKEIHH---RVKNNLQIissLLDlQAEKLHDEEAKCAFA 644
PAS_8 pfam13188
PAS domain; PAS domains are involved in many signalling proteins where they are used as a ...
 17-51 2.69e-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: 35.99  E-value: 2.69e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 653594720   17 MLHTVLELVSDGIWDWNANTGFVYRNPGWYEMLGY 51
Cdd:pfam13188   2 RLRALFESSPDGILVLDEGGRIIYVNPAALELLGY 36
 
Name Accession Description Interval E-value
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 179-331 1.03e-58

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


Pssm-ID: 143635 [Multi-domain]  Cd Length: 158  Bit Score: 186.22  E-value: 1.03e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720 179 RDALTLVANRYRLEKVLLEECDRAQRFRLPLALIAMDIDDFKPINDQHGHGVGDQTLLQVVECLESCLRPGDLLARWGGD 258
Cdd:cd01949    2 TDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGD 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 653594720 259 EFIAVLPKSALETARELAEKICQKMRKIPMRGG--LHVTLSVGVAERRMD-ESPSALMARADQALYRAKAAGKDGV 331
Cdd:cd01949   82 EFAILLPGTDLEEAEALAERLREAIEEPFFIDGqeIRVTASIGIATYPEDgEDAEELLRRADEALYRAKRSGRNRV 157
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 104-332 5.82e-58

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: 188.26  E-value: 5.82e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720 104 LWIEDRGYVIARNPDGSVARMVGAHRDIHIRKCSVEQLERRNQSLEALVAERTRELSRVNQQLQLQLDENRSLAERDALT 183
Cdd:COG2199   41 LLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLLLLALEDITELRRLEERLRRLATHDPLT 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720 184 LVANRYRLEKVLLEECDRAQRFRLPLALIAMDIDDFKPINDQHGHGVGDQTLLQVVECLESCLRPGDLLARWGGDEFIAV 263
Cdd:COG2199  121 GLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVL 200

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 653594720 264 LPKSALETARELAEKICQKMRKIPMR---GGLHVTLSVGVAERRMD-ESPSALMARADQALYRAKAAGKDGVS 332
Cdd:COG2199  201 LPGTDLEEAEALAERLREALEQLPFElegKELRVTVSIGVALYPEDgDSAEELLRRADLALYRAKRAGRNRVV 273
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 176-332 5.21e-51

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 166.65  E-value: 5.21e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720   176 LAERDALTLVANRYRLEKVLLEECDRAQRFRLPLALIAMDIDDFKPINDQHGHGVGDQTLLQVVECLESCLRPGDLLARW 255
Cdd:smart00267   2 LAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720   256 GGDEFIAVLPKSALETARELAEKICQKMRK--IPMRGGLHVTLSVGVAERRMD-ESPSALMARADQALYRAKAAGKDGVS 332
Cdd:smart00267  82 GGDEFALLLPETSLEEAIALAERILQQLREpiIIHGIPLYLTISIGVAAYPNPgEDAEDLLKRADTALYQAKKAGRNQVA 161
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 177-329 8.56e-50

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: 163.19  E-value: 8.56e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720  177 AERDALTLVANRYRLEKVLLEECDRAQRFRLPLALIAMDIDDFKPINDQHGHGVGDQTLLQVVECLESCLRPGDLLARWG 256
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 653594720  257 GDEFIAVLPKSALETARELAEKICQ--KMRKIPMRGG---LHVTLSVGVAERRMD-ESPSALMARADQALYRAKAAGKD 329
Cdd:pfam00990  81 GDEFAILLPETSLEGAQELAERIRRllAKLKIPHTVSglpLYVTISIGIAAYPNDgEDPEDLLKRADTALYQAKQAGRN 159
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 100-332 4.32e-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: 4.32e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720 100 DGSYLWIEDRGYVIARNPDGSVARMVGAHRDIHIRKCSVEQLERRNQSLEALVAERTRELSRVNQQLQLQlDENRSLAER 179
Cdd:COG5001  175 LLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAE-ERLRHLAYH 253

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720 180 DALTLVANRYRLEKVLLEECDRAQRFRLPLALIAMDIDDFKPINDQHGHGVGDQTLLQVVECLESCLRPGDLLARWGGDE 259
Cdd:COG5001  254 DPLTGLPNRRLFLDRLEQALARARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDE 333

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 653594720 260 FIAVLP-KSALETARELAEKICQKMRKiPMRGG---LHVTLSVGVAERRMD-ESPSALMARADQALYRAKAAGKDGVS 332
Cdd:COG5001  334 FAVLLPdLDDPEDAEAVAERILAALAE-PFELDgheLYVSASIGIALYPDDgADAEELLRNADLAMYRAKAAGRNRYR 410
diguan_SiaD NF038266
biofilm regulation diguanylate cyclase SiaD;
144-329 1.81e-44

biofilm regulation diguanylate cyclase SiaD;


Pssm-ID: 468439 [Multi-domain]  Cd Length: 252  Bit Score: 152.83  E-value: 1.81e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720 144 RNQSLEALVAERTRELSRVN------QQLQLQLDEN-RSLAERDALTLVANRYRLEKVLLEECDRAQRFRLPLALIAMDI 216
Cdd:NF038266  54 RELSLAERYDRQLRRLEKIVrisdryQRMMRDLNEAlREASTRDPLTGLPNRRLLMERLREEVERARRSGRPFTLAMLDV 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720 217 DDFKPINDQHGHGVGDQTLLQVVECLESCLRPGDLLARWGGDEFIAVLPKSALETARELAEKICQKMRKIPMRGG---LH 293
Cdd:NF038266 134 DHFKRINDRYGHEVGDRVLVEIARTLRAELREYDLCGRWGGEEFLLLLPETGLEEAQVVLERLREAVRALAVRVGddvLS 213

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 653594720 294 VTLSVGVAERRMDESP-SALMARADQALYRAKAAGKD 329
Cdd:NF038266 214 VTASAGLAEHRPPEEGlSATLSRADQALYQAKRAGRD 250
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 176-331 9.84e-41

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: 140.16  E-value: 9.84e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720  176 LAERDALTLVANRYRLEKVLLEECDRAQRFRLPLALIAMDIDDFKPINDQHGHGVGDQTLLQVVECLESCLRPGDLLARW 255
Cdd:TIGR00254   1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720  256 GGDEFIAVLPKSALETARELAEKICQKMRKIPM----RGGLHVTLSVGVAERRMD-ESPSALMARADQALYRAKAAGKDG 330
Cdd:TIGR00254  81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPIevagSETLTVTVSIGVACYPGHgLTLEELLKRADEALYQAKKAGRNR 160


                  .
gi 653594720  331 V 331
Cdd:TIGR00254 161 V 161
pleD PRK09581
response regulator PleD; Reviewed
 161-333 4.99e-40

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 146.20  E-value: 4.99e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720 161 RVNQQLQLQLDENRSLAERDALTLVANRYRLEKVLLEECDRAQRFRLPLALIAMDIDDFKPINDQHGHGVGDQTLLQVVE 240
Cdd:PRK09581 276 RYQDALRNNLEQSIEMAVTDGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAK 355

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720 241 CLESCLRPGDLLARWGGDEFIAVLPKSALETARELAEKICQKMRKIPMR--GG---LHVTLSVGVAE-RRMDESPSALMA 314
Cdd:PRK09581 356 RLRNNIRGTDLIARYGGEEFVVVMPDTDIEDAIAVAERIRRKIAEEPFIisDGkerLNVTVSIGVAElRPSGDTIEALIK 435

                        170
                 ....*....|....*....
gi 653594720 315 RADQALYRAKAAGKDGVSA 333
Cdd:PRK09581 436 RADKALYEAKNTGRNRVVA 454
PRK09894 PRK09894
diguanylate cyclase; Provisional
 121-331 1.86e-32

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 122.48  E-value: 1.86e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720 121 VARMVGAHRDIHirKCSVEQLER------RNQSLEAlVAERTRELSRVNQQLQLQLDENRSlaERDALTLVANRyrleKV 194
Cdd:PRK09894  72 VRLLDSAHQHMH--NCARELLLAiveghwQDAHFDA-FQEGLLSFTAALTDYKIYLLTIRS--NMDVLTGLPGR----RV 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720 195 LLEECD--RAQRFRLPLALIAMDIDDFKPINDQHGHGVGDQTLLQVVECLESCLRPGDLLARWGGDEFIAVLPKSALETA 272
Cdd:PRK09894 143 LDESFDhqLRNREPQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGGEEFIICLKAATDEEA 222

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 653594720 273 RELAEKICQKMRKIPM---RGGLHVTLSVGVAERRMDESPSALMARADQALYRAKAAGKDGV 331
Cdd:PRK09894 223 CRAGERIRQLIANHAIthsDGRINITATFGVSRAFPEETLDVVIGRADRAMYEGKQTGRNRV 284
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 28-332 6.97e-32

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 126.33  E-value: 6.97e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720   28 GIWDWNANTGFVYRNPGWYEMLGYPRHsLENSVFTWETVIHPEDYPHVMTLFDDYIHRRAPhYQIEYRCRKKDGSYlWIE 107
Cdd:PRK09776  422 GIWEWDLKPNIISWDKRMFELYEIPPH-IKPTWQVWYACLHPEDRQRVEKEIRDALQGRSP-FKLEFRIVVKDGVR-HIR 498

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720  108 DRGYVIaRNPDGSVARMVGAHRDIHIRKCSVEQL----ERRNQSLEAL------------------VAE----------- 154
Cdd:PRK09776  499 ALANRV-LNKDGEVERLLGINMDMTEVRQLNEALfqekERLHITLDSIgeavvctdmamkvtfmnpVAEkmtgwtqeeal 577

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720  155 --------------------------RTRELSRVNQQLQLQ------------------LD--------------ENRSL 176
Cdd:PRK09776  578 gvplltvlhitfgdngplmeniysclTSRSAAYLEQDVVLHcrsggsydvhysitplstLDgenigsvlviqdvtESRKM 657

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720  177 -------AERDALTLVANRYRLEKVLLEECDRAQRFRLPLALIAMDIDDFKPINDQHGHGVGDQTLLQVVECLESCLRPG 249
Cdd:PRK09776  658 lrqlsysASHDALTHLANRASFEKQLRRLLQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSS 737

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720  250 DLLARWGGDEFIAVLPKSALETARELAEKICQKMR--KIPMRGGLH-VTLSVGVAERRMDESPSA-LMARADQALYRAKA 325
Cdd:PRK09776  738 DVLARLGGDEFGLLLPDCNVESARFIATRIISAINdyHFPWEGRVYrVGASAGITLIDANNHQASeVMSQADIACYAAKN 817


                  ....*..
gi 653594720  326 AGKDGVS 332
Cdd:PRK09776  818 AGRGRVT 824
PRK15426 PRK15426
cellulose biosynthesis regulator YedQ;
174-333 6.37e-29

cellulose biosynthesis regulator YedQ;


Pssm-ID: 237964 [Multi-domain]  Cd Length: 570  Bit Score: 116.65  E-value: 6.37e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720 174 RSLAERDALTLVANRYRLEKVLLEECDRAQRFRLPLALIAMDIDDFKPINDQHGHGVGDQTLLQVVECLESCLRPGDLLA 253
Cdd:PRK15426 395 QWQAWHDPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVAG 474

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720 254 RWGGDEFIAVLPKSALETARELAEKICQKM--------RKIPMRgglhVTLSVGVAERRMDESPS--ALMARADQALYRA 323
Cdd:PRK15426 475 RVGGEEFCVVLPGASLAEAAQVAERIRLRInekeilvaKSTTIR----ISASLGVSSAEEDGDYDfeQLQSLADRRLYLA 550

                        170
                 ....*....|
gi 653594720 324 KAAGKDGVSA 333
Cdd:PRK15426 551 KQAGRNRVCA 560
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 38-128 1.52e-24

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.


Pssm-ID: 430001 [Multi-domain]  Cd Length: 89  Bit Score: 95.10  E-value: 1.52e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720   38 FVYRNPGWYEMLGYPRHSLENSVFTWETVIHPEDYPHVMTLFDDYIHRRAPhYQIEYRCRKKDGSYLWIEDRGYVIaRNP 117
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELLGKGESWLDLVHPDDRERVREALWEALKGGEP-YSGEYRIRRKDGEYRWVEARARPI-RDE 78

                          90
                  ....*....|.
gi 653594720  118 DGSVARMVGAH 128
Cdd:pfam08447  79 NGKPVRVIGVA 89
adrA PRK10245
diguanylate cyclase AdrA; Provisional
 160-329 1.79e-22

diguanylate cyclase AdrA; Provisional


Pssm-ID: 182329 [Multi-domain]  Cd Length: 366  Bit Score: 96.44  E-value: 1.79e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720 160 SRVNQQLQLQLDENRS----LAERDALTLVANRYRLEKVLLEECDRAQRFRLPLALIAMDIDDFKPINDQHGHGVGDQTL 235
Cdd:PRK10245 184 AWVSYQTATKLAEHKRrlqvMSTRDGMTGVYNRRHWETLLRNEFDNCRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAI 263

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720 236 LQVVECLESCLRPGDLLARWGGDEFIAVLPKSALETARELAEKICQKMRKIPMRGGLHVTL--SVGVA--ERRMDESPSA 311
Cdd:PRK10245 264 VALTRQLQITLRGSDVIGRFGGDEFAVIMSGTPAESAITAMSRVHEGLNTLRLPNAPQVTLriSVGVAplNPQMSHYREW 343

                        170
                 ....*....|....*...
gi 653594720 312 LMArADQALYRAKAAGKD 329
Cdd:PRK10245 344 LKS-ADLALYKAKNAGRN 360
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
174-328 2.76e-20

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 91.67  E-value: 2.76e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720 174 RSLAERDALTLVANRYRLEKVL---LEECDRAQrfrlpLALIAMDIDDFKPINDQHGHGVGDQTLLQVVECLESCLRPGD 250
Cdd:PRK10060 234 RILANTDSITGLPNRNAIQELIdhaINAADNNQ-----VGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQ 308

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720 251 LLARWGGDEFIAVLPKSALETARELAEKICQKMRKiPMRGGL---HVTLSVGVA-ERRMDESPSALMARADQALYRAKAA 326
Cdd:PRK10060 309 TLARLGGDEFLVLASHTSQAALEAMASRILTRLRL-PFRIGLievYTGCSIGIAlAPEHGDDSESLIRSADTAMYTAKEG 387


                 ..
gi 653594720 327 GK 328
Cdd:PRK10060 388 GR 389
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 67-327 1.85e-16

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 80.20  E-value: 1.85e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720  67 IHPEDYPHVMTLFDDY-IHRRAPHYQIEYRCRKkdgsyLWiedrGYVIARNpDGSVARMV------GAHRDIHIrkcsvE 139
Cdd:PRK11359 285 VLNESHVSLFALRNGMpIHWASSSHGAEYQNAQ-----SW----SATIRQR-DGAPAGTLqiktssGAETSAFI-----E 349

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720 140 QLERRNQSLEALVAERTRELSRVNQQLQLqldenrslaerDALTLVANRYRLEKVLLEECDRAQrfrlPLALIAMDIDDF 219
Cdd:PRK11359 350 RVADISQHLAALALEQEKSRQHIEQLIQF-----------DPLTGLPNRNNLHNYLDDLVDKAV----SPVVYLIGVDHF 414

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720 220 KPINDQHGHGVGDQTLLQVVECLESCLRPGDLLARWGGDEFIAVLPKSALETARELAEKICQKMRKIPMRGG--LHVTLS 297
Cdd:PRK11359 415 QDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGTQFVLVSLENDVSNITQIADELRNVVSKPIMIDDkpFPLTLS 494

                        250       260       270
                 ....*....|....*....|....*....|.
gi 653594720 298 VGVAErRMDESPSALMARADQAL-YRAKAAG 327
Cdd:PRK11359 495 IGISY-DVGKNRDYLLSTAHNAMdYIRKNGG 524
PAS COG2202
PAS domain [Signal transduction mechanisms];
16-178 6.64e-16

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 76.22  E-value: 6.64e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720  16 DMLHTVLELVSDGIWDWNANTGFVYRNPGWYEMLGYPRHSLENSvfTWETVIHPEDYPHVMTLFDDYIHRRaPHYQIEYR 95
Cdd:COG2202   11 RRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGK--TLRDLLPPEDDDEFLELLRAALAGG-GVWRGELR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720  96 CRKKDGSYLWIEDRGYVIaRNPDGSVARMVGAHRDIHIRKCSVEQLERRNQSLEALVAERTRELSRVNQQLQLqLDENRS 175
Cdd:COG2202   88 NRRKDGSLFWVELSISPV-RDEDGEITGFVGIARDITERKRAEEALRESEERLRLLVENAPDGIFVLDLDGRI-LYVNPA 165


                 ...
gi 653594720 176 LAE 178
Cdd:COG2202  166 AEE 168
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 212-324 3.03e-15

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: 72.63  E-value: 3.03e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720 212 IAMDIDDF--KPINDQhghgvgdqTLLQVVeclesclrpgDLLARWGGDEFIAVLPKSALETARELAEKICQKMRKIPmr 289
Cdd:COG3706   94 LEAGADDYltKPFDPE--------ELLARV----------DLVARYGGEEFAILLPGTDLEGALAVAERIREAVAELP-- 153

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 653594720 290 gGLHVTLSVGVAErrmdespSALMARADqALYRAK 324
Cdd:COG3706  154 -SLRVTVSIGVAG-------DSLLKRAD-ALYQAR 179
PAS COG2202
PAS domain [Signal transduction mechanisms];
17-141 1.05e-14

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 72.75  E-value: 1.05e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720  17 MLHTVLELVSDGIWDWNANTGFVYRNPGWYEMLGYPRHSLENSvfTWETVIHPEDYPHVMTLFDDYIHRRAPHYQIEYRC 96
Cdd:COG2202  138 RLRLLVENAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGK--SLLDLLHPEDRERLLELLRRLLEGGRESYELELRL 215

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 653594720  97 RKKDGSYLWIEDRgyVIARNPDGSVARMVGAHRDIHIRKCSVEQL 141
Cdd:COG2202  216 KDGDGRWVWVEAS--AVPLRDGGEVIGVLGIVRDITERKRAEEAL 258
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
 208-325 2.93e-13

Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse group of nucleotidyl cyclases (NC's) containing prokaryotic and eukaryotic proteins. They can be divided into two major groups; the mononucleotidyl cyclases (MNC's) and the diguanylate cyclases (DGC's). The MNC's, which include the adenylate cyclases (AC's) and the guanylate cyclases (GC's), have a conserved cyclase homology domain (CHD), while the DGC's have a conserved GGDEF domain, named after a conserved motif within this subgroup. Their products, cyclic guanylyl and adenylyl nucleotides, are second messengers that play important roles in eukaryotic signal transduction and prokaryotic sensory pathways.


Pssm-ID: 143637 [Multi-domain]  Cd Length: 133  Bit Score: 65.84  E-value: 2.93e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720 208 PLALIAMDIDDFKPINDQHGHGVGDQTLLQVVECLES-CLRPGDLLARWGGDEFIAVLPKSALETARELAEKICQKMRKI 286
Cdd:cd07556    1 PVTILFADIVGFTSLADALGPDEGDELLNELAGRFDSlIRRSGDLKIKTIGDEFMVVSGLDHPAAAVAFAEDMREAVSAL 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 653594720 287 PMRGGLHVTLSVGVA----------ERRMDESPSALMARADQALYRAKA 325
Cdd:cd07556   81 NQSEGNPVRVRIGIHtgpvvvgvigSRPQYDVWGALVNLASRMESQAKA 129
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
 21-154 1.34e-10

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: 61.91  E-value: 1.34e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720  21 VLELVSDGIWDWNANTGFVYRNPGWYEMLGYPRHSLENSVFTweTVIHPEDYPHVMTLFDDyIHRRAPHYQIEYRCRKKD 100
Cdd:COG5809  146 IFNHSPDGIIVTDLDGRIIYANPAACKLLGISIEELIGKSIL--ELIHSDDQENVAAFISQ-LLKDGGIAQGEVRFWTKD 222

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 653594720 101 GSYLWIEDRGYVIarNPDGSVARMVGAHRDIHIRKcSVEQLERRNQSLeALVAE 154
Cdd:COG5809  223 GRWRLLEASGAPI--KKNGEVDGIVIIFRDITERK-KLEELLRKSEKL-SVVGE 272
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 26-131 2.95e-10

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: 56.49  E-value: 2.95e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720  26 SDGIWDWNANTGFVYRNPGWYEMLGYPRHSLENSvfTWETVIHPEDYPHVMTLFDDYIHRRAPhYQIEYRCRKKDGSYLW 105
Cdd:cd00130    2 PDGVIVLDLDGRILYANPAAEQLLGYSPEELIGK--SLLDLIHPEDREELRERLENLLSGGEP-VTLEVRLRRKDGSVIW 78

                         90       100
                 ....*....|....*....|....*.
gi 653594720 106 IEDRGYVIaRNPDGSVARMVGAHRDI 131
Cdd:cd00130   79 VLVSLTPI-RDEGGEVIGLLGVVRDI 103
PRK09966 PRK09966
diguanylate cyclase DgcN;
143-324 1.26e-09

diguanylate cyclase DgcN;


Pssm-ID: 182171 [Multi-domain]  Cd Length: 407  Bit Score: 58.86  E-value: 1.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720 143 RRNQSLEALVA-ERTRELSRVNQ------------QLQLQLDENRSL--AERDALTLVANR--YRLEKVLLEECDRAqrf 205
Cdd:PRK09966 199 RSNRNFSRRVSeERIAEFHRFALdfnslldemeewQLRLQAKNAQLLrtALHDPLTGLANRaaFRSGINTLMNNSDA--- 275

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720 206 RLPLALIAMDIDDFKPINDQHGHGVGDQTLLQVVECLESCLRPGDLLARWGGDEFIAVLPKSALETArelAEKICQKMRK 285
Cdd:PRK09966 276 RKTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHKAYRLGGDEFAMVLYDVQSESE---VQQICSALTQ 352

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 653594720 286 IPMRG-GLH------VTLSVGVAERRMDESPSALMARADQALYRAK 324
Cdd:PRK09966 353 IFNLPfDLHnghqttMTLSIGYAMTIEHASAEKLQELADHNMYQAK 398
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
 16-141 5.73e-09

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: 53.45  E-value: 5.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720   16 DMLHTVLELVSDGIWDWNANTGFVYRNPGWYEMLGYPRHSLENSvfTWETVIHPEDYPHVMTLFDDYIHRRAPHYQIEYR 95
Cdd:TIGR00229   3 ERYRAIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGR--NVLELIPEEDREEVRERIERRLEGEPEPVSEERR 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 653594720   96 CRKKDGSYLWIEDRGYVIARNpdGSVARMVGAHRDIHIRKCSVEQL 141
Cdd:TIGR00229  81 VRRKDGSEIWVEVSVSPIRTN--GGELGVVGIVRDITERKEAEEAL 124
PRK13561 PRK13561
putative diguanylate cyclase; Provisional
 163-331 6.22e-09

putative diguanylate cyclase; Provisional


Pssm-ID: 184143 [Multi-domain]  Cd Length: 651  Bit Score: 57.03  E-value: 6.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720 163 NQQ-LQLQLDENRSLAERDALTLVANRYRLEKVLLEECDRAQRFrlplALIAMDIDdfkPINDQHGHGVGDQT---LLQV 238
Cdd:PRK13561 216 NQQlLQRQYEEQSRNATRFPVSDLPNKALLMALLEQVVARKQTT----ALMIITCE---TLRDTAGVLKEAQReilLLTL 288

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720 239 VECLESCLRPGDLLARWGGDEFiAVLPKSALET--ARELAEKICQKM-RKIPMRGG-LHVTLSVGVAERRMDESPSALMA 314
Cdd:PRK13561 289 VEKLKSVLSPRMVLAQISGYDF-AIIANGVKEPwhAITLGQQVLTIInERLPIQRIqLRPSCSIGIAMFYGDLTAEQLYS 367

                        170
                 ....*....|....*..
gi 653594720 315 RADQALYRAKAAGKDGV 331
Cdd:PRK13561 368 RAISAAFTARRKGKNQI 384
PRK11059 PRK11059
regulatory protein CsrD; Provisional
 139-323 3.23e-08

regulatory protein CsrD; Provisional


Pssm-ID: 236833 [Multi-domain]  Cd Length: 640  Bit Score: 54.87  E-value: 3.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720 139 EQLERR-----NQSLEALVAERTRE----LSRVNQQLQLQLDEN-----------RSLAERDALTLVANRY----RLEKV 194
Cdd:PRK11059 170 ELLEERarrilNGEREQAVAGSGYEwprtASRALDHLLSELQDAreersrfdtfiRSNAFQDAKTGLGNRLffdnQLATL 249

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720 195 LLEECDRAQrfrlPLALIAMDIDDFKPINDQHGHGVGDQTLLQVVECLESCLR--PGDLLARWGGDEFIAVLPKSALETA 272
Cdd:PRK11059 250 LEDQEMVGA----HGVVMLIRLPDFDLLQEEWGESQVEELLFELINLLSTFVMryPGALLARYSRSDFAVLLPHRSLKEA 325

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 653594720 273 RELAEKICQKMRKIPMRGGL------HvtlsVGVAERRMDESPSALMARADQALYRA 323
Cdd:PRK11059 326 DSLASQLLKAVDALPPPKMLdrddflH----IGICAYRSGQSTEQVMEEAEMALRSA 378
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 17-131 5.58e-08

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: 50.49  E-value: 5.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720   17 MLHTVLELVSDGIWDWNANTGFVYRNPGWYEMLGYPRHSLEN-SVFtweTVIHPEDYPHVMTLFDDYIHRRAPHYQIEYR 95
Cdd:pfam00989   2 DLRAILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGkSLL---DLIPEEDDAEVAELLRQALLQGEESRGFEVS 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 653594720   96 CRKKDGSYLWIEDRGyVIARNPDGSVARMVGAHRDI 131
Cdd:pfam00989  79 FRVPDGRPRHVEVRA-SPVRDAGGEILGFLGVLRDI 113
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 16-76 3.94e-07

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: 46.62  E-value: 3.94e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 653594720    16 DMLHTVLELVSDGIWDWNANTGFVYRNPGWYEMLGYPRHSLENSvfTWETVIHPEDYPHVM 76
Cdd:smart00091   1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGK--SLLELIHPEDRERVQ 59
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
 91-131 7.09e-07

Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif occurs C-terminal to a subset of all known PAS motifs. It is proposed to contribute to the PAS domain fold.


Pssm-ID: 197509  Cd Length: 43  Bit Score: 45.25  E-value: 7.09e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 653594720    91 QIEYRCRKKDGSYLWIEDRGYVIaRNPDGSVARMVGAHRDI 131
Cdd:smart00086   1 TVEYRLRRKDGSYIWVLVSASPI-RDEDGEVEGILGVVRDI 40
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
16-204 1.30e-06

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 49.46  E-value: 1.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720  16 DMLHTVLELVSDGIWDWNANTGFVYRNPGWYEMLGYPRHSLENSvfTWETVIHPEDypHVMTLFDDYIHRRAPHYQIEYR 95
Cdd:COG3852    7 ELLRAILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGR--PLAELFPEDS--PLRELLERALAEGQPVTEREVT 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720  96 CRKKDGSYLWIEDRGYVIaRNPDGSVARMVGAhRDIHIRKcsveQLERRNQSLEALVAerTRELSR-----VN------- 163
Cdd:COG3852   83 LRRKDGEERPVDVSVSPL-RDAEGEGGVLLVL-RDITERK----RLERELRRAEKLAA--VGELAAglaheIRnpltgir 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 653594720 164 ---QQLQLQLDENrslaERDALTlvanryrleKVLLEECDRAQR 204
Cdd:COG3852  155 gaaQLLERELPDD----ELREYT---------QLIIEEADRLNN 185
PRK13560 PRK13560
hypothetical protein; Provisional
 43-186 2.28e-05

hypothetical protein; Provisional


Pssm-ID: 106506 [Multi-domain]  Cd Length: 807  Bit Score: 46.20  E-value: 2.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720  43 PGWYEML--------GYPRHSLENSVFTWETVIHPEDYPHVMTLFDDYIHRRAPHYQIEYRCRKKDGSYLWIEDRGYViA 114
Cdd:PRK13560 493 EGWPVELvsknitqfGYEPDEFISGKRMFAAIIHPADLEQVAAEVAEFAAQGVDRFEQEYRILGKGGAVCWIDDQSAA-E 571

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 653594720 115 RNPDGSVARMVGAHRDIHIRKCSVEQLERRNQSLEALVAERTRelsRVNQQLQL---QLD-ENRSLAERDALTLVA 186
Cdd:PRK13560 572 RDEEGQISHFEGIVIDISERKHAEEKIKAALTEKEVLLKEIHH---RVKNNLQIissLLDlQAEKLHDEEAKCAFA 644
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
 38-131 3.08e-05

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: 42.06  E-value: 3.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720   38 FVYRNPGWYEMLGYPRHSLENSVFTWetVIHPEDYPHvmtLFDDYIHRRAPHYQIEYRCRKKDGSYLWIEDRGYVIaRNP 117
Cdd:pfam13426   4 IIYVNDAALRLLGYTREELLGKSITD--LFAEPEDSE---RLREALREGKAVREFEVVLYRKDGEPFPVLVSLAPI-RDD 77

                          90
                  ....*....|....
gi 653594720  118 DGSVARMVGAHRDI 131
Cdd:pfam13426  78 GGELVGIIAILRDI 91
PRK11829 PRK11829
biofilm formation regulator HmsP; Provisional
 195-331 4.29e-05

biofilm formation regulator HmsP; Provisional


Pssm-ID: 183329 [Multi-domain]  Cd Length: 660  Bit Score: 45.32  E-value: 4.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720 195 LLEECDRAQRFRLPLALIAMDIDDFKPINDQHGHGVGDQTLLQVVECLESCLRPGDLLARWGGDEFI-----AVLPKSAL 269
Cdd:PRK11829 249 LLEKEIASSTRTDHFHLLVIGIETLQEVSGAMSEAQHQQLLLTIVQRIEQCIDDSDLLAQLSKTEFAvlargTRRSFPAM 328

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 653594720 270 ETARELAEKICQK--MRKIPMRGglhvTLSVGVAERR-MDESPSALMARADQALYRAKAAGKDGV 331
Cdd:PRK11829 329 QLARRIMSQVTQPlfFDEITLRP----SASIGITRYQaQQDTAESMMRNASTAMMAAHHEGRNQI 389
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
 5-142 7.37e-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: 7.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720   5 SDNGNFSHLNA--DMLHTVLELVSDGIWDWNANTGFVYRNPGWYEMLGYPRHSLENSvfTWETVIHPEDYPhvmtLFDDY 82
Cdd:COG5809    2 KSSKMELQLRKseQRFRSLFENAPDAILILDLEGKILKVNPAAERIFGYTEDELLGT--NILDFLHPDDEK----ELREI 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 653594720  83 IHRRAPH---YQIEYRCRKKDGSYLWIEDRGYVIArNPDGSVARMVGAHRDIHIRKCSVEQLE 142
Cdd:COG5809   76 LKLLKEGesrDELEFELRHKNGKRLEFSSKLSPIF-DQNGDIEGMLAISRDITERKRMEEALR 137
PAS_8 pfam13188
PAS domain; PAS domains are involved in many signalling proteins where they are used as a ...
 17-51 2.69e-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: 35.99  E-value: 2.69e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 653594720   17 MLHTVLELVSDGIWDWNANTGFVYRNPGWYEMLGY 51
Cdd:pfam13188   2 RLRALFESSPDGILVLDEGGRIIYVNPAALELLGY 36
Sugar-bind pfam04198
Putative sugar-binding domain; This probable domain is found in bacterial transcriptional ...
 202-322 3.09e-03

Putative sugar-binding domain; This probable domain is found in bacterial transcriptional regulators such as DeoR and SorC. These proteins have an amino-terminal helix-turn-helix pfam00325 that binds to DNA. This domain is probably the ligand regulator binding region. SorC is regulated by sorbose and other members of this family are likely to be regulated by other sugar substrates.


Pssm-ID: 427778  Cd Length: 256  Bit Score: 38.76  E-value: 3.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653594720  202 AQRFRLPLALIAMDI-DDFKPINDQHGHGVGDqtllqvveCLESCLRPGDLLARWGGDEFIAVlpksaletARELAEKIC 280
Cdd:pfam04198  14 KEKFGLKEAIVVPGDsDENDLVLERLGRAAAQ--------YLESLLKDGDIVGVGWGRTLSAV--------AEALTPKSL 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 653594720  281 QKMRKIPMRGGLHVTLSVGVAErrmdesPSALMARADQALYR 322
Cdd:pfam04198  78 RNLKFVPLIGGLGRDGSAHSNT------VIARLAQKFGGSYY 113
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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