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Conserved domains on  [gi|694110604|ref|WP_032452941|]
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MULTISPECIES: sensor domain-containing diguanylate cyclase [Klebsiella]

Protein Classification

sensor domain-containing diguanylate cyclase( domain architecture ID 12140355)

sensor domain-containing diguanylate cyclase containing PAS sensor domain(s), catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules

CATH:  3.30.70.1230
EC:  2.7.7.65
Gene Ontology:  GO:0046872|GO:0052621|GO:0007165
PubMed:  11119645|9382818|15009198
SCOP:  4001316

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 229-401 2.35e-60

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: 197.12  E-value: 2.35e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110604 229 IRLMLCIIHDITEEVHLKKELEFSAAHDPLTGLLNRREFYRLVDApsFIA------HGFCLLLIDIDHFKSINDIHGHQK 302
Cdd:COG2199   90 LLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLER--ELArarregRPLALLLIDLDHFKRINDTYGHAA 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110604 303 GDEVLLVISRILETSVDREDKIYRWGGEEFLLFLPHSPIARALMVAEAIRQAVSEY------QTLSVTVSIGVAE-HHDG 375
Cdd:COG2199  168 GDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLpfelegKELRVTVSIGVALyPEDG 247

                        170       180
                 ....*....|....*....|....*.
gi 694110604 376 EAIDQLFYRVDKALYAAKNDGRNRVT 401
Cdd:COG2199  248 DSAEELLRRADLALYRAKRAGRNRVV 273
NtrB super family cl34682
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
141-262 1.07e-07

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: 53.31  E-value: 1.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110604 141 PMLLIDPQkeGRIVDANIAALRFYHYSDEEMRTKHTWQINTLGRDVIPIMNNIANMPGGHKPLNFTHILADGSLRHVQTY 220
Cdd:COG3852   19 AVIVLDAD--GRITYVNPAAERLLGLSAEELLGRPLAELFPEDSPLRELLERALAEGQPVTEREVTLRRKDGEERPVDVS 96

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 694110604 221 AGPVVLYNIRL-MLCIIHDITEEVHLKKELEFSA------------AHD---PLTGLL 262
Cdd:COG3852   97 VSPLRDAEGEGgVLLVLRDITERKRLERELRRAEklaavgelaaglAHEirnPLTGIR 154
 
Name Accession Description Interval E-value
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 229-401 2.35e-60

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: 197.12  E-value: 2.35e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110604 229 IRLMLCIIHDITEEVHLKKELEFSAAHDPLTGLLNRREFYRLVDApsFIA------HGFCLLLIDIDHFKSINDIHGHQK 302
Cdd:COG2199   90 LLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLER--ELArarregRPLALLLIDLDHFKRINDTYGHAA 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110604 303 GDEVLLVISRILETSVDREDKIYRWGGEEFLLFLPHSPIARALMVAEAIRQAVSEY------QTLSVTVSIGVAE-HHDG 375
Cdd:COG2199  168 GDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLpfelegKELRVTVSIGVALyPEDG 247

                        170       180
                 ....*....|....*....|....*.
gi 694110604 376 EAIDQLFYRVDKALYAAKNDGRNRVT 401
Cdd:COG2199  248 DSAEELLRRADLALYRAKRAGRNRVV 273
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 255-400 1.66e-57

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: 185.84  E-value: 1.66e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110604 255 HDPLTGLLNRREFY----RLVDAPSFIAHGFCLLLIDIDHFKSINDIHGHQKGDEVLLVISRILETSVDREDKIYRWGGE 330
Cdd:cd01949    2 TDPLTGLPNRRAFEerleRLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGD 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 694110604 331 EFLLFLPHSPIARALMVAEAIRQAVSEY-----QTLSVTVSIGVAEHH-DGEAIDQLFYRVDKALYAAKNDGRNRV 400
Cdd:cd01949   82 EFAILLPGTDLEEAEALAERLREAIEEPffidgQEIRVTASIGIATYPeDGEDAEELLRRADEALYRAKRSGRNRV 157
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 253-399 3.23e-48

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: 161.65  E-value: 3.23e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110604  253 AAHDPLTGLLNRREFY----RLVDAPSFIAHGFCLLLIDIDHFKSINDIHGHQKGDEVLLVISRILETSVDREDKIYRWG 328
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEeqleQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110604  329 GEEFLLFLPHSPIARALMVAEAIRQAVSEYQT--------LSVTVSIGVAEHH-DGEAIDQLFYRVDKALYAAKNDGRNR 399
Cdd:pfam00990  81 GDEFAILLPETSLEGAQELAERIRRLLAKLKIphtvsglpLYVTISIGIAAYPnDGEDPEDLLKRADTALYQAKQAGRNR 160
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 253-400 1.11e-46

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 157.79  E-value: 1.11e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110604   253 AAHDPLTGLLNRREFYRLVDA--PSFIAHG--FCLLLIDIDHFKSINDIHGHQKGDEVLLVISRILETSVDREDKIYRWG 328
Cdd:smart00267   3 AFRDPLTGLPNRRYFEEELEQelQRAQRQGspFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARLG 82

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 694110604   329 GEEFLLFLPHSPIARALMVAEAIRQAVSEY-----QTLSVTVSIGVAEHH-DGEAIDQLFYRVDKALYAAKNDGRNRV 400
Cdd:smart00267  83 GDEFALLLPETSLEEAIALAERILQQLREPiiihgIPLYLTISIGVAAYPnPGEDAEDLLKRADTALYQAKKAGRNQV 160
diguan_SiaD NF038266
biofilm regulation diguanylate cyclase SiaD;
245-400 3.52e-45

biofilm regulation diguanylate cyclase SiaD;


Pssm-ID: 468439 [Multi-domain]  Cd Length: 252  Bit Score: 156.68  E-value: 3.52e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110604 245 LKKELEFSAAHDPLTGLLNRREFY-RLVDAPSFI-AHG--FCLLLIDIDHFKSINDIHGHQKGDEVLLVISRILETSVDR 320
Cdd:NF038266  86 LNEALREASTRDPLTGLPNRRLLMeRLREEVERArRSGrpFTLAMLDVDHFKRINDRYGHEVGDRVLVEIARTLRAELRE 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110604 321 EDKIYRWGGEEFLLFLPHSPIARALMVAEAIRQAVSEYQ------TLSVTVSIGVAEHHDGE-AIDQLFYRVDKALYAAK 393
Cdd:NF038266 166 YDLCGRWGGEEFLLLLPETGLEEAQVVLERLREAVRALAvrvgddVLSVTASAGLAEHRPPEeGLSATLSRADQALYQAK 245


                 ....*..
gi 694110604 394 NDGRNRV 400
Cdd:NF038266 246 RAGRDRV 252
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 253-400 4.56e-43

diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by many proteins carrying the domain. There is evidence that the domain has diguanylate cyclase activity. Several proteins carrying this domain also carry domains with functions relating to environmental sensing. These include PleD, a response regulator protein involved in the swarmer-to-stalked cell transition in Caulobacter crescentus, and FixL, a heme-containing oxygen sensor protein. [Regulatory functions, Small molecule interactions, Signal transduction, Other]


Pssm-ID: 272984 [Multi-domain]  Cd Length: 165  Bit Score: 148.25  E-value: 4.56e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110604  253 AAHDPLTGLLNRREFYRLVDAPSFIA----HGFCLLLIDIDHFKSINDIHGHQKGDEVLLVISRILETSVDREDKIYRWG 328
Cdd:TIGR00254   2 AVRDPLTGLYNRRYLEEMLDSELKRArrfqRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110604  329 GEEFLLFLPHSPIARALMVAEAIRQA-------VSEYQTLSVTVSIGVAEH-HDGEAIDQLFYRVDKALYAAKNDGRNRV 400
Cdd:TIGR00254  82 GEEFVVILPGTPLEDALSKAERLRDAinskpieVAGSETLTVTVSIGVACYpGHGLTLEELLKRADEALYQAKKAGRNRV 161
pleD PRK09581
response regulator PleD; Reviewed
 244-400 5.77e-43

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 156.21  E-value: 5.77e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110604 244 HLKKELEFS---AAHDPLTGLLNRREF----YRLVDAPSFIAHGFCLLLIDIDHFKSINDIHGHQKGDEVLLVISRILET 316
Cdd:PRK09581 280 ALRNNLEQSiemAVTDGLTGLHNRRYFdmhlKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRN 359

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110604 317 SVDREDKIYRWGGEEFLLFLPHSPIARALMVAEAIRQAVSEY--------QTLSVTVSIGVAEH-HDGEAIDQLFYRVDK 387
Cdd:PRK09581 360 NIRGTDLIARYGGEEFVVVMPDTDIEDAIAVAERIRRKIAEEpfiisdgkERLNVTVSIGVAELrPSGDTIEALIKRADK 439

                        170
                 ....*....|...
gi 694110604 388 ALYAAKNDGRNRV 400
Cdd:PRK09581 440 ALYEAKNTGRNRV 452
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
141-262 1.07e-07

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 53.31  E-value: 1.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110604 141 PMLLIDPQkeGRIVDANIAALRFYHYSDEEMRTKHTWQINTLGRDVIPIMNNIANMPGGHKPLNFTHILADGSLRHVQTY 220
Cdd:COG3852   19 AVIVLDAD--GRITYVNPAAERLLGLSAEELLGRPLAELFPEDSPLRELLERALAEGQPVTEREVTLRRKDGEERPVDVS 96

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 694110604 221 AGPVVLYNIRL-MLCIIHDITEEVHLKKELEFSA------------AHD---PLTGLL 262
Cdd:COG3852   97 VSPLRDAEGEGgVLLVLRDITERKRLERELRRAEklaavgelaaglAHEirnPLTGIR 154
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
 150-241 4.38e-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: 47.84  E-value: 4.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110604  150 EGRIVDANIAALRFYHYSDEEMRTKHTWQINTLGRDVIPIMNNIANMPGGHkPLNFTHILADGSLRHVQTYAGPVVL--Y 227
Cdd:pfam13426   1 DGRIIYVNDAALRLLGYTREELLGKSITDLFAEPEDSERLREALREGKAVR-EFEVVLYRKDGEPFPVLVSLAPIRDdgG 79

                          90
                  ....*....|....
gi 694110604  228 NIRLMLCIIHDITE 241
Cdd:pfam13426  80 ELVGIIAILRDITE 93
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
 130-250 6.83e-07

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: 48.06  E-value: 6.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110604  130 FFARFFMTNTAPMLLIDPqkEGRIVDANIAALRFYHYSDEEMRTKHTWQINT-LGRDVIP-IMNNIAnmPGGHKP--LNF 205
Cdd:TIGR00229   4 RYRAIFESSPDAIIVIDL--EGNILYVNPAFEEIFGYSAEELIGRNVLELIPeEDREEVReRIERRL--EGEPEPvsEER 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 694110604  206 THILADGSLRHVQTYAGPVVLYNIRL-MLCIIHDITEevhlKKELE 250
Cdd:TIGR00229  80 RVRRKDGSEIWVEVSVSPIRTNGGELgVVGIVRDITE----RKEAE 121
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 141-239 5.16e-05

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: 42.24  E-value: 5.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110604 141 PMLLIDPQkeGRIVDANIAALRFYHYSDEEMRTKHTWQInTLGRDVIPIMNNIANM--PGGHKPLNFTHILADGSLRHVQ 218
Cdd:cd00130    4 GVIVLDLD--GRILYANPAAEQLLGYSPEELIGKSLLDL-IHPEDREELRERLENLlsGGEPVTLEVRLRRKDGSVIWVL 80

                         90       100
                 ....*....|....*....|...
gi 694110604 219 TYAGPVV--LYNIRLMLCIIHDI 239
Cdd:cd00130   81 VSLTPIRdeGGEVIGLLGVVRDI 103
 
Name Accession Description Interval E-value
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 229-401 2.35e-60

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: 197.12  E-value: 2.35e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110604 229 IRLMLCIIHDITEEVHLKKELEFSAAHDPLTGLLNRREFYRLVDApsFIA------HGFCLLLIDIDHFKSINDIHGHQK 302
Cdd:COG2199   90 LLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLER--ELArarregRPLALLLIDLDHFKRINDTYGHAA 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110604 303 GDEVLLVISRILETSVDREDKIYRWGGEEFLLFLPHSPIARALMVAEAIRQAVSEY------QTLSVTVSIGVAE-HHDG 375
Cdd:COG2199  168 GDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLpfelegKELRVTVSIGVALyPEDG 247

                        170       180
                 ....*....|....*....|....*.
gi 694110604 376 EAIDQLFYRVDKALYAAKNDGRNRVT 401
Cdd:COG2199  248 DSAEELLRRADLALYRAKRAGRNRVV 273
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 255-400 1.66e-57

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: 185.84  E-value: 1.66e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110604 255 HDPLTGLLNRREFY----RLVDAPSFIAHGFCLLLIDIDHFKSINDIHGHQKGDEVLLVISRILETSVDREDKIYRWGGE 330
Cdd:cd01949    2 TDPLTGLPNRRAFEerleRLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGD 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 694110604 331 EFLLFLPHSPIARALMVAEAIRQAVSEY-----QTLSVTVSIGVAEHH-DGEAIDQLFYRVDKALYAAKNDGRNRV 400
Cdd:cd01949   82 EFAILLPGTDLEEAEALAERLREAIEEPffidgQEIRVTASIGIATYPeDGEDAEELLRRADEALYRAKRSGRNRV 157
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 253-399 3.23e-48

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: 161.65  E-value: 3.23e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110604  253 AAHDPLTGLLNRREFY----RLVDAPSFIAHGFCLLLIDIDHFKSINDIHGHQKGDEVLLVISRILETSVDREDKIYRWG 328
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEeqleQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110604  329 GEEFLLFLPHSPIARALMVAEAIRQAVSEYQT--------LSVTVSIGVAEHH-DGEAIDQLFYRVDKALYAAKNDGRNR 399
Cdd:pfam00990  81 GDEFAILLPETSLEGAQELAERIRRLLAKLKIphtvsglpLYVTISIGIAAYPnDGEDPEDLLKRADTALYQAKQAGRNR 160
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 253-400 1.11e-46

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 157.79  E-value: 1.11e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110604   253 AAHDPLTGLLNRREFYRLVDA--PSFIAHG--FCLLLIDIDHFKSINDIHGHQKGDEVLLVISRILETSVDREDKIYRWG 328
Cdd:smart00267   3 AFRDPLTGLPNRRYFEEELEQelQRAQRQGspFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARLG 82

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 694110604   329 GEEFLLFLPHSPIARALMVAEAIRQAVSEY-----QTLSVTVSIGVAEHH-DGEAIDQLFYRVDKALYAAKNDGRNRV 400
Cdd:smart00267  83 GDEFALLLPETSLEEAIALAERILQQLREPiiihgIPLYLTISIGVAAYPnPGEDAEDLLKRADTALYQAKKAGRNQV 160
diguan_SiaD NF038266
biofilm regulation diguanylate cyclase SiaD;
245-400 3.52e-45

biofilm regulation diguanylate cyclase SiaD;


Pssm-ID: 468439 [Multi-domain]  Cd Length: 252  Bit Score: 156.68  E-value: 3.52e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110604 245 LKKELEFSAAHDPLTGLLNRREFY-RLVDAPSFI-AHG--FCLLLIDIDHFKSINDIHGHQKGDEVLLVISRILETSVDR 320
Cdd:NF038266  86 LNEALREASTRDPLTGLPNRRLLMeRLREEVERArRSGrpFTLAMLDVDHFKRINDRYGHEVGDRVLVEIARTLRAELRE 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110604 321 EDKIYRWGGEEFLLFLPHSPIARALMVAEAIRQAVSEYQ------TLSVTVSIGVAEHHDGE-AIDQLFYRVDKALYAAK 393
Cdd:NF038266 166 YDLCGRWGGEEFLLLLPETGLEEAQVVLERLREAVRALAvrvgddVLSVTASAGLAEHRPPEeGLSATLSRADQALYQAK 245


                 ....*..
gi 694110604 394 NDGRNRV 400
Cdd:NF038266 246 RAGRDRV 252
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 203-400 1.56e-43

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: 161.48  E-value: 1.56e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110604 203 LNFTHILADGSLRHVQTYAGPVVLYNIRLMLCIIHDITEEVHLKKELEFSAAHDPLTGLLNRREFY-RLVDApsfIA--- 278
Cdd:COG5001  201 RGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEERLRHLAYHDPLTGLPNRRLFLdRLEQA---LArar 277

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110604 279 ---HGFCLLLIDIDHFKSINDIHGHQKGDEVLLVISRILETSVDREDKIYRWGGEEFLLFLPH-SPIARALMVAEAIRQA 354
Cdd:COG5001  278 rsgRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVLLPDlDDPEDAEAVAERILAA 357

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 694110604 355 VSE-----YQTLSVTVSIGVAE-HHDGEAIDQLFYRVDKALYAAKNDGRNRV 400
Cdd:COG5001  358 LAEpfeldGHELYVSASIGIALyPDDGADAEELLRNADLAMYRAKAAGRNRY 409
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 253-400 4.56e-43

diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by many proteins carrying the domain. There is evidence that the domain has diguanylate cyclase activity. Several proteins carrying this domain also carry domains with functions relating to environmental sensing. These include PleD, a response regulator protein involved in the swarmer-to-stalked cell transition in Caulobacter crescentus, and FixL, a heme-containing oxygen sensor protein. [Regulatory functions, Small molecule interactions, Signal transduction, Other]


Pssm-ID: 272984 [Multi-domain]  Cd Length: 165  Bit Score: 148.25  E-value: 4.56e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110604  253 AAHDPLTGLLNRREFYRLVDAPSFIA----HGFCLLLIDIDHFKSINDIHGHQKGDEVLLVISRILETSVDREDKIYRWG 328
Cdd:TIGR00254   2 AVRDPLTGLYNRRYLEEMLDSELKRArrfqRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110604  329 GEEFLLFLPHSPIARALMVAEAIRQA-------VSEYQTLSVTVSIGVAEH-HDGEAIDQLFYRVDKALYAAKNDGRNRV 400
Cdd:TIGR00254  82 GEEFVVILPGTPLEDALSKAERLRDAinskpieVAGSETLTVTVSIGVACYpGHGLTLEELLKRADEALYQAKKAGRNRV 161
pleD PRK09581
response regulator PleD; Reviewed
 244-400 5.77e-43

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 156.21  E-value: 5.77e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110604 244 HLKKELEFS---AAHDPLTGLLNRREF----YRLVDAPSFIAHGFCLLLIDIDHFKSINDIHGHQKGDEVLLVISRILET 316
Cdd:PRK09581 280 ALRNNLEQSiemAVTDGLTGLHNRRYFdmhlKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRN 359

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110604 317 SVDREDKIYRWGGEEFLLFLPHSPIARALMVAEAIRQAVSEY--------QTLSVTVSIGVAEH-HDGEAIDQLFYRVDK 387
Cdd:PRK09581 360 NIRGTDLIARYGGEEFVVVMPDTDIEDAIAVAERIRRKIAEEpfiisdgkERLNVTVSIGVAELrPSGDTIEALIKRADK 439

                        170
                 ....*....|...
gi 694110604 388 ALYAAKNDGRNRV 400
Cdd:PRK09581 440 ALYEAKNTGRNRV 452
PRK09894 PRK09894
diguanylate cyclase; Provisional
 256-404 1.22e-38

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 140.97  E-value: 1.22e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110604 256 DPLTGLLNRREFYRLVDAPSFIAHG--FCLLLIDIDHFKSINDIHGHQKGDEVLLVISRILETSVDREDKIYRWGGEEFL 333
Cdd:PRK09894 132 DVLTGLPGRRVLDESFDHQLRNREPqnLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGGEEFI 211

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 694110604 334 LFLPHSPIARALMVAEAIRQAVSEYQT------LSVTVSIGVAEHHDGEAIDQLFYRVDKALYAAKNDGRNRVTRMP 404
Cdd:PRK09894 212 ICLKAATDEEACRAGERIRQLIANHAIthsdgrINITATFGVSRAFPEETLDVVIGRADRAMYEGKQTGRNRVMFID 288
PRK15426 PRK15426
cellulose biosynthesis regulator YedQ;
245-400 3.40e-33

cellulose biosynthesis regulator YedQ;


Pssm-ID: 237964 [Multi-domain]  Cd Length: 570  Bit Score: 130.91  E-value: 3.40e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110604 245 LKKELEFSAAHDPLTGLLNRREFYRL--VDAPSFIAHG--FCLLLIDIDHFKSINDIHGHQKGDEVLLVISRILETSVDR 320
Cdd:PRK15426 390 LQSSLQWQAWHDPLTRLYNRGALFEKarALAKRCQRDQqpFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRA 469

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110604 321 EDKIYRWGGEEFLLFLPHSPIARALMVAEAIRQAVSEYQ-------TLSVTVSIGVAEHHDGEA--IDQLFYRVDKALYA 391
Cdd:PRK15426 470 QDVAGRVGGEEFCVVLPGASLAEAAQVAERIRLRINEKEilvakstTIRISASLGVSSAEEDGDydFEQLQSLADRRLYL 549


                 ....*....
gi 694110604 392 AKNDGRNRV 400
Cdd:PRK15426 550 AKQAGRNRV 558
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 235-412 1.83e-27

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 115.15  E-value: 1.83e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110604  235 IIHDITEEVHLKKELEFSAAHDPLTGLLNRREF----YRLVDAPSFIAHGFCLLLIDIDHFKSINDIHGHQKGDEVLLVI 310
Cdd:PRK09776  647 VIQDVTESRKMLRQLSYSASHDALTHLANRASFekqlRRLLQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLREL 726

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110604  311 SRILETSVDREDKIYRWGGEEFLLFLPHSPIARALMVAEAIRQAVSEYQ------TLSVTVSIGVAehhdgeAIDQ---- 380
Cdd:PRK09776  727 ASLMLSMLRSSDVLARLGGDEFGLLLPDCNVESARFIATRIISAINDYHfpwegrVYRVGASAGIT------LIDAnnhq 800

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 694110604  381 ---LFYRVDKALYAAKNDGRNRVTRMPFDSAELLR 412
Cdd:PRK09776  801 aseVMSQADIACYAAKNAGRGRVTVYEPQQAAAHS 835
adrA PRK10245
diguanylate cyclase AdrA; Provisional
 246-399 6.96e-20

diguanylate cyclase AdrA; Provisional


Pssm-ID: 182329 [Multi-domain]  Cd Length: 366  Bit Score: 90.27  E-value: 6.96e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110604 246 KKELEFSAAHDPLTGLLNRREFYRLV----DAPSFIAHGFCLLLIDIDHFKSINDIHGHQKGDEVLLVISRILETSVDRE 321
Cdd:PRK10245 198 KRRLQVMSTRDGMTGVYNRRHWETLLrnefDNCRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGS 277

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110604 322 DKIYRWGGEEFLLFLPHSP----IARALMVAE---AIRQAVSEYQTLSvtVSIGVAE-----HHDGEAIDQlfyrVDKAL 389
Cdd:PRK10245 278 DVIGRFGGDEFAVIMSGTPaesaITAMSRVHEglnTLRLPNAPQVTLR--ISVGVAPlnpqmSHYREWLKS----ADLAL 351

                        170
                 ....*....|
gi 694110604 390 YAAKNDGRNR 399
Cdd:PRK10245 352 YKAKNAGRNR 361
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
228-397 1.98e-15

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 78.18  E-value: 1.98e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110604 228 NIRLMLCIIHDITEEVHLKKELEFSAAHDPLTGLLNRREFYRLVDAPSFIAHG--FCLLLIDIDHFKSINDIHGHQKGDE 305
Cdd:PRK10060 212 NEIFLICSGTDITEERRAQERLRILANTDSITGLPNRNAIQELIDHAINAADNnqVGIVYLDLDNFKKVNDAYGHMFGDQ 291

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110604 306 VLLVISRILETSVDREDKIYRWGGEEFLLFLPHSpiARALMVAEA----------IRQAVSEYQTlsvTVSIGVA---EH 372
Cdd:PRK10060 292 LLQDVSLAILSCLEEDQTLARLGGDEFLVLASHT--SQAALEAMAsriltrlrlpFRIGLIEVYT---GCSIGIAlapEH 366

                        170       180
                 ....*....|....*....|....*
gi 694110604 373 hdGEAIDQLFYRVDKALYAAKNDGR 397
Cdd:PRK10060 367 --GDDSESLIRSADTAMYTAKEGGR 389
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 322-393 2.60e-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: 73.40  E-value: 2.60e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 694110604 322 DKIYRWGGEEFLLFLPHSPIARALMVAEAIRQAVSEYQTLSVTVSIGVAEhhdgeaiDQLFYRVDkALYAAK 393
Cdd:COG3706  116 DLVARYGGEEFAILLPGTDLEGALAVAERIREAVAELPSLRVTVSIGVAG-------DSLLKRAD-ALYQAR 179
PRK09966 PRK09966
diguanylate cyclase DgcN;
238-402 3.57e-15

diguanylate cyclase DgcN;


Pssm-ID: 182171 [Multi-domain]  Cd Length: 407  Bit Score: 76.58  E-value: 3.57e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110604 238 DITEEVHLK-----KELEFSAAHDPLTGLLNRREFYRLVDA---PSFIAHGFCLLLIDIDHFKSINDIHGHQKGDEVLLV 309
Cdd:PRK09966 228 DEMEEWQLRlqaknAQLLRTALHDPLTGLANRAAFRSGINTlmnNSDARKTSALLFLDGDNFKYINDTWGHATGDRVLIE 307

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110604 310 ISRILETSVDREDKIYRWGGEEF--LLFLPHSPiARALMVAEAIRQA------VSEYQTLSVTVSIGVA---EHHDGEAI 378
Cdd:PRK09966 308 IAKRLAEFGGLRHKAYRLGGDEFamVLYDVQSE-SEVQQICSALTQIfnlpfdLHNGHQTTMTLSIGYAmtiEHASAEKL 386

                        170       180
                 ....*....|....*....|....
gi 694110604 379 DQLfyrVDKALYAAKNDGRNRVTR 402
Cdd:PRK09966 387 QEL---ADHNMYQAKHQRAEKLVR 407
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 256-396 1.07e-13

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 72.88  E-value: 1.07e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110604 256 DPLTGLLNRREFYRLVDAPSFIAHGFCLLLIDIDHFKSINDIHGHQKGDEVLLVISRILETSVDREDKIYRWGGEEFLLF 335
Cdd:PRK11359 379 DPLTGLPNRNNLHNYLDDLVDKAVSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGTQFVLV 458

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 694110604 336 LPHSPIARALMVAEAIRQAVSEY-----QTLSVTVSIGVAeHHDGEAIDQLFYRVDKAL-YAAKNDG 396
Cdd:PRK11359 459 SLENDVSNITQIADELRNVVSKPimiddKPFPLTLSIGIS-YDVGKNRDYLLSTAHNAMdYIRKNGG 524
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
 282-378 5.37e-11

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


Pssm-ID: 143637 [Multi-domain]  Cd Length: 133  Bit Score: 60.06  E-value: 5.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110604 282 CLLLIDIDHFKSINDIHGHQKGDEVLLVISRILETSVDR-EDKIYRWGGEEFLLFLPHSPIARALMVAEAIRQAVSEYQT 360
Cdd:cd07556    3 TILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRsGDLKIKTIGDEFMVVSGLDHPAAAVAFAEDMREAVSALNQ 82

                         90       100
                 ....*....|....*....|.
gi 694110604 361 LS---VTVSIGVaehHDGEAI 378
Cdd:cd07556   83 SEgnpVRVRIGI---HTGPVV 100
PAS COG2202
PAS domain [Signal transduction mechanisms];
121-336 9.39e-11

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 61.96  E-value: 9.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110604 121 RRYQRRNNGFFARFFMTNTAPMLLIDPqkEGRIVDANIAALRFYHYSDEEMRTKHTWQINTLG-RDVIPIMNNIANMPGG 199
Cdd:COG2202    3 EEALEESERRLRALVESSPDAIIITDL--DGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEdDDEFLELLRAALAGGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110604 200 HKPLNFTHILADGSLRHVQTYAGPVVLY--NIRLMLCIIHDITEEVHLKKELEFSAAHDPLTgLLNRREFYRLVDA---P 274
Cdd:COG2202   81 VWRGELRNRRKDGSLFWVELSISPVRDEdgEITGFVGIARDITERKRAEEALRESEERLRLL-VENAPDGIFVLDLdgrI 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 694110604 275 SFIAHGFCLLL---IDIDHFKSINDIHGHQKGDEVLLVISRILETSVDREDKIYRWGGEEFLLFL 336
Cdd:COG2202  160 LYVNPAAEELLgysPEELLGKSLLDLLHPEDRERLLELLRRLLEGGRESYELELRLKDGDGRWVW 224
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
141-262 1.07e-07

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 53.31  E-value: 1.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110604 141 PMLLIDPQkeGRIVDANIAALRFYHYSDEEMRTKHTWQINTLGRDVIPIMNNIANMPGGHKPLNFTHILADGSLRHVQTY 220
Cdd:COG3852   19 AVIVLDAD--GRITYVNPAAERLLGLSAEELLGRPLAELFPEDSPLRELLERALAEGQPVTEREVTLRRKDGEERPVDVS 96

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 694110604 221 AGPVVLYNIRL-MLCIIHDITEEVHLKKELEFSA------------AHD---PLTGLL 262
Cdd:COG3852   97 VSPLRDAEGEGgVLLVLRDITERKRLERELRRAEklaavgelaaglAHEirnPLTGIR 154
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
 150-241 4.38e-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: 47.84  E-value: 4.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110604  150 EGRIVDANIAALRFYHYSDEEMRTKHTWQINTLGRDVIPIMNNIANMPGGHkPLNFTHILADGSLRHVQTYAGPVVL--Y 227
Cdd:pfam13426   1 DGRIIYVNDAALRLLGYTREELLGKSITDLFAEPEDSERLREALREGKAVR-EFEVVLYRKDGEPFPVLVSLAPIRDdgG 79

                          90
                  ....*....|....
gi 694110604  228 NIRLMLCIIHDITE 241
Cdd:pfam13426  80 ELVGIIAILRDITE 93
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
 130-250 6.83e-07

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: 48.06  E-value: 6.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110604  130 FFARFFMTNTAPMLLIDPqkEGRIVDANIAALRFYHYSDEEMRTKHTWQINT-LGRDVIP-IMNNIAnmPGGHKP--LNF 205
Cdd:TIGR00229   4 RYRAIFESSPDAIIVIDL--EGNILYVNPAFEEIFGYSAEELIGRNVLELIPeEDREEVReRIERRL--EGEPEPvsEER 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 694110604  206 THILADGSLRHVQTYAGPVVLYNIRL-MLCIIHDITEevhlKKELE 250
Cdd:TIGR00229  80 RVRRKDGSEIWVEVSVSPIRTNGGELgVVGIVRDITE----RKEAE 121
PAS COG2202
PAS domain [Signal transduction mechanisms];
125-249 7.43e-07

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 50.02  E-value: 7.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110604 125 RRNNGFFARFFMTNTAPMLLIDPqkEGRIVDANIAALRFYHYSDEEMRTKHTWQI--NTLGRDVIPIMNNIANMPGGHKP 202
Cdd:COG2202  133 RESEERLRLLVENAPDGIFVLDL--DGRILYVNPAAEELLGYSPEELLGKSLLDLlhPEDRERLLELLRRLLEGGRESYE 210

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 694110604 203 LNFTHILADGSLRHVQTYAGPV-VLYNIRLMLCIIHDITEEVHLKKEL 249
Cdd:COG2202  211 LELRLKDGDGRWVWVEASAVPLrDGGEVIGVLGIVRDITERKRAEEAL 258
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 140-243 2.54e-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 is associated to signalling systems and works as a signal sensor domain. It recognizes differently substituted aromatic hydrocarbons, oxygen, different dodecanoic acids, autoinducers, 3,5-dimethyl-pyrazin-2-ol and N-alanyl-aminoacetone (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 312075 [Multi-domain]  Cd Length: 110  Bit Score: 45.87  E-value: 2.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110604  140 APMLLIDPQkeGRIVDANIAALRFYHYSDEEMRTKHTWQI--NTLGRDVIPIMNNIANmpgGHKPLNFTHIL-ADGSLRH 216
Cdd:pfam08448   6 DALAVLDPD--GRVRYANAAAAELFGLPPEELLGKTLAELlpPEDAARLERALRRALE---GEEPIDFLEELlLNGEERH 80

                          90       100
                  ....*....|....*....|....*....
gi 694110604  217 VQTYAGPV--VLYNIRLMLCIIHDITEEV 243
Cdd:pfam08448  81 YELRLTPLrdPDGEVIGVLVISRDITERR 109
PRK11059 PRK11059
regulatory protein CsrD; Provisional
 253-392 1.97e-05

regulatory protein CsrD; Provisional


Pssm-ID: 236833 [Multi-domain]  Cd Length: 640  Bit Score: 46.78  E-value: 1.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110604 253 AAHDPLTGLLNRREF-----YRLVDAPSFIAHGfCLLLIDIDHFKSINDIHGHQKGDEVLLVISRILETSVDR-EDKIY- 325
Cdd:PRK11059 228 AFQDAKTGLGNRLFFdnqlaTLLEDQEMVGAHG-VVMLIRLPDFDLLQEEWGESQVEELLFELINLLSTFVMRyPGALLa 306

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 694110604 326 RWGGEEFLLFLPHspiaRALMVAEAI-RQAVSEYQTLSVT--------VSIGVAEHHDGEAIDQLFYRVDKALYAA 392
Cdd:PRK11059 307 RYSRSDFAVLLPH----RSLKEADSLaSQLLKAVDALPPPkmldrddfLHIGICAYRSGQSTEQVMEEAEMALRSA 378
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
 55-261 4.14e-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: 45.74  E-value: 4.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110604  55 ETQLQHYLRYLdAMTEIFEVWTLQ-TAKGLQSVYCKTTLVETEDS-GTLLLFeavklLAQNQSIhTGSRRYQRRNNGFFA 132
Cdd:COG5809   69 EKELREILKLL-KEGESRDELEFElRHKNGKRLEFSSKLSPIFDQnGDIEGM-----LAISRDI-TERKRMEEALRESEE 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110604 133 RFF-MTNTAPMLLIDPQKEGRIVDANIAALRFYHYSDEE-MRTKHTWQINTLGRDVIPIMNNIANMPGGHKPLNFTHILA 210
Cdd:COG5809  142 KFRlIFNHSPDGIIVTDLDGRIIYANPAACKLLGISIEElIGKSILELIHSDDQENVAAFISQLLKDGGIAQGEVRFWTK 221

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 694110604 211 DGSLRHVQTYAGPVVLYNIRLMLCII-HDITEEVHLKKEL----------EFSA--AHD---PLTGL 261
Cdd:COG5809  222 DGRWRLLEASGAPIKKNGEVDGIVIIfRDITERKKLEELLrkseklsvvgELAAgiAHEirnPLTSL 288
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 141-239 5.16e-05

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: 42.24  E-value: 5.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110604 141 PMLLIDPQkeGRIVDANIAALRFYHYSDEEMRTKHTWQInTLGRDVIPIMNNIANM--PGGHKPLNFTHILADGSLRHVQ 218
Cdd:cd00130    4 GVIVLDLD--GRILYANPAAEQLLGYSPEELIGKSLLDL-IHPEDREELRERLENLlsGGEPVTLEVRLRRKDGSVIWVL 80

                         90       100
                 ....*....|....*....|...
gi 694110604 219 TYAGPVV--LYNIRLMLCIIHDI 239
Cdd:cd00130   81 VSLTPIRdeGGEVIGLLGVVRDI 103
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
 141-250 7.90e-04

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: 41.68  E-value: 7.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110604 141 PMLLIDpqKEGRIVDANIAALRFYHYSDEEMRTKHTWQI--NTLGRDVI----PIMNNIANMPGGHKPLNFTH--ILADG 212
Cdd:COG3829   23 GIIVVD--ADGRITYVNRAAERILGLPREEVIGKNVTELipNSPLLEVLktgkPVTGVIQKTGGKGKTVIVTAipIFEDG 100

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 694110604 213 slrhvqtyagpvvlyNIRLMLCIIHDITEEVHLKKELE 250
Cdd:COG3829  101 ---------------EVIGAVETFRDITELKRLERKLR 123
PRK11829 PRK11829
biofilm formation regulator HmsP; Provisional
 257-400 1.43e-03

biofilm formation regulator HmsP; Provisional


Pssm-ID: 183329 [Multi-domain]  Cd Length: 660  Bit Score: 41.08  E-value: 1.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110604 257 PLTGLLNRREFYRLVD---APSFIAHGFCLLLIDIDHFKSINDIHGHQKGDEVLLVISRILETSVDREDKIYRWGGEEFL 333
Cdd:PRK11829 236 PVTELPNRSLFISLLEkeiASSTRTDHFHLLVIGIETLQEVSGAMSEAQHQQLLLTIVQRIEQCIDDSDLLAQLSKTEFA 315

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 694110604 334 LFLPHSP-------IARALMvaEAIRQAVS-EYQTLSVTVSIGVAEHHDGEAI-DQLFYRVDKALYAAKNDGRNRV 400
Cdd:PRK11829 316 VLARGTRrsfpamqLARRIM--SQVTQPLFfDEITLRPSASIGITRYQAQQDTaESMMRNASTAMMAAHHEGRNQI 389
Cas10_III cd09679
CRISPR/Cas system-associated protein Cas10; CRISPR (Clustered Regularly Interspaced Short ...
 328-399 4.39e-03

CRISPR/Cas system-associated protein Cas10; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Multidomain protein with permuted HD nuclease domain, palm domain and Zn-ribbon; MTH326-like has inactivated polymerase catalytic domain; alr1562 and slr7011 - predicted only on the basis of size, presence of HD domain, and location with RAMPs in one operon; signature gene for type III; also known as Crm2 family


Pssm-ID: 187810 [Multi-domain]  Cd Length: 475  Bit Score: 39.36  E-value: 4.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110604 328 GGEEFLLFLPhspIARALMVAEAIRQAVSE--------YQTLSVTVSIGVA-EHHD---GEAIDqlfyRVDKALYAAKND 395
Cdd:cd09679  387 GGDDVLALLP---VDKALDCAKKLRKAFSGilnkeigeDMGEGPTMSAGIViAHHKeplQDALE----LARRAEKRAKKE 459


                 ....
gi 694110604 396 GRNR 399
Cdd:cd09679  460 GRNR 463
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 129-239 4.84e-03

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: 36.63  E-value: 4.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110604  129 GFFARFFMTNTAPMLLIDPQkeGRIVDANIAALRFYHYSDEEMRTKHtwqintLGRDVIPIMNNI------ANMPGGHKP 202
Cdd:pfam00989   1 EDLRAILESLPDGIFVVDED--GRILYVNAAAEELLGLSREEVIGKS------LLDLIPEEDDAEvaellrQALLQGEES 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 694110604  203 LNFTH--ILADGSLRHVQTYAGPVV--LYNIRLMLCIIHDI 239
Cdd:pfam00989  73 RGFEVsfRVPDGRPRHVEVRASPVRdaGGEILGFLGVLRDI 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.
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