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Conserved domains on  [gi|491601983|ref|WP_005459545|]
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sensor domain-containing diguanylate cyclase [Vibrio parahaemolyticus]

Protein Classification

sensor domain-containing diguanylate cyclase( domain architecture ID 13567017)

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 ...
 85-308 6.51e-70

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: 219.08  E-value: 6.51e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491601983  85 LSLHDHLLLPIEELEALENPEEMWFEAIIKPVNAPENANKLVIWSVRDITKTHLLEQRLKQLSETDALTGLLNRRAFISN 164
Cdd:COG2199   52 LLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEER 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491601983 165 LDNAIIQHTKRSQTLSCLMIDIDHFKDINDSVGHFSGDHVITRIAHVCQGVIRGSDFIGRLGGEEFAVILTDTNAIQAYE 244
Cdd:COG2199  132 LERELARARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEA 211

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491601983 245 VAERIRQAIQATICHVDDVEITTTVSIGVAELNSQQSNAKELLIEADKAMYYSKHSGRNQVTLA 308
Cdd:COG2199  212 LAERLREALEQLPFELEGKELRVTVSIGVALYPEDGDSAEELLRRADLALYRAKRAGRNRVVVY 275
NtrB super family cl34682
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
4-155 1.01e-05

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: 46.76  E-value: 1.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491601983   4 KERETWLEAILNTLPDHVFILDESGRYI------ESFGGthhsktFNAERYIGLQLSDVLSPtkADELMGFIFDVMQDNE 77
Cdd:COG3852    3 RESEELLRAILDSLPDAVIVLDADGRITyvnpaaERLLG------LSAEELLGRPLAELFPE--DSPLRELLERALAEGQ 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491601983  78 TkVVKYNLSLHDHlllpieelealeNPEEMWFEAIIKPVNAPENANKLVIwSVRDITKTHLLEQRLKQLSETDALTGL 155
Cdd:COG3852   75 P-VTEREVTLRRK------------DGEERPVDVSVSPLRDAEGEGGVLL-VLRDITERKRLERELRRAEKLAAVGEL 138
 
Name Accession Description Interval E-value
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 85-308 6.51e-70

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: 219.08  E-value: 6.51e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491601983  85 LSLHDHLLLPIEELEALENPEEMWFEAIIKPVNAPENANKLVIWSVRDITKTHLLEQRLKQLSETDALTGLLNRRAFISN 164
Cdd:COG2199   52 LLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEER 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491601983 165 LDNAIIQHTKRSQTLSCLMIDIDHFKDINDSVGHFSGDHVITRIAHVCQGVIRGSDFIGRLGGEEFAVILTDTNAIQAYE 244
Cdd:COG2199  132 LERELARARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEA 211

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491601983 245 VAERIRQAIQATICHVDDVEITTTVSIGVAELNSQQSNAKELLIEADKAMYYSKHSGRNQVTLA 308
Cdd:COG2199  212 LAERLREALEQLPFELEGKELRVTVSIGVALYPEDGDSAEELLRRADLALYRAKRAGRNRVVVY 275
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 149-305 3.28e-64

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: 200.09  E-value: 3.28e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491601983 149 TDALTGLLNRRAFISNLDNAIIQHTKRSQTLSCLMIDIDHFKDINDSVGHFSGDHVITRIAHVCQGVIRGSDFIGRLGGE 228
Cdd:cd01949    2 TDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGD 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491601983 229 EFAVILTDTNAIQAYEVAERIRQAIQATIcHVDDVEITTTVSIGVAELNSQQSNAKELLIEADKAMYYSKHSGRNQV 305
Cdd:cd01949   82 EFAILLPGTDLEEAEALAERLREAIEEPF-FIDGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNRV 157
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 149-304 4.70e-53

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: 171.67  E-value: 4.70e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491601983  149 TDALTGLLNRRAFISNLDNAIIQHTKRSQTLSCLMIDIDHFKDINDSVGHFSGDHVITRIAHVCQGVIRGSDFIGRLGGE 228
Cdd:pfam00990   3 HDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLGGD 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491601983  229 EFAVILTDTNAIQAYEVAERIRQAIQ--ATICHVDDVEITTTVSIGVAELNSQQSNAKELLIEADKAMYYSKHSGRNQ 304
Cdd:pfam00990  83 EFAILLPETSLEGAQELAERIRRLLAklKIPHTVSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGRNR 160
pleD PRK09581
response regulator PleD; Reviewed
 74-305 1.13e-52

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 179.71  E-value: 1.13e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491601983  74 QDNETKVVK-YNLSLHDHLLLPIEELEALenpeemwfeAIIKPvnapenanklviwSVRDITKTHLLEQRLKQ---LSET 149
Cdd:PRK09581 237 EDDDPRLVKaLELGVNDYLMRPIDKNELL---------ARVRT-------------QIRRKRYQDALRNNLEQsieMAVT 294

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491601983 150 DALTGLLNRRAFISNLDNAIIQHTKRSQTLSCLMIDIDHFKDINDSVGHFSGDHVITRIAHVCQGVIRGSDFIGRLGGEE 229
Cdd:PRK09581 295 DGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARYGGEE 374

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491601983 230 FAVILTDTNAIQAYEVAERIRQAIQAT--ICHVDDVEITTTVSIGVAELNSQQSNAKELLIEADKAMYYSKHSGRNQV 305
Cdd:PRK09581 375 FVVVMPDTDIEDAIAVAERIRRKIAEEpfIISDGKERLNVTVSIGVAELRPSGDTIEALIKRADKALYEAKNTGRNRV 452
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 145-305 3.41e-51

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 167.04  E-value: 3.41e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491601983   145 QLSETDALTGLLNRRAFISNLDNAIIQHTKRSQTLSCLMIDIDHFKDINDSVGHFSGDHVITRIAHVCQGVIRGSDFIGR 224
Cdd:smart00267   1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491601983   225 LGGEEFAVILTDTNAIQAYEVAERIRQAIQATIcHVDDVEITTTVSIGVAELNSQQSNAKELLIEADKAMYYSKHSGRNQ 304
Cdd:smart00267  81 LGGDEFALLLPETSLEEAIALAERILQQLREPI-IIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQ 159


                   .
gi 491601983   305 V 305
Cdd:smart00267 160 V 160
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 146-308 6.53e-48

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: 158.65  E-value: 6.53e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491601983  146 LSETDALTGLLNRRAFISNLDNAIIQHTKRSQTLSCLMIDIDHFKDINDSVGHFSGDHVITRIAHVCQGVIRGSDFIGRL 225
Cdd:TIGR00254   1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491601983  226 GGEEFAVILTDTNAIQAYEVAERIRQAIQAT-ICHVDDVEITTTVSIGVAELNSQQSNAKELLIEADKAMYYSKHSGRNQ 304
Cdd:TIGR00254  81 GGEEFVVILPGTPLEDALSKAERLRDAINSKpIEVAGSETLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRNR 160


                  ....
gi 491601983  305 VTLA 308
Cdd:TIGR00254 161 VVVA 164
diguan_SiaD NF038266
biofilm regulation diguanylate cyclase SiaD;
139-305 1.09e-42

biofilm regulation diguanylate cyclase SiaD;


Pssm-ID: 468439 [Multi-domain]  Cd Length: 252  Bit Score: 147.82  E-value: 1.09e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491601983 139 LEQRLKQLSETDALTGLLNRRAFISNLDNAIiQHTKRSQTLSCL-MIDIDHFKDINDSVGHFSGDHVITRIAHVCQGVIR 217
Cdd:NF038266  86 LNEALREASTRDPLTGLPNRRLLMERLREEV-ERARRSGRPFTLaMLDVDHFKRINDRYGHEVGDRVLVEIARTLRAELR 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491601983 218 GSDFIGRLGGEEFAVILTDTNAIQAYEVAERIRQAIQATICHVDDVEITTTVSIGVAELNSQQSNAKELLIEADKAMYYS 297
Cdd:NF038266 165 EYDLCGRWGGEEFLLLLPETGLEEAQVVLERLREAVRALAVRVGDDVLSVTASAGLAEHRPPEEGLSATLSRADQALYQA 244


                 ....*...
gi 491601983 298 KHSGRNQV 305
Cdd:NF038266 245 KRAGRDRV 252
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
4-155 1.01e-05

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 46.76  E-value: 1.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491601983   4 KERETWLEAILNTLPDHVFILDESGRYI------ESFGGthhsktFNAERYIGLQLSDVLSPtkADELMGFIFDVMQDNE 77
Cdd:COG3852    3 RESEELLRAILDSLPDAVIVLDADGRITyvnpaaERLLG------LSAEELLGRPLAELFPE--DSPLRELLERALAEGQ 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491601983  78 TkVVKYNLSLHDHlllpieelealeNPEEMWFEAIIKPVNAPENANKLVIwSVRDITKTHLLEQRLKQLSETDALTGL 155
Cdd:COG3852   75 P-VTEREVTLRRK------------DGEERPVDVSVSPLRDAEGEGGVLL-VLRDITERKRLERELRRAEKLAAVGEL 138
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 14-134 1.28e-04

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: 40.86  E-value: 1.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491601983   14 LNTLPDHVFILDESGRYIESFGGTHHSKTFNAERYIGLQLSDVLSPTKADELMGFIFDVMQDNETkvvkynLSLHDHLLL 93
Cdd:pfam08448   1 LDSLPDALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAELLPPEDAARLERALRRALEGEEP------IDFLEELLL 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 491601983   94 pieelealeNPEEMWFEAIIKPVNAPENANKLVIWSVRDIT 134
Cdd:pfam08448  75 ---------NGEERHYELRLTPLRDPDGEVIGVLVISRDIT 106
 
Name Accession Description Interval E-value
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 85-308 6.51e-70

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: 219.08  E-value: 6.51e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491601983  85 LSLHDHLLLPIEELEALENPEEMWFEAIIKPVNAPENANKLVIWSVRDITKTHLLEQRLKQLSETDALTGLLNRRAFISN 164
Cdd:COG2199   52 LLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEER 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491601983 165 LDNAIIQHTKRSQTLSCLMIDIDHFKDINDSVGHFSGDHVITRIAHVCQGVIRGSDFIGRLGGEEFAVILTDTNAIQAYE 244
Cdd:COG2199  132 LERELARARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEA 211

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491601983 245 VAERIRQAIQATICHVDDVEITTTVSIGVAELNSQQSNAKELLIEADKAMYYSKHSGRNQVTLA 308
Cdd:COG2199  212 LAERLREALEQLPFELEGKELRVTVSIGVALYPEDGDSAEELLRRADLALYRAKRAGRNRVVVY 275
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 149-305 3.28e-64

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: 200.09  E-value: 3.28e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491601983 149 TDALTGLLNRRAFISNLDNAIIQHTKRSQTLSCLMIDIDHFKDINDSVGHFSGDHVITRIAHVCQGVIRGSDFIGRLGGE 228
Cdd:cd01949    2 TDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGD 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491601983 229 EFAVILTDTNAIQAYEVAERIRQAIQATIcHVDDVEITTTVSIGVAELNSQQSNAKELLIEADKAMYYSKHSGRNQV 305
Cdd:cd01949   82 EFAILLPGTDLEEAEALAERLREAIEEPF-FIDGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNRV 157
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 130-305 1.59e-53

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: 186.13  E-value: 1.59e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491601983 130 VRDITKTHLLEQRLKQLSETDALTGLLNRRAFISNLDNAIIQHTKRSQTLSCLMIDIDHFKDINDSVGHFSGDHVITRIA 209
Cdd:COG5001  234 ARLITERKRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVA 313

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491601983 210 HVCQGVIRGSDFIGRLGGEEFAVILTDTNAI-QAYEVAERIRQAIQATIcHVDDVEITTTVSIGVAELNSQQSNAKELLI 288
Cdd:COG5001  314 RRLRACLREGDTVARLGGDEFAVLLPDLDDPeDAEAVAERILAALAEPF-ELDGHELYVSASIGIALYPDDGADAEELLR 392

                        170
                 ....*....|....*..
gi 491601983 289 EADKAMYYSKHSGRNQV 305
Cdd:COG5001  393 NADLAMYRAKAAGRNRY 409
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 149-304 4.70e-53

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: 171.67  E-value: 4.70e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491601983  149 TDALTGLLNRRAFISNLDNAIIQHTKRSQTLSCLMIDIDHFKDINDSVGHFSGDHVITRIAHVCQGVIRGSDFIGRLGGE 228
Cdd:pfam00990   3 HDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLGGD 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491601983  229 EFAVILTDTNAIQAYEVAERIRQAIQ--ATICHVDDVEITTTVSIGVAELNSQQSNAKELLIEADKAMYYSKHSGRNQ 304
Cdd:pfam00990  83 EFAILLPETSLEGAQELAERIRRLLAklKIPHTVSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGRNR 160
pleD PRK09581
response regulator PleD; Reviewed
 74-305 1.13e-52

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 179.71  E-value: 1.13e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491601983  74 QDNETKVVK-YNLSLHDHLLLPIEELEALenpeemwfeAIIKPvnapenanklviwSVRDITKTHLLEQRLKQ---LSET 149
Cdd:PRK09581 237 EDDDPRLVKaLELGVNDYLMRPIDKNELL---------ARVRT-------------QIRRKRYQDALRNNLEQsieMAVT 294

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491601983 150 DALTGLLNRRAFISNLDNAIIQHTKRSQTLSCLMIDIDHFKDINDSVGHFSGDHVITRIAHVCQGVIRGSDFIGRLGGEE 229
Cdd:PRK09581 295 DGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARYGGEE 374

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491601983 230 FAVILTDTNAIQAYEVAERIRQAIQAT--ICHVDDVEITTTVSIGVAELNSQQSNAKELLIEADKAMYYSKHSGRNQV 305
Cdd:PRK09581 375 FVVVMPDTDIEDAIAVAERIRRKIAEEpfIISDGKERLNVTVSIGVAELRPSGDTIEALIKRADKALYEAKNTGRNRV 452
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 145-305 3.41e-51

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 167.04  E-value: 3.41e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491601983   145 QLSETDALTGLLNRRAFISNLDNAIIQHTKRSQTLSCLMIDIDHFKDINDSVGHFSGDHVITRIAHVCQGVIRGSDFIGR 224
Cdd:smart00267   1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491601983   225 LGGEEFAVILTDTNAIQAYEVAERIRQAIQATIcHVDDVEITTTVSIGVAELNSQQSNAKELLIEADKAMYYSKHSGRNQ 304
Cdd:smart00267  81 LGGDEFALLLPETSLEEAIALAERILQQLREPI-IIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQ 159


                   .
gi 491601983   305 V 305
Cdd:smart00267 160 V 160
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 146-308 6.53e-48

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: 158.65  E-value: 6.53e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491601983  146 LSETDALTGLLNRRAFISNLDNAIIQHTKRSQTLSCLMIDIDHFKDINDSVGHFSGDHVITRIAHVCQGVIRGSDFIGRL 225
Cdd:TIGR00254   1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491601983  226 GGEEFAVILTDTNAIQAYEVAERIRQAIQAT-ICHVDDVEITTTVSIGVAELNSQQSNAKELLIEADKAMYYSKHSGRNQ 304
Cdd:TIGR00254  81 GGEEFVVILPGTPLEDALSKAERLRDAINSKpIEVAGSETLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRNR 160


                  ....
gi 491601983  305 VTLA 308
Cdd:TIGR00254 161 VVVA 164
PRK15426 PRK15426
cellulose biosynthesis regulator YedQ;
139-305 6.04e-44

cellulose biosynthesis regulator YedQ;


Pssm-ID: 237964 [Multi-domain]  Cd Length: 570  Bit Score: 158.64  E-value: 6.04e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491601983 139 LEQRLKQLSETDALTGLLNRRAFiSNLDNAIIQHTKRSQT-LSCLMIDIDHFKDINDSVGHFSGDHVITRIAHVCQGVIR 217
Cdd:PRK15426 390 LQSSLQWQAWHDPLTRLYNRGAL-FEKARALAKRCQRDQQpFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLR 468

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491601983 218 GSDFIGRLGGEEFAVILTDTNAIQAYEVAERIRQAIQATICHV-DDVEITTTVSIGVAELNSQQS-NAKELLIEADKAMY 295
Cdd:PRK15426 469 AQDVAGRVGGEEFCVVLPGASLAEAAQVAERIRLRINEKEILVaKSTTIRISASLGVSSAEEDGDyDFEQLQSLADRRLY 548

                        170
                 ....*....|
gi 491601983 296 YSKHSGRNQV 305
Cdd:PRK15426 549 LAKQAGRNRV 558
diguan_SiaD NF038266
biofilm regulation diguanylate cyclase SiaD;
139-305 1.09e-42

biofilm regulation diguanylate cyclase SiaD;


Pssm-ID: 468439 [Multi-domain]  Cd Length: 252  Bit Score: 147.82  E-value: 1.09e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491601983 139 LEQRLKQLSETDALTGLLNRRAFISNLDNAIiQHTKRSQTLSCL-MIDIDHFKDINDSVGHFSGDHVITRIAHVCQGVIR 217
Cdd:NF038266  86 LNEALREASTRDPLTGLPNRRLLMERLREEV-ERARRSGRPFTLaMLDVDHFKRINDRYGHEVGDRVLVEIARTLRAELR 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491601983 218 GSDFIGRLGGEEFAVILTDTNAIQAYEVAERIRQAIQATICHVDDVEITTTVSIGVAELNSQQSNAKELLIEADKAMYYS 297
Cdd:NF038266 165 EYDLCGRWGGEEFLLLLPETGLEEAQVVLERLREAVRALAVRVGDDVLSVTASAGLAEHRPPEEGLSATLSRADQALYQA 244


                 ....*...
gi 491601983 298 KHSGRNQV 305
Cdd:NF038266 245 KRAGRDRV 252
PRK09894 PRK09894
diguanylate cyclase; Provisional
 129-312 2.79e-37

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 135.19  E-value: 2.79e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491601983 129 SVRDItKTHLLEQRlkqlSETDALTGLLNRRAFISNLDNAIIQHTKrsQTLSCLMIDIDHFKDINDSVGHFSGDHVITRI 208
Cdd:PRK09894 116 ALTDY-KIYLLTIR----SNMDVLTGLPGRRVLDESFDHQLRNREP--QNLYLALLDIDRFKLVNDTYGHLIGDVVLRTL 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491601983 209 AHVCQGVIRGSDFIGRLGGEEFAVILTDTNAIQAYEVAERIRQAIQATICHVDDVEITTTVSIGVAELNSQQSnAKELLI 288
Cdd:PRK09894 189 ATYLASWTRDYETVYRYGGEEFIICLKAATDEEACRAGERIRQLIANHAITHSDGRINITATFGVSRAFPEET-LDVVIG 267

                        170       180
                 ....*....|....*....|....
gi 491601983 289 EADKAMYYSKHSGRNQVTLAYENL 312
Cdd:PRK09894 268 RADRAMYEGKQTGRNRVMFIDEQN 291
adrA PRK10245
diguanylate cyclase AdrA; Provisional
 134-308 1.07e-31

diguanylate cyclase AdrA; Provisional


Pssm-ID: 182329 [Multi-domain]  Cd Length: 366  Bit Score: 121.86  E-value: 1.07e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491601983 134 TKTHLLE--QRLKQLSETDALTGLLNRRAFISNLDNAIiQHTKRSQ-TLSCLMIDIDHFKDINDSVGHFSGDHVITRIAH 210
Cdd:PRK10245 190 TATKLAEhkRRLQVMSTRDGMTGVYNRRHWETLLRNEF-DNCRRHHrDATLLIIDIDHFKSINDTWGHDVGDEAIVALTR 268

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491601983 211 VCQGVIRGSDFIGRLGGEEFAVILTDTNAIQAYEVAERIRQAIqATICHVDDVEITTTVSIGVAELNSQQSNAKELLIEA 290
Cdd:PRK10245 269 QLQITLRGSDVIGRFGGDEFAVIMSGTPAESAITAMSRVHEGL-NTLRLPNAPQVTLRISVGVAPLNPQMSHYREWLKSA 347

                        170
                 ....*....|....*...
gi 491601983 291 DKAMYYSKHSGRNQVTLA 308
Cdd:PRK10245 348 DLALYKAKNAGRNRTEVA 365
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 125-327 4.80e-31

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 123.63  E-value: 4.80e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491601983  125 LVIwsvRDITKTHLLEQRLKQLSETDALTGLLNRRAFISNLDNAIIQHTKRSQTLSCLMIDIDHFKDINDSVGHFSGDHV 204
Cdd:PRK09776  646 LVI---QDVTESRKMLRQLSYSASHDALTHLANRASFEKQLRRLLQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDAL 722

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491601983  205 ITRIAHVCQGVIRGSDFIGRLGGEEFAVILTDTNAIQAYEVAERIRQAIQATICHVDDVEITTTVSIGVAELNSQQSNAK 284
Cdd:PRK09776  723 LRELASLMLSMLRSSDVLARLGGDEFGLLLPDCNVESARFIATRIISAINDYHFPWEGRVYRVGASAGITLIDANNHQAS 802

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 491601983  285 ELLIEADKAMYYSKHSGRNQVTlayenlpdlkLYQAGHLKIQR 327
Cdd:PRK09776  803 EVMSQADIACYAAKNAGRGRVT----------VYEPQQAAAHS 835
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
127-304 7.19e-28

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 114.01  E-value: 7.19e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491601983 127 IWSVRDITKTHLLEQRLKQLSETDALTGLLNRRAfISNLDNAIIQHTKRSQTlSCLMIDIDHFKDINDSVGHFSGDHVIT 206
Cdd:PRK10060 217 ICSGTDITEERRAQERLRILANTDSITGLPNRNA-IQELIDHAINAADNNQV-GIVYLDLDNFKKVNDAYGHMFGDQLLQ 294

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491601983 207 RIAHVCQGVIRGSDFIGRLGGEEFAVILTDTNA----IQAYEVAERIRQAIqaticHVDDVEITTTVSIGVAeLNSQQSN 282
Cdd:PRK10060 295 DVSLAILSCLEEDQTLARLGGDEFLVLASHTSQaaleAMASRILTRLRLPF-----RIGLIEVYTGCSIGIA-LAPEHGD 368

                        170       180
                 ....*....|....*....|...
gi 491601983 283 AKELLIE-ADKAMYYSKHSGRNQ 304
Cdd:PRK10060 369 DSESLIRsADTAMYTAKEGGRGQ 391
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 141-303 3.06e-20

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 91.37  E-value: 3.06e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491601983 141 QRLKQLSETDALTGLLNRRAFISNLDNAIiqhtKRSQTLSCLMIDIDHFKDINDSVGHFSGDHVITRIAHVCQGVIRGSD 220
Cdd:PRK11359 370 QHIEQLIQFDPLTGLPNRNNLHNYLDDLV----DKAVSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDQ 445

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491601983 221 FIGRLGGEEFAVILTDTNAIQAYEVAERIRQAIQATIcHVDDVEITTTVSIGVAElnSQQSNAKELLIEADKAMYYSKHS 300
Cdd:PRK11359 446 YLCRIEGTQFVLVSLENDVSNITQIADELRNVVSKPI-MIDDKPFPLTLSIGISY--DVGKNRDYLLSTAHNAMDYIRKN 522


                 ...
gi 491601983 301 GRN 303
Cdd:PRK11359 523 GGN 525
PRK09966 PRK09966
diguanylate cyclase DgcN;
128-299 1.26e-18

diguanylate cyclase DgcN;


Pssm-ID: 182171 [Multi-domain]  Cd Length: 407  Bit Score: 85.83  E-value: 1.26e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491601983 128 WSVRditkthlLEQRLKQLSET---DALTGLLNRRAFISNLdNAIIQHTKRSQTLSCLMIDIDHFKDINDSVGHFSGDHV 204
Cdd:PRK09966 233 WQLR-------LQAKNAQLLRTalhDPLTGLANRAAFRSGI-NTLMNNSDARKTSALLFLDGDNFKYINDTWGHATGDRV 304

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491601983 205 ITRIAHvcqgviRGSDFIG------RLGGEEFAVILTDTNAiqAYEVaERIRQAIQATICHVDDVE----ITTTVSIGVA 274
Cdd:PRK09966 305 LIEIAK------RLAEFGGlrhkayRLGGDEFAMVLYDVQS--ESEV-QQICSALTQIFNLPFDLHnghqTTMTLSIGYA 375

                        170       180
                 ....*....|....*....|....*
gi 491601983 275 eLNSQQSNAKELLIEADKAMYYSKH 299
Cdd:PRK09966 376 -MTIEHASAEKLQELADHNMYQAKH 399
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 199-298 3.08e-14

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: 69.94  E-value: 3.08e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491601983 199 FSGDHVITRIahvcqgvirgsDFIGRLGGEEFAVILTDTNAIQAYEVAERIRQAIQATIchvddvEITTTVSIGVAELNs 278
Cdd:COG3706  106 FDPEELLARV-----------DLVARYGGEEFAILLPGTDLEGALAVAERIREAVAELP------SLRVTVSIGVAGDS- 167

                         90       100
                 ....*....|....*....|
gi 491601983 279 qqsnakeLLIEADkAMYYSK 298
Cdd:COG3706  168 -------LLKRAD-ALYQAR 179
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
 179-274 1.00e-09

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: 55.83  E-value: 1.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491601983 179 LSCLMIDIDHFKDINDSVGHFSGDHVITRIA-HVCQGVIRGSDFIGRLGGEEFAVILTDTNAIQAYEVAERIRQAiqati 257
Cdd:cd07556    2 VTILFADIVGFTSLADALGPDEGDELLNELAgRFDSLIRRSGDLKIKTIGDEFMVVSGLDHPAAAVAFAEDMREA----- 76

                         90       100
                 ....*....|....*....|.
gi 491601983 258 chVDDVEITT----TVSIGVA 274
Cdd:cd07556   77 --VSALNQSEgnpvRVRIGIH 95
PRK11829 PRK11829
biofilm formation regulator HmsP; Provisional
 141-305 4.24e-09

biofilm formation regulator HmsP; Provisional


Pssm-ID: 183329 [Multi-domain]  Cd Length: 660  Bit Score: 57.64  E-value: 4.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491601983 141 QRLKQLSETDALTGLLNRRAFISNLDNAIIQHTKRsQTLSCLMIDIDHFKDINDSVGHFSGDHVITRIAHVCQGVIRGSD 220
Cdd:PRK11829 226 ADMGRISHRFPVTELPNRSLFISLLEKEIASSTRT-DHFHLLVIGIETLQEVSGAMSEAQHQQLLLTIVQRIEQCIDDSD 304

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491601983 221 FIGRLGGEEFAVILTDT-NAIQAYEVAERIRQAIQATIChVDDVEITTTVSIGVAELNSQQSNAKELLIEADKAMYYSKH 299
Cdd:PRK11829 305 LLAQLSKTEFAVLARGTrRSFPAMQLARRIMSQVTQPLF-FDEITLRPSASIGITRYQAQQDTAESMMRNASTAMMAAHH 383


                 ....*.
gi 491601983 300 SGRNQV 305
Cdd:PRK11829 384 EGRNQI 389
PAS COG2202
PAS domain [Signal transduction mechanisms];
4-250 9.95e-06

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 46.17  E-value: 9.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491601983   4 KERETWLEAILNTLPDHVFILDESGRYIESFGGTHHSKTFNAERYIGLQLSDVLSPTKADELMGFIFDVMQDNETKVVKY 83
Cdd:COG2202    7 EESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGVWRGEL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491601983  84 NLSLHDHlllpieelealenpEEMWFEAIIKPVNAPENANKLVIWSVRDITKTHLLEQRLKQLSETDALTGLLNRRA-FI 162
Cdd:COG2202   87 RNRRKDG--------------SLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALRESEERLRLLVENAPDGiFV 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491601983 163 SNLDNAIIQHTKRSQTLSCLMIDIDHFKDINDSVGHFSGDHVITRIAHVCQGVIRGSDFIGRLGGEEFAVILTDTNAIQA 242
Cdd:COG2202  153 LDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLEGGRESYELELRLKDGDGRWVWVEASAVPL 232


                 ....*...
gi 491601983 243 YEVAERIR 250
Cdd:COG2202  233 RDGGEVIG 240
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
4-155 1.01e-05

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 46.76  E-value: 1.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491601983   4 KERETWLEAILNTLPDHVFILDESGRYI------ESFGGthhsktFNAERYIGLQLSDVLSPtkADELMGFIFDVMQDNE 77
Cdd:COG3852    3 RESEELLRAILDSLPDAVIVLDADGRITyvnpaaERLLG------LSAEELLGRPLAELFPE--DSPLRELLERALAEGQ 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491601983  78 TkVVKYNLSLHDHlllpieelealeNPEEMWFEAIIKPVNAPENANKLVIwSVRDITKTHLLEQRLKQLSETDALTGL 155
Cdd:COG3852   75 P-VTEREVTLRRK------------DGEERPVDVSVSPLRDAEGEGGVLL-VLRDITERKRLERELRRAEKLAAVGEL 138
PRK13561 PRK13561
putative diguanylate cyclase; Provisional
 137-305 1.70e-05

putative diguanylate cyclase; Provisional


Pssm-ID: 184143 [Multi-domain]  Cd Length: 651  Bit Score: 46.25  E-value: 1.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491601983 137 HLLEQRLKQLSETD---ALTGLLNRRAFISNLDnaiiQHTKRSQTLSCLMIDIDHFKDINDSVGHFSGDHVITRIAHVCQ 213
Cdd:PRK13561 218 QLLQRQYEEQSRNAtrfPVSDLPNKALLMALLE----QVVARKQTTALMIITCETLRDTAGVLKEAQREILLLTLVEKLK 293

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491601983 214 GVIRGSDFIGRLGGEEFAVILTDTN-AIQAYEVAERIRQAIQATIcHVDDVEITTTVSIGVAELNSQQSnAKELLIEADK 292
Cdd:PRK13561 294 SVLSPRMVLAQISGYDFAIIANGVKePWHAITLGQQVLTIINERL-PIQRIQLRPSCSIGIAMFYGDLT-AEQLYSRAIS 371

                        170
                 ....*....|...
gi 491601983 293 AMYYSKHSGRNQV 305
Cdd:PRK13561 372 AAFTARRKGKNQI 384
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
 2-156 1.07e-04

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


Pssm-ID: 444507 [Multi-domain]  Cd Length: 496  Bit Score: 43.57  E-value: 1.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491601983   2 IYKERETWLEAILNTLPDHVFILDESGRYIE-SFGGThhsKTFNAER--YIGLQLSDVLSPTKADELMGFIFDVM-QDNE 77
Cdd:COG5805  151 ILQEQEERLQTLIENSPDLICVIDTDGRILFiNESIE---RLFGAPReeLIGKNLLELLHPCDKEEFKERIESITeVWQE 227

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491601983  78 TKVVKYNLSLHDHLLlpieelealenpeemWFEAIIKPVNAPENANKLVIWSVRDITKTHLLEQRLKQlSETDALTGLL 156
Cdd:COG5805  228 FIIEREIITKDGRIR---------------YFEAVIVPLIDTDGSVKGILVILRDITEKKEAEELMAR-SEKLSIAGQL 290
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 14-134 1.28e-04

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: 40.86  E-value: 1.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491601983   14 LNTLPDHVFILDESGRYIESFGGTHHSKTFNAERYIGLQLSDVLSPTKADELMGFIFDVMQDNETkvvkynLSLHDHLLL 93
Cdd:pfam08448   1 LDSLPDALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAELLPPEDAARLERALRRALEGEEP------IDFLEELLL 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 491601983   94 pieelealeNPEEMWFEAIIKPVNAPENANKLVIWSVRDIT 134
Cdd:pfam08448  75 ---------NGEERHYELRLTPLRDPDGEVIGVLVISRDIT 106
 
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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