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Conserved domains on  [gi|746447641|ref|WP_039487545|]
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MULTISPECIES: sensor domain-containing diguanylate cyclase [Pseudoalteromonas]

Protein Classification

sensor domain-containing diguanylate cyclase( domain architecture ID 10637542)

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

CATH:  3.30.70.1230|3.30.450.40
EC:  2.7.7.65
Gene Ontology:  GO:0046872|GO:0052621|GO:0005515
PubMed:  11119645|9433123
SCOP:  4001316|4001852

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 ...
 147-317 1.92e-46

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: 158.22  E-value: 1.92e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746447641 147 LKDLGTLVEQEIQSIQLATIDELTRISNRRGFLNLAEHTLNICRRNKVSMSFILFDLNKFKQINDVYGHHEGDFVLNKFA 226
Cdd:COG2199   97 LEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVA 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746447641 227 QIMLSSFCDCEVIGRLGGDEFVVMLSDLDETKAEFVLQRFADAIA-YANNTLNKPYKIDYSVGVTHFKyDTGKSVEDMIQ 305
Cdd:COG2199  177 RRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEqLPFELEGKELRVTVSIGVALYP-EDGDSAEELLR 255

                        170
                 ....*....|..
gi 746447641 306 DADVAMYQQKKQ 317
Cdd:COG2199  256 RADLALYRAKRA 267
GAF COG2203
GAF domain [Signal transduction mechanisms];
10-271 3.34e-23

GAF domain [Signal transduction mechanisms];


:

Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 100.27  E-value: 3.34e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746447641  10 EAERLHALKTL--KIL-DTSHEERFDRVTRIAKRMFNVSISLLTLIDEDRQ--WFKSRQGLDAP---ELPRETSFCGHTI 81
Cdd:COG2203  188 ELERLALLNEIsqALRsALDLEELLQRILELAGELLGADRGAILLVDEDGGelELVAAPGLPEEelgRLPLGEGLAGRAL 267

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746447641  82 NQDELLIIPDTVQDKRFFDNPF-VTGDPKVRFYAGFPLkLRQGVIIGTLCLADNKPRHLNDEEKQLLKDLGTLVEQEIQS 160
Cdd:COG2203  268 RTGEPVVVNDASTDPRFAPSLReLLLALGIRSLLCVPL-LVDGRLIGVLALYSKEPRAFTEEDLELLEALADQAAIAIER 346

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746447641 161 IQL--------------------ATIDELTRISNRRGFLNLAEHTLNICRRNKVSMSFILFDLNKFKQINDVYGHHEGDF 220
Cdd:COG2203  347 ARLyealeaalaallqelallrlLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADLSGLLALEGLLLLDL 426

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 746447641 221 VLNKFAQIMLSSFCDCEVIGRLGGDEFVVMLSDLDETKAEFVLQRFADAIA 271
Cdd:COG2203  427 LLLLLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVI 477
 
Name Accession Description Interval E-value
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 147-317 1.92e-46

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: 158.22  E-value: 1.92e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746447641 147 LKDLGTLVEQEIQSIQLATIDELTRISNRRGFLNLAEHTLNICRRNKVSMSFILFDLNKFKQINDVYGHHEGDFVLNKFA 226
Cdd:COG2199   97 LEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVA 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746447641 227 QIMLSSFCDCEVIGRLGGDEFVVMLSDLDETKAEFVLQRFADAIA-YANNTLNKPYKIDYSVGVTHFKyDTGKSVEDMIQ 305
Cdd:COG2199  177 RRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEqLPFELEGKELRVTVSIGVALYP-EDGDSAEELLR 255

                        170
                 ....*....|..
gi 746447641 306 DADVAMYQQKKQ 317
Cdd:COG2199  256 RADLALYRAKRA 267
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 165-317 1.35e-45

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: 151.94  E-value: 1.35e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746447641 165 TIDELTRISNRRGFLNLAEHTLNICRRNKVSMSFILFDLNKFKQINDVYGHHEGDFVLNKFAQIMLSSFCDCEVIGRLGG 244
Cdd:cd01949    1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 746447641 245 DEFVVMLSDLDETKAEFVLQRFADAIAYANNTLNKPYKIDYSVGVTHFKYDtGKSVEDMIQDADVAMYQQKKQ 317
Cdd:cd01949   81 DEFAILLPGTDLEEAEALAERLREAIEEPFFIDGQEIRVTASIGIATYPED-GEDAEELLRRADEALYRAKRS 152
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 162-317 5.09e-40

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 137.76  E-value: 5.09e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746447641   162 QLATIDELTRISNRRGFLNLAEHTLNICRRNKVSMSFILFDLNKFKQINDVYGHHEGDFVLNKFAQIMLSSFCDCEVIGR 241
Cdd:smart00267   1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 746447641   242 LGGDEFVVMLSDLDETKAEFVLQRFADAIAYANNTLNKPYKIDYSVGVTHFKYDtGKSVEDMIQDADVAMYQQKKQ 317
Cdd:smart00267  81 LGGDEFALLLPETSLEEAIALAERILQQLREPIIIHGIPLYLTISIGVAAYPNP-GEDAEDLLKRADTALYQAKKA 155
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 164-317 8.55e-35

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: 124.29  E-value: 8.55e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746447641  164 ATIDELTRISNRRGFLNLAEHTLNICRRNKVSMSFILFDLNKFKQINDVYGHHEGDFVLNKFAQIMLSSFCDCEVIGRLG 243
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 746447641  244 GDEFVVMLSDLDETKA----EFVLQRFAD-AIAYANNTLNKPYKIdySVGVTHFKYDtGKSVEDMIQDADVAMYQQKKQ 317
Cdd:pfam00990  81 GDEFAILLPETSLEGAqelaERIRRLLAKlKIPHTVSGLPLYVTI--SIGIAAYPND-GEDPEDLLKRADTALYQAKQA 156
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 163-316 7.44e-33

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: 119.36  E-value: 7.44e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746447641  163 LATIDELTRISNRRGFLNLAEHTLNICRRNKVSMSFILFDLNKFKQINDVYGHHEGDFVLNKFAQIMLSSFCDCEVIGRL 242
Cdd:TIGR00254   1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746447641  243 GGDEFVVMLSDLDETKAEFVLQRFADAIayanNTLNKPYKIDY------SVGVTHFKYDtGKSVEDMIQDADVAMYQQKK 316
Cdd:TIGR00254  81 GGEEFVVILPGTPLEDALSKAERLRDAI----NSKPIEVAGSEtltvtvSIGVACYPGH-GLTLEELLKRADEALYQAKK 155
GAF COG2203
GAF domain [Signal transduction mechanisms];
10-271 3.34e-23

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 100.27  E-value: 3.34e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746447641  10 EAERLHALKTL--KIL-DTSHEERFDRVTRIAKRMFNVSISLLTLIDEDRQ--WFKSRQGLDAP---ELPRETSFCGHTI 81
Cdd:COG2203  188 ELERLALLNEIsqALRsALDLEELLQRILELAGELLGADRGAILLVDEDGGelELVAAPGLPEEelgRLPLGEGLAGRAL 267

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746447641  82 NQDELLIIPDTVQDKRFFDNPF-VTGDPKVRFYAGFPLkLRQGVIIGTLCLADNKPRHLNDEEKQLLKDLGTLVEQEIQS 160
Cdd:COG2203  268 RTGEPVVVNDASTDPRFAPSLReLLLALGIRSLLCVPL-LVDGRLIGVLALYSKEPRAFTEEDLELLEALADQAAIAIER 346

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746447641 161 IQL--------------------ATIDELTRISNRRGFLNLAEHTLNICRRNKVSMSFILFDLNKFKQINDVYGHHEGDF 220
Cdd:COG2203  347 ARLyealeaalaallqelallrlLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADLSGLLALEGLLLLDL 426

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 746447641 221 VLNKFAQIMLSSFCDCEVIGRLGGDEFVVMLSDLDETKAEFVLQRFADAIA 271
Cdd:COG2203  427 LLLLLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVI 477
PRK09894 PRK09894
diguanylate cyclase; Provisional
 163-315 8.45e-22

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 93.21  E-value: 8.45e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746447641 163 LATIDELTRISNRRGFLNLAEHtlNICRRNKVSMSFILFDLNKFKQINDVYGHHEGDFVLNKFAQIMLSSFCDCEVIGRL 242
Cdd:PRK09894 128 RSNMDVLTGLPGRRVLDESFDH--QLRNREPQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRY 205

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 746447641 243 GGDEFVVMLSDLDETKAEFVLQRFADAIAyANNTL--NKPYKIDYSVGVThfKYDTGKSVEDMIQDADVAMYQQK 315
Cdd:PRK09894 206 GGEEFIICLKAATDEEACRAGERIRQLIA-NHAIThsDGRINITATFGVS--RAFPEETLDVVIGRADRAMYEGK 277
diguan_SiaD NF038266
biofilm regulation diguanylate cyclase SiaD;
162-317 2.85e-20

biofilm regulation diguanylate cyclase SiaD;


Pssm-ID: 468439 [Multi-domain]  Cd Length: 252  Bit Score: 88.11  E-value: 2.85e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746447641 162 QLATIDELTRISNRRGFLNLAEHTLNICRRNKVSMSFILFDLNKFKQINDVYGHHEGDFVLNKFAQIMLSSFCDCEVIGR 241
Cdd:NF038266  92 EASTRDPLTGLPNRRLLMERLREEVERARRSGRPFTLAMLDVDHFKRINDRYGHEVGDRVLVEIARTLRAELREYDLCGR 171

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 746447641 242 LGGDEFVVMLSDLDETKAEFVLQRFADAI-AYANNTLNKPYKIDYSVGVTHFKYDtGKSVEDMIQDADVAMYQQKKQ 317
Cdd:NF038266 172 WGGEEFLLLLPETGLEEAQVVLERLREAVrALAVRVGDDVLSVTASAGLAEHRPP-EEGLSATLSRADQALYQAKRA 247
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
 27-163 4.13e-17

Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these domains in PDE6B result in autosomal recessive inheritance of retinitis pigmentosa.


Pssm-ID: 214500 [Multi-domain]  Cd Length: 149  Bit Score: 77.04  E-value: 4.13e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746447641    27 HEERFDRVTRIAKRMFNVSISLLTLIDED---RQWFKSRQGLDAPEL----PRETSFCGHTINQDELLIIPDTVQDkRFF 99
Cdd:smart00065   2 LEELLQTILEELRQLLGADRVLIYLVDENdrgELVLVAADGLTLPTLgirfPLDEGLAGRVAETGRPLNIPDVEAD-PLF 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 746447641   100 DNPFVTGDPKVRFYAGFPLKlRQGVIIGTLCLADNK-PRHLNDEEKQLLKDLGTLVEQEIQSIQL 163
Cdd:smart00065  81 AEDLLGRYQGVRSFLAVPLV-ADGELVGVLALHNKKsPRPFTEEDEELLQALANQLAIALANAQL 144
diguan_DgcJ NF040885
diguanylate cyclase DgcJ;
167-317 8.62e-16

diguanylate cyclase DgcJ;


Pssm-ID: 468821 [Multi-domain]  Cd Length: 490  Bit Score: 77.69  E-value: 8.62e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746447641 167 DELTRISNRRGFLNLAEHTLNICRRNKVSMSFILFDLNKFKQINDVYGHHEGDFVLNKFAQIMLSSFCDCEVIGRLGGDE 246
Cdd:NF040885 344 DSMTGLYNRKILTPTLEQRLQRLTEKGIPVTFIALDCDKLKHINDTLGHHEGDRAITLLAQAISASIRKSDYGIRLGGDE 423

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 746447641 247 FVVMLSDLDETKAEFVLQRFADAIAyannTLNKPYKIDYSVGVTHFKydTGKSVEDMIQDADVAMYQQKKQ 317
Cdd:NF040885 424 FCIILIDYEEAEAQNLIERIRQHLR----TIDPDKRVSFSWGAYQMQ--PGDTLDDAYKAADERLYLNKKQ 488
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
 28-158 3.03e-15

GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl cyclases, phytochromes, FhlA and NifA. Adenylyl and guanylyl cyclases catalyze ATP and GTP to the second messengers cAMP and cGMP, respectively, these products up-regulating catalytic activity by binding to the regulatory GAF domain(s). The opposite hydrolysis reaction is catalyzed by phosphodiesterase. cGMP-dependent 3',5'-cyclic phosphodiesterase catalyzes the conversion of guanosine 3',5'-cyclic phosphate to guanosine 5'-phosphate. Here too, cGMP regulates catalytic activity by GAF-domain binding. Phytochromes are regulatory photoreceptors in plants and bacteria which exist in two thermally-stable states that are reversibly inter-convertible by light: the Pr state absorbs maximally in the red region of the spectrum, while the Pfr state absorbs maximally in the far-red region. This domain is also found in FhlA (formate hydrogen lyase transcriptional activator) and NifA, a transcriptional activator which is required for activation of most Nif operons which are directly involved in nitrogen fixation. NifA interacts with sigma-54. This domain can bind biliverdine and phycocyanobilin (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 460259 [Multi-domain]  Cd Length: 133  Bit Score: 71.36  E-value: 3.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746447641   28 EERFDRVTRIAKRMFNVSISLLTLIDED--------RQWFKSRQGLDAPELPretsfcGHTINQDELLIIPDTVQDKRFF 99
Cdd:pfam01590   3 EEILQTILEELRELLGADRCALYLPDADgleylppgARWLKAAGLEIPPGTG------VTVLRTGRPLVVPDAAGDPRFL 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 746447641  100 DNPFVTGDPKVRFYAGFPLkLRQGVIIGTLCLADNKPrHLNDEEKQLLKDLGTLVEQEI 158
Cdd:pfam01590  77 DPLLLLRNFGIRSLLAVPI-IDDGELLGVLVLHHPRP-PFTEEELELLEVLADQVAIAL 133
 
Name Accession Description Interval E-value
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 147-317 1.92e-46

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: 158.22  E-value: 1.92e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746447641 147 LKDLGTLVEQEIQSIQLATIDELTRISNRRGFLNLAEHTLNICRRNKVSMSFILFDLNKFKQINDVYGHHEGDFVLNKFA 226
Cdd:COG2199   97 LEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVA 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746447641 227 QIMLSSFCDCEVIGRLGGDEFVVMLSDLDETKAEFVLQRFADAIA-YANNTLNKPYKIDYSVGVTHFKyDTGKSVEDMIQ 305
Cdd:COG2199  177 RRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEqLPFELEGKELRVTVSIGVALYP-EDGDSAEELLR 255

                        170
                 ....*....|..
gi 746447641 306 DADVAMYQQKKQ 317
Cdd:COG2199  256 RADLALYRAKRA 267
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 165-317 1.35e-45

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: 151.94  E-value: 1.35e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746447641 165 TIDELTRISNRRGFLNLAEHTLNICRRNKVSMSFILFDLNKFKQINDVYGHHEGDFVLNKFAQIMLSSFCDCEVIGRLGG 244
Cdd:cd01949    1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 746447641 245 DEFVVMLSDLDETKAEFVLQRFADAIAYANNTLNKPYKIDYSVGVTHFKYDtGKSVEDMIQDADVAMYQQKKQ 317
Cdd:cd01949   81 DEFAILLPGTDLEEAEALAERLREAIEEPFFIDGQEIRVTASIGIATYPED-GEDAEELLRRADEALYRAKRS 152
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 162-317 5.09e-40

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 137.76  E-value: 5.09e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746447641   162 QLATIDELTRISNRRGFLNLAEHTLNICRRNKVSMSFILFDLNKFKQINDVYGHHEGDFVLNKFAQIMLSSFCDCEVIGR 241
Cdd:smart00267   1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 746447641   242 LGGDEFVVMLSDLDETKAEFVLQRFADAIAYANNTLNKPYKIDYSVGVTHFKYDtGKSVEDMIQDADVAMYQQKKQ 317
Cdd:smart00267  81 LGGDEFALLLPETSLEEAIALAERILQQLREPIIIHGIPLYLTISIGVAAYPNP-GEDAEDLLKRADTALYQAKKA 155
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 155-317 1.53e-38

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: 144.53  E-value: 1.53e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746447641 155 EQEIQsiQLATIDELTRISNRRGFLNLAEHTLNICRRNKVSMSFILFDLNKFKQINDVYGHHEGDFVLNKFAQIMLSSFC 234
Cdd:COG5001  244 EERLR--HLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLR 321

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746447641 235 DCEVIGRLGGDEFVVMLSDLDETKAefvLQRFADAIayaNNTLNKPYKIDY-------SVGVTHFKYDtGKSVEDMIQDA 307
Cdd:COG5001  322 EGDTVARLGGDEFAVLLPDLDDPED---AEAVAERI---LAALAEPFELDGhelyvsaSIGIALYPDD-GADAEELLRNA 394

                        170
                 ....*....|
gi 746447641 308 DVAMYQQKKQ 317
Cdd:COG5001  395 DLAMYRAKAA 404
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 164-317 8.55e-35

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: 124.29  E-value: 8.55e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746447641  164 ATIDELTRISNRRGFLNLAEHTLNICRRNKVSMSFILFDLNKFKQINDVYGHHEGDFVLNKFAQIMLSSFCDCEVIGRLG 243
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 746447641  244 GDEFVVMLSDLDETKA----EFVLQRFAD-AIAYANNTLNKPYKIdySVGVTHFKYDtGKSVEDMIQDADVAMYQQKKQ 317
Cdd:pfam00990  81 GDEFAILLPETSLEGAqelaERIRRLLAKlKIPHTVSGLPLYVTI--SIGIAAYPND-GEDPEDLLKRADTALYQAKQA 156
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 163-316 7.44e-33

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: 119.36  E-value: 7.44e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746447641  163 LATIDELTRISNRRGFLNLAEHTLNICRRNKVSMSFILFDLNKFKQINDVYGHHEGDFVLNKFAQIMLSSFCDCEVIGRL 242
Cdd:TIGR00254   1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746447641  243 GGDEFVVMLSDLDETKAEFVLQRFADAIayanNTLNKPYKIDY------SVGVTHFKYDtGKSVEDMIQDADVAMYQQKK 316
Cdd:TIGR00254  81 GGEEFVVILPGTPLEDALSKAERLRDAI----NSKPIEVAGSEtltvtvSIGVACYPGH-GLTLEELLKRADEALYQAKK 155
GAF COG2203
GAF domain [Signal transduction mechanisms];
10-271 3.34e-23

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 100.27  E-value: 3.34e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746447641  10 EAERLHALKTL--KIL-DTSHEERFDRVTRIAKRMFNVSISLLTLIDEDRQ--WFKSRQGLDAP---ELPRETSFCGHTI 81
Cdd:COG2203  188 ELERLALLNEIsqALRsALDLEELLQRILELAGELLGADRGAILLVDEDGGelELVAAPGLPEEelgRLPLGEGLAGRAL 267

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746447641  82 NQDELLIIPDTVQDKRFFDNPF-VTGDPKVRFYAGFPLkLRQGVIIGTLCLADNKPRHLNDEEKQLLKDLGTLVEQEIQS 160
Cdd:COG2203  268 RTGEPVVVNDASTDPRFAPSLReLLLALGIRSLLCVPL-LVDGRLIGVLALYSKEPRAFTEEDLELLEALADQAAIAIER 346

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746447641 161 IQL--------------------ATIDELTRISNRRGFLNLAEHTLNICRRNKVSMSFILFDLNKFKQINDVYGHHEGDF 220
Cdd:COG2203  347 ARLyealeaalaallqelallrlLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADLSGLLALEGLLLLDL 426

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 746447641 221 VLNKFAQIMLSSFCDCEVIGRLGGDEFVVMLSDLDETKAEFVLQRFADAIA 271
Cdd:COG2203  427 LLLLLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVI 477
PRK09894 PRK09894
diguanylate cyclase; Provisional
 163-315 8.45e-22

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 93.21  E-value: 8.45e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746447641 163 LATIDELTRISNRRGFLNLAEHtlNICRRNKVSMSFILFDLNKFKQINDVYGHHEGDFVLNKFAQIMLSSFCDCEVIGRL 242
Cdd:PRK09894 128 RSNMDVLTGLPGRRVLDESFDH--QLRNREPQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRY 205

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 746447641 243 GGDEFVVMLSDLDETKAEFVLQRFADAIAyANNTL--NKPYKIDYSVGVThfKYDTGKSVEDMIQDADVAMYQQK 315
Cdd:PRK09894 206 GGEEFIICLKAATDEEACRAGERIRQLIA-NHAIThsDGRINITATFGVS--RAFPEETLDVVIGRADRAMYEGK 277
pleD PRK09581
response regulator PleD; Reviewed
 159-316 1.70e-21

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 94.20  E-value: 1.70e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746447641 159 QSIQLATIDELTRISNRRGFlnlAEHTLNICRRNKV---SMSFILFDLNKFKQINDVYGHHEGDFVLNKFAQIMLSSFCD 235
Cdd:PRK09581 287 QSIEMAVTDGLTGLHNRRYF---DMHLKNLIERANErgkPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRG 363

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746447641 236 CEVIGRLGGDEFVVMLSDLDETKAEFVLQRFADAIAYANNTL---NKPYKIDYSVGVTHFKyDTGKSVEDMIQDADVAMY 312
Cdd:PRK09581 364 TDLIARYGGEEFVVVMPDTDIEDAIAVAERIRRKIAEEPFIIsdgKERLNVTVSIGVAELR-PSGDTIEALIKRADKALY 442


                 ....
gi 746447641 313 QQKK 316
Cdd:PRK09581 443 EAKN 446
diguan_SiaD NF038266
biofilm regulation diguanylate cyclase SiaD;
162-317 2.85e-20

biofilm regulation diguanylate cyclase SiaD;


Pssm-ID: 468439 [Multi-domain]  Cd Length: 252  Bit Score: 88.11  E-value: 2.85e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746447641 162 QLATIDELTRISNRRGFLNLAEHTLNICRRNKVSMSFILFDLNKFKQINDVYGHHEGDFVLNKFAQIMLSSFCDCEVIGR 241
Cdd:NF038266  92 EASTRDPLTGLPNRRLLMERLREEVERARRSGRPFTLAMLDVDHFKRINDRYGHEVGDRVLVEIARTLRAELREYDLCGR 171

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 746447641 242 LGGDEFVVMLSDLDETKAEFVLQRFADAI-AYANNTLNKPYKIDYSVGVTHFKYDtGKSVEDMIQDADVAMYQQKKQ 317
Cdd:NF038266 172 WGGEEFLLLLPETGLEEAQVVLERLREAVrALAVRVGDDVLSVTASAGLAEHRPP-EEGLSATLSRADQALYQAKRA 247
PRK15426 PRK15426
cellulose biosynthesis regulator YedQ;
162-317 1.78e-18

cellulose biosynthesis regulator YedQ;


Pssm-ID: 237964 [Multi-domain]  Cd Length: 570  Bit Score: 85.84  E-value: 1.78e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746447641 162 QLATIDELTRISNRRGFLNLAEHTLNICRRNKVSMSFILFDLNKFKQINDVYGHHEGDFVLNKFAQIMLSSFCDCEVIGR 241
Cdd:PRK15426 396 WQAWHDPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGR 475

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746447641 242 LGGDEFVVML--SDLDETK--AEFVLQRFAD-AIAYANNTlnkPYKIDYSVGVTHFKYDTGKSVEDMIQDADVAMYQQKK 316
Cdd:PRK15426 476 VGGEEFCVVLpgASLAEAAqvAERIRLRINEkEILVAKST---TIRISASLGVSSAEEDGDYDFEQLQSLADRRLYLAKQ 552


                 .
gi 746447641 317 Q 317
Cdd:PRK15426 553 A 553
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 164-315 2.10e-18

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 85.88  E-value: 2.10e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746447641  164 ATIDELTRISNRRGFlnlAEHTLNIC-----RRNKVSMSFIlfDLNKFKQINDVYGHHEGDFVLNKFAQIMLSSFCDCEV 238
Cdd:PRK09776  665 ASHDALTHLANRASF---EKQLRRLLqtvnsTHQRHALVFI--DLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSDV 739

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 746447641  239 IGRLGGDEFVVMLSDLDETKAEFVLQRFADAI-AYANNTLNKPYKIDYSVGVTHFKYDTGKSVEDMIQdADVAMYQQK 315
Cdd:PRK09776  740 LARLGGDEFGLLLPDCNVESARFIATRIISAInDYHFPWEGRVYRVGASAGITLIDANNHQASEVMSQ-ADIACYAAK 816
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
 27-163 4.13e-17

Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these domains in PDE6B result in autosomal recessive inheritance of retinitis pigmentosa.


Pssm-ID: 214500 [Multi-domain]  Cd Length: 149  Bit Score: 77.04  E-value: 4.13e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746447641    27 HEERFDRVTRIAKRMFNVSISLLTLIDED---RQWFKSRQGLDAPEL----PRETSFCGHTINQDELLIIPDTVQDkRFF 99
Cdd:smart00065   2 LEELLQTILEELRQLLGADRVLIYLVDENdrgELVLVAADGLTLPTLgirfPLDEGLAGRVAETGRPLNIPDVEAD-PLF 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 746447641   100 DNPFVTGDPKVRFYAGFPLKlRQGVIIGTLCLADNK-PRHLNDEEKQLLKDLGTLVEQEIQSIQL 163
Cdd:smart00065  81 AEDLLGRYQGVRSFLAVPLV-ADGELVGVLALHNKKsPRPFTEEDEELLQALANQLAIALANAQL 144
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
162-315 1.23e-16

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 80.50  E-value: 1.23e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746447641 162 QLATIDELTRISNRRGFLNLAEHTLNICRRNKVSMSFIlfDLNKFKQINDVYGHHEGDFVLNKFAQIMLSSFCDCEVIGR 241
Cdd:PRK10060 235 ILANTDSITGLPNRNAIQELIDHAINAADNNQVGIVYL--DLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQTLAR 312

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746447641 242 LGGDEFVVMLSDLDETKAEFVLQRFADaiayannTLNKPYKID----Y---SVGVTHFKyDTGKSVEDMIQDADVAMYQQ 314
Cdd:PRK10060 313 LGGDEFLVLASHTSQAALEAMASRILT-------RLRLPFRIGlievYtgcSIGIALAP-EHGDDSESLIRSADTAMYTA 384


                 .
gi 746447641 315 K 315
Cdd:PRK10060 385 K 385
diguan_DgcJ NF040885
diguanylate cyclase DgcJ;
167-317 8.62e-16

diguanylate cyclase DgcJ;


Pssm-ID: 468821 [Multi-domain]  Cd Length: 490  Bit Score: 77.69  E-value: 8.62e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746447641 167 DELTRISNRRGFLNLAEHTLNICRRNKVSMSFILFDLNKFKQINDVYGHHEGDFVLNKFAQIMLSSFCDCEVIGRLGGDE 246
Cdd:NF040885 344 DSMTGLYNRKILTPTLEQRLQRLTEKGIPVTFIALDCDKLKHINDTLGHHEGDRAITLLAQAISASIRKSDYGIRLGGDE 423

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 746447641 247 FVVMLSDLDETKAEFVLQRFADAIAyannTLNKPYKIDYSVGVTHFKydTGKSVEDMIQDADVAMYQQKKQ 317
Cdd:NF040885 424 FCIILIDYEEAEAQNLIERIRQHLR----TIDPDKRVSFSWGAYQMQ--PGDTLDDAYKAADERLYLNKKQ 488
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
 28-158 3.03e-15

GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl cyclases, phytochromes, FhlA and NifA. Adenylyl and guanylyl cyclases catalyze ATP and GTP to the second messengers cAMP and cGMP, respectively, these products up-regulating catalytic activity by binding to the regulatory GAF domain(s). The opposite hydrolysis reaction is catalyzed by phosphodiesterase. cGMP-dependent 3',5'-cyclic phosphodiesterase catalyzes the conversion of guanosine 3',5'-cyclic phosphate to guanosine 5'-phosphate. Here too, cGMP regulates catalytic activity by GAF-domain binding. Phytochromes are regulatory photoreceptors in plants and bacteria which exist in two thermally-stable states that are reversibly inter-convertible by light: the Pr state absorbs maximally in the red region of the spectrum, while the Pfr state absorbs maximally in the far-red region. This domain is also found in FhlA (formate hydrogen lyase transcriptional activator) and NifA, a transcriptional activator which is required for activation of most Nif operons which are directly involved in nitrogen fixation. NifA interacts with sigma-54. This domain can bind biliverdine and phycocyanobilin (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 460259 [Multi-domain]  Cd Length: 133  Bit Score: 71.36  E-value: 3.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746447641   28 EERFDRVTRIAKRMFNVSISLLTLIDED--------RQWFKSRQGLDAPELPretsfcGHTINQDELLIIPDTVQDKRFF 99
Cdd:pfam01590   3 EEILQTILEELRELLGADRCALYLPDADgleylppgARWLKAAGLEIPPGTG------VTVLRTGRPLVVPDAAGDPRFL 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 746447641  100 DNPFVTGDPKVRFYAGFPLkLRQGVIIGTLCLADNKPrHLNDEEKQLLKDLGTLVEQEI 158
Cdd:pfam01590  77 DPLLLLRNFGIRSLLAVPI-IDDGELLGVLVLHHPRP-PFTEEELELLEVLADQVAIAL 133
adrA PRK10245
diguanylate cyclase AdrA; Provisional
 163-316 4.35e-13

diguanylate cyclase AdrA; Provisional


Pssm-ID: 182329 [Multi-domain]  Cd Length: 366  Bit Score: 69.09  E-value: 4.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746447641 163 LATIDELTRISNRRGFLNLAEHTLNICRRNKVSMSFILFDLNKFKQINDVYGHHEGD---FVLNKFAQIMLSSfcdCEVI 239
Cdd:PRK10245 204 MSTRDGMTGVYNRRHWETLLRNEFDNCRRHHRDATLLIIDIDHFKSINDTWGHDVGDeaiVALTRQLQITLRG---SDVI 280

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746447641 240 GRLGGDEFVVMLSDLDETKAEFVLQRFADAIayanNTLNKP----YKIDYSVGVTHFKYDTGKSVEdMIQDADVAMYQQK 315
Cdd:PRK10245 281 GRFGGDEFAVIMSGTPAESAITAMSRVHEGL----NTLRLPnapqVTLRISVGVAPLNPQMSHYRE-WLKSADLALYKAK 355


                 .
gi 746447641 316 K 316
Cdd:PRK10245 356 N 356
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 116-316 3.07e-12

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 67.10  E-value: 3.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746447641 116 FPLKLRQGVIIGTLCLadnKPRHLND---------EEKQLLKDLGTLVEQEIQSI-QLATIDELTRISNRrgflNLAEHT 185
Cdd:PRK11359 321 ATIRQRDGAPAGTLQI---KTSSGAEtsafiervaDISQHLAALALEQEKSRQHIeQLIQFDPLTGLPNR----NNLHNY 393

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746447641 186 LNICRRNKVSMSFILFDLNKFKQINDVYGHHEGDFVLNKFAQIMLSSFCDCEVIGRLGGDEFVVMLSDLDETKAEFVLQR 265
Cdd:PRK11359 394 LDDLVDKAVSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGTQFVLVSLENDVSNITQIADE 473

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 746447641 266 FADAIAYANNTLNKPYKIDYSVGVTHfkyDTGKSVEDMIQDADVAMYQQKK 316
Cdd:PRK11359 474 LRNVVSKPIMIDDKPFPLTLSIGISY---DVGKNRDYLLSTAHNAMDYIRK 521
PRK09966 PRK09966
diguanylate cyclase DgcN;
142-319 2.87e-11

diguanylate cyclase DgcN;


Pssm-ID: 182171 [Multi-domain]  Cd Length: 407  Bit Score: 63.87  E-value: 2.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746447641 142 EEKQLlkdlgTLVEQEIQSIQLATIDELTRISNRRGFLNLAEHTLNICRRNKVSmSFILFDLNKFKQINDVYGHHEGDFV 221
Cdd:PRK09966 231 EEWQL-----RLQAKNAQLLRTALHDPLTGLANRAAFRSGINTLMNNSDARKTS-ALLFLDGDNFKYINDTWGHATGDRV 304

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746447641 222 LNKFAQIMlssfcdCEVIG------RLGGDEFVVMLSDLdetKAEFVLQRFADAIAYAnntLNKPYK------------I 283
Cdd:PRK09966 305 LIEIAKRL------AEFGGlrhkayRLGGDEFAMVLYDV---QSESEVQQICSALTQI---FNLPFDlhnghqttmtlsI 372

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 746447641 284 DYSVGVTHfkydtgKSVEDMIQDADVAMYQQKKQQS 319
Cdd:PRK09966 373 GYAMTIEH------ASAEKLQELADHNMYQAKHQRA 402
GAF_2 pfam13185
GAF domain; The GAF domain is named after some of the proteins it is found in, including ...
 24-159 6.19e-10

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


Pssm-ID: 433019 [Multi-domain]  Cd Length: 137  Bit Score: 56.71  E-value: 6.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746447641   24 DTSHEERFDRVTRIAKRMFNVSISLLTLIDEDRQ---WFKSRQGL-DAPELPRETSFCGHTINQDELLIIPDTVQDKRFF 99
Cdd:pfam13185   1 AADLEELLDAVLEAAVELGASAVGFILLVDDDGRlaaWGGAADELsAALDDPPGEGLVGEALRTGRPVIVNDLAADPAKK 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 746447641  100 DNPFvtGDPKVRFYAGFPLkLRQGVIIGTLCLADNKPRHLNDEEKQLLKDLGTLVEQEIQ 159
Cdd:pfam13185  81 GLPA--GHAGLRSFLSVPL-VSGGRVVGVLALGSNRPGAFDEEDLELLELLAEQAAIAIE 137
PtsP COG3605
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];
24-184 9.03e-10

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


Pssm-ID: 442824 [Multi-domain]  Cd Length: 188  Bit Score: 57.21  E-value: 9.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746447641  24 DTSHEERFDRVTRIAKRMFNVSISLLTLIDEDRQWFKSR--QGLDAPE-----LPRETSFCGHTINQDELLIIPDTVQDK 96
Cdd:COG3605   16 ALDLDEALDRIVRRIAEALGVDVCSIYLLDPDGGRLELRatEGLNPEAvgkvrLPLGEGLVGLVAERGEPLNLADAASHP 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746447641  97 RFFDNPFvTGDPKVRFYAGFPLkLRQGVIIGTLCLADNKPRHLNDEEKQLLKdlgTLVEQEIQSIQLATIDELTRISNRR 176
Cdd:COG3605   96 RFKYFPE-TGEEGFRSFLGVPI-IRRGRVLGVLVVQSREPREFTEEEVEFLV---TLAAQLAEAIANAELLGELRAALAE 170


                 ....*...
gi 746447641 177 GFLNLAEH 184
Cdd:COG3605  171 LSLAREEE 178
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 237-313 2.54e-06

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: 46.83  E-value: 2.54e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 746447641 237 EVIGRLGGDEFVVMLSDLDETKAEFVLQRFADAIAYANntlnkPYKIDYSVGVthfkydtgkSVEDMIQDADvAMYQ 313
Cdd:COG3706  116 DLVARYGGEEFAILLPGTDLEGALAVAERIREAVAELP-----SLRVTVSIGV---------AGDSLLKRAD-ALYQ 177
GAF_3 pfam13492
GAF domain;
28-154 9.29e-06

GAF domain;


Pssm-ID: 433253 [Multi-domain]  Cd Length: 129  Bit Score: 44.28  E-value: 9.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746447641   28 EERFDRVTRIAKRMFNVSISLLTLIDEDRQWFKSRQGLDAPE-----LPRETSFCGHTINQDELLIIPDtvqdkrffdNP 102
Cdd:pfam13492   3 DEILEALLKLLVRLLGAERAAVYLLDEDGNKLQVAAGYDGEPdpsesLDADSPLARRALSSGEPISGLG---------SA 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 746447641  103 FVTGDPKVRFYAGfPLKLRQGVIiGTLCLADNKPRHLNDEEKQLLKDLGTLV 154
Cdd:pfam13492  74 GEDGLPDGPALVV-PLVAGRRVI-GVLALASSKPRAFDAEDLRLLESLAAQI 123
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
 199-291 9.42e-06

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: 44.65  E-value: 9.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746447641 199 ILF-DLNKFKQINDVYGHHEGDFVLNKFAQIM--LSSFCDCEVIgRLGGDEFVVMLSDLDETKAEFVLQRFADAIAYANN 275
Cdd:cd07556    4 ILFaDIVGFTSLADALGPDEGDELLNELAGRFdsLIRRSGDLKI-KTIGDEFMVVSGLDHPAAAVAFAEDMREAVSALNQ 82

                         90
                 ....*....|....*.
gi 746447641 276 TLNKPYKIdySVGVTH 291
Cdd:cd07556   83 SEGNPVRV--RIGIHT 96
 
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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