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Conserved domains on  [gi|1686965737|gb|QDD39492|]
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GGDEF domain-containing protein [Pseudomonas aeruginosa]

Protein Classification

GGDEF domain-containing protein( domain architecture ID 17609202)

GGDEF domain-containing protein similar to E.coli diguanylate cyclases DgcZ (YdeH) and DgcT (YcdT), and to E. coli CdgI (YeaI), a c-di-GMP-binding effector with a degenerate GGDEF domain which binds c-di-GMP

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
diguan_SiaD super family cl45718
biofilm regulation diguanylate cyclase SiaD;
2-217 2.91e-128

biofilm regulation diguanylate cyclase SiaD;


The actual alignment was detected with superfamily member NF038266:

Pssm-ID: 468439 [Multi-domain]  Cd Length: 252  Bit Score: 362.38  E-value: 2.91e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686965737   2 RLERIARISDGFQSMAREQNLSLSERYHKQLRRLEKVARISDRYQQMMRDLNLALKEASIRDPLTGLPNRRMLLERLREE 81
Cdd:NF038266   36 RLERLTRISDGYQSAARERELSLAERYDRQLRRLEKIVRISDRYQRMMRDLNEALREASTRDPLTGLPNRRLLMERLREE 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686965737  82 NERSQRHGQSYVLAMLDVDFFKQVNDTWGHDSGDRVLVEIARAMESELREYDLCGRWGGEEFLLLLPQTRLQDAGPVLER 161
Cdd:NF038266  116 VERARRSGRPFTLAMLDVDHFKRINDRYGHEVGDRVLVEIARTLRAELREYDLCGRWGGEEFLLLLPETGLEEAQVVLER 195

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1686965737 162 VRDSVRTLAVRVGTEALSVTASVGVTEHRIGET-YSQTVNRADAALLDAKRSGRDKC 217
Cdd:NF038266  196 LREAVRALAVRVGDDVLSVTASAGLAEHRPPEEgLSATLSRADQALYQAKRAGRDRV 252
 
Name Accession Description Interval E-value
diguan_SiaD NF038266
biofilm regulation diguanylate cyclase SiaD;
2-217 2.91e-128

biofilm regulation diguanylate cyclase SiaD;


Pssm-ID: 468439 [Multi-domain]  Cd Length: 252  Bit Score: 362.38  E-value: 2.91e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686965737   2 RLERIARISDGFQSMAREQNLSLSERYHKQLRRLEKVARISDRYQQMMRDLNLALKEASIRDPLTGLPNRRMLLERLREE 81
Cdd:NF038266   36 RLERLTRISDGYQSAARERELSLAERYDRQLRRLEKIVRISDRYQRMMRDLNEALREASTRDPLTGLPNRRLLMERLREE 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686965737  82 NERSQRHGQSYVLAMLDVDFFKQVNDTWGHDSGDRVLVEIARAMESELREYDLCGRWGGEEFLLLLPQTRLQDAGPVLER 161
Cdd:NF038266  116 VERARRSGRPFTLAMLDVDHFKRINDRYGHEVGDRVLVEIARTLRAELREYDLCGRWGGEEFLLLLPETGLEEAQVVLER 195

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1686965737 162 VRDSVRTLAVRVGTEALSVTASVGVTEHRIGET-YSQTVNRADAALLDAKRSGRDKC 217
Cdd:NF038266  196 LREAVRALAVRVGDDVLSVTASAGLAEHRPPEEgLSATLSRADQALYQAKRAGRDRV 252
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 62-218 1.86e-62

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: 192.39  E-value: 1.86e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686965737  62 RDPLTGLPNRRMLLERLREENERSQRHGQSYVLAMLDVDFFKQVNDTWGHDSGDRVLVEIARAMESELREYDLCGRWGGE 141
Cdd:cd01949     2 TDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGD 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1686965737 142 EFLLLLPQTRLQDAGPVLERVRDSVRTLAVRVGTEaLSVTASVGVTE-HRIGETYSQTVNRADAALLDAKRSGRDKCV 218
Cdd:cd01949    82 EFAILLPGTDLEEAEALAERLREAIEEPFFIDGQE-IRVTASIGIATyPEDGEDAEELLRRADEALYRAKRSGRNRVV 158
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 2-220 4.36e-61

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: 192.89  E-value: 4.36e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686965737   2 RLERIARISDGFQSMAREQNLSLSERYHKQLRRLEKVARISDRYQQMMRdlnlaLKEASIRDPLTGLPNRRMLLERLREE 81
Cdd:COG2199    61 VLLLLALGLLLLALLLLSLVLELLLLLLALLLLLLALEDITELRRLEER-----LRRLATHDPLTGLPNRRAFEERLERE 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686965737  82 NERSQRHGQSYVLAMLDVDFFKQVNDTWGHDSGDRVLVEIARAMESELREYDLCGRWGGEEFLLLLPQTRLQDAGPVLER 161
Cdd:COG2199   136 LARARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAER 215

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686965737 162 VRDSVRTLAVRVGTEALSVTASVGVTE-HRIGETYSQTVNRADAALLDAKRSGRDKCVFA 220
Cdd:COG2199   216 LREALEQLPFELEGKELRVTVSIGVALyPEDGDSAEELLRRADLALYRAKRAGRNRVVVY 275
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 60-216 5.85e-56

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: 175.90  E-value: 5.85e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686965737  60 SIRDPLTGLPNRRMLLERLREENERSQRHGQSYVLAMLDVDFFKQVNDTWGHDSGDRVLVEIARAMESELREYDLCGRWG 139
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686965737 140 GEEFLLLLPQTRLQDAGPVLERVRDSVRTLA--VRVGTEALSVTASVGVTEHRI-GETYSQTVNRADAALLDAKRSGRDK 216
Cdd:pfam00990  81 GDEFAILLPETSLEGAQELAERIRRLLAKLKipHTVSGLPLYVTISIGIAAYPNdGEDPEDLLKRADTALYQAKQAGRNR 160
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 58-220 4.28e-53

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 168.58  E-value: 4.28e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686965737   58 EASIRDPLTGLPNRRMLLERLREENERSQRHGQSYVLAMLDVDFFKQVNDTWGHDSGDRVLVEIARAMESELREYDLCGR 137
Cdd:smart00267   1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686965737  138 WGGEEFLLLLPQTRLQDAGPVLERVRDSVRTLAVrVGTEALSVTASVGVTEHRI-GETYSQTVNRADAALLDAKRSGRDK 216
Cdd:smart00267  81 LGGDEFALLLPETSLEEAIALAERILQQLREPII-IHGIPLYLTISIGVAAYPNpGEDAEDLLKRADTALYQAKKAGRNQ 159


                   ....
gi 1686965737  217 CVFA 220
Cdd:smart00267 160 VAVY 163
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 60-221 2.08e-51

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: 164.43  E-value: 2.08e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686965737  60 SIRDPLTGLPNRRMLLERLREENERSQRHGQSYVLAMLDVDFFKQVNDTWGHDSGDRVLVEIARAMESELREYDLCGRWG 139
Cdd:TIGR00254   2 AVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686965737 140 GEEFLLLLPQTRLQDAGPVLERVRDSVRTLAVRV-GTEALSVTASVGVT---EHriGETYSQTVNRADAALLDAKRSGRD 215
Cdd:TIGR00254  82 GEEFVVILPGTPLEDALSKAERLRDAINSKPIEVaGSETLTVTVSIGVAcypGH--GLTLEELLKRADEALYQAKKAGRN 159


                  ....*.
gi 1686965737 216 KCVFAA 221
Cdd:TIGR00254 160 RVVVAD 165
PRK09894 PRK09894
diguanylate cyclase; Provisional
 59-220 4.57e-50

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 165.24  E-value: 4.57e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686965737  59 ASIRDPLTGLPNRRMLLERLreENERSQRHGQSYVLAMLDVDFFKQVNDTWGHDSGDRVLVEIARAMESELREYDLCGRW 138
Cdd:PRK09894  128 RSNMDVLTGLPGRRVLDESF--DHQLRNREPQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRY 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686965737 139 GGEEFLLLLPQTRLQDAGPVLERVRDSVRTLAVRVGTEALSVTASVGVTEHRIGETYSQTVNRADAALLDAKRSGRDKCV 218
Cdd:PRK09894  206 GGEEFIICLKAATDEEACRAGERIRQLIANHAITHSDGRINITATFGVSRAFPEETLDVVIGRADRAMYEGKQTGRNRVM 285


                  ..
gi 1686965737 219 FA 220
Cdd:PRK09894  286 FI 287
diguan_DgcJ NF040885
diguanylate cyclase DgcJ;
46-214 1.65e-21

diguanylate cyclase DgcJ;


Pssm-ID: 468821 [Multi-domain]  Cd Length: 490  Bit Score: 92.33  E-value: 1.65e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686965737  46 QQMMRDLNLAlKEaSIRDPLTGLPNRRMLLERLREENERSQRHGQSYVLAMLDVDFFKQVNDTWGHDSGDRVLVEIARAM 125
Cdd:NF040885  329 MHFRLYHNVS-RE-NISDSMTGLYNRKILTPTLEQRLQRLTEKGIPVTFIALDCDKLKHINDTLGHHEGDRAITLLAQAI 406

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686965737 126 ESELREYDLCGRWGGEEFLLLLPQTRLQDAGPVLERVRDSVRTLAvrvgTEALsVTASVGVTEHRIGETYSQTVNRADAA 205
Cdd:NF040885  407 SASIRKSDYGIRLGGDEFCIILIDYEEAEAQNLIERIRQHLRTID----PDKR-VSFSWGAYQMQPGDTLDDAYKAADER 481


                  ....*....
gi 1686965737 206 LLDAKRSGR 214
Cdd:NF040885  482 LYLNKKQKH 490
 
Name Accession Description Interval E-value
diguan_SiaD NF038266
biofilm regulation diguanylate cyclase SiaD;
2-217 2.91e-128

biofilm regulation diguanylate cyclase SiaD;


Pssm-ID: 468439 [Multi-domain]  Cd Length: 252  Bit Score: 362.38  E-value: 2.91e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686965737   2 RLERIARISDGFQSMAREQNLSLSERYHKQLRRLEKVARISDRYQQMMRDLNLALKEASIRDPLTGLPNRRMLLERLREE 81
Cdd:NF038266   36 RLERLTRISDGYQSAARERELSLAERYDRQLRRLEKIVRISDRYQRMMRDLNEALREASTRDPLTGLPNRRLLMERLREE 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686965737  82 NERSQRHGQSYVLAMLDVDFFKQVNDTWGHDSGDRVLVEIARAMESELREYDLCGRWGGEEFLLLLPQTRLQDAGPVLER 161
Cdd:NF038266  116 VERARRSGRPFTLAMLDVDHFKRINDRYGHEVGDRVLVEIARTLRAELREYDLCGRWGGEEFLLLLPETGLEEAQVVLER 195

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1686965737 162 VRDSVRTLAVRVGTEALSVTASVGVTEHRIGET-YSQTVNRADAALLDAKRSGRDKC 217
Cdd:NF038266  196 LREAVRALAVRVGDDVLSVTASAGLAEHRPPEEgLSATLSRADQALYQAKRAGRDRV 252
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 62-218 1.86e-62

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: 192.39  E-value: 1.86e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686965737  62 RDPLTGLPNRRMLLERLREENERSQRHGQSYVLAMLDVDFFKQVNDTWGHDSGDRVLVEIARAMESELREYDLCGRWGGE 141
Cdd:cd01949     2 TDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGD 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1686965737 142 EFLLLLPQTRLQDAGPVLERVRDSVRTLAVRVGTEaLSVTASVGVTE-HRIGETYSQTVNRADAALLDAKRSGRDKCV 218
Cdd:cd01949    82 EFAILLPGTDLEEAEALAERLREAIEEPFFIDGQE-IRVTASIGIATyPEDGEDAEELLRRADEALYRAKRSGRNRVV 158
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 2-220 4.36e-61

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: 192.89  E-value: 4.36e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686965737   2 RLERIARISDGFQSMAREQNLSLSERYHKQLRRLEKVARISDRYQQMMRdlnlaLKEASIRDPLTGLPNRRMLLERLREE 81
Cdd:COG2199    61 VLLLLALGLLLLALLLLSLVLELLLLLLALLLLLLALEDITELRRLEER-----LRRLATHDPLTGLPNRRAFEERLERE 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686965737  82 NERSQRHGQSYVLAMLDVDFFKQVNDTWGHDSGDRVLVEIARAMESELREYDLCGRWGGEEFLLLLPQTRLQDAGPVLER 161
Cdd:COG2199   136 LARARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAER 215

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686965737 162 VRDSVRTLAVRVGTEALSVTASVGVTE-HRIGETYSQTVNRADAALLDAKRSGRDKCVFA 220
Cdd:COG2199   216 LREALEQLPFELEGKELRVTVSIGVALyPEDGDSAEELLRRADLALYRAKRAGRNRVVVY 275
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 60-216 5.85e-56

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: 175.90  E-value: 5.85e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686965737  60 SIRDPLTGLPNRRMLLERLREENERSQRHGQSYVLAMLDVDFFKQVNDTWGHDSGDRVLVEIARAMESELREYDLCGRWG 139
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686965737 140 GEEFLLLLPQTRLQDAGPVLERVRDSVRTLA--VRVGTEALSVTASVGVTEHRI-GETYSQTVNRADAALLDAKRSGRDK 216
Cdd:pfam00990  81 GDEFAILLPETSLEGAQELAERIRRLLAKLKipHTVSGLPLYVTISIGIAAYPNdGEDPEDLLKRADTALYQAKQAGRNR 160
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 58-220 4.28e-53

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 168.58  E-value: 4.28e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686965737   58 EASIRDPLTGLPNRRMLLERLREENERSQRHGQSYVLAMLDVDFFKQVNDTWGHDSGDRVLVEIARAMESELREYDLCGR 137
Cdd:smart00267   1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686965737  138 WGGEEFLLLLPQTRLQDAGPVLERVRDSVRTLAVrVGTEALSVTASVGVTEHRI-GETYSQTVNRADAALLDAKRSGRDK 216
Cdd:smart00267  81 LGGDEFALLLPETSLEEAIALAERILQQLREPII-IHGIPLYLTISIGVAAYPNpGEDAEDLLKRADTALYQAKKAGRNQ 159


                   ....
gi 1686965737  217 CVFA 220
Cdd:smart00267 160 VAVY 163
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 60-221 2.08e-51

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: 164.43  E-value: 2.08e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686965737  60 SIRDPLTGLPNRRMLLERLREENERSQRHGQSYVLAMLDVDFFKQVNDTWGHDSGDRVLVEIARAMESELREYDLCGRWG 139
Cdd:TIGR00254   2 AVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686965737 140 GEEFLLLLPQTRLQDAGPVLERVRDSVRTLAVRV-GTEALSVTASVGVT---EHriGETYSQTVNRADAALLDAKRSGRD 215
Cdd:TIGR00254  82 GEEFVVILPGTPLEDALSKAERLRDAINSKPIEVaGSETLTVTVSIGVAcypGH--GLTLEELLKRADEALYQAKKAGRN 159


                  ....*.
gi 1686965737 216 KCVFAA 221
Cdd:TIGR00254 160 RVVVAD 165
PRK09894 PRK09894
diguanylate cyclase; Provisional
 59-220 4.57e-50

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 165.24  E-value: 4.57e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686965737  59 ASIRDPLTGLPNRRMLLERLreENERSQRHGQSYVLAMLDVDFFKQVNDTWGHDSGDRVLVEIARAMESELREYDLCGRW 138
Cdd:PRK09894  128 RSNMDVLTGLPGRRVLDESF--DHQLRNREPQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRY 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686965737 139 GGEEFLLLLPQTRLQDAGPVLERVRDSVRTLAVRVGTEALSVTASVGVTEHRIGETYSQTVNRADAALLDAKRSGRDKCV 218
Cdd:PRK09894  206 GGEEFIICLKAATDEEACRAGERIRQLIANHAITHSDGRINITATFGVSRAFPEETLDVVIGRADRAMYEGKQTGRNRVM 285


                  ..
gi 1686965737 219 FA 220
Cdd:PRK09894  286 FI 287
pleD PRK09581
response regulator PleD; Reviewed
 24-221 8.28e-45

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 155.44  E-value: 8.28e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686965737  24 LSERYHKQLRRlekvarisDRYQQMMRDlNLALK-EASIRDPLTGLPNRRMLLERLREENERSQRHGQSYVLAMLDVDFF 102
Cdd:PRK09581  264 LLARVRTQIRR--------KRYQDALRN-NLEQSiEMAVTDGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHF 334

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686965737 103 KQVNDTWGHDSGDRVLVEIARAMESELREYDLCGRWGGEEFLLLLPQTRLQDAGPVLERVRDSVRTLAVRV--GTEALSV 180
Cdd:PRK09581  335 KKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARYGGEEFVVVMPDTDIEDAIAVAERIRRKIAEEPFIIsdGKERLNV 414

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1686965737 181 TASVGVTEHR-IGETYSQTVNRADAALLDAKRSGRDKCVFAA 221
Cdd:PRK09581  415 TVSIGVAELRpSGDTIEALIKRADKALYEAKNTGRNRVVALA 456
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 2-219 4.04e-43

Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain [Signal transduction mechanisms];


Pssm-ID: 444025 [Multi-domain]  Cd Length: 678  Bit Score: 154.16  E-value: 4.04e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686965737   2 RLERIARISDGFQSMAREQNLSLSERYHKQLRRLEKVARISDRYQQMMRDLNLALkeasiRDPLTGLPNRRMLLERLREE 81
Cdd:COG5001   198 LLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEERLRHLAY-----HDPLTGLPNRRLFLDRLEQA 272

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686965737  82 NERSQRHGQSYVLAMLDVDFFKQVNDTWGHDSGDRVLVEIARAMESELREYDLCGRWGGEEFLLLLPQTR-LQDAGPVLE 160
Cdd:COG5001   273 LARARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVLLPDLDdPEDAEAVAE 352

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1686965737 161 RVRDSVRTlAVRVGTEALSVTASVGVT---EHriGETYSQTVNRADAALLDAKRSGRDKCVF 219
Cdd:COG5001   353 RILAALAE-PFELDGHELYVSASIGIAlypDD--GADAEELLRNADLAMYRAKAAGRNRYRF 411
PRK15426 PRK15426
cellulose biosynthesis regulator YedQ;
55-230 1.11e-39

cellulose biosynthesis regulator YedQ;


Pssm-ID: 237964 [Multi-domain]  Cd Length: 570  Bit Score: 143.62  E-value: 1.11e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686965737  55 ALKEASIRDPLTGLPNRRMLLERLREENERSQRHGQSYVLAMLDVDFFKQVNDTWGHDSGDRVLVEIARAMESELREYDL 134
Cdd:PRK15426  393 SLQWQAWHDPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDV 472

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686965737 135 CGRWGGEEFLLLLPQTRLQDAGPVLERVRDSVRTLAVRVG-TEALSVTASVGVTEHRIGETYS--QTVNRADAALLDAKR 211
Cdd:PRK15426  473 AGRVGGEEFCVVLPGASLAEAAQVAERIRLRINEKEILVAkSTTIRISASLGVSSAEEDGDYDfeQLQSLADRRLYLAKQ 552

                         170
                  ....*....|....*....
gi 1686965737 212 SGRDKcVFAALPPLPAPSR 230
Cdd:PRK15426  553 AGRNR-VCASDNAHEREVK 570
adrA PRK10245
diguanylate cyclase AdrA; Provisional
 56-221 2.70e-26

diguanylate cyclase AdrA; Provisional


Pssm-ID: 182329 [Multi-domain]  Cd Length: 366  Bit Score: 104.53  E-value: 2.70e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686965737  56 LKEASIRDPLTGLPNRRMLLERLREENERSQRHGQSYVLAMLDVDFFKQVNDTWGHDSGDRVLVEIARAMESELREYDLC 135
Cdd:PRK10245  201 LQVMSTRDGMTGVYNRRHWETLLRNEFDNCRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSDVI 280

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686965737 136 GRWGGEEFLLLLPQTRLQDAGPVLERVRDSVRTLAVRvGTEALSVTASVGVT--EHRIGEtYSQTVNRADAALLDAKRSG 213
Cdd:PRK10245  281 GRFGGDEFAVIMSGTPAESAITAMSRVHEGLNTLRLP-NAPQVTLRISVGVAplNPQMSH-YREWLKSADLALYKAKNAG 358


                  ....*...
gi 1686965737 214 RDKCVFAA 221
Cdd:PRK10245  359 RNRTEVAA 366
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 48-214 1.51e-25

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 104.37  E-value: 1.51e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686965737   48 MMRDLNLAlkeASiRDPLTGLPNRRMLLERLREENERSQRHGQSYVLAMLDVDFFKQVNDTWGHDSGDRVLVEIARAMES 127
Cdd:PRK09776   657 MLRQLSYS---AS-HDALTHLANRASFEKQLRRLLQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLS 732

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686965737  128 ELREYDLCGRWGGEEFLLLLPQTRLQDAGPVLERVRDSVRTLAVRVGTEALSVTASVGVTEhrIGETYSQT---VNRADA 204
Cdd:PRK09776   733 MLRSSDVLARLGGDEFGLLLPDCNVESARFIATRIISAINDYHFPWEGRVYRVGASAGITL--IDANNHQAsevMSQADI 810

                          170
                   ....*....|
gi 1686965737  205 ALLDAKRSGR 214
Cdd:PRK09776   811 ACYAAKNAGR 820
diguan_DgcJ NF040885
diguanylate cyclase DgcJ;
46-214 1.65e-21

diguanylate cyclase DgcJ;


Pssm-ID: 468821 [Multi-domain]  Cd Length: 490  Bit Score: 92.33  E-value: 1.65e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686965737  46 QQMMRDLNLAlKEaSIRDPLTGLPNRRMLLERLREENERSQRHGQSYVLAMLDVDFFKQVNDTWGHDSGDRVLVEIARAM 125
Cdd:NF040885  329 MHFRLYHNVS-RE-NISDSMTGLYNRKILTPTLEQRLQRLTEKGIPVTFIALDCDKLKHINDTLGHHEGDRAITLLAQAI 406

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686965737 126 ESELREYDLCGRWGGEEFLLLLPQTRLQDAGPVLERVRDSVRTLAvrvgTEALsVTASVGVTEHRIGETYSQTVNRADAA 205
Cdd:NF040885  407 SASIRKSDYGIRLGGDEFCIILIDYEEAEAQNLIERIRQHLRTID----PDKR-VSFSWGAYQMQPGDTLDDAYKAADER 481


                  ....*....
gi 1686965737 206 LLDAKRSGR 214
Cdd:NF040885  482 LYLNKKQKH 490
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
56-220 2.67e-20

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 88.97  E-value: 2.67e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686965737  56 LKEASIRDPLTGLPNRRMLLERLREENErsQRHGQSYVLAMLDVDFFKQVNDTWGHDSGDRVLVEIARAMESELREYDLC 135
Cdd:PRK10060  233 LRILANTDSITGLPNRNAIQELIDHAIN--AADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQTL 310

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686965737 136 GRWGGEEFLLLLPQTR---LQD-AGPVLERVRDSVRTLAVRVGTealsvTASVGVT---EHriGETYSQTVNRADAALLD 208
Cdd:PRK10060  311 ARLGGDEFLVLASHTSqaaLEAmASRILTRLRLPFRIGLIEVYT-----GCSIGIAlapEH--GDDSESLIRSADTAMYT 383

                         170
                  ....*....|...
gi 1686965737 209 AKRSGRDK-CVFA 220
Cdd:PRK10060  384 AKEGGRGQfCVFS 396
PRK09966 PRK09966
diguanylate cyclase DgcN;
4-147 9.09e-15

diguanylate cyclase DgcN;


Pssm-ID: 182171 [Multi-domain]  Cd Length: 407  Bit Score: 72.73  E-value: 9.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686965737   4 ERIARisdgFQSMAREQNLSLSERYHKQLRRLEKVArisdryqQMMRdlnlalkeASIRDPLTGLPNRRMLLERLRE-EN 82
Cdd:PRK09966  211 ERIAE----FHRFALDFNSLLDEMEEWQLRLQAKNA-------QLLR--------TALHDPLTGLANRAAFRSGINTlMN 271

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1686965737  83 ERSQRhgQSYVLAMLDVDFFKQVNDTWGHDSGDRVLVEIARAME----SELREYdlcgRWGGEEFLLLL 147
Cdd:PRK09966  272 NSDAR--KTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAefggLRHKAY----RLGGDEFAMVL 334
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 63-213 4.62e-14

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 70.95  E-value: 4.62e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686965737  63 DPLTGLPNRRMLLERLREenerSQRHGQSYVLAMLDVDFFKQVNDTWGHDSGDRVLVEIARAMESELREYDLCGRWGGEE 142
Cdd:PRK11359  379 DPLTGLPNRNNLHNYLDD----LVDKAVSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGTQ 454

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1686965737 143 FLLLLPQTRLQDAGPVLERVRdSVRTLAVRVGTEALSVTASVGVTeHRIGETYSQTVNRADAALLDAKRSG 213
Cdd:PRK11359  455 FVLVSLENDVSNITQIADELR-NVVSKPIMIDDKPFPLTLSIGIS-YDVGKNRDYLLSTAHNAMDYIRKNG 523
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
 94-210 1.19e-13

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


Pssm-ID: 143637 [Multi-domain]  Cd Length: 133  Bit Score: 65.46  E-value: 1.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686965737  94 LAMLDVDFFKQVNDTWGHDSGDRVLVEIARAMESELREY-DLCGRWGGEEFLLLLPQTRLQDAGPVLERVRDSVRTLA-- 170
Cdd:cd07556     4 ILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSgDLKIKTIGDEFMVVSGLDHPAAAVAFAEDMREAVSALNqs 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1686965737 171 ------VRVGTEALSVTASVGVTEHRIGeTYSQTVNRADAALLDAK 210
Cdd:cd07556    84 egnpvrVRIGIHTGPVVVGVIGSRPQYD-VWGALVNLASRMESQAK 128
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 133-210 2.20e-10

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: 57.61  E-value: 2.20e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1686965737 133 DLCGRWGGEEFLLLLPQTRLQDAGPVLERVRDSVRTLavrvgtEALSVTASVGVTEHRIgetysqtVNRADaALLDAK 210
Cdd:COG3706   116 DLVARYGGEEFAILLPGTDLEGALAVAERIREAVAEL------PSLRVTVSIGVAGDSL-------LKRAD-ALYQAR 179
PRK11829 PRK11829
biofilm formation regulator HmsP; Provisional
 13-219 4.81e-08

biofilm formation regulator HmsP; Provisional


Pssm-ID: 183329 [Multi-domain]  Cd Length: 660  Bit Score: 53.02  E-value: 4.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686965737  13 FQSMARE-QNLSLSERYHKQL--------RRLEKVARISDRYQQMMRDLNLALKEASIRDPLTGLPNRRMLLERLREENE 83
Cdd:PRK11829  176 LRAMAKElEDIGDHGVLHHQLtlpahhqdDELGVLVRNYNRNQQLLADAYADMGRISHRFPVTELPNRSLFISLLEKEIA 255

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686965737  84 RSQRHGQSYVLaMLDVDFFKQVNDTWGHDSGDRVLVEIARAMESELREYDLCGRWGGEEFLLLLPQT-RLQDAGPVLERV 162
Cdd:PRK11829  256 SSTRTDHFHLL-VIGIETLQEVSGAMSEAQHQQLLLTIVQRIEQCIDDSDLLAQLSKTEFAVLARGTrRSFPAMQLARRI 334

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1686965737 163 RdSVRTLAVRVGTEALSVTASVGVTEHRIG-ETYSQTVNRADAALLDAKRSGRDKCVF 219
Cdd:PRK11829  335 M-SQVTQPLFFDEITLRPSASIGITRYQAQqDTAESMMRNASTAMMAAHHEGRNQIMV 391
PRK11059 PRK11059
regulatory protein CsrD; Provisional
 4-206 3.16e-07

regulatory protein CsrD; Provisional


Pssm-ID: 236833 [Multi-domain]  Cd Length: 640  Bit Score: 50.63  E-value: 3.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686965737   4 ERIARISDGfqsmAREQNLSLSERyhkqlrrlEKVARISDRYQQMMRDLNLALKEAS-----IR-----DPLTGLPNRRM 73
Cdd:PRK11059  174 ERARRILNG----EREQAVAGSGY--------EWPRTASRALDHLLSELQDAREERSrfdtfIRsnafqDAKTGLGNRLF 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686965737  74 L---LERLREENERSQRHGqsyVLAMLDVDFFKQVNDTWGHDSGDRVLVEIARAMESELREYD--LCGRWGGEEFLLLLP 148
Cdd:PRK11059  242 FdnqLATLLEDQEMVGAHG---VVMLIRLPDFDLLQEEWGESQVEELLFELINLLSTFVMRYPgaLLARYSRSDFAVLLP 318

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1686965737 149 QTRLQDAgpvlervrDSVRTLAVRVgTEALSVTASV--------GVTEHRIGETYSQTVNRADAAL 206
Cdd:PRK11059  319 HRSLKEA--------DSLASQLLKA-VDALPPPKMLdrddflhiGICAYRSGQSTEQVMEEAEMAL 375
PRK13561 PRK13561
putative diguanylate cyclase; Provisional
 16-219 1.30e-04

putative diguanylate cyclase; Provisional


Pssm-ID: 184143 [Multi-domain]  Cd Length: 651  Bit Score: 42.39  E-value: 1.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686965737  16 MARE-QNLSLSERYHKQLR--RLEK------VARISDRYQQMMRDLNLALKEASIRDPLTGLPNRRMLLERLreenERSQ 86
Cdd:PRK13561  178 IARElNDIPPQELVGHQLAlpRLHQddeigmLVRSYNLNQQLLQRQYEEQSRNATRFPVSDLPNKALLMALL----EQVV 253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686965737  87 RHGQSYVLAMLDVDFFKQVNDTWGHDSGDRVLVEIARAMESELREYDLCGRWGGEEFLLLL-----PQTRLQDAGPVLER 161
Cdd:PRK13561  254 ARKQTTALMIITCETLRDTAGVLKEAQREILLLTLVEKLKSVLSPRMVLAQISGYDFAIIAngvkePWHAITLGQQVLTI 333

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1686965737 162 VRDSVRTLAVrvgteALSVTASVGVTEHRIGETYSQTVNRADAALLDAKRSGRDKCVF 219
Cdd:PRK13561  334 INERLPIQRI-----QLRPSCSIGIAMFYGDLTAEQLYSRAISAAFTARRKGKNQIQF 386
 
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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