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Conserved domains on  [gi|1675083031|ref|WP_138599888|]
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MULTISPECIES: GGDEF domain-containing protein [unclassified Pseudoalteromonas]

Protein Classification

GGDEF domain-containing protein( domain architecture ID 10005578)

GGDEF domain-containing protein may have diguanylate cyclase (DGC) activity, similar to Escherichia coli DgcT (YcdT) and to E. coli CdgI (YeaI), a c-di-GMP-binding effector with a degenerate GGDEF domain which binds c-di-GMP

CATH:  3.30.70.270
EC:  2.7.7.65
Gene Ontology:  GO:0005525|GO:0046872|GO:0052621|GO:0005886
PubMed:  11119645|15063857|15289546|15306016|16530465|16045609

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 ...
 11-254 3.43e-65

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: 204.06  E-value: 3.43e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675083031  11 LMDYREREKSRWLRMLFITVISIAISLLITFLILLATGTEMMPIIFIIATIAPAVTAPIVSWSISGLMIKVQKLEETHRK 90
Cdd:COG2199    33 LLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLLLLALEDITELRRLEERLRR 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675083031  91 LAMYDHLTGLLSRREFLAQGNELLQMCQSNNQPVVFAYLDLDHFKKINDTYGHAAGDEVLVSFANLVKKTLRQEDLLGRL 170
Cdd:COG2199   113 LATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDLVARL 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675083031 171 GGEEFALILVNTRVVEAKQKLELLRKSVAKMTINYAEQPLKITVSLGVADWDrPHKENLISLMKRADNALYSAKSSGRNQ 250
Cdd:COG2199   193 GGDEFAVLLPGTDLEEAEALAERLREALEQLPFELEGKELRVTVSIGVALYP-EDGDSAEELLRRADLALYRAKRAGRNR 271


                  ....
gi 1675083031 251 LAFA 254
Cdd:COG2199   272 VVVY 275
 
Name Accession Description Interval E-value
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 11-254 3.43e-65

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: 204.06  E-value: 3.43e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675083031  11 LMDYREREKSRWLRMLFITVISIAISLLITFLILLATGTEMMPIIFIIATIAPAVTAPIVSWSISGLMIKVQKLEETHRK 90
Cdd:COG2199    33 LLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLLLLALEDITELRRLEERLRR 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675083031  91 LAMYDHLTGLLSRREFLAQGNELLQMCQSNNQPVVFAYLDLDHFKKINDTYGHAAGDEVLVSFANLVKKTLRQEDLLGRL 170
Cdd:COG2199   113 LATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDLVARL 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675083031 171 GGEEFALILVNTRVVEAKQKLELLRKSVAKMTINYAEQPLKITVSLGVADWDrPHKENLISLMKRADNALYSAKSSGRNQ 250
Cdd:COG2199   193 GGDEFAVLLPGTDLEEAEALAERLREALEQLPFELEGKELRVTVSIGVALYP-EDGDSAEELLRRADLALYRAKRAGRNR 271


                  ....
gi 1675083031 251 LAFA 254
Cdd:COG2199   272 VVVY 275
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 93-250 5.13e-63

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: 194.31  E-value: 5.13e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675083031  93 MYDHLTGLLSRREFLAQGNELLQMCQSNNQPVVFAYLDLDHFKKINDTYGHAAGDEVLVSFANLVKKTLRQEDLLGRLGG 172
Cdd:cd01949     1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1675083031 173 EEFALILVNTRVVEAKQKLELLRKSVAKMTINYaEQPLKITVSLGVADWDrPHKENLISLMKRADNALYSAKSSGRNQ 250
Cdd:cd01949    81 DEFAILLPGTDLEEAEALAERLREAIEEPFFID-GQEIRVTASIGIATYP-EDGEDAEELLRRADEALYRAKRSGRNR 156
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 92-250 2.46e-57

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: 180.14  E-value: 2.46e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675083031  92 AMYDHLTGLLSRREFLAQGNELLQMCQSNNQPVVFAYLDLDHFKKINDTYGHAAGDEVLVSFANLVKKTLRQEDLLGRLG 171
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675083031 172 GEEFALILVNTRVVEAKQKLELLRKSVAKMTI--NYAEQPLKITVSLGVADWDRPHkENLISLMKRADNALYSAKSSGRN 249
Cdd:pfam00990  81 GDEFAILLPETSLEGAQELAERIRRLLAKLKIphTVSGLPLYVTISIGIAAYPNDG-EDPEDLLKRADTALYQAKQAGRN 159


                  .
gi 1675083031 250 Q 250
Cdd:pfam00990 160 R 160
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 90-254 1.71e-56

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 178.21  E-value: 1.71e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675083031   90 KLAMYDHLTGLLSRREFLAQGNELLQMCQSNNQPVVFAYLDLDHFKKINDTYGHAAGDEVLVSFANLVKKTLRQEDLLGR 169
Cdd:smart00267   1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675083031  170 LGGEEFALILVNTRVVEAKQKLELLRKSVAKMTINyAEQPLKITVSLGVADWDRPHkENLISLMKRADNALYSAKSSGRN 249
Cdd:smart00267  81 LGGDEFALLLPETSLEEAIALAERILQQLREPIII-HGIPLYLTISIGVAAYPNPG-EDAEDLLKRADTALYQAKKAGRN 158


                   ....*
gi 1675083031  250 QLAFA 254
Cdd:smart00267 159 QVAVY 163
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 91-249 1.30e-47

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: 155.57  E-value: 1.30e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675083031  91 LAMYDHLTGLLSRREFLAQGNELLQMCQSNNQPVVFAYLDLDHFKKINDTYGHAAGDEVLVSFANLVKKTLRQEDLLGRL 170
Cdd:TIGR00254   1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675083031 171 GGEEFALILVNTRVVEAKQKLELLRKSVAKMTINYAEQP-LKITVSLGVADWdRPHKENLISLMKRADNALYSAKSSGRN 249
Cdd:TIGR00254  81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSEtLTVTVSIGVACY-PGHGLTLEELLKRADEALYQAKKAGRN 159
pleD PRK09581
response regulator PleD; Reviewed
 90-250 1.07e-43

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 153.52  E-value: 1.07e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675083031  90 KLAMYDHLTGLLSRREFLAQGNELLQMCQSNNQPVVFAYLDLDHFKKINDTYGHAAGDEVLVSFANLVKKTLRQEDLLGR 169
Cdd:PRK09581  290 EMAVTDGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIAR 369

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675083031 170 LGGEEFALILVNTRVVEAKQKLELLRKSVAKM--TINYAEQPLKITVSLGVADWdRPHKENLISLMKRADNALYSAKSSG 247
Cdd:PRK09581  370 YGGEEFVVVMPDTDIEDAIAVAERIRRKIAEEpfIISDGKERLNVTVSIGVAEL-RPSGDTIEALIKRADKALYEAKNTG 448


                  ...
gi 1675083031 248 RNQ 250
Cdd:PRK09581  449 RNR 451
diguan_SiaD NF038266
biofilm regulation diguanylate cyclase SiaD;
84-251 1.15e-43

biofilm regulation diguanylate cyclase SiaD;


Pssm-ID: 468439 [Multi-domain]  Cd Length: 252  Bit Score: 148.21  E-value: 1.15e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675083031  84 LEETHRKLAMYDHLTGLLSRREFLAQGNELLQMCQSNNQPVVFAYLDLDHFKKINDTYGHAAGDEVLVSFANLVKKTLRQ 163
Cdd:NF038266   86 LNEALREASTRDPLTGLPNRRLLMERLREEVERARRSGRPFTLAMLDVDHFKRINDRYGHEVGDRVLVEIARTLRAELRE 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675083031 164 EDLLGRLGGEEFALILVNTRVVEAKQKLELLRKSVAKMTINYAEQPLKITVSLGVADWDRPhKENLISLMKRADNALYSA 243
Cdd:NF038266  166 YDLCGRWGGEEFLLLLPETGLEEAQVVLERLREAVRALAVRVGDDVLSVTASAGLAEHRPP-EEGLSATLSRADQALYQA 244


                  ....*...
gi 1675083031 244 KSSGRNQL 251
Cdd:NF038266  245 KRAGRDRV 252
 
Name Accession Description Interval E-value
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 11-254 3.43e-65

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: 204.06  E-value: 3.43e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675083031  11 LMDYREREKSRWLRMLFITVISIAISLLITFLILLATGTEMMPIIFIIATIAPAVTAPIVSWSISGLMIKVQKLEETHRK 90
Cdd:COG2199    33 LLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLLLLALEDITELRRLEERLRR 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675083031  91 LAMYDHLTGLLSRREFLAQGNELLQMCQSNNQPVVFAYLDLDHFKKINDTYGHAAGDEVLVSFANLVKKTLRQEDLLGRL 170
Cdd:COG2199   113 LATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDLVARL 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675083031 171 GGEEFALILVNTRVVEAKQKLELLRKSVAKMTINYAEQPLKITVSLGVADWDrPHKENLISLMKRADNALYSAKSSGRNQ 250
Cdd:COG2199   193 GGDEFAVLLPGTDLEEAEALAERLREALEQLPFELEGKELRVTVSIGVALYP-EDGDSAEELLRRADLALYRAKRAGRNR 271


                  ....
gi 1675083031 251 LAFA 254
Cdd:COG2199   272 VVVY 275
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 93-250 5.13e-63

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: 194.31  E-value: 5.13e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675083031  93 MYDHLTGLLSRREFLAQGNELLQMCQSNNQPVVFAYLDLDHFKKINDTYGHAAGDEVLVSFANLVKKTLRQEDLLGRLGG 172
Cdd:cd01949     1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1675083031 173 EEFALILVNTRVVEAKQKLELLRKSVAKMTINYaEQPLKITVSLGVADWDrPHKENLISLMKRADNALYSAKSSGRNQ 250
Cdd:cd01949    81 DEFAILLPGTDLEEAEALAERLREAIEEPFFID-GQEIRVTASIGIATYP-EDGEDAEELLRRADEALYRAKRSGRNR 156
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 92-250 2.46e-57

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: 180.14  E-value: 2.46e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675083031  92 AMYDHLTGLLSRREFLAQGNELLQMCQSNNQPVVFAYLDLDHFKKINDTYGHAAGDEVLVSFANLVKKTLRQEDLLGRLG 171
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675083031 172 GEEFALILVNTRVVEAKQKLELLRKSVAKMTI--NYAEQPLKITVSLGVADWDRPHkENLISLMKRADNALYSAKSSGRN 249
Cdd:pfam00990  81 GDEFAILLPETSLEGAQELAERIRRLLAKLKIphTVSGLPLYVTISIGIAAYPNDG-EDPEDLLKRADTALYQAKQAGRN 159


                  .
gi 1675083031 250 Q 250
Cdd:pfam00990 160 R 160
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 90-254 1.71e-56

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 178.21  E-value: 1.71e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675083031   90 KLAMYDHLTGLLSRREFLAQGNELLQMCQSNNQPVVFAYLDLDHFKKINDTYGHAAGDEVLVSFANLVKKTLRQEDLLGR 169
Cdd:smart00267   1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675083031  170 LGGEEFALILVNTRVVEAKQKLELLRKSVAKMTINyAEQPLKITVSLGVADWDRPHkENLISLMKRADNALYSAKSSGRN 249
Cdd:smart00267  81 LGGDEFALLLPETSLEEAIALAERILQQLREPIII-HGIPLYLTISIGVAAYPNPG-EDAEDLLKRADTALYQAKKAGRN 158


                   ....*
gi 1675083031  250 QLAFA 254
Cdd:smart00267 159 QVAVY 163
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 91-249 1.30e-47

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: 155.57  E-value: 1.30e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675083031  91 LAMYDHLTGLLSRREFLAQGNELLQMCQSNNQPVVFAYLDLDHFKKINDTYGHAAGDEVLVSFANLVKKTLRQEDLLGRL 170
Cdd:TIGR00254   1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675083031 171 GGEEFALILVNTRVVEAKQKLELLRKSVAKMTINYAEQP-LKITVSLGVADWdRPHKENLISLMKRADNALYSAKSSGRN 249
Cdd:TIGR00254  81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSEtLTVTVSIGVACY-PGHGLTLEELLKRADEALYQAKKAGRN 159
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 3-253 6.77e-45

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: 159.94  E-value: 6.77e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675083031   3 RFYETERTLMDYREREKSRWLRMLFITVISIAISLLITFLILLATGTEMMPIIFIIATIAPAVTAPIVSWSISGLMIKVQ 82
Cdd:COG5001   161 LLALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITER 240

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675083031  83 K-LEETHRKLAMYDHLTGLLSRREFLAQGNELLQMCQSNNQPVVFAYLDLDHFKKINDTYGHAAGDEVLVSFANLVKKTL 161
Cdd:COG5001   241 KrAEERLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACL 320

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675083031 162 RQEDLLGRLGGEEFALILVNTR-VVEAKQKLELLRKSVAKmTINYAEQPLKITVSLGVADWDRpHKENLISLMKRADNAL 240
Cdd:COG5001   321 REGDTVARLGGDEFAVLLPDLDdPEDAEAVAERILAALAE-PFELDGHELYVSASIGIALYPD-DGADAEELLRNADLAM 398

                         250
                  ....*....|...
gi 1675083031 241 YSAKSSGRNQLAF 253
Cdd:COG5001   399 YRAKAAGRNRYRF 411
pleD PRK09581
response regulator PleD; Reviewed
 90-250 1.07e-43

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 153.52  E-value: 1.07e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675083031  90 KLAMYDHLTGLLSRREFLAQGNELLQMCQSNNQPVVFAYLDLDHFKKINDTYGHAAGDEVLVSFANLVKKTLRQEDLLGR 169
Cdd:PRK09581  290 EMAVTDGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIAR 369

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675083031 170 LGGEEFALILVNTRVVEAKQKLELLRKSVAKM--TINYAEQPLKITVSLGVADWdRPHKENLISLMKRADNALYSAKSSG 247
Cdd:PRK09581  370 YGGEEFVVVMPDTDIEDAIAVAERIRRKIAEEpfIISDGKERLNVTVSIGVAEL-RPSGDTIEALIKRADKALYEAKNTG 448


                  ...
gi 1675083031 248 RNQ 250
Cdd:PRK09581  449 RNR 451
diguan_SiaD NF038266
biofilm regulation diguanylate cyclase SiaD;
84-251 1.15e-43

biofilm regulation diguanylate cyclase SiaD;


Pssm-ID: 468439 [Multi-domain]  Cd Length: 252  Bit Score: 148.21  E-value: 1.15e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675083031  84 LEETHRKLAMYDHLTGLLSRREFLAQGNELLQMCQSNNQPVVFAYLDLDHFKKINDTYGHAAGDEVLVSFANLVKKTLRQ 163
Cdd:NF038266   86 LNEALREASTRDPLTGLPNRRLLMERLREEVERARRSGRPFTLAMLDVDHFKRINDRYGHEVGDRVLVEIARTLRAELRE 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675083031 164 EDLLGRLGGEEFALILVNTRVVEAKQKLELLRKSVAKMTINYAEQPLKITVSLGVADWDRPhKENLISLMKRADNALYSA 243
Cdd:NF038266  166 YDLCGRWGGEEFLLLLPETGLEEAQVVLERLREAVRALAVRVGDDVLSVTASAGLAEHRPP-EEGLSATLSRADQALYQA 244


                  ....*...
gi 1675083031 244 KSSGRNQL 251
Cdd:NF038266  245 KRAGRDRV 252
PRK15426 PRK15426
cellulose biosynthesis regulator YedQ;
69-250 2.46e-42

cellulose biosynthesis regulator YedQ;


Pssm-ID: 237964 [Multi-domain]  Cd Length: 570  Bit Score: 151.71  E-value: 2.46e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675083031  69 IVSWSISGLMIK-VQKLEETHRKLAMYDHLTGLLSRREFLAQGNELLQMCQSNNQPVVFAYLDLDHFKKINDTYGHAAGD 147
Cdd:PRK15426  374 LISWYVIRRMVSnMFVLQSSLQWQAWHDPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGD 453

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675083031 148 EVLVSFANLVKKTLRQEDLLGRLGGEEFALILVNTRVVEAKQKLELLRKSVAKMTINYA-EQPLKITVSLGVADWDRPHK 226
Cdd:PRK15426  454 RVLSHAAGLISSSLRAQDVAGRVGGEEFCVVLPGASLAEAAQVAERIRLRINEKEILVAkSTTIRISASLGVSSAEEDGD 533

                         170       180
                  ....*....|....*....|....
gi 1675083031 227 ENLISLMKRADNALYSAKSSGRNQ 250
Cdd:PRK15426  534 YDFEQLQSLADRRLYLAKQAGRNR 557
PRK09894 PRK09894
diguanylate cyclase; Provisional
 94-254 4.12e-36

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 129.80  E-value: 4.12e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675083031  94 YDHLTGLLSRREFLAQGNELLQMCQsnNQPVVFAYLDLDHFKKINDTYGHAAGDEVLVSFANLVKKTLRQEDLLGRLGGE 173
Cdd:PRK09894  131 MDVLTGLPGRRVLDESFDHQLRNRE--PQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGGE 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675083031 174 EFALILVNTRVVEAKQKLELLRKSVAKMTINYAEQPLKITVSLGVADWDRphKENLISLMKRADNALYSAKSSGRNQLAF 253
Cdd:PRK09894  209 EFIICLKAATDEEACRAGERIRQLIANHAITHSDGRINITATFGVSRAFP--EETLDVVIGRADRAMYEGKQTGRNRVMF 286


                  .
gi 1675083031 254 A 254
Cdd:PRK09894  287 I 287
adrA PRK10245
diguanylate cyclase AdrA; Provisional
 23-254 7.22e-26

diguanylate cyclase AdrA; Provisional


Pssm-ID: 182329 [Multi-domain]  Cd Length: 366  Bit Score: 104.14  E-value: 7.22e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675083031  23 LRMLFITVISIAISLLITfliLLATGTemmPIIFIIATIAPAVTAP-IVSWSISGLMIKVQ---KLEETHRKL---AMYD 95
Cdd:PRK10245  135 PRLFVAGLVLMVVSCLVT---LELTGI---TVSFNSAPLEWWLSLPvIVIYPLLFAWVSYQtatKLAEHKRRLqvmSTRD 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675083031  96 HLTGLLSRR--EFLAQgNELlQMCQSNNQPVVFAYLDLDHFKKINDTYGHAAGDEVLVSFANLVKKTLRQEDLLGRLGGE 173
Cdd:PRK10245  209 GMTGVYNRRhwETLLR-NEF-DNCRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSDVIGRFGGD 286

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675083031 174 EFALILVNTRVVEAKQKLELLRKSVAKMTINYAEQpLKITVSLGVADWDrPHKENLISLMKRADNALYSAKSSGRNQLAF 253
Cdd:PRK10245  287 EFAVIMSGTPAESAITAMSRVHEGLNTLRLPNAPQ-VTLRISVGVAPLN-PQMSHYREWLKSADLALYKAKNAGRNRTEV 364


                  .
gi 1675083031 254 A 254
Cdd:PRK10245  365 A 365
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 89-250 1.72e-25

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 105.14  E-value: 1.72e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675083031   89 RKL---AMYDHLTGLLSRREFLAQGNELLQMCQSNNQPVVFAYLDLDHFKKINDTYGHAAGDEVLVSFANLVKKTLRQED 165
Cdd:PRK09776   659 RQLsysASHDALTHLANRASFEKQLRRLLQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSD 738

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675083031  166 LLGRLGGEEFALILVNTRVVEAKQKLELLRKSVAKMTINYAEQPLKITVSLGVADWD---RPHKEnlisLMKRADNALYS 242
Cdd:PRK09776   739 VLARLGGDEFGLLLPDCNVESARFIATRIISAINDYHFPWEGRVYRVGASAGITLIDannHQASE----VMSQADIACYA 814


                   ....*...
gi 1675083031  243 AKSSGRNQ 250
Cdd:PRK09776   815 AKNAGRGR 822
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
85-250 1.44e-21

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 93.59  E-value: 1.44e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675083031  85 EETHRKLAMYDHLTGLLSRREFLAQGNELLQmcQSNNQPVVFAYLDLDHFKKINDTYGHAAGDEVLVSFANLVKKTLRQE 164
Cdd:PRK10060  230 QERLRILANTDSITGLPNRNAIQELIDHAIN--AADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEED 307

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675083031 165 DLLGRLGGEEFalilvntrVVEAKQKLELLRKSVAKMTINYAEQPLKITV-------SLGVADWDRpHKENLISLMKRAD 237
Cdd:PRK10060  308 QTLARLGGDEF--------LVLASHTSQAALEAMASRILTRLRLPFRIGLievytgcSIGIALAPE-HGDDSESLIRSAD 378

                         170
                  ....*....|...
gi 1675083031 238 NALYSAKSSGRNQ 250
Cdd:PRK10060  379 TAMYTAKEGGRGQ 391
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 90-253 1.80e-21

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 93.30  E-value: 1.80e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675083031  90 KLAMYDHLTGLLSRREFLAQGNELLQmcqsNNQPVVFAYLDLDHFKKINDTYGHAAGDEVLVSFANLVKKTLRQEDLLGR 169
Cdd:PRK11359  374 QLIQFDPLTGLPNRNNLHNYLDDLVD----KAVSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCR 449

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675083031 170 LGGEEFALILVNTRVVEAKQKLELLRkSVAKMTINYAEQPLKITVSLGVADWDRPHKENLISlmkRADNALYSAKSSGRN 249
Cdd:PRK11359  450 IEGTQFVLVSLENDVSNITQIADELR-NVVSKPIMIDDKPFPLTLSIGISYDVGKNRDYLLS---TAHNAMDYIRKNGGN 525


                  ....
gi 1675083031 250 QLAF 253
Cdd:PRK11359  526 GWQF 529
PRK09966 PRK09966
diguanylate cyclase DgcN;
90-244 1.55e-15

diguanylate cyclase DgcN;


Pssm-ID: 182171 [Multi-domain]  Cd Length: 407  Bit Score: 75.43  E-value: 1.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675083031  90 KLAMYDHLTGLLSRREFLAQGNELLQMCQSNNQPVVFaYLDLDHFKKINDTYGHAAGDEVLVSFANLVKKTLRQEDLLGR 169
Cdd:PRK09966  246 RTALHDPLTGLANRAAFRSGINTLMNNSDARKTSALL-FLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHKAYR 324

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1675083031 170 LGGEEFALILVNTRV-VEAKQKLELLRKSVAKMTINYAEQPLKITVSLGVA-DWDRPHKENLISLmkrADNALYSAK 244
Cdd:PRK09966  325 LGGDEFAMVLYDVQSeSEVQQICSALTQIFNLPFDLHNGHQTTMTLSIGYAmTIEHASAEKLQEL---ADHNMYQAK 398
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 165-244 4.17e-13

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: 65.70  E-value: 4.17e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675083031 165 DLLGRLGGEEFALILVNTRVVEAKQKLELLRKSVAKMtinyaeQPLKITVSLGVADwdrphkenlISLMKRADnALYSAK 244
Cdd:COG3706   116 DLVARYGGEEFAILLPGTDLEGALAVAERIREAVAEL------PSLRVTVSIGVAG---------DSLLKRAD-ALYQAR 179
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
 123-219 6.30e-05

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: 41.57  E-value: 6.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675083031 123 PVVFAYLDLDHFKKINDTYGHAAGDEVLVSFANLVKKTLRQ-EDLLGRLGGEEFALILVNTRVVEAKQKLELLRKSVAKM 201
Cdd:cd07556     1 PVTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRsGDLKIKTIGDEFMVVSGLDHPAAAVAFAEDMREAVSAL 80

                          90
                  ....*....|....*...
gi 1675083031 202 TInyaEQPLKITVSLGVA 219
Cdd:cd07556    81 NQ---SEGNPVRVRIGIH 95
PRK11829 PRK11829
biofilm formation regulator HmsP; Provisional
 82-253 8.50e-03

biofilm formation regulator HmsP; Provisional


Pssm-ID: 183329 [Multi-domain]  Cd Length: 660  Bit Score: 37.23  E-value: 8.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675083031  82 QKLEETHRKLAMYDH---LTGLLSRREFLAqgneLLQ---MCQSNNQPVVFAYLDLDHFKKINDTYGHAAGDEVLVSFAN 155
Cdd:PRK11829  219 QLLADAYADMGRISHrfpVTELPNRSLFIS----LLEkeiASSTRTDHFHLLVIGIETLQEVSGAMSEAQHQQLLLTIVQ 294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675083031 156 LVKKTLRQEDLLGRLGGEEFALILVNT-RVVEAKQKLELLRKSVAKmTINYAEQPLKITVSLGVADWdRPHKENLISLMK 234
Cdd:PRK11829  295 RIEQCIDDSDLLAQLSKTEFAVLARGTrRSFPAMQLARRIMSQVTQ-PLFFDEITLRPSASIGITRY-QAQQDTAESMMR 372

                         170
                  ....*....|....*....
gi 1675083031 235 RADNALYSAKSSGRNQLAF 253
Cdd:PRK11829  373 NASTAMMAAHHEGRNQIMV 391
 
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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