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Conserved domains on  [gi|2276204793|dbj|GKN98554|]
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hypothetical protein NUKP99_08150 [Klebsiella variicola]

Protein Classification

GGDEF domain-containing protein( domain architecture ID 10112692)

GGDEF domain-containing protein may function as a diguanylate cyclase and be involved in regulating cell surface adhesion in bacteria

CATH:  3.30.70.1230
Gene Ontology:  GO:0005525|GO:0005886|GO:0007165|GO:0046872|GO:0052621
PubMed:  16166544|17208514|11119645|15569936

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 7-156 7.81e-56

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: 172.36  E-value: 7.81e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276204793   7 LPNRRFFEQKMESAFRATRKKRIHSYLMLIDVDNFKKINDTYGHEVGDAVLSRISTILRECAGEKDVPARFGGDELAIIV 86
Cdd:cd01949     8 LPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGDEFAILL 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2276204793  87 NNSNSKLVIAMVHIIQKKIKDLSLPSHHDIYCTVSIGISCA-ENKESIIEWIKEADEMLYEVKRNGKNGYC 156
Cdd:cd01949    88 PGTDLEEAEALAERLREAIEEPFFIDGQEIRVTASIGIATYpEDGEDAEELLRRADEALYRAKRSGRNRVV 158
 
Name Accession Description Interval E-value
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 7-156 7.81e-56

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: 172.36  E-value: 7.81e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276204793   7 LPNRRFFEQKMESAFRATRKKRIHSYLMLIDVDNFKKINDTYGHEVGDAVLSRISTILRECAGEKDVPARFGGDELAIIV 86
Cdd:cd01949     8 LPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGDEFAILL 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2276204793  87 NNSNSKLVIAMVHIIQKKIKDLSLPSHHDIYCTVSIGISCA-ENKESIIEWIKEADEMLYEVKRNGKNGYC 156
Cdd:cd01949    88 PGTDLEEAEALAERLREAIEEPFFIDGQEIRVTASIGIATYpEDGEDAEELLRRADEALYRAKRSGRNRVV 158
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 1-153 4.05e-52

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: 163.19  E-value: 4.05e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276204793   1 MDPGLDLPNRRFFEQKMESAFRATRKKRIHSYLMLIDVDNFKKINDTYGHEVGDAVLSRISTILRECAGEKDVPARFGGD 80
Cdd:pfam00990   3 HDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLGGD 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2276204793  81 ELAIIVNNSNSKLVIAMVHIIQKKIKDLSLP---SHHDIYCTVSIGISCA-ENKESIIEWIKEADEMLYEVKRNGKN 153
Cdd:pfam00990  83 EFAILLPETSLEGAQELAERIRRLLAKLKIPhtvSGLPLYVTISIGIAAYpNDGEDPEDLLKRADTALYQAKQAGRN 159
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 7-157 8.34e-52

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: 166.31  E-value: 8.34e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276204793   7 LPNRRFFEQKMESAFRATRKKRIHSYLMLIDVDNFKKINDTYGHEVGDAVLSRISTILRECAGEKDVPARFGGDELAIIV 86
Cdd:COG2199   122 LPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLL 201

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2276204793  87 NNSNSKLVIAMVHIIQKKIKDLSLP-SHHDIYCTVSIGISCA-ENKESIIEWIKEADEMLYEVKRNGKNGYCM 157
Cdd:COG2199   202 PGTDLEEAEALAERLREALEQLPFElEGKELRVTVSIGVALYpEDGDSAEELLRRADLALYRAKRAGRNRVVV 274
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 1-156 1.59e-47

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 151.63  E-value: 1.59e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276204793    1 MDPGLDLPNRRFFEQKMESAFRATRKKRIHSYLMLIDVDNFKKINDTYGHEVGDAVLSRISTILRECAGEKDVPARFGGD 80
Cdd:smart00267   5 RDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARLGGD 84

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2276204793   81 ELAIIVNNSNSKLVIAMVHIIQKKIKDLSLPSHHDIYCTVSIGISCAENKESIIE-WIKEADEMLYEVKRNGKNGYC 156
Cdd:smart00267  85 EFALLLPETSLEEAIALAERILQQLREPIIIHGIPLYLTISIGVAAYPNPGEDAEdLLKRADTALYQAKKAGRNQVA 161
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 2-158 5.85e-45

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: 145.17  E-value: 5.85e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276204793   2 DPGLDLPNRRFFEQKMESAF-RATRKKRIHSYLMlIDVDNFKKINDTYGHEVGDAVLSRISTILRECAGEKDVPARFGGD 80
Cdd:TIGR00254   5 DPLTGLYNRRYLEEMLDSELkRARRFQRSFSVLM-IDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYGGE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276204793  81 ELAIIVNNSNSKLVIAMVHIIQKKIKDLSLPSHHD--IYCTVSIGISCAENK-ESIIEWIKEADEMLYEVKRNGKNGYCM 157
Cdd:TIGR00254  84 EFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSetLTVTVSIGVACYPGHgLTLEELLKRADEALYQAKKAGRNRVVV 163


                  .
gi 2276204793 158 P 158
Cdd:TIGR00254 164 A 164
pleD PRK09581
response regulator PleD; Reviewed
 2-153 3.05e-30

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 113.46  E-value: 3.05e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276204793   2 DPGLDLPNRRFFEQKMESAFRATRKKRIHSYLMLIDVDNFKKINDTYGHEVGDAVLSRISTILRECAGEKDVPARFGGDE 81
Cdd:PRK09581  295 DGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARYGGEE 374

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2276204793  82 LAIIVNNSNSKLVIAMVHIIQKKIKDLSLPSHHD---IYCTVSIGISCAENK-ESIIEWIKEADEMLYEVKRNGKN 153
Cdd:PRK09581  375 FVVVMPDTDIEDAIAVAERIRRKIAEEPFIISDGkerLNVTVSIGVAELRPSgDTIEALIKRADKALYEAKNTGRN 450
diguan_SiaD NF038266
biofilm regulation diguanylate cyclase SiaD;
2-153 2.36e-26

biofilm regulation diguanylate cyclase SiaD;


Pssm-ID: 468439 [Multi-domain]  Cd Length: 252  Bit Score: 99.67  E-value: 2.36e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276204793   2 DPGLDLPNRRFFEQKM-ESAFRATRKKRIHSyLMLIDVDNFKKINDTYGHEVGDAVLSRISTILRECAGEKDVPARFGGD 80
Cdd:NF038266   97 DPLTGLPNRRLLMERLrEEVERARRSGRPFT-LAMLDVDHFKRINDRYGHEVGDRVLVEIARTLRAELREYDLCGRWGGE 175

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2276204793  81 ELAIIVNNSNSKLVIAMVHIIQKKIKDLSLPSHHDIYC-TVSIGISCAENKESII-EWIKEADEMLYEVKRNGKN 153
Cdd:NF038266  176 EFLLLLPETGLEEAQVVLERLREAVRALAVRVGDDVLSvTASAGLAEHRPPEEGLsATLSRADQALYQAKRAGRD 250
 
Name Accession Description Interval E-value
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 7-156 7.81e-56

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: 172.36  E-value: 7.81e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276204793   7 LPNRRFFEQKMESAFRATRKKRIHSYLMLIDVDNFKKINDTYGHEVGDAVLSRISTILRECAGEKDVPARFGGDELAIIV 86
Cdd:cd01949     8 LPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGDEFAILL 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2276204793  87 NNSNSKLVIAMVHIIQKKIKDLSLPSHHDIYCTVSIGISCA-ENKESIIEWIKEADEMLYEVKRNGKNGYC 156
Cdd:cd01949    88 PGTDLEEAEALAERLREAIEEPFFIDGQEIRVTASIGIATYpEDGEDAEELLRRADEALYRAKRSGRNRVV 158
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 1-153 4.05e-52

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: 163.19  E-value: 4.05e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276204793   1 MDPGLDLPNRRFFEQKMESAFRATRKKRIHSYLMLIDVDNFKKINDTYGHEVGDAVLSRISTILRECAGEKDVPARFGGD 80
Cdd:pfam00990   3 HDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLGGD 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2276204793  81 ELAIIVNNSNSKLVIAMVHIIQKKIKDLSLP---SHHDIYCTVSIGISCA-ENKESIIEWIKEADEMLYEVKRNGKN 153
Cdd:pfam00990  83 EFAILLPETSLEGAQELAERIRRLLAKLKIPhtvSGLPLYVTISIGIAAYpNDGEDPEDLLKRADTALYQAKQAGRN 159
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 7-157 8.34e-52

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: 166.31  E-value: 8.34e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276204793   7 LPNRRFFEQKMESAFRATRKKRIHSYLMLIDVDNFKKINDTYGHEVGDAVLSRISTILRECAGEKDVPARFGGDELAIIV 86
Cdd:COG2199   122 LPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLL 201

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2276204793  87 NNSNSKLVIAMVHIIQKKIKDLSLP-SHHDIYCTVSIGISCA-ENKESIIEWIKEADEMLYEVKRNGKNGYCM 157
Cdd:COG2199   202 PGTDLEEAEALAERLREALEQLPFElEGKELRVTVSIGVALYpEDGDSAEELLRRADLALYRAKRAGRNRVVV 274
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 1-156 1.59e-47

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 151.63  E-value: 1.59e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276204793    1 MDPGLDLPNRRFFEQKMESAFRATRKKRIHSYLMLIDVDNFKKINDTYGHEVGDAVLSRISTILRECAGEKDVPARFGGD 80
Cdd:smart00267   5 RDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARLGGD 84

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2276204793   81 ELAIIVNNSNSKLVIAMVHIIQKKIKDLSLPSHHDIYCTVSIGISCAENKESIIE-WIKEADEMLYEVKRNGKNGYC 156
Cdd:smart00267  85 EFALLLPETSLEEAIALAERILQQLREPIIIHGIPLYLTISIGVAAYPNPGEDAEdLLKRADTALYQAKKAGRNQVA 161
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 2-158 5.85e-45

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: 145.17  E-value: 5.85e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276204793   2 DPGLDLPNRRFFEQKMESAF-RATRKKRIHSYLMlIDVDNFKKINDTYGHEVGDAVLSRISTILRECAGEKDVPARFGGD 80
Cdd:TIGR00254   5 DPLTGLYNRRYLEEMLDSELkRARRFQRSFSVLM-IDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYGGE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276204793  81 ELAIIVNNSNSKLVIAMVHIIQKKIKDLSLPSHHD--IYCTVSIGISCAENK-ESIIEWIKEADEMLYEVKRNGKNGYCM 157
Cdd:TIGR00254  84 EFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSetLTVTVSIGVACYPGHgLTLEELLKRADEALYQAKKAGRNRVVV 163


                  .
gi 2276204793 158 P 158
Cdd:TIGR00254 164 A 164
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 6-157 4.12e-44

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: 153.78  E-value: 4.12e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276204793   6 DLPNRRFFEQKMESAFRATRKKRIHSYLMLIDVDNFKKINDTYGHEVGDAVLSRISTILRECAGEKDVPARFGGDELAII 85
Cdd:COG5001   258 GLPNRRLFLDRLEQALARARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVL 337

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2276204793  86 VNNSNSKLVIAmvHIIQKKIKDLSLP---SHHDIYCTVSIGISCA-ENKESIIEWIKEADEMLYEVKRNGKNGYCM 157
Cdd:COG5001   338 LPDLDDPEDAE--AVAERILAALAEPfelDGHELYVSASIGIALYpDDGADAEELLRNADLAMYRAKAAGRNRYRF 411
pleD PRK09581
response regulator PleD; Reviewed
 2-153 3.05e-30

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 113.46  E-value: 3.05e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276204793   2 DPGLDLPNRRFFEQKMESAFRATRKKRIHSYLMLIDVDNFKKINDTYGHEVGDAVLSRISTILRECAGEKDVPARFGGDE 81
Cdd:PRK09581  295 DGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARYGGEE 374

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2276204793  82 LAIIVNNSNSKLVIAMVHIIQKKIKDLSLPSHHD---IYCTVSIGISCAENK-ESIIEWIKEADEMLYEVKRNGKN 153
Cdd:PRK09581  375 FVVVMPDTDIEDAIAVAERIRRKIAEEPFIISDGkerLNVTVSIGVAELRPSgDTIEALIKRADKALYEAKNTGRN 450
diguan_SiaD NF038266
biofilm regulation diguanylate cyclase SiaD;
2-153 2.36e-26

biofilm regulation diguanylate cyclase SiaD;


Pssm-ID: 468439 [Multi-domain]  Cd Length: 252  Bit Score: 99.67  E-value: 2.36e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276204793   2 DPGLDLPNRRFFEQKM-ESAFRATRKKRIHSyLMLIDVDNFKKINDTYGHEVGDAVLSRISTILRECAGEKDVPARFGGD 80
Cdd:NF038266   97 DPLTGLPNRRLLMERLrEEVERARRSGRPFT-LAMLDVDHFKRINDRYGHEVGDRVLVEIARTLRAELREYDLCGRWGGE 175

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2276204793  81 ELAIIVNNSNSKLVIAMVHIIQKKIKDLSLPSHHDIYC-TVSIGISCAENKESII-EWIKEADEMLYEVKRNGKN 153
Cdd:NF038266  176 EFLLLLPETGLEEAQVVLERLREAVRALAVRVGDDVLSvTASAGLAEHRPPEEGLsATLSRADQALYQAKRAGRD 250
adrA PRK10245
diguanylate cyclase AdrA; Provisional
 9-153 2.95e-25

diguanylate cyclase AdrA; Provisional


Pssm-ID: 182329 [Multi-domain]  Cd Length: 366  Bit Score: 99.13  E-value: 2.95e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276204793   9 NRRFFEQKMESAFRATRKKRIHSYLMLIDVDNFKKINDTYGHEVGDAVLSRISTILRECAGEKDVPARFGGDELAIIVNN 88
Cdd:PRK10245  215 NRRHWETLLRNEFDNCRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSDVIGRFGGDEFAVIMSG 294

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2276204793  89 SNSKLVIAMVHIIQKKIKDLSLPSHHDIYCTVSIGISCAENKES-IIEWIKEADEMLYEVKRNGKN 153
Cdd:PRK10245  295 TPAESAITAMSRVHEGLNTLRLPNAPQVTLRISVGVAPLNPQMShYREWLKSADLALYKAKNAGRN 360
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
7-156 1.35e-23

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 95.90  E-value: 1.35e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276204793   7 LPNRRFFEQKMESAFRATRKKRIHsyLMLIDVDNFKKINDTYGHEVGDAVLSRISTILRECAGEKDVPARFGGDELAIIV 86
Cdd:PRK10060  245 LPNRNAIQELIDHAINAADNNQVG--IVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQTLARLGGDEFLVLA 322

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2276204793  87 NNSNSKLVIAMVHIIqkkIKDLSLPSH---HDIYCTVSIGISCA----ENKESIiewIKEADEMLYEVKRNGKNGYC 156
Cdd:PRK10060  323 SHTSQAALEAMASRI---LTRLRLPFRiglIEVYTGCSIGIALApehgDDSESL---IRSADTAMYTAKEGGRGQFC 393
PRK15426 PRK15426
cellulose biosynthesis regulator YedQ;
2-156 5.27e-23

cellulose biosynthesis regulator YedQ;


Pssm-ID: 237964 [Multi-domain]  Cd Length: 570  Bit Score: 93.93  E-value: 5.27e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276204793   2 DPGLDLPNRR-FFEQKMESAFRATRKKRIHSYLMLiDVDNFKKINDTYGHEVGDAVLSRISTILRECAGEKDVPARFGGD 80
Cdd:PRK15426  401 DPLTRLYNRGaLFEKARALAKRCQRDQQPFSVIQL-DLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRVGGE 479

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276204793  81 ELAIIVNNSNSKLVIAMVHIIQKKIKDLSLPSHHD--IYCTVSIGISCAENKE--------SIiewikeADEMLYEVKRN 150
Cdd:PRK15426  480 EFCVVLPGASLAEAAQVAERIRLRINEKEILVAKSttIRISASLGVSSAEEDGdydfeqlqSL------ADRRLYLAKQA 553


                  ....*.
gi 2276204793 151 GKNGYC 156
Cdd:PRK15426  554 GRNRVC 559
PRK09894 PRK09894
diguanylate cyclase; Provisional
 1-153 7.59e-22

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 88.97  E-value: 7.59e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276204793   1 MDPGLDLPNRRFFEQKMESAFRATRKKRIhsYLMLIDVDNFKKINDTYGHEVGDAVLSRISTILRECAGEKDVPARFGGD 80
Cdd:PRK09894  131 MDVLTGLPGRRVLDESFDHQLRNREPQNL--YLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGGE 208

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2276204793  81 ELAIIVNNSNSKLVIAMVHIIQKKIKDLSLPS-HHDIYCTVSIGISCAENKESIIEWIKEADEMLYEVKRNGKN 153
Cdd:PRK09894  209 EFIICLKAATDEEACRAGERIRQLIANHAITHsDGRINITATFGVSRAFPEETLDVVIGRADRAMYEGKQTGRN 282
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 7-153 1.58e-17

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 78.56  E-value: 1.58e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276204793    7 LPNRRFFEQKMESAFRATRKKRIHSYLMLIDVDNFKKINDTYGHEVGDAVLSRISTILRECAGEKDVPARFGGDELAIIV 86
Cdd:PRK09776   673 LANRASFEKQLRRLLQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSDVLARLGGDEFGLLL 752

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2276204793   87 NNSNSKLVIAMVHIIQKKIKDLSLPSH---HDIycTVSIGISC-AENKESIIEWIKEADEMLYEVKRNGKN 153
Cdd:PRK09776   753 PDCNVESARFIATRIISAINDYHFPWEgrvYRV--GASAGITLiDANNHQASEVMSQADIACYAAKNAGRG 821
PRK09966 PRK09966
diguanylate cyclase DgcN;
2-148 3.67e-16

diguanylate cyclase DgcN;


Pssm-ID: 182171 [Multi-domain]  Cd Length: 407  Bit Score: 74.27  E-value: 3.67e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276204793   2 DPGLDLPNRRFFEQKMeSAFRATRKKRIHSYLMLIDVDNFKKINDTYGHEVGDAVLSRISTILRECAGEKDVPARFGGDE 81
Cdd:PRK09966  251 DPLTGLANRAAFRSGI-NTLMNNSDARKTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHKAYRLGGDE 329

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2276204793  82 LAIIVNNSNSKLVIAMVHIIQKKIKDLSLPSH--HDIYCTVSIGISCAENKESIIEWIKEADEMLYEVK 148
Cdd:PRK09966  330 FAMVLYDVQSESEVQQICSALTQIFNLPFDLHngHQTTMTLSIGYAMTIEHASAEKLQELADHNMYQAK 398
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 2-155 3.71e-11

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 60.17  E-value: 3.71e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276204793   2 DPGLDLPNRRFFEQKMESAFRATRKkrihSYLMLIDVDNFKKINDTYGHEVGDAVLSRISTILRECAGEKDVPARFGGDE 81
Cdd:PRK11359  379 DPLTGLPNRNNLHNYLDDLVDKAVS----PVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGTQ 454

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276204793  82 LAIIVNNSN----SKLVIAMVHIIQKKIkdlsLPSHHDIYCTVSIGIS--CAENKESIIEWIKEAdeMLYeVKRNGKNGY 155
Cdd:PRK11359  455 FVLVSLENDvsniTQIADELRNVVSKPI----MIDDKPFPLTLSIGISydVGKNRDYLLSTAHNA--MDY-IRKNGGNGW 527
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
 33-125 2.26e-08

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: 50.05  E-value: 2.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276204793  33 LMLIDVDNFKKINDTYGHEVGDAVLSRISTILRE-CAGEKDVPARFGGDELAIIVNNSNSKLVIAMVHIIQKKIKDLSLP 111
Cdd:cd07556     4 ILFADIVGFTSLADALGPDEGDELLNELAGRFDSlIRRSGDLKIKTIGDEFMVVSGLDHPAAAVAFAEDMREAVSALNQS 83

                          90
                  ....*....|....
gi 2276204793 112 SHHDIycTVSIGIS 125
Cdd:cd07556    84 EGNPV--RVRIGIH 95
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 72-146 4.26e-07

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: 47.21  E-value: 4.26e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2276204793  72 DVPARFGGDELAIIVNNSNSKLVIAMVHIIQKKIKDLslpshHDIYCTVSIGIscaenkeSIIEWIKEADeMLYE 146
Cdd:COG3706   116 DLVARYGGEEFAILLPGTDLEGALAVAERIREAVAEL-----PSLRVTVSIGV-------AGDSLLKRAD-ALYQ 177
PRK11059 PRK11059
regulatory protein CsrD; Provisional
 2-157 4.76e-05

regulatory protein CsrD; Provisional


Pssm-ID: 236833 [Multi-domain]  Cd Length: 640  Bit Score: 42.16  E-value: 4.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276204793   2 DPGLDLPNRRFFEQKMESAFRATRKKRIHSYLMLIDVDNFKKINDTYGHEVGD----AVLSRISTILRECAGEkdVPARF 77
Cdd:PRK11059  231 DAKTGLGNRLFFDNQLATLLEDQEMVGAHGVVMLIRLPDFDLLQEEWGESQVEellfELINLLSTFVMRYPGA--LLARY 308

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276204793  78 GGDELAIIVNNSNSKlviAMVHIIQKKIKDL-SLPSHH-----DIyctVSIGISC---AENKESIIEwikEADEMLYEVK 148
Cdd:PRK11059  309 SRSDFAVLLPHRSLK---EADSLASQLLKAVdALPPPKmldrdDF---LHIGICAyrsGQSTEQVME---EAEMALRSAQ 379


                  ....*....
gi 2276204793 149 RNGKNGYCM 157
Cdd:PRK11059  380 LQGGNGWFV 388
 
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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