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Conserved domains on  [gi|2771150745|ref|WP_367088886|]
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GGDEF domain-containing protein, partial [Enterobacter cloacae]

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: ...
 12-168 1.57e-61

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: 187.38  E-value: 1.57e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771150745  12 MMDPLLDIANRRLLEKRIDHELNKLRQTCRESALMFIDIDNFKDVNDRFGHKVGDALLAAVSQILHLSTRPNDTPARLGG 91
Cdd:cd01949     1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2771150745  92 DEFVVLLPDTTLEEAQVVARRIMDAAAMKKEVAQETVHCTLSIGIACATREMISVTDWLQAADNALYRAKRDGKNRI 168
Cdd:cd01949    81 DEFAILLPGTDLEEAEALAERLREAIEEPFFIDGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNRV 157
 
Name Accession Description Interval E-value
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 12-168 1.57e-61

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: 187.38  E-value: 1.57e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771150745  12 MMDPLLDIANRRLLEKRIDHELNKLRQTCRESALMFIDIDNFKDVNDRFGHKVGDALLAAVSQILHLSTRPNDTPARLGG 91
Cdd:cd01949     1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2771150745  92 DEFVVLLPDTTLEEAQVVARRIMDAAAMKKEVAQETVHCTLSIGIACATREMISVTDWLQAADNALYRAKRDGKNRI 168
Cdd:cd01949    81 DEFAILLPGTDLEEAEALAERLREAIEEPFFIDGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNRV 157
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 11-167 4.02e-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: 176.29  E-value: 4.02e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771150745  11 AMMDPLLDIANRRLLEKRIDHELNKLRQTCRESALMFIDIDNFKDVNDRFGHKVGDALLAAVSQILHLSTRPNDTPARLG 90
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771150745  91 GDEFVVLLPDTTLEEAQVVA---RRIMDAAAMKKEVAQETVHCTLSIGIACATREMISVTDWLQAADNALYRAKRDGKNR 167
Cdd:pfam00990  81 GDEFAILLPETSLEGAQELAeriRRLLAKLKIPHTVSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGRNR 160
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 5-168 8.66e-57

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: 179.40  E-value: 8.66e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771150745   5 RELERIAMMDPLLDIANRRLLEKRIDHELNKLRQTCRESALMFIDIDNFKDVNDRFGHKVGDALLAAVSQILHLSTRPND 84
Cdd:COG2199   108 ERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESD 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771150745  85 TPARLGGDEFVVLLPDTTLEEAQVVARRIMDA-AAMKKEVAQETVHCTLSIGIACATREMISVTDWLQAADNALYRAKRD 163
Cdd:COG2199   188 LVARLGGDEFAVLLPGTDLEEAEALAERLREAlEQLPFELEGKELRVTVSIGVALYPEDGDSAEELLRRADLALYRAKRA 267


                  ....*
gi 2771150745 164 GKNRI 168
Cdd:COG2199   268 GRNRV 272
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 9-171 3.74e-56

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 173.97  E-value: 3.74e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771150745    9 RIAMMDPLLDIANRRLLEKRIDHELNKLRQTCRESALMFIDIDNFKDVNDRFGHKVGDALLAAVSQILHLSTRPNDTPAR 88
Cdd:smart00267   1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771150745   89 LGGDEFVVLLPDTTLEEAQVVARRIMDAAAMKKEVAQETVHCTLSIGIACATREMISVTDWLQAADNALYRAKRDGKNRI 168
Cdd:smart00267  81 LGGDEFALLLPETSLEEAIALAERILQQLREPIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQV 160


                   ...
gi 2771150745  169 FAH 171
Cdd:smart00267 161 AVY 163
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 11-170 6.21e-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: 160.58  E-value: 6.21e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771150745  11 AMMDPLLDIANRRLLEKRIDHELNKLRQTCRESALMFIDIDNFKDVNDRFGHKVGDALLAAVSQILHLSTRPNDTPARLG 90
Cdd:TIGR00254   2 AVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771150745  91 GDEFVVLLPDTTLEEAQVVARRIMDAA-AMKKEVAQ-ETVHCTLSIGIACATREMISVTDWLQAADNALYRAKRDGKNRI 168
Cdd:TIGR00254  82 GEEFVVILPGTPLEDALSKAERLRDAInSKPIEVAGsETLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRNRV 161


                  ..
gi 2771150745 169 FA 170
Cdd:TIGR00254 162 VV 163
pleD PRK09581
response regulator PleD; Reviewed
 11-170 2.17e-36

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 130.79  E-value: 2.17e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771150745  11 AMMDPLLDIANRRLLEKRIDHELNKLRQTCRESALMFIDIDNFKDVNDRFGHKVGDALLAAVSQILHLSTRPNDTPARLG 90
Cdd:PRK09581  292 AVTDGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARYG 371

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771150745  91 GDEFVVLLPDTTLEEAQVVA---RRIMDAAAMKKEVAQETVHCTLSIGIACATREMISVTDWLQAADNALYRAKRDGKNR 167
Cdd:PRK09581  372 GEEFVVVMPDTDIEDAIAVAeriRRKIAEEPFIISDGKERLNVTVSIGVAELRPSGDTIEALIKRADKALYEAKNTGRNR 451


                  ...
gi 2771150745 168 IFA 170
Cdd:PRK09581  452 VVA 454
 
Name Accession Description Interval E-value
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 12-168 1.57e-61

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: 187.38  E-value: 1.57e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771150745  12 MMDPLLDIANRRLLEKRIDHELNKLRQTCRESALMFIDIDNFKDVNDRFGHKVGDALLAAVSQILHLSTRPNDTPARLGG 91
Cdd:cd01949     1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2771150745  92 DEFVVLLPDTTLEEAQVVARRIMDAAAMKKEVAQETVHCTLSIGIACATREMISVTDWLQAADNALYRAKRDGKNRI 168
Cdd:cd01949    81 DEFAILLPGTDLEEAEALAERLREAIEEPFFIDGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNRV 157
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 11-167 4.02e-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: 176.29  E-value: 4.02e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771150745  11 AMMDPLLDIANRRLLEKRIDHELNKLRQTCRESALMFIDIDNFKDVNDRFGHKVGDALLAAVSQILHLSTRPNDTPARLG 90
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771150745  91 GDEFVVLLPDTTLEEAQVVA---RRIMDAAAMKKEVAQETVHCTLSIGIACATREMISVTDWLQAADNALYRAKRDGKNR 167
Cdd:pfam00990  81 GDEFAILLPETSLEGAQELAeriRRLLAKLKIPHTVSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGRNR 160
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 5-168 8.66e-57

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: 179.40  E-value: 8.66e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771150745   5 RELERIAMMDPLLDIANRRLLEKRIDHELNKLRQTCRESALMFIDIDNFKDVNDRFGHKVGDALLAAVSQILHLSTRPND 84
Cdd:COG2199   108 ERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESD 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771150745  85 TPARLGGDEFVVLLPDTTLEEAQVVARRIMDA-AAMKKEVAQETVHCTLSIGIACATREMISVTDWLQAADNALYRAKRD 163
Cdd:COG2199   188 LVARLGGDEFAVLLPGTDLEEAEALAERLREAlEQLPFELEGKELRVTVSIGVALYPEDGDSAEELLRRADLALYRAKRA 267


                  ....*
gi 2771150745 164 GKNRI 168
Cdd:COG2199   268 GRNRV 272
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 9-171 3.74e-56

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 173.97  E-value: 3.74e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771150745    9 RIAMMDPLLDIANRRLLEKRIDHELNKLRQTCRESALMFIDIDNFKDVNDRFGHKVGDALLAAVSQILHLSTRPNDTPAR 88
Cdd:smart00267   1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771150745   89 LGGDEFVVLLPDTTLEEAQVVARRIMDAAAMKKEVAQETVHCTLSIGIACATREMISVTDWLQAADNALYRAKRDGKNRI 168
Cdd:smart00267  81 LGGDEFALLLPETSLEEAIALAERILQQLREPIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQV 160


                   ...
gi 2771150745  169 FAH 171
Cdd:smart00267 161 AVY 163
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 5-168 3.86e-53

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


Pssm-ID: 444025 [Multi-domain]  Cd Length: 678  Bit Score: 178.81  E-value: 3.86e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771150745   5 RELERIAMMDPLLDIANRRLLEKRIDHELNKLRQTCRESALMFIDIDNFKDVNDRFGHKVGDALLAAVSQILHLSTRPND 84
Cdd:COG5001   245 ERLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGD 324

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771150745  85 TPARLGGDEFVVLLPDTT-LEEAQVVARRIMDAAAMKKEVAQETVHCTLSIGIACATREMISVTDWLQAADNALYRAKRD 163
Cdd:COG5001   325 TVARLGGDEFAVLLPDLDdPEDAEAVAERILAALAEPFELDGHELYVSASIGIALYPDDGADAEELLRNADLAMYRAKAA 404


                  ....*
gi 2771150745 164 GKNRI 168
Cdd:COG5001   405 GRNRY 409
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 11-170 6.21e-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: 160.58  E-value: 6.21e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771150745  11 AMMDPLLDIANRRLLEKRIDHELNKLRQTCRESALMFIDIDNFKDVNDRFGHKVGDALLAAVSQILHLSTRPNDTPARLG 90
Cdd:TIGR00254   2 AVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771150745  91 GDEFVVLLPDTTLEEAQVVARRIMDAA-AMKKEVAQ-ETVHCTLSIGIACATREMISVTDWLQAADNALYRAKRDGKNRI 168
Cdd:TIGR00254  82 GEEFVVILPGTPLEDALSKAERLRDAInSKPIEVAGsETLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRNRV 161


                  ..
gi 2771150745 169 FA 170
Cdd:TIGR00254 162 VV 163
pleD PRK09581
response regulator PleD; Reviewed
 11-170 2.17e-36

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 130.79  E-value: 2.17e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771150745  11 AMMDPLLDIANRRLLEKRIDHELNKLRQTCRESALMFIDIDNFKDVNDRFGHKVGDALLAAVSQILHLSTRPNDTPARLG 90
Cdd:PRK09581  292 AVTDGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARYG 371

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771150745  91 GDEFVVLLPDTTLEEAQVVA---RRIMDAAAMKKEVAQETVHCTLSIGIACATREMISVTDWLQAADNALYRAKRDGKNR 167
Cdd:PRK09581  372 GEEFVVVMPDTDIEDAIAVAeriRRKIAEEPFIISDGKERLNVTVSIGVAELRPSGDTIEALIKRADKALYEAKNTGRNR 451


                  ...
gi 2771150745 168 IFA 170
Cdd:PRK09581  452 VVA 454
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 5-168 1.06e-33

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 125.56  E-value: 1.06e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771150745    5 RELERIAMMDPLLDIANRRLLEKRIDHELNKLRQTCRESALMFIDIDNFKDVNDRFGHKVGDALLAAVSQILHLSTRPND 84
Cdd:PRK09776   659 RQLSYSASHDALTHLANRASFEKQLRRLLQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSD 738

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771150745   85 TPARLGGDEFVVLLPDTTLEEAQVVARRIMDAAAMKKEVAQETVH-CTLSIGIACATREMISVTDWLQAADNALYRAKRD 163
Cdd:PRK09776   739 VLARLGGDEFGLLLPDCNVESARFIATRIISAINDYHFPWEGRVYrVGASAGITLIDANNHQASEVMSQADIACYAAKNA 818


                   ....*
gi 2771150745  164 GKNRI 168
Cdd:PRK09776   819 GRGRV 823
PRK15426 PRK15426
cellulose biosynthesis regulator YedQ;
5-171 2.33e-33

cellulose biosynthesis regulator YedQ;


Pssm-ID: 237964 [Multi-domain]  Cd Length: 570  Bit Score: 123.59  E-value: 2.33e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771150745   5 RELERIAMMDPLLDIANRRLLEKRIDHELnklrQTCRESALMF----IDIDNFKDVNDRFGHKVGDALLAAVSQILHLST 80
Cdd:PRK15426  392 SSLQWQAWHDPLTRLYNRGALFEKARALA----KRCQRDQQPFsviqLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSL 467

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771150745  81 RPNDTPARLGGDEFVVLLPDTTLEEAQVVARRIMDAAAMKKEVAQ--ETVHCTLSIGIACATREMISVTDWLQA-ADNAL 157
Cdd:PRK15426  468 RAQDVAGRVGGEEFCVVLPGASLAEAAQVAERIRLRINEKEILVAksTTIRISASLGVSSAEEDGDYDFEQLQSlADRRL 547

                         170
                  ....*....|....
gi 2771150745 158 YRAKRDGKNRIFAH 171
Cdd:PRK15426  548 YLAKQAGRNRVCAS 561
PRK09894 PRK09894
diguanylate cyclase; Provisional
 5-168 2.63e-33

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 119.40  E-value: 2.63e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771150745   5 RELERIAM-MDPLLDIANRRLLEKRIDHELnkLRQTCRESALMFIDIDNFKDVNDRFGHKVGDALLAAVSQILHLSTRPN 83
Cdd:PRK09894  122 IYLLTIRSnMDVLTGLPGRRVLDESFDHQL--RNREPQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDY 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771150745  84 DTPARLGGDEFVVLLPDTTLEEAQVVARRI-MDAAAMKKEVAQETVHCTLSIGIACATREMiSVTDWLQAADNALYRAKR 162
Cdd:PRK09894  200 ETVYRYGGEEFIICLKAATDEEACRAGERIrQLIANHAITHSDGRINITATFGVSRAFPEE-TLDVVIGRADRAMYEGKQ 278


                  ....*.
gi 2771150745 163 DGKNRI 168
Cdd:PRK09894  279 TGRNRV 284
adrA PRK10245
diguanylate cyclase AdrA; Provisional
 5-167 9.46e-31

diguanylate cyclase AdrA; Provisional


Pssm-ID: 182329 [Multi-domain]  Cd Length: 366  Bit Score: 114.16  E-value: 9.46e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771150745   5 RELERIAMMDPLLDIANRRLLEKRIDHELNKLRQTCRESALMFIDIDNFKDVNDRFGHKVGDALLAAVSQILHLSTRPND 84
Cdd:PRK10245  199 RRLQVMSTRDGMTGVYNRRHWETLLRNEFDNCRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSD 278

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771150745  85 TPARLGGDEFVVLLPDTTLEEAQVVARRIMDAAAMKKEVAQETVHCTLSIGIACATREMISVTDWLQAADNALYRAKRDG 164
Cdd:PRK10245  279 VIGRFGGDEFAVIMSGTPAESAITAMSRVHEGLNTLRLPNAPQVTLRISVGVAPLNPQMSHYREWLKSADLALYKAKNAG 358


                  ...
gi 2771150745 165 KNR 167
Cdd:PRK10245  359 RNR 361
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
7-170 6.46e-28

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 108.62  E-value: 6.46e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771150745   7 LERIAMMDPLLDIANRRLLEKRIDHELNklRQTCRESALMFIDIDNFKDVNDRFGHKVGDALLAAVSQILHLSTRPNDTP 86
Cdd:PRK10060  233 LRILANTDSITGLPNRNAIQELIDHAIN--AADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQTL 310

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771150745  87 ARLGGDEFVVLLPDTTLEEAQVVARRIMDAAAMKKEVAQETVHCTLSIGIACATREMISVTDWLQAADNALYRAKRDGKN 166
Cdd:PRK10060  311 ARLGGDEFLVLASHTSQAALEAMASRILTRLRLPFRIGLIEVYTGCSIGIALAPEHGDDSESLIRSADTAMYTAKEGGRG 390


                  ....*.
gi 2771150745 167 --RIFA 170
Cdd:PRK10060  391 qfCVFS 396
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 1-166 7.33e-18

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 79.81  E-value: 7.33e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771150745   1 RIKSRE-LERIAMMDPLLDIANRRLLEkridHELNKLRQTCRESALMFIDIDNFKDVNDRFGHKVGDALLAAVSQILHLS 79
Cdd:PRK11359  365 QEKSRQhIEQLIQFDPLTGLPNRNNLH----NYLDDLVDKAVSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREK 440

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771150745  80 TRPNDTPARLGGDEFVVLLPDTTLEEAQVVARRIMDAAAMKKEVAQETVHCTLSIGI---ACATREmisvtDWLQAADNA 156
Cdd:PRK11359  441 LKPDQYLCRIEGTQFVLVSLENDVSNITQIADELRNVVSKPIMIDDKPFPLTLSIGIsydVGKNRD-----YLLSTAHNA 515

                         170
                  ....*....|
gi 2771150745 157 LYRAKRDGKN 166
Cdd:PRK11359  516 MDYIRKNGGN 525
PRK09966 PRK09966
diguanylate cyclase DgcN;
3-161 2.92e-17

diguanylate cyclase DgcN;


Pssm-ID: 182171 [Multi-domain]  Cd Length: 407  Bit Score: 77.74  E-value: 2.92e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771150745   3 KSRELERIAMMDPLLDIANRRLLEKRIDhELNKLRQTCRESALMFIDIDNFKDVNDRFGHKVGDALLAAVSQILHLSTRP 82
Cdd:PRK09966  240 KNAQLLRTALHDPLTGLANRAAFRSGIN-TLMNNSDARKTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGL 318

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771150745  83 NDTPARLGGDEFVVLLPDTTLE-EAQVVARRIMDAAAMKKEVAQ-ETVHCTLSIGIACaTREMISVTDWLQAADNALYRA 160
Cdd:PRK09966  319 RHKAYRLGGDEFAMVLYDVQSEsEVQQICSALTQIFNLPFDLHNgHQTTMTLSIGYAM-TIEHASAEKLQELADHNMYQA 397


                  .
gi 2771150745 161 K 161
Cdd:PRK09966  398 K 398
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 84-161 3.94e-15

Two-component response regulator, PleD family, consists of two REC domains and a diguanylate cyclase (GGDEF) domain [Signal transduction mechanisms, Transcription];


Pssm-ID: 442920 [Multi-domain]  Cd Length: 179  Bit Score: 69.17  E-value: 3.94e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2771150745  84 DTPARLGGDEFVVLLPDTTLEEAQVVARRIMDAAAmkkevAQETVHCTLSIGIAcatremisVTDWLQAADnALYRAK 161
Cdd:COG3706   116 DLVARYGGEEFAILLPGTDLEGALAVAERIREAVA-----ELPSLRVTVSIGVA--------GDSLLKRAD-ALYQAR 179
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
 45-137 1.43e-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: 63.91  E-value: 1.43e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771150745  45 LMFIDIDNFKDVNDRFGHKVGDALLAAVSQIL-HLSTRPNDTPARLGGDEFVVLLPDTTLEEAQVVARRIMDAAAmkKEV 123
Cdd:cd07556     4 ILFADIVGFTSLADALGPDEGDELLNELAGRFdSLIRRSGDLKIKTIGDEFMVVSGLDHPAAAVAFAEDMREAVS--ALN 81

                          90
                  ....*....|....
gi 2771150745 124 AQETVHCTLSIGIA 137
Cdd:cd07556    82 QSEGNPVRVRIGIH 95
PRK11829 PRK11829
biofilm formation regulator HmsP; Provisional
 6-168 4.02e-08

biofilm formation regulator HmsP; Provisional


Pssm-ID: 183329 [Multi-domain]  Cd Length: 660  Bit Score: 51.48  E-value: 4.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771150745   6 ELERIAMMDPLLDIANRRLLEKRIDHELNKlrQTCRES-ALMFIDIDNFKDVNDRFGHKVGDALLAAVSQILHLSTRPND 84
Cdd:PRK11829  227 DMGRISHRFPVTELPNRSLFISLLEKEIAS--STRTDHfHLLVIGIETLQEVSGAMSEAQHQQLLLTIVQRIEQCIDDSD 304

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771150745  85 TPARLGGDEFVVLLPDTTLE-EAQVVARRIMDAAAMKKEVAQETVHCTLSIGIACATREMISVTDWLQAADNALYRAKRD 163
Cdd:PRK11829  305 LLAQLSKTEFAVLARGTRRSfPAMQLARRIMSQVTQPLFFDEITLRPSASIGITRYQAQQDTAESMMRNASTAMMAAHHE 384


                  ....*
gi 2771150745 164 GKNRI 168
Cdd:PRK11829  385 GRNQI 389
PRK13561 PRK13561
putative diguanylate cyclase; Provisional
 6-168 2.52e-06

putative diguanylate cyclase; Provisional


Pssm-ID: 184143 [Multi-domain]  Cd Length: 651  Bit Score: 46.25  E-value: 2.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771150745   6 ELERIAMMDPLLDIANRRLLEKRIDHELNKlRQTcreSALMFIDIDNFKDVNDRFGHKVGDALLAAVSQILHLSTRPNDT 85
Cdd:PRK13561  226 EQSRNATRFPVSDLPNKALLMALLEQVVAR-KQT---TALMIITCETLRDTAGVLKEAQREILLLTLVEKLKSVLSPRMV 301

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771150745  86 PARLGGDEFVVLL-PDTTLEEAQVVARRIMDAAAMKKEVAQETVHCTLSIGIACATREMiSVTDWLQAADNALYRAKRDG 164
Cdd:PRK13561  302 LAQISGYDFAIIAnGVKEPWHAITLGQQVLTIINERLPIQRIQLRPSCSIGIAMFYGDL-TAEQLYSRAISAAFTARRKG 380


                  ....
gi 2771150745 165 KNRI 168
Cdd:PRK13561  381 KNQI 384
PRK11059 PRK11059
regulatory protein CsrD; Provisional
 11-110 1.85e-05

regulatory protein CsrD; Provisional


Pssm-ID: 236833 [Multi-domain]  Cd Length: 640  Bit Score: 43.70  E-value: 1.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771150745  11 AMMDPLLDIANRRLLEKRIDHELNKLRQTCRESALMFIDIDNFKDVNDRFGHKVGDALL-AAVSQILHLSTR-PNDTPAR 88
Cdd:PRK11059  228 AFQDAKTGLGNRLFFDNQLATLLEDQEMVGAHGVVMLIRLPDFDLLQEEWGESQVEELLfELINLLSTFVMRyPGALLAR 307

                          90       100
                  ....*....|....*....|..
gi 2771150745  89 LGGDEFVVLLPDTTLEEAQVVA 110
Cdd:PRK11059  308 YSRSDFAVLLPHRSLKEADSLA 329
 
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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