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Conserved domains on  [gi|759432114|ref|WP_043154967|]
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MULTISPECIES: sensor domain-containing diguanylate cyclase [Aeromonas]

Protein Classification

sensor domain-containing diguanylate cyclase( domain architecture ID 13295427)

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

CATH:  3.30.70.1230
EC:  2.7.7.65
Gene Ontology:  GO:0046872|GO:0052621|GO:0007165
PubMed:  11119645|15009198|9382818
SCOP:  4001316

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 ...
 125-330 7.37e-55

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: 180.56  E-value: 7.37e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432114 125 VGAHRNIHAQRELYARLELQNRTLEQQVAQRTAELERLNQaLQFQVEENRRLAETDSLTGAASRYRLEQAVRLEHERAKR 204
Cdd:COG2199   63 LLLALGLLLLALLLLSLVLELLLLLLALLLLLLALEDITE-LRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARR 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432114 205 FKEPFAVIAMDVDDFKQINDRHGHGVGDQTLIDIVQLTRGCIREIDLLARWGGDEFMLVLPNTRLPDARVVAEKLRQRLS 284
Cdd:COG2199  142 EGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALE 221

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 759432114 285 HARVKGIE---PVTLSFGLVESDPD-EQVSHLMARVDRALYRAKLAGKDQ 330
Cdd:COG2199  222 QLPFELEGkelRVTVSIGVALYPEDgDSAEELLRRADLALYRAKRAGRNR 271
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 38-128 3.72e-24

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.


:

Pssm-ID: 430001 [Multi-domain]  Cd Length: 89  Bit Score: 94.33  E-value: 3.72e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432114   38 YVHRYPGWYQMLGYEPHSLDNTVFTWENLIHPDDLAQVMESFDACLSGRaADYRAEYRCRCRNGDYLWVADCGRIVtRNP 117
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELLGKGESWLDLVHPDDRERVREALWEALKGG-EPYSGEYRIRRKDGEYRWVEARARPI-RDE 78

                          90
                  ....*....|.
gi 759432114  118 DGSVARMVGAH 128
Cdd:pfam08447  79 NGKPVRVIGVA 89
 
Name Accession Description Interval E-value
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 125-330 7.37e-55

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: 180.56  E-value: 7.37e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432114 125 VGAHRNIHAQRELYARLELQNRTLEQQVAQRTAELERLNQaLQFQVEENRRLAETDSLTGAASRYRLEQAVRLEHERAKR 204
Cdd:COG2199   63 LLLALGLLLLALLLLSLVLELLLLLLALLLLLLALEDITE-LRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARR 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432114 205 FKEPFAVIAMDVDDFKQINDRHGHGVGDQTLIDIVQLTRGCIREIDLLARWGGDEFMLVLPNTRLPDARVVAEKLRQRLS 284
Cdd:COG2199  142 EGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALE 221

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 759432114 285 HARVKGIE---PVTLSFGLVESDPD-EQVSHLMARVDRALYRAKLAGKDQ 330
Cdd:COG2199  222 QLPFELEGkelRVTVSIGVALYPEDgDSAEELLRRADLALYRAKRAGRNR 271
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 179-330 1.40e-52

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: 170.43  E-value: 1.40e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432114 179 TDSLTGAASRYRLEQAVRLEHERAKRFKEPFAVIAMDVDDFKQINDRHGHGVGDQTLIDIVQLTRGCIREIDLLARWGGD 258
Cdd:cd01949    2 TDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGD 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 759432114 259 EFMLVLPNTRLPDARVVAEKLRQRLSHARVKGIE--PVTLSFGLVESDPD-EQVSHLMARVDRALYRAKLAGKDQ 330
Cdd:cd01949   82 EFAILLPGTDLEEAEALAERLREAIEEPFFIDGQeiRVTASIGIATYPEDgEDAEELLRRADEALYRAKRSGRNR 156
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 177-330 1.98e-47

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: 157.41  E-value: 1.98e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432114  177 AETDSLTGAASRYRLEQAVRLEHERAKRFKEPFAVIAMDVDDFKQINDRHGHGVGDQTLIDIVQLTRGCIREIDLLARWG 256
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432114  257 GDEFMLVLPNTRLPDARVVAEKLRQRLSHAR----VKGIE-PVTLSFGLVESDPD-EQVSHLMARVDRALYRAKLAGKDQ 330
Cdd:pfam00990  81 GDEFAILLPETSLEGAQELAERIRRLLAKLKiphtVSGLPlYVTISIGIAAYPNDgEDPEDLLKRADTALYQAKQAGRNR 160
diguan_SiaD NF038266
biofilm regulation diguanylate cyclase SiaD;
121-331 2.41e-43

biofilm regulation diguanylate cyclase SiaD;


Pssm-ID: 468439 [Multi-domain]  Cd Length: 252  Bit Score: 149.75  E-value: 2.41e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432114 121 VARMVGAHRNIHAQRE--LYARLELQNRTLEQ--QVAQRTAELER-LNQALqfqveenRRLAETDSLTGAASRYRLEQAV 195
Cdd:NF038266  40 LTRISDGYQSAARERElsLAERYDRQLRRLEKivRISDRYQRMMRdLNEAL-------REASTRDPLTGLPNRRLLMERL 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432114 196 RLEHERAKRFKEPFAVIAMDVDDFKQINDRHGHGVGDQTLIDIVQLTRGCIREIDLLARWGGDEFMLVLPNTRLPDARVV 275
Cdd:NF038266 113 REEVERARRSGRPFTLAMLDVDHFKRINDRYGHEVGDRVLVEIARTLRAELREYDLCGRWGGEEFLLLLPETGLEEAQVV 192

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432114 276 AEKLRQRLSHARVKGIEP---VTLSFGLVESDPDEQ-VSHLMARVDRALYRAKLAGKDQL 331
Cdd:NF038266 193 LERLREAVRALAVRVGDDvlsVTASAGLAEHRPPEEgLSATLSRADQALYQAKRAGRDRV 252
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 175-333 8.02e-43

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 145.47  E-value: 8.02e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432114   175 RLAETDSLTGAASRYRLEQAVRLEHERAKRFKEPFAVIAMDVDDFKQINDRHGHGVGDQTLIDIVQLTRGCIREIDLLAR 254
Cdd:smart00267   1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432114   255 WGGDEFMLVLPNTRLPDARVVAEKLRQRLS-HARVKGIE-PVTLSFGLVE-SDPDEQVSHLMARVDRALYRAKLAGKDQL 331
Cdd:smart00267  81 LGGDEFALLLPETSLEEAIALAERILQQLRePIIIHGIPlYLTISIGVAAyPNPGEDAEDLLKRADTALYQAKKAGRNQV 160


                   ..
gi 759432114   332 SG 333
Cdd:smart00267 161 AV 162
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 176-328 4.11e-36

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: 128.22  E-value: 4.11e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432114  176 LAETDSLTGAASRYRLEQAVRLEHERAKRFKEPFAVIAMDVDDFKQINDRHGHGVGDQTLIDIVQLTRGCIREIDLLARW 255
Cdd:TIGR00254   1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 759432114  256 GGDEFMLVLPNTRLPDARVVAEKLRQRLSHAR--VKGIEPVTL--SFGLVESDPD-EQVSHLMARVDRALYRAKLAGK 328
Cdd:TIGR00254  81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPieVAGSETLTVtvSIGVACYPGHgLTLEELLKRADEALYQAKKAGR 158
pleD PRK09581
response regulator PleD; Reviewed
 136-330 2.77e-35

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 133.10  E-value: 2.77e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432114 136 ELYARLELQNRTleqqvaqrtaelERLNQALQFQVEENRRLAETDSLTGAASRYRLEQAVRLEHERAKRFKEPFAVIAMD 215
Cdd:PRK09581 263 ELLARVRTQIRR------------KRYQDALRNNLEQSIEMAVTDGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMID 330

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432114 216 VDDFKQINDRHGHGVGDQTLIDIVQLTRGCIREIDLLARWGGDEFMLVLPNTRLPDARVVAEKLRQRLSH---ARVKGIE 292
Cdd:PRK09581 331 IDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARYGGEEFVVVMPDTDIEDAIAVAERIRRKIAEepfIISDGKE 410

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 759432114 293 P--VTLSFGLVESDP-DEQVSHLMARVDRALYRAKLAGKDQ 330
Cdd:PRK09581 411 RlnVTVSIGVAELRPsGDTIEALIKRADKALYEAKNTGRNR 451
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 38-128 3.72e-24

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.


Pssm-ID: 430001 [Multi-domain]  Cd Length: 89  Bit Score: 94.33  E-value: 3.72e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432114   38 YVHRYPGWYQMLGYEPHSLDNTVFTWENLIHPDDLAQVMESFDACLSGRaADYRAEYRCRCRNGDYLWVADCGRIVtRNP 117
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELLGKGESWLDLVHPDDRERVREALWEALKGG-EPYSGEYRIRRKDGEYRWVEARARPI-RDE 78

                          90
                  ....*....|.
gi 759432114  118 DGSVARMVGAH 128
Cdd:pfam08447  79 NGKPVRVIGVA 89
PAS COG2202
PAS domain [Signal transduction mechanisms];
21-141 1.06e-08

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 55.42  E-value: 1.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432114  21 MLEVVSDGLWDWNANTGYVHRYPGWYQMLGYEPHSLDNTvfTWENLIHPDDLAQVMESFDACLSGRAADYRAEYRCRCRN 100
Cdd:COG2202  142 LVENAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGK--SLLDLLHPEDRERLLELLRRLLEGGRESYELELRLKDGD 219

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 759432114 101 GDYLWVAdcGRIVTRNPDGSVARMVGAHRNIHAQRELYARL 141
Cdd:COG2202  220 GRWVWVE--ASAVPLRDGGEVIGVLGIVRDITERKRAEEAL 258
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 26-131 3.62e-06

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 44.93  E-value: 3.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432114  26 SDGLWDWNANTGYVHRYPGWYQMLGYEPHSLDNTvfTWENLIHPDDLAQVMESFDACLSGRaADYRAEYRCRCRNGDYLW 105
Cdd:cd00130    2 PDGVIVLDLDGRILYANPAAEQLLGYSPEELIGK--SLLDLIHPEDREELRERLENLLSGG-EPVTLEVRLRRKDGSVIW 78

                         90       100
                 ....*....|....*....|....*.
gi 759432114 106 VAdCGRIVTRNPDGSVARMVGAHRNI 131
Cdd:cd00130   79 VL-VSLTPIRDEGGEVIGLLGVVRDI 103
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
 20-141 3.21e-05

PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions]


Pssm-ID: 272971 [Multi-domain]  Cd Length: 124  Bit Score: 42.66  E-value: 3.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432114   20 GMLEVVSDGLW-DWNantgyvhryPGWYQMLGYEPHSLDNTvfTWENLIHPDDLAQVMESFDACLSGRAADYRAEYRCRC 98
Cdd:TIGR00229  15 AIIVIDLEGNIlYVN---------PAFEEIFGYSAEELIGR--NVLELIPEEDREEVRERIERRLEGEPEPVSEERRVRR 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 759432114   99 RNGDYLWVADCGRIVTRNpdGSVARMVGAHRNIHAQRELYARL 141
Cdd:TIGR00229  84 KDGSEIWVEVSVSPIRTN--GGELGVVGIVRDITERKEAEEAL 124
PRK13560 PRK13560
hypothetical protein; Provisional
 29-207 1.70e-04

hypothetical protein; Provisional


Pssm-ID: 106506 [Multi-domain]  Cd Length: 807  Bit Score: 43.51  E-value: 1.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432114  29 LWDWNANtgyvhryPGWYQML--------GYEPHSLDNTVFTWENLIHPDDLAQVMESFDACLSGRAADYRAEYRCRCRN 100
Cdd:PRK13560 486 LFRWKAE-------EGWPVELvsknitqfGYEPDEFISGKRMFAAIIHPADLEQVAAEVAEFAAQGVDRFEQEYRILGKG 558

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432114 101 GDYLWVADCGRiVTRNPDGSVARMVGAHRNI----HAQRELYARLeLQNRTLEQQVAQRTA-ELERLNQALQFQVEENRR 175
Cdd:PRK13560 559 GAVCWIDDQSA-AERDEEGQISHFEGIVIDIserkHAEEKIKAAL-TEKEVLLKEIHHRVKnNLQIISSLLDLQAEKLHD 636

                        170       180       190
                 ....*....|....*....|....*....|..
gi 759432114 176 LAETDSLTGAASRYRleqAVRLEHERAKRFKE 207
Cdd:PRK13560 637 EEAKCAFAESQDRIC---AMALAHEKLYQSED 665
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
 93-134 3.68e-03

Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif occurs C-terminal to a subset of all known PAS motifs. It is proposed to contribute to the PAS domain fold.


Pssm-ID: 197509  Cd Length: 43  Bit Score: 34.85  E-value: 3.68e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 759432114    93 EYRCRCRNGDYLWVADCGRIVtRNPDGSVARMVGAHRNIHAQ 134
Cdd:smart00086   3 EYRLRRKDGSYIWVLVSASPI-RDEDGEVEGILGVVRDITER 43
 
Name Accession Description Interval E-value
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 125-330 7.37e-55

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: 180.56  E-value: 7.37e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432114 125 VGAHRNIHAQRELYARLELQNRTLEQQVAQRTAELERLNQaLQFQVEENRRLAETDSLTGAASRYRLEQAVRLEHERAKR 204
Cdd:COG2199   63 LLLALGLLLLALLLLSLVLELLLLLLALLLLLLALEDITE-LRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARR 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432114 205 FKEPFAVIAMDVDDFKQINDRHGHGVGDQTLIDIVQLTRGCIREIDLLARWGGDEFMLVLPNTRLPDARVVAEKLRQRLS 284
Cdd:COG2199  142 EGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALE 221

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 759432114 285 HARVKGIE---PVTLSFGLVESDPD-EQVSHLMARVDRALYRAKLAGKDQ 330
Cdd:COG2199  222 QLPFELEGkelRVTVSIGVALYPEDgDSAEELLRRADLALYRAKRAGRNR 271
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 179-330 1.40e-52

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: 170.43  E-value: 1.40e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432114 179 TDSLTGAASRYRLEQAVRLEHERAKRFKEPFAVIAMDVDDFKQINDRHGHGVGDQTLIDIVQLTRGCIREIDLLARWGGD 258
Cdd:cd01949    2 TDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGD 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 759432114 259 EFMLVLPNTRLPDARVVAEKLRQRLSHARVKGIE--PVTLSFGLVESDPD-EQVSHLMARVDRALYRAKLAGKDQ 330
Cdd:cd01949   82 EFAILLPGTDLEEAEALAERLREAIEEPFFIDGQeiRVTASIGIATYPEDgEDAEELLRRADEALYRAKRSGRNR 156
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 177-330 1.98e-47

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: 157.41  E-value: 1.98e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432114  177 AETDSLTGAASRYRLEQAVRLEHERAKRFKEPFAVIAMDVDDFKQINDRHGHGVGDQTLIDIVQLTRGCIREIDLLARWG 256
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432114  257 GDEFMLVLPNTRLPDARVVAEKLRQRLSHAR----VKGIE-PVTLSFGLVESDPD-EQVSHLMARVDRALYRAKLAGKDQ 330
Cdd:pfam00990  81 GDEFAILLPETSLEGAQELAERIRRLLAKLKiphtVSGLPlYVTISIGIAAYPNDgEDPEDLLKRADTALYQAKQAGRNR 160
diguan_SiaD NF038266
biofilm regulation diguanylate cyclase SiaD;
121-331 2.41e-43

biofilm regulation diguanylate cyclase SiaD;


Pssm-ID: 468439 [Multi-domain]  Cd Length: 252  Bit Score: 149.75  E-value: 2.41e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432114 121 VARMVGAHRNIHAQRE--LYARLELQNRTLEQ--QVAQRTAELER-LNQALqfqveenRRLAETDSLTGAASRYRLEQAV 195
Cdd:NF038266  40 LTRISDGYQSAARERElsLAERYDRQLRRLEKivRISDRYQRMMRdLNEAL-------REASTRDPLTGLPNRRLLMERL 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432114 196 RLEHERAKRFKEPFAVIAMDVDDFKQINDRHGHGVGDQTLIDIVQLTRGCIREIDLLARWGGDEFMLVLPNTRLPDARVV 275
Cdd:NF038266 113 REEVERARRSGRPFTLAMLDVDHFKRINDRYGHEVGDRVLVEIARTLRAELREYDLCGRWGGEEFLLLLPETGLEEAQVV 192

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432114 276 AEKLRQRLSHARVKGIEP---VTLSFGLVESDPDEQ-VSHLMARVDRALYRAKLAGKDQL 331
Cdd:NF038266 193 LERLREAVRALAVRVGDDvlsVTASAGLAEHRPPEEgLSATLSRADQALYQAKRAGRDRV 252
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 175-333 8.02e-43

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 145.47  E-value: 8.02e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432114   175 RLAETDSLTGAASRYRLEQAVRLEHERAKRFKEPFAVIAMDVDDFKQINDRHGHGVGDQTLIDIVQLTRGCIREIDLLAR 254
Cdd:smart00267   1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432114   255 WGGDEFMLVLPNTRLPDARVVAEKLRQRLS-HARVKGIE-PVTLSFGLVE-SDPDEQVSHLMARVDRALYRAKLAGKDQL 331
Cdd:smart00267  81 LGGDEFALLLPETSLEEAIALAERILQQLRePIIIHGIPlYLTISIGVAAyPNPGEDAEDLLKRADTALYQAKKAGRNQV 160


                   ..
gi 759432114   332 SG 333
Cdd:smart00267 161 AV 162
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 128-330 7.75e-39

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: 145.69  E-value: 7.75e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432114 128 HRNIHAQRELYARLELQNRTLEQQVAQRTAELERLNQALQFQVEENRRLAETDSLTGAASRYRLEQavRLEH--ERAKRF 205
Cdd:COG5001  202 GGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEERLRHLAYHDPLTGLPNRRLFLD--RLEQalARARRS 279

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432114 206 KEPFAVIAMDVDDFKQINDRHGHGVGDQTLIDIVQLTRGCIREIDLLARWGGDEFMLVLPNTR-LPDARVVAEKLRQRLS 284
Cdd:COG5001  280 GRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVLLPDLDdPEDAEAVAERILAALA 359

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 759432114 285 HA-RVKGIE-PVTLSFGLVESDPD-EQVSHLMARVDRALYRAKLAGKDQ 330
Cdd:COG5001  360 EPfELDGHElYVSASIGIALYPDDgADAEELLRNADLAMYRAKAAGRNR 408
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 176-328 4.11e-36

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: 128.22  E-value: 4.11e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432114  176 LAETDSLTGAASRYRLEQAVRLEHERAKRFKEPFAVIAMDVDDFKQINDRHGHGVGDQTLIDIVQLTRGCIREIDLLARW 255
Cdd:TIGR00254   1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 759432114  256 GGDEFMLVLPNTRLPDARVVAEKLRQRLSHAR--VKGIEPVTL--SFGLVESDPD-EQVSHLMARVDRALYRAKLAGK 328
Cdd:TIGR00254  81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPieVAGSETLTVtvSIGVACYPGHgLTLEELLKRADEALYQAKKAGR 158
pleD PRK09581
response regulator PleD; Reviewed
 136-330 2.77e-35

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 133.10  E-value: 2.77e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432114 136 ELYARLELQNRTleqqvaqrtaelERLNQALQFQVEENRRLAETDSLTGAASRYRLEQAVRLEHERAKRFKEPFAVIAMD 215
Cdd:PRK09581 263 ELLARVRTQIRR------------KRYQDALRNNLEQSIEMAVTDGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMID 330

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432114 216 VDDFKQINDRHGHGVGDQTLIDIVQLTRGCIREIDLLARWGGDEFMLVLPNTRLPDARVVAEKLRQRLSH---ARVKGIE 292
Cdd:PRK09581 331 IDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARYGGEEFVVVMPDTDIEDAIAVAERIRRKIAEepfIISDGKE 410

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 759432114 293 P--VTLSFGLVESDP-DEQVSHLMARVDRALYRAKLAGKDQ 330
Cdd:PRK09581 411 RlnVTVSIGVAELRPsGDTIEALIKRADKALYEAKNTGRNR 451
PRK15426 PRK15426
cellulose biosynthesis regulator YedQ;
162-330 6.05e-34

cellulose biosynthesis regulator YedQ;


Pssm-ID: 237964 [Multi-domain]  Cd Length: 570  Bit Score: 130.91  E-value: 6.05e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432114 162 LNQALQFQveenrrlAETDSLTGAASRYRLEQAVRLEHERAKRFKEPFAVIAMDVDDFKQINDRHGHGVGDQTLIDIVQL 241
Cdd:PRK15426 390 LQSSLQWQ-------AWHDPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGL 462

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432114 242 TRGCIREIDLLARWGGDEFMLVLPNTRLPDARVVAEKLRQRLSHARVKGIEPVTL----SFGLVESDPDE--QVSHLMAR 315
Cdd:PRK15426 463 ISSSLRAQDVAGRVGGEEFCVVLPGASLAEAAQVAERIRLRINEKEILVAKSTTIrisaSLGVSSAEEDGdyDFEQLQSL 542

                        170
                 ....*....|....*
gi 759432114 316 VDRALYRAKLAGKDQ 330
Cdd:PRK15426 543 ADRRLYLAKQAGRNR 557
PRK09894 PRK09894
diguanylate cyclase; Provisional
 121-329 1.90e-32

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 122.48  E-value: 1.90e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432114 121 VARMVGAHRNIHAQ-RELYARLELQNRTLEQQVAQRTAELERLNQALQFQVEENRRLAETDSLTGAASRYRLEQAvrLEH 199
Cdd:PRK09894  72 VRLLDSAHQHMHNCaRELLLAIVEGHWQDAHFDAFQEGLLSFTAALTDYKIYLLTIRSNMDVLTGLPGRRVLDES--FDH 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432114 200 ERAKRFKEPFAVIAMDVDDFKQINDRHGHGVGDQTLIDIVQLTRGCIREIDLLARWGGDEFMLVLPNTRLPDARVVAEKL 279
Cdd:PRK09894 150 QLRNREPQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGGEEFIICLKAATDEEACRAGERI 229

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 759432114 280 RQRLSHARV---KGIEPVTLSFGLVESDPDEQVSHLMARVDRALYRAKLAGKD 329
Cdd:PRK09894 230 RQLIANHAIthsDGRINITATFGVSRAFPEETLDVVIGRADRAMYEGKQTGRN 282
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 28-332 2.03e-24

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 103.98  E-value: 2.03e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432114   28 GLWDWNANTGYVHRYPGWYQMLGYEPHSLDnTVFTWENLIHPDDLAQVMESFDACLSGRAAdYRAEYRCRCRNGDYLWVA 107
Cdd:PRK09776  422 GIWEWDLKPNIISWDKRMFELYEIPPHIKP-TWQVWYACLHPEDRQRVEKEIRDALQGRSP-FKLEFRIVVKDGVRHIRA 499

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432114  108 DCGRivTRNPDGSVARMVGAHRNIHAQRELY------------------------------------------------- 138
Cdd:PRK09776  500 LANR--VLNKDGEVERLLGINMDMTEVRQLNealfqekerlhitldsigeavvctdmamkvtfmnpvaekmtgwtqeeal 577

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432114  139 -------------------------------ARLE----LQNRTLEQQVAQ------RTAELERLNQALQFQ-VEENRRL 176
Cdd:PRK09776  578 gvplltvlhitfgdngplmeniyscltsrsaAYLEqdvvLHCRSGGSYDVHysitplSTLDGENIGSVLVIQdVTESRKM 657

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432114  177 -------AETDSLTGAASRYRLE-------QAVRLEHERAkrfkepfAVIAMDVDDFKQINDRHGHGVGDQTLIDIVQLT 242
Cdd:PRK09776  658 lrqlsysASHDALTHLANRASFEkqlrrllQTVNSTHQRH-------ALVFIDLDRFKAVNDSAGHAAGDALLRELASLM 730

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432114  243 RGCIREIDLLARWGGDEFMLVLPNTRLPDARVVAEKL------RQRLSHARVkgiEPVTLSFGLVESDPDE-QVSHLMAR 315
Cdd:PRK09776  731 LSMLRSSDVLARLGGDEFGLLLPDCNVESARFIATRIisaindYHFPWEGRV---YRVGASAGITLIDANNhQASEVMSQ 807

                         410
                  ....*....|....*..
gi 759432114  316 VDRALYRAKLAGKDQLS 332
Cdd:PRK09776  808 ADIACYAAKNAGRGRVT 824
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 38-128 3.72e-24

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.


Pssm-ID: 430001 [Multi-domain]  Cd Length: 89  Bit Score: 94.33  E-value: 3.72e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432114   38 YVHRYPGWYQMLGYEPHSLDNTVFTWENLIHPDDLAQVMESFDACLSGRaADYRAEYRCRCRNGDYLWVADCGRIVtRNP 117
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELLGKGESWLDLVHPDDRERVREALWEALKGG-EPYSGEYRIRRKDGEYRWVEARARPI-RDE 78

                          90
                  ....*....|.
gi 759432114  118 DGSVARMVGAH 128
Cdd:pfam08447  79 NGKPVRVIGVA 89
adrA PRK10245
diguanylate cyclase AdrA; Provisional
 151-330 2.63e-20

diguanylate cyclase AdrA; Provisional


Pssm-ID: 182329 [Multi-domain]  Cd Length: 366  Bit Score: 90.27  E-value: 2.63e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432114 151 QVAQRTAELERlnqalQFQVEENRrlaetDSLTGAASRYRLEQAVRLEHERAKRFKEPFAVIAMDVDDFKQINDRHGHGV 230
Cdd:PRK10245 189 QTATKLAEHKR-----RLQVMSTR-----DGMTGVYNRRHWETLLRNEFDNCRRHHRDATLLIIDIDHFKSINDTWGHDV 258

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432114 231 GDQTLIDIVQLTRGCIREIDLLARWGGDEFMLVLPNTRLPDARVVAEKLRQRLSHARVKGIEPVTL--SFGLVESDPdeQ 308
Cdd:PRK10245 259 GDEAIVALTRQLQITLRGSDVIGRFGGDEFAVIMSGTPAESAITAMSRVHEGLNTLRLPNAPQVTLriSVGVAPLNP--Q 336

                        170       180
                 ....*....|....*....|....*
gi 759432114 309 VSHL---MARVDRALYRAKLAGKDQ 330
Cdd:PRK10245 337 MSHYrewLKSADLALYKAKNAGRNR 361
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
160-330 9.64e-18

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 83.96  E-value: 9.64e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432114 160 ERLNQalqfqvEENRRLAETDSLTGAASRYRLEQAVRleHERAKRFKEPFAVIAMDVDDFKQINDRHGHGVGDQTLIDIV 239
Cdd:PRK10060 226 ERRAQ------ERLRILANTDSITGLPNRNAIQELID--HAINAADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVS 297

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432114 240 QLTRGCIREIDLLARWGGDEFMLVLPNTRLPDARVVAEKLRQRLSHA-RVKGIEPVT-LSFGLVESdPD--EQVSHLMAR 315
Cdd:PRK10060 298 LAILSCLEEDQTLARLGGDEFLVLASHTSQAALEAMASRILTRLRLPfRIGLIEVYTgCSIGIALA-PEhgDDSESLIRS 376

                        170
                 ....*....|....*
gi 759432114 316 VDRALYRAKLAGKDQ 330
Cdd:PRK10060 377 ADTAMYTAKEGGRGQ 391
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 246-324 1.19e-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: 73.79  E-value: 1.19e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 759432114 246 IREIDLLARWGGDEFMLVLPNTRLPDARVVAEKLRQRLSHARVkgiEPVTLSFGLVESDpdeqvshLMARVDrALYRAK 324
Cdd:COG3706  112 LARVDLVARYGGEEFAILLPGTDLEGALAVAERIREAVAELPS---LRVTVSIGVAGDS-------LLKRAD-ALYQAR 179
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 151-280 2.05e-10

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 61.71  E-value: 2.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432114 151 QVAQRTAELERLNQ------ALQFQVEENR----RLAETDSLTGAASRYRLEQAVR--LEHERakrfkePFAVIAMDVDD 218
Cdd:PRK11359 340 SGAETSAFIERVADisqhlaALALEQEKSRqhieQLIQFDPLTGLPNRNNLHNYLDdlVDKAV------SPVVYLIGVDH 413

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 759432114 219 FKQINDRHGHGVGDQTLIDIVQLTRGCIREIDLLARWGGDEFMLVLPNTRLPDARVVAEKLR 280
Cdd:PRK11359 414 FQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGTQFVLVSLENDVSNITQIADELR 475
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
 208-300 2.25e-09

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: 55.05  E-value: 2.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432114 208 PFAVIAMDVDDFKQINDRHGHGVGDQTLIDIVQL-TRGCIREIDLLARWGGDEFMLVLPNTRLPDARVVAEKLRQRLSHA 286
Cdd:cd07556    1 PVTILFADIVGFTSLADALGPDEGDELLNELAGRfDSLIRRSGDLKIKTIGDEFMVVSGLDHPAAAVAFAEDMREAVSAL 80

                         90
                 ....*....|....
gi 759432114 287 RVKGIEPVTLSFGL 300
Cdd:cd07556   81 NQSEGNPVRVRIGI 94
PAS COG2202
PAS domain [Signal transduction mechanisms];
21-141 1.06e-08

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 55.42  E-value: 1.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432114  21 MLEVVSDGLWDWNANTGYVHRYPGWYQMLGYEPHSLDNTvfTWENLIHPDDLAQVMESFDACLSGRAADYRAEYRCRCRN 100
Cdd:COG2202  142 LVENAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGK--SLLDLLHPEDRERLLELLRRLLEGGRESYELELRLKDGD 219

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 759432114 101 GDYLWVAdcGRIVTRNPDGSVARMVGAHRNIHAQRELYARL 141
Cdd:COG2202  220 GRWVWVE--ASAVPLRDGGEVIGVLGIVRDITERKRAEEAL 258
PAS COG2202
PAS domain [Signal transduction mechanisms];
21-178 1.35e-08

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 55.03  E-value: 1.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432114  21 MLEVVSDGLWDWNANTGYVHRYPGWYQMLGYEPHSLDNTvfTWENLIHPDDLAQVMESFDACLSGRAAdYRAEYRCRCRN 100
Cdd:COG2202   16 LVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGK--TLRDLLPPEDDDEFLELLRAALAGGGV-WRGELRNRRKD 92

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 759432114 101 GDYLWVADCGRIVtRNPDGSVARMVGAHRNIHAQRELYARLELQNRTLEQQVAQRTAELERLNQALQFqVEENRRLAE 178
Cdd:COG2202   93 GSLFWVELSISPV-RDEDGEITGFVGIARDITERKRAEEALRESEERLRLLVENAPDGIFVLDLDGRI-LYVNPAAEE 168
PRK09966 PRK09966
diguanylate cyclase DgcN;
145-324 8.07e-08

diguanylate cyclase DgcN;


Pssm-ID: 182171 [Multi-domain]  Cd Length: 407  Bit Score: 53.47  E-value: 8.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432114 145 NRTLEQQVA-QRTAELERLNQ---ALQFQVEE--------NRRLAET---DSLTGAASRYRLEQAVR-LEHERAKRFKEp 208
Cdd:PRK09966 201 NRNFSRRVSeERIAEFHRFALdfnSLLDEMEEwqlrlqakNAQLLRTalhDPLTGLANRAAFRSGINtLMNNSDARKTS- 279

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432114 209 fAVIAMDVDDFKQINDRHGHGVGDQTLIDIVQLTR--GCIREIDLlaRWGGDEFMLVLPNtrlpdarVVAEKLRQRLSHA 286
Cdd:PRK09966 280 -ALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAefGGLRHKAY--RLGGDEFAMVLYD-------VQSESEVQQICSA 349

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 759432114 287 RVKGIE-----------PVTLSFGLVESDPDEQVSHLMARVDRALYRAK 324
Cdd:PRK09966 350 LTQIFNlpfdlhnghqtTMTLSIGYAMTIEHASAEKLQELADHNMYQAK 398
Cas10 COG1353
CRISPR/Cas system-associated protein Cas10, large subunit of type III CRISPR-Cas systems, ...
 158-329 2.64e-07

CRISPR/Cas system-associated protein Cas10, large subunit of type III CRISPR-Cas systems, contains HD superfamily nuclease domain [Defense mechanisms]; CRISPR/Cas system-associated protein Cas10, large subunit of type III CRISPR-Cas systems, contains HD superfamily nuclease domain is part of the Pathway/BioSystem: CRISPR-Cas system


Pssm-ID: 440964 [Multi-domain]  Cd Length: 477  Bit Score: 52.06  E-value: 2.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432114 158 ELERLNQALQFQVEENRRLAETdsltgaASRYRLEQAVRLEH-ERAKRFKEPF-AVIAMDVDD----FKQINDRhghgvg 231
Cdd:COG1353  204 KLKELYLLNDGELLEERLLANY------VPKKKLEEPKTLEElAEKSGEGIPYlAVLKADGDNmgkiFSGEKEA------ 271

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432114 232 dqTLIDIVQLTR-------GCIREIdlLARW---------GGDEFMLVLPntrLPDARVVAEKLRQRLShARVKGIEP-V 294
Cdd:COG1353  272 --TPSRHATLSRalslffkKAVNEI--VEELrhngyviyaGGDDVLAIGP---WDEALEFARELREAFE-EYTGNLNPeI 343

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 759432114 295 TLSFGLVESDPDEQVSHLMARVDRALYRAK---LAGKD 329
Cdd:COG1353  344 TLSAGIVIAHPKYPLYRALELAEELLKKAKkvsEKGKN 381
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 26-131 3.62e-06

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 44.93  E-value: 3.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432114  26 SDGLWDWNANTGYVHRYPGWYQMLGYEPHSLDNTvfTWENLIHPDDLAQVMESFDACLSGRaADYRAEYRCRCRNGDYLW 105
Cdd:cd00130    2 PDGVIVLDLDGRILYANPAAEQLLGYSPEELIGK--SLLDLIHPEDREELRERLENLLSGG-EPVTLEVRLRRKDGSVIW 78

                         90       100
                 ....*....|....*....|....*.
gi 759432114 106 VAdCGRIVTRNPDGSVARMVGAHRNI 131
Cdd:cd00130   79 VL-VSLTPIRDEGGEVIGLLGVVRDI 103
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
 20-141 3.21e-05

PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions]


Pssm-ID: 272971 [Multi-domain]  Cd Length: 124  Bit Score: 42.66  E-value: 3.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432114   20 GMLEVVSDGLW-DWNantgyvhryPGWYQMLGYEPHSLDNTvfTWENLIHPDDLAQVMESFDACLSGRAADYRAEYRCRC 98
Cdd:TIGR00229  15 AIIVIDLEGNIlYVN---------PAFEEIFGYSAEELIGR--NVLELIPEEDREEVRERIERRLEGEPEPVSEERRVRR 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 759432114   99 RNGDYLWVADCGRIVTRNpdGSVARMVGAHRNIHAQRELYARL 141
Cdd:TIGR00229  84 KDGSEIWVEVSVSPIRTN--GGELGVVGIVRDITERKEAEEAL 124
PRK13560 PRK13560
hypothetical protein; Provisional
 29-207 1.70e-04

hypothetical protein; Provisional


Pssm-ID: 106506 [Multi-domain]  Cd Length: 807  Bit Score: 43.51  E-value: 1.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432114  29 LWDWNANtgyvhryPGWYQML--------GYEPHSLDNTVFTWENLIHPDDLAQVMESFDACLSGRAADYRAEYRCRCRN 100
Cdd:PRK13560 486 LFRWKAE-------EGWPVELvsknitqfGYEPDEFISGKRMFAAIIHPADLEQVAAEVAEFAAQGVDRFEQEYRILGKG 558

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432114 101 GDYLWVADCGRiVTRNPDGSVARMVGAHRNI----HAQRELYARLeLQNRTLEQQVAQRTA-ELERLNQALQFQVEENRR 175
Cdd:PRK13560 559 GAVCWIDDQSA-AERDEEGQISHFEGIVIDIserkHAEEKIKAAL-TEKEVLLKEIHHRVKnNLQIISSLLDLQAEKLHD 636

                        170       180       190
                 ....*....|....*....|....*....|..
gi 759432114 176 LAETDSLTGAASRYRleqAVRLEHERAKRFKE 207
Cdd:PRK13560 637 EEAKCAFAESQDRIC---AMALAHEKLYQSED 665
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
 93-134 3.68e-03

Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif occurs C-terminal to a subset of all known PAS motifs. It is proposed to contribute to the PAS domain fold.


Pssm-ID: 197509  Cd Length: 43  Bit Score: 34.85  E-value: 3.68e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 759432114    93 EYRCRCRNGDYLWVADCGRIVtRNPDGSVARMVGAHRNIHAQ 134
Cdd:smart00086   3 EYRLRRKDGSYIWVLVSASPI-RDEDGEVEGILGVVRDITER 43
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 21-84 6.28e-03

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.


Pssm-ID: 214512  Cd Length: 67  Bit Score: 34.68  E-value: 6.28e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 759432114    21 MLEVVSDGLWDWNANTGYVHRYPGWYQMLGYEPHSLDNTvfTWENLIHPDDLAQVMESFDACLS 84
Cdd:smart00091   6 ILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGK--SLLELIHPEDRERVQEALQRLLS 67
PRK10600 PRK10600
nitrate/nitrite two-component system sensor histidine kinase NarX;
146-176 8.15e-03

nitrate/nitrite two-component system sensor histidine kinase NarX;


Pssm-ID: 182581 [Multi-domain]  Cd Length: 569  Bit Score: 37.73  E-value: 8.15e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 759432114 146 RTLEQQVAQRTAELERLNQALQFQVEENRRL 176
Cdd:PRK10600 199 AVLEQRVQEKTAGLEQKNQILSFLWQANRRL 229
 
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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