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Conserved domains on  [gi|1831082346|ref|WP_168345455|]
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MULTISPECIES: diguanylate cyclase [Rhizobium]

Protein Classification

sensor domain-containing diguanylate cyclase( domain architecture ID 13413304)

sensor domain-containing diguanylate cyclase (GGDEF) with a GAF family sensor domain

CATH:  3.30.450.40|3.30.70.1230
EC:  2.7.7.65
Gene Ontology:  GO:0005525|GO:0005886|GO:0005515|GO:0046872|GO:0052621|GO:0007165
PubMed:  16166544|9433123
SCOP:  4001852|4001316

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: ...
 352-513 5.07e-58

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: 190.08  E-value: 5.07e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831082346 352 QTDLLTGLYNRRGFEVAASALLTQAEHGSRGISVVLFDLDHFKKINDVHGHDAGDAVLRQVAGIARQNFRSFDLLVRHGG 431
Cdd:cd01949     1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831082346 432 EEFLALLPDSTPDDAAIVAERVRLAIEaaEIPLPSGDVLKVTASFGCAgrANEVSNRNFEDLVKRADLALYAAKASGRNC 511
Cdd:cd01949    81 DEFAILLPGTDLEEAEALAERLREAIE--EPFFIDGQEIRVTASIGIA--TYPEDGEDAEELLRRADEALYRAKRSGRNR 156


                  ..
gi 1831082346 512 VV 513
Cdd:cd01949   157 VV 158
COG5001 super family cl34859
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 103-513 3.39e-44

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


The actual alignment was detected with superfamily member COG5001:

Pssm-ID: 444025 [Multi-domain]  Cd Length: 678  Bit Score: 166.10  E-value: 3.39e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831082346 103 RDALDEGLVGELSILSLAYSRIVATRSAVDHGRYAGSDPGSIYWYAALKQLAVVDALSPLISDPVLLEKSNQLMGILLTY 182
Cdd:COG5001     3 ALAALLLLLLALLLALLLLALLLLALLLAALLALALLLLLLLLLLALLLAALLLLALLALLALLLLAAALLALALAALLL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831082346 183 YGERLITGIGTRYLNQGVSARLPVELFVQGKVMLGEGMDHMVFHSSAPVVRNIVAYLGRSSQVKANAITDAILAGSRPTP 262
Cdd:COG5001    83 AALLAALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARALL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831082346 263 AVHDVWAAAQSERMAFLQQKMIEAAQDIHETGENLSTRSHIHLTRILALCAGLLILATLVLLLAAKGLRLIDRLTQDRET 342
Cdd:COG5001   163 ALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKR 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831082346 343 LVGELRSAAQTDLLTGLYNRRGFEVAASALLTQAEHGSRGISVVLFDLDHFKKINDVHGHDAGDAVLRQVAGIARQNFRS 422
Cdd:COG5001   243 AEERLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLRE 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831082346 423 FDLLVRHGGEEFLALLPD-STPDDAAIVAERVRLAIEAaeiPLP-SGDVLKVTASFGCAGRANEvsNRNFEDLVKRADLA 500
Cdd:COG5001   323 GDTVARLGGDEFAVLLPDlDDPEDAEAVAERILAALAE---PFElDGHELYVSASIGIALYPDD--GADAEELLRNADLA 397

                         410
                  ....*....|...
gi 1831082346 501 LYAAKASGRNCVV 513
Cdd:COG5001   398 MYRAKAAGRNRYR 410
 
Name Accession Description Interval E-value
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 352-513 5.07e-58

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: 190.08  E-value: 5.07e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831082346 352 QTDLLTGLYNRRGFEVAASALLTQAEHGSRGISVVLFDLDHFKKINDVHGHDAGDAVLRQVAGIARQNFRSFDLLVRHGG 431
Cdd:cd01949     1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831082346 432 EEFLALLPDSTPDDAAIVAERVRLAIEaaEIPLPSGDVLKVTASFGCAgrANEVSNRNFEDLVKRADLALYAAKASGRNC 511
Cdd:cd01949    81 DEFAILLPGTDLEEAEALAERLREAIE--EPFFIDGQEIRVTASIGIA--TYPEDGEDAEELLRRADEALYRAKRSGRNR 156


                  ..
gi 1831082346 512 VV 513
Cdd:cd01949   157 VV 158
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 235-513 8.68e-58

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: 193.66  E-value: 8.68e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831082346 235 IVAYLGRSSQVKANAITDAILAGSRPTPAVHDVWAAAQSERMAFLQQKMIEAAQDIHETGENLSTRSHIHLTRILALCAG 314
Cdd:COG2199     2 LLLLLLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831082346 315 LLILATLVLLLAAKGLRLIDRLTQDREtlvgELRSAAQTDLLTGLYNRRGFEVAASALLTQAEHGSRGISVVLFDLDHFK 394
Cdd:COG2199    82 ELLLLLLALLLLLLALEDITELRRLEE----RLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831082346 395 KINDVHGHDAGDAVLRQVAGIARQNFRSFDLLVRHGGEEFLALLPDSTPDDAAIVAERVRLAIEAAEIPLPsGDVLKVTA 474
Cdd:COG2199   158 RINDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELE-GKELRVTV 236

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1831082346 475 SFGCAGRANEvsNRNFEDLVKRADLALYAAKASGRNCVV 513
Cdd:COG2199   237 SIGVALYPED--GDSAEELLRRADLALYRAKRAGRNRVV 273
pleD PRK09581
response regulator PleD; Reviewed
 351-514 1.34e-51

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 182.79  E-value: 1.34e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831082346 351 AQTDLLTGLYNRRGFEVAASALLTQAEHGSRGISVVLFDLDHFKKINDVHGHDAGDAVLRQVAGIARQNFRSFDLLVRHG 430
Cdd:PRK09581  292 AVTDGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARYG 371

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831082346 431 GEEFLALLPDSTPDDAAIVAERVRLAIEAAEIPLPSGDV-LKVTASFGCAGRANEVSnrNFEDLVKRADLALYAAKASGR 509
Cdd:PRK09581  372 GEEFVVVMPDTDIEDAIAVAERIRRKIAEEPFIISDGKErLNVTVSIGVAELRPSGD--TIEALIKRADKALYEAKNTGR 449


                  ....*
gi 1831082346 510 NCVVS 514
Cdd:PRK09581  450 NRVVA 454
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 351-511 3.29e-50

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: 169.74  E-value: 3.29e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831082346 351 AQTDLLTGLYNRRGFEVAASALLTQAEHGSRGISVVLFDLDHFKKINDVHGHDAGDAVLRQVAGIARQNFRSFDLLVRHG 430
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831082346 431 GEEFLALLPDSTPDDAAIVAERVRLAIEAAEIPLP-SGDVLKVTASFGCAgrANEVSNRNFEDLVKRADLALYAAKASGR 509
Cdd:pfam00990  81 GDEFAILLPETSLEGAQELAERIRRLLAKLKIPHTvSGLPLYVTISIGIA--AYPNDGEDPEDLLKRADTALYQAKQAGR 158


                  ..
gi 1831082346 510 NC 511
Cdd:pfam00990 159 NR 160
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 351-513 1.38e-49

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: 168.28  E-value: 1.38e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831082346 351 AQTDLLTGLYNRRGFEVAASALLTQAEHGSRGISVVLFDLDHFKKINDVHGHDAGDAVLRQVAGIARQNFRSFDLLVRHG 430
Cdd:TIGR00254   2 AVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831082346 431 GEEFLALLPDSTPDDAAIVAERVRLAIEAAEIPLPSGDVLKVTASFGCAGRANEvsNRNFEDLVKRADLALYAAKASGRN 510
Cdd:TIGR00254  82 GEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSETLTVTVSIGVACYPGH--GLTLEELLKRADEALYQAKKAGRN 159


                  ...
gi 1831082346 511 CVV 513
Cdd:TIGR00254 160 RVV 162
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 351-513 8.86e-47

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 160.88  E-value: 8.86e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831082346  351 AQTDLLTGLYNRRGFEVAASALLTQAEHGSRGISVVLFDLDHFKKINDVHGHDAGDAVLRQVAGIARQNFRSFDLLVRHG 430
Cdd:smart00267   3 AFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARLG 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831082346  431 GEEFLALLPDSTPDDAAIVAERVRLAIEaaEIPLPSGDVLKVTASFGCAgrANEVSNRNFEDLVKRADLALYAAKASGRN 510
Cdd:smart00267  83 GDEFALLLPETSLEEAIALAERILQQLR--EPIIIHGIPLYLTISIGVA--AYPNPGEDAEDLLKRADTALYQAKKAGRN 158


                   ...
gi 1831082346  511 CVV 513
Cdd:smart00267 159 QVA 161
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 103-513 3.39e-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: 166.10  E-value: 3.39e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831082346 103 RDALDEGLVGELSILSLAYSRIVATRSAVDHGRYAGSDPGSIYWYAALKQLAVVDALSPLISDPVLLEKSNQLMGILLTY 182
Cdd:COG5001     3 ALAALLLLLLALLLALLLLALLLLALLLAALLALALLLLLLLLLLALLLAALLLLALLALLALLLLAAALLALALAALLL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831082346 183 YGERLITGIGTRYLNQGVSARLPVELFVQGKVMLGEGMDHMVFHSSAPVVRNIVAYLGRSSQVKANAITDAILAGSRPTP 262
Cdd:COG5001    83 AALLAALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARALL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831082346 263 AVHDVWAAAQSERMAFLQQKMIEAAQDIHETGENLSTRSHIHLTRILALCAGLLILATLVLLLAAKGLRLIDRLTQDRET 342
Cdd:COG5001   163 ALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKR 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831082346 343 LVGELRSAAQTDLLTGLYNRRGFEVAASALLTQAEHGSRGISVVLFDLDHFKKINDVHGHDAGDAVLRQVAGIARQNFRS 422
Cdd:COG5001   243 AEERLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLRE 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831082346 423 FDLLVRHGGEEFLALLPD-STPDDAAIVAERVRLAIEAaeiPLP-SGDVLKVTASFGCAGRANEvsNRNFEDLVKRADLA 500
Cdd:COG5001   323 GDTVARLGGDEFAVLLPDlDDPEDAEAVAERILAALAE---PFElDGHELYVSASIGIALYPDD--GADAEELLRNADLA 397

                         410
                  ....*....|...
gi 1831082346 501 LYAAKASGRNCVV 513
Cdd:COG5001   398 MYRAKAAGRNRYR 410
diguan_SiaD NF038266
biofilm regulation diguanylate cyclase SiaD;
347-512 1.59e-43

biofilm regulation diguanylate cyclase SiaD;


Pssm-ID: 468439 [Multi-domain]  Cd Length: 252  Bit Score: 155.14  E-value: 1.59e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831082346 347 LRSAAQTDLLTGLYNRRGFEVAASALLTQAEHGSRGISVVLFDLDHFKKINDVHGHDAGDAVLRQVAGIARQNFRSFDLL 426
Cdd:NF038266   90 LREASTRDPLTGLPNRRLLMERLREEVERARRSGRPFTLAMLDVDHFKRINDRYGHEVGDRVLVEIARTLRAELREYDLC 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831082346 427 VRHGGEEFLALLPDSTPDDAAIVAERVRLAIEAAEIPlPSGDVLKVTASFGCAgrANEVSNRNFEDLVKRADLALYAAKA 506
Cdd:NF038266  170 GRWGGEEFLLLLPETGLEEAQVVLERLREAVRALAVR-VGDDVLSVTASAGLA--EHRPPEEGLSATLSRADQALYQAKR 246


                  ....*.
gi 1831082346 507 SGRNCV 512
Cdd:NF038266  247 AGRDRV 252
 
Name Accession Description Interval E-value
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 352-513 5.07e-58

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: 190.08  E-value: 5.07e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831082346 352 QTDLLTGLYNRRGFEVAASALLTQAEHGSRGISVVLFDLDHFKKINDVHGHDAGDAVLRQVAGIARQNFRSFDLLVRHGG 431
Cdd:cd01949     1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831082346 432 EEFLALLPDSTPDDAAIVAERVRLAIEaaEIPLPSGDVLKVTASFGCAgrANEVSNRNFEDLVKRADLALYAAKASGRNC 511
Cdd:cd01949    81 DEFAILLPGTDLEEAEALAERLREAIE--EPFFIDGQEIRVTASIGIA--TYPEDGEDAEELLRRADEALYRAKRSGRNR 156


                  ..
gi 1831082346 512 VV 513
Cdd:cd01949   157 VV 158
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 235-513 8.68e-58

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: 193.66  E-value: 8.68e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831082346 235 IVAYLGRSSQVKANAITDAILAGSRPTPAVHDVWAAAQSERMAFLQQKMIEAAQDIHETGENLSTRSHIHLTRILALCAG 314
Cdd:COG2199     2 LLLLLLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831082346 315 LLILATLVLLLAAKGLRLIDRLTQDREtlvgELRSAAQTDLLTGLYNRRGFEVAASALLTQAEHGSRGISVVLFDLDHFK 394
Cdd:COG2199    82 ELLLLLLALLLLLLALEDITELRRLEE----RLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831082346 395 KINDVHGHDAGDAVLRQVAGIARQNFRSFDLLVRHGGEEFLALLPDSTPDDAAIVAERVRLAIEAAEIPLPsGDVLKVTA 474
Cdd:COG2199   158 RINDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELE-GKELRVTV 236

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1831082346 475 SFGCAGRANEvsNRNFEDLVKRADLALYAAKASGRNCVV 513
Cdd:COG2199   237 SIGVALYPED--GDSAEELLRRADLALYRAKRAGRNRVV 273
pleD PRK09581
response regulator PleD; Reviewed
 351-514 1.34e-51

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 182.79  E-value: 1.34e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831082346 351 AQTDLLTGLYNRRGFEVAASALLTQAEHGSRGISVVLFDLDHFKKINDVHGHDAGDAVLRQVAGIARQNFRSFDLLVRHG 430
Cdd:PRK09581  292 AVTDGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARYG 371

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831082346 431 GEEFLALLPDSTPDDAAIVAERVRLAIEAAEIPLPSGDV-LKVTASFGCAGRANEVSnrNFEDLVKRADLALYAAKASGR 509
Cdd:PRK09581  372 GEEFVVVMPDTDIEDAIAVAERIRRKIAEEPFIISDGKErLNVTVSIGVAELRPSGD--TIEALIKRADKALYEAKNTGR 449


                  ....*
gi 1831082346 510 NCVVS 514
Cdd:PRK09581  450 NRVVA 454
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 351-511 3.29e-50

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: 169.74  E-value: 3.29e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831082346 351 AQTDLLTGLYNRRGFEVAASALLTQAEHGSRGISVVLFDLDHFKKINDVHGHDAGDAVLRQVAGIARQNFRSFDLLVRHG 430
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831082346 431 GEEFLALLPDSTPDDAAIVAERVRLAIEAAEIPLP-SGDVLKVTASFGCAgrANEVSNRNFEDLVKRADLALYAAKASGR 509
Cdd:pfam00990  81 GDEFAILLPETSLEGAQELAERIRRLLAKLKIPHTvSGLPLYVTISIGIA--AYPNDGEDPEDLLKRADTALYQAKQAGR 158


                  ..
gi 1831082346 510 NC 511
Cdd:pfam00990 159 NR 160
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 351-513 1.38e-49

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: 168.28  E-value: 1.38e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831082346 351 AQTDLLTGLYNRRGFEVAASALLTQAEHGSRGISVVLFDLDHFKKINDVHGHDAGDAVLRQVAGIARQNFRSFDLLVRHG 430
Cdd:TIGR00254   2 AVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831082346 431 GEEFLALLPDSTPDDAAIVAERVRLAIEAAEIPLPSGDVLKVTASFGCAGRANEvsNRNFEDLVKRADLALYAAKASGRN 510
Cdd:TIGR00254  82 GEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSETLTVTVSIGVACYPGH--GLTLEELLKRADEALYQAKKAGRN 159


                  ...
gi 1831082346 511 CVV 513
Cdd:TIGR00254 160 RVV 162
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 351-513 8.86e-47

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 160.88  E-value: 8.86e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831082346  351 AQTDLLTGLYNRRGFEVAASALLTQAEHGSRGISVVLFDLDHFKKINDVHGHDAGDAVLRQVAGIARQNFRSFDLLVRHG 430
Cdd:smart00267   3 AFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARLG 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831082346  431 GEEFLALLPDSTPDDAAIVAERVRLAIEaaEIPLPSGDVLKVTASFGCAgrANEVSNRNFEDLVKRADLALYAAKASGRN 510
Cdd:smart00267  83 GDEFALLLPETSLEEAIALAERILQQLR--EPIIIHGIPLYLTISIGVA--AYPNPGEDAEDLLKRADTALYQAKKAGRN 158


                   ...
gi 1831082346  511 CVV 513
Cdd:smart00267 159 QVA 161
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 103-513 3.39e-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: 166.10  E-value: 3.39e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831082346 103 RDALDEGLVGELSILSLAYSRIVATRSAVDHGRYAGSDPGSIYWYAALKQLAVVDALSPLISDPVLLEKSNQLMGILLTY 182
Cdd:COG5001     3 ALAALLLLLLALLLALLLLALLLLALLLAALLALALLLLLLLLLLALLLAALLLLALLALLALLLLAAALLALALAALLL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831082346 183 YGERLITGIGTRYLNQGVSARLPVELFVQGKVMLGEGMDHMVFHSSAPVVRNIVAYLGRSSQVKANAITDAILAGSRPTP 262
Cdd:COG5001    83 AALLAALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARALL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831082346 263 AVHDVWAAAQSERMAFLQQKMIEAAQDIHETGENLSTRSHIHLTRILALCAGLLILATLVLLLAAKGLRLIDRLTQDRET 342
Cdd:COG5001   163 ALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKR 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831082346 343 LVGELRSAAQTDLLTGLYNRRGFEVAASALLTQAEHGSRGISVVLFDLDHFKKINDVHGHDAGDAVLRQVAGIARQNFRS 422
Cdd:COG5001   243 AEERLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLRE 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831082346 423 FDLLVRHGGEEFLALLPD-STPDDAAIVAERVRLAIEAaeiPLP-SGDVLKVTASFGCAGRANEvsNRNFEDLVKRADLA 500
Cdd:COG5001   323 GDTVARLGGDEFAVLLPDlDDPEDAEAVAERILAALAE---PFElDGHELYVSASIGIALYPDD--GADAEELLRNADLA 397

                         410
                  ....*....|...
gi 1831082346 501 LYAAKASGRNCVV 513
Cdd:COG5001   398 MYRAKAAGRNRYR 410
diguan_SiaD NF038266
biofilm regulation diguanylate cyclase SiaD;
347-512 1.59e-43

biofilm regulation diguanylate cyclase SiaD;


Pssm-ID: 468439 [Multi-domain]  Cd Length: 252  Bit Score: 155.14  E-value: 1.59e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831082346 347 LRSAAQTDLLTGLYNRRGFEVAASALLTQAEHGSRGISVVLFDLDHFKKINDVHGHDAGDAVLRQVAGIARQNFRSFDLL 426
Cdd:NF038266   90 LREASTRDPLTGLPNRRLLMERLREEVERARRSGRPFTLAMLDVDHFKRINDRYGHEVGDRVLVEIARTLRAELREYDLC 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831082346 427 VRHGGEEFLALLPDSTPDDAAIVAERVRLAIEAAEIPlPSGDVLKVTASFGCAgrANEVSNRNFEDLVKRADLALYAAKA 506
Cdd:NF038266  170 GRWGGEEFLLLLPETGLEEAQVVLERLREAVRALAVR-VGDDVLSVTASAGLA--EHRPPEEGLSATLSRADQALYQAKR 246


                  ....*.
gi 1831082346 507 SGRNCV 512
Cdd:NF038266  247 AGRDRV 252
PRK15426 PRK15426
cellulose biosynthesis regulator YedQ;
330-514 1.63e-43

cellulose biosynthesis regulator YedQ;


Pssm-ID: 237964 [Multi-domain]  Cd Length: 570  Bit Score: 162.88  E-value: 1.63e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831082346 330 LRLIDRLTQDRETLVGELRSAAQTDLLTGLYNRRG-FEVAASALLTQAEHGsRGISVVLFDLDHFKKINDVHGHDAGDAV 408
Cdd:PRK15426  377 WYVIRRMVSNMFVLQSSLQWQAWHDPLTRLYNRGAlFEKARALAKRCQRDQ-QPFSVIQLDLDHFKSINDRFGHQAGDRV 455

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831082346 409 LRQVAGIARQNFRSFDLLVRHGGEEFLALLPDSTPDDAAIVAERVRLAIEAAEIPLPSGDVLKVTASFGCAGrANEVSNR 488
Cdd:PRK15426  456 LSHAAGLISSSLRAQDVAGRVGGEEFCVVLPGASLAEAAQVAERIRLRINEKEILVAKSTTIRISASLGVSS-AEEDGDY 534

                         170       180
                  ....*....|....*....|....*.
gi 1831082346 489 NFEDLVKRADLALYAAKASGRNCVVS 514
Cdd:PRK15426  535 DFEQLQSLADRRLYLAKQAGRNRVCA 560
PRK09894 PRK09894
diguanylate cyclase; Provisional
 347-513 1.16e-41

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 151.37  E-value: 1.16e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831082346 347 LRSAAQTDLLTGLYNRRGFEVAASALLTQAehGSRGISVVLFDLDHFKKINDVHGHDAGDAVLRQVAGIARQNFRSFDLL 426
Cdd:PRK09894  125 LTIRSNMDVLTGLPGRRVLDESFDHQLRNR--EPQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETV 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831082346 427 VRHGGEEFLALLPDSTPDDAAIVAERVRLAIEAAEIPLPSGDvLKVTASFGCAgRANEvsNRNFEDLVKRADLALYAAKA 506
Cdd:PRK09894  203 YRYGGEEFIICLKAATDEEACRAGERIRQLIANHAITHSDGR-INITATFGVS-RAFP--EETLDVVIGRADRAMYEGKQ 278


                  ....*..
gi 1831082346 507 SGRNCVV 513
Cdd:PRK09894  279 TGRNRVM 285
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 346-512 6.97e-29

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 121.70  E-value: 6.97e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831082346  346 ELRSAAQTDLLTGLYNRRGFEVAASALLTQA-EHGSRGiSVVLFDLDHFKKINDVHGHDAGDAVLRQVAGIARQNFRSFD 424
Cdd:PRK09776   660 QLSYSASHDALTHLANRASFEKQLRRLLQTVnSTHQRH-ALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSD 738

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831082346  425 LLVRHGGEEFLALLPDSTPDDAAIVAERVRLAIEAAEIPLpSGDVLKVTASFGCAgrANEVSNRNFEDLVKRADLALYAA 504
Cdd:PRK09776   739 VLARLGGDEFGLLLPDCNVESARFIATRIISAINDYHFPW-EGRVYRVGASAGIT--LIDANNHQASEVMSQADIACYAA 815


                   ....*...
gi 1831082346  505 KASGRNCV 512
Cdd:PRK09776   816 KNAGRGRV 823
adrA PRK10245
diguanylate cyclase AdrA; Provisional
 354-510 2.43e-20

diguanylate cyclase AdrA; Provisional


Pssm-ID: 182329 [Multi-domain]  Cd Length: 366  Bit Score: 92.58  E-value: 2.43e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831082346 354 DLLTGLYNRRGFEVAASALLTQAEHGSRGISVVLFDLDHFKKINDVHGHDAGD----AVLRQVagiaRQNFRSFDLLVRH 429
Cdd:PRK10245  208 DGMTGVYNRRHWETLLRNEFDNCRRHHRDATLLIIDIDHFKSINDTWGHDVGDeaivALTRQL----QITLRGSDVIGRF 283

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831082346 430 GGEEFlALLPDSTPDDAAIVA-ERVRLAIEAAEIPLPSGDVLKVtaSFGCAGRANEVSnrNFEDLVKRADLALYAAKASG 508
Cdd:PRK10245  284 GGDEF-AVIMSGTPAESAITAmSRVHEGLNTLRLPNAPQVTLRI--SVGVAPLNPQMS--HYREWLKSADLALYKAKNAG 358


                  ..
gi 1831082346 509 RN 510
Cdd:PRK10245  359 RN 360
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
334-514 1.01e-19

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 92.82  E-value: 1.01e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831082346 334 DRLTQDRetlvgeLRSAAQTDLLTGLYNRRGFEVAASALLTQAEHGSRGIsvVLFDLDHFKKINDVHGHDAGDAVLRQVA 413
Cdd:PRK10060  226 ERRAQER------LRILANTDSITGLPNRNAIQELIDHAINAADNNQVGI--VYLDLDNFKKVNDAYGHMFGDQLLQDVS 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831082346 414 GIARQNFRSFDLLVRHGGEEFLALLPDSTPDD----AAIVAERVRLAIEAAEIPLPSGdvlkvtASFGCAgRANEVSNrN 489
Cdd:PRK10060  298 LAILSCLEEDQTLARLGGDEFLVLASHTSQAAleamASRILTRLRLPFRIGLIEVYTG------CSIGIA-LAPEHGD-D 369

                         170       180
                  ....*....|....*....|....*..
gi 1831082346 490 FEDLVKRADLALYAAKASGRN--CVVS 514
Cdd:PRK10060  370 SESLIRSADTAMYTAKEGGRGqfCVFS 396
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
 383-507 1.99e-14

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: 70.08  E-value: 1.99e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831082346 383 ISVVLFDLDHFKKINDVHGHDAGDAVLRQVAGIARQN-FRSFDLLVRHGGEEFLALLPDSTPDDAAIVAERVRLAIEAae 461
Cdd:cd07556     2 VTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLiRRSGDLKIKTIGDEFMVVSGLDHPAAAVAFAEDMREAVSA-- 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1831082346 462 ipLPSGDVLKVTASFG-----CAGRANEVSNRN--FEDLVKRADLALYAAKAS 507
Cdd:cd07556    80 --LNQSEGNPVRVRIGihtgpVVVGVIGSRPQYdvWGALVNLASRMESQAKAG 130
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 424-505 2.49e-12

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


Pssm-ID: 442920 [Multi-domain]  Cd Length: 179  Bit Score: 65.32  E-value: 2.49e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831082346 424 DLLVRHGGEEFLALLPDSTPDDAAIVAERVRLAIEAAEiplpsgdVLKVTASFGCAGranevsnrnfEDLVKRADlALYA 503
Cdd:COG3706   116 DLVARYGGEEFAILLPGTDLEGALAVAERIREAVAELP-------SLRVTVSIGVAG----------DSLLKRAD-ALYQ 177


                  ..
gi 1831082346 504 AK 505
Cdd:COG3706   178 AR 179
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 352-510 5.16e-12

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 68.64  E-value: 5.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831082346 352 QTDLLTGLYNRRGFEVAASALLTQAehgsRGISVVLFDLDHFKKINDVHGHDAGDAVLRQVAGIARQNFRSFDLLVRHGG 431
Cdd:PRK11359  377 QFDPLTGLPNRNNLHNYLDDLVDKA----VSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEG 452

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1831082346 432 EEFLALLPDSTPDDAAIVAERVRlAIEAAEIPLpSGDVLKVTASFGCagrANEVSnRNFEDLVKRADLALYAAKASGRN 510
Cdd:PRK11359  453 TQFVLVSLENDVSNITQIADELR-NVVSKPIMI-DDKPFPLTLSIGI---SYDVG-KNRDYLLSTAHNAMDYIRKNGGN 525
PRK09966 PRK09966
diguanylate cyclase DgcN;
347-505 3.91e-09

diguanylate cyclase DgcN;


Pssm-ID: 182171 [Multi-domain]  Cd Length: 407  Bit Score: 58.86  E-value: 3.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831082346 347 LRSAAQtDLLTGLYNRRGFEVAASALLTqaEHGSRGISVVLF-DLDHFKKINDVHGHDAGDAVLRQVAGIARQNFRSFDL 425
Cdd:PRK09966  245 LRTALH-DPLTGLANRAAFRSGINTLMN--NSDARKTSALLFlDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHK 321

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831082346 426 LVRHGGEEFLALLPDSTPDDAaivAERVRLAI-EAAEIP--LPSGDVLKVTASFGCAGRANEVSNRNFEDLvkrADLALY 502
Cdd:PRK09966  322 AYRLGGDEFAMVLYDVQSESE---VQQICSALtQIFNLPfdLHNGHQTTMTLSIGYAMTIEHASAEKLQEL---ADHNMY 395


                  ...
gi 1831082346 503 AAK 505
Cdd:PRK09966  396 QAK 398
 
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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