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Conserved domains on  [gi|496892140|ref|WP_009399895|]
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sensor domain-containing diguanylate cyclase [Pseudomonas bharatica]

Protein Classification

sensor domain-containing diguanylate cyclase( domain architecture ID 13503960)

sensor domain-containing diguanylate cyclase with double PDC (PhoQ/DcuS/CitA) 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
PubMed:  11119645
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 ...
263-486 2.54e-65

GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants [Signal transduction mechanisms];


:

Pssm-ID: 441801 [Multi-domain]  Cd Length: 275  Bit Score: 212.53  E-value: 2.54e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496892140 263 LHFLNVRFIPELDWYLFVEKPVGASLDGVKQSLYLNLAICAIISAVVLAMINGMVRRHQDgIQELATLDSLTHLHNRRAF 342
Cdd:COG2199   50 LLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLLLLALEDITELRRLEER-LRRLATHDPLTGLPNRRAF 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496892140 343 DLLAAQALLDAERGALPLTAVLIDLDHFKELNDTHGHLAGDEVLRQFARLLEGSLRQADILCRWGGEEFVVLLKDTELAK 422
Cdd:COG2199  129 EERLERELARARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEE 208
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496892140 423 GMAVAEKIRQRTERSEFTFDASRVSLTASFGVTGL-ASGDTLRSLIARADQALYRAKQSGRNRVC 486
Cdd:COG2199  209 AEALAERLREALEQLPFELEGKELRVTVSIGVALYpEDGDSAEELLRRADLALYRAKRAGRNRVV 273
dCache_1 pfam02743
Cache domain; Double cache domain 1 covers the last three strands from the membrane distal ...
45-281 5.15e-12

Cache domain; Double cache domain 1 covers the last three strands from the membrane distal PAS-like domain, the first two strands of the membrane proximal domain, and the connecting elements between the two domains. This domain when present in chemoreceptors recognize several signals such as proteinogenic amino acids, GABA, Histamine and polyamines, decanoic acid, Autoinducer-2, purine derivatives, quaternary amines, citrate and taurine, among others. When associated with histidine kinases, it recognizes C3/C4-dicarboxylic acids, Spermine, guanosine and Autoinducer-2 (Mantilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1 https://doi.org/10.1093/femsre/fuab043).


:

Pssm-ID: 460673 [Multi-domain]  Cd Length: 237  Bit Score: 65.82  E-value: 5.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496892140   45 INTELPLTSDTVYSEIQKDLIRPIVVSSMLAQNTLLRDWTLAGEHDPEVmtrYLSEVERQQRAYTAFYVSEASGIYYQAK 124
Cdd:pfam02743   7 AEEQLLSLAKQLAENIESYLDSLEEILELLASNPDLQDLLSAPAEEELA---KLESLLRSNPGISSIYLVDADGRVLASS 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496892140  125 GILKKIDPSTPRDL-WYARVKQMQAPYE--INVDMDMANKDRMTVFINYKVLDEQNRFMGAAGVGLTVDAVVKLIDAYQL 201
Cdd:pfam02743  84 DESPSYPGLDVSERpWYKEALKGGGGIIwvFSSPYPSSESGEPVLTIARPIYDDDGEVIGVLVADLDLDTLQELLSQIKL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496892140  202 RYKRSVYFVDPRGQIVLtgstggpeGARPGTTLQSIPSLARLVERMPIPSTGSRE--YQRDDQLHFLNVRFIPELDWYLF 279
Cdd:pfam02743 164 GEGGYVFIVDSDGRILA--------HPLGKNLRSLLAPFLGKSLADALPGSGITEiaVDLDGEDYLVAYAPIPGTGWTLV 235

                  ..
gi 496892140  280 VE 281
Cdd:pfam02743 236 VV 237
 
Name Accession Description Interval E-value
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
263-486 2.54e-65

GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants [Signal transduction mechanisms];


Pssm-ID: 441801 [Multi-domain]  Cd Length: 275  Bit Score: 212.53  E-value: 2.54e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496892140 263 LHFLNVRFIPELDWYLFVEKPVGASLDGVKQSLYLNLAICAIISAVVLAMINGMVRRHQDgIQELATLDSLTHLHNRRAF 342
Cdd:COG2199   50 LLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLLLLALEDITELRRLEER-LRRLATHDPLTGLPNRRAF 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496892140 343 DLLAAQALLDAERGALPLTAVLIDLDHFKELNDTHGHLAGDEVLRQFARLLEGSLRQADILCRWGGEEFVVLLKDTELAK 422
Cdd:COG2199  129 EERLERELARARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEE 208
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496892140 423 GMAVAEKIRQRTERSEFTFDASRVSLTASFGVTGL-ASGDTLRSLIARADQALYRAKQSGRNRVC 486
Cdd:COG2199  209 AEALAERLREALEQLPFELEGKELRVTVSIGVALYpEDGDSAEELLRRADLALYRAKRAGRNRVV 273
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
331-486 4.37e-60

Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as a domain of unknown function 1 (DUF1). This domain is widely present in bacteria, linked to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain shows homology to the adenylyl cyclase catalytic domain. This correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesion in bacteria.


Pssm-ID: 143635 [Multi-domain]  Cd Length: 158  Bit Score: 194.31  E-value: 4.37e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496892140 331 DSLTHLHNRRAFDLLAAQALLDAERGALPLTAVLIDLDHFKELNDTHGHLAGDEVLRQFARLLEGSLRQADILCRWGGEE 410
Cdd:cd01949    3 DPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGDE 82
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496892140 411 FVVLLKDTELAKGMAVAEKIRQRTERSEFTFDASrVSLTASFGV-TGLASGDTLRSLIARADQALYRAKQSGRNRVC 486
Cdd:cd01949   83 FAILLPGTDLEEAEALAERLREAIEEPFFIDGQE-IRVTASIGIaTYPEDGEDAEELLRRADEALYRAKRSGRNRVV 158
pleD PRK09581
response regulator PleD; Reviewed
310-490 4.20e-54

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 188.19  E-value: 4.20e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496892140 310 LAMINGMVRR--HQDGIQ-------ELATLDSLTHLHNRRAFDLLAAQALLDAERGALPLTAVLIDLDHFKELNDTHGHL 380
Cdd:PRK09581 265 LARVRTQIRRkrYQDALRnnleqsiEMAVTDGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHD 344
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496892140 381 AGDEVLRQFARLLEGSLRQADILCRWGGEEFVVLLKDTELAKGMAVAEKIRQRTERSEFTF--DASRVSLTASFGVTGLA 458
Cdd:PRK09581 345 AGDEVLREFAKRLRNNIRGTDLIARYGGEEFVVVMPDTDIEDAIAVAERIRRKIAEEPFIIsdGKERLNVTVSIGVAELR 424
                        170       180       190
                 ....*....|....*....|....*....|...
gi 496892140 459 -SGDTLRSLIARADQALYRAKQSGRNRVCSEPA 490
Cdd:PRK09581 425 pSGDTIEALIKRADKALYEAKNTGRNRVVALAA 457
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
328-484 7.93e-52

Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of non-homologous domains in a variety of bacteria. It has been shown to be homologous to the adenylyl cyclase catalytic domain and has diguanylate cyclase activity. This observation correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. In the WspR protein of Pseudomonas aeruginosa, the GGDEF domain acts as a diguanylate cyclase, PDB:3bre, when the whole molecule appears to form a tetramer consisting of two symmetrically-related dimers representing a biological unit. The active site is the GGD/EF motif, buried in the structure, and the cyclic dimeric guanosine monophosphate (c-di-GMP) bind to the inhibitory-motif RxxD on the surface. The enzyme thus catalyzes the cyclization of two guanosine triphosphate (GTP) molecules to one c-di-GMP molecule.


Pssm-ID: 425976 [Multi-domain]  Cd Length: 160  Bit Score: 173.21  E-value: 7.93e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496892140  328 ATLDSLTHLHNRRAFDLLAAQALLDAERGALPLTAVLIDLDHFKELNDTHGHLAGDEVLRQFARLLEGSLRQADILCRWG 407
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496892140  408 GEEFVVLLKDTELAKGMAVAEKIRQRTERSEFTFDASRVS--LTASFGVTGLA-SGDTLRSLIARADQALYRAKQSGRNR 484
Cdd:pfam00990  81 GDEFAILLPETSLEGAQELAERIRRLLAKLKIPHTVSGLPlyVTISIGIAAYPnDGEDPEDLLKRADTALYQAKQAGRNR 160
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
326-486 4.49e-51

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 171.28  E-value: 4.49e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496892140   326 ELATLDSLTHLHNRRAFDLLAAQALLDAERGALPLTAVLIDLDHFKELNDTHGHLAGDEVLRQFARLLEGSLRQADILCR 405
Cdd:smart00267   1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496892140   406 WGGEEFVVLLKDTELAKGMAVAEKIRQRTERSeFTFDASRVSLTASFGV-TGLASGDTLRSLIARADQALYRAKQSGRNR 484
Cdd:smart00267  81 LGGDEFALLLPETSLEEAIALAERILQQLREP-IIIHGIPLYLTISIGVaAYPNPGEDAEDLLKRADTALYQAKKAGRNQ 159

                   ..
gi 496892140   485 VC 486
Cdd:smart00267 160 VA 161
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
327-485 1.30e-48

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: 164.82  E-value: 1.30e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496892140  327 LATLDSLTHLHNRRAFDLLAAQALLDAERGALPLTAVLIDLDHFKELNDTHGHLAGDEVLRQFARLLEGSLRQADILCRW 406
Cdd:TIGR00254   1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496892140  407 GGEEFVVLLKDTELAKGMAVAEKIRQRTERSEFTFDAS-RVSLTASFGVTGLAS-GDTLRSLIARADQALYRAKQSGRNR 484
Cdd:TIGR00254  81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSeTLTVTVSIGVACYPGhGLTLEELLKRADEALYQAKKAGRNR 160

                  .
gi 496892140  485 V 485
Cdd:TIGR00254 161 V 161
diguan_SiaD NF038266
biofilm regulation diguanylate cyclase SiaD;
316-485 1.13e-45

biofilm regulation diguanylate cyclase SiaD;


Pssm-ID: 468439 [Multi-domain]  Cd Length: 252  Bit Score: 160.15  E-value: 1.13e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496892140 316 MVRRHQDGIQELATLDSLTHLHNRRAFDLLAAQALLDAERGALPLTAVLIDLDHFKELNDTHGHLAGDEVLRQFARLLEG 395
Cdd:NF038266  82 MMRDLNEALREASTRDPLTGLPNRRLLMERLREEVERARRSGRPFTLAMLDVDHFKRINDRYGHEVGDRVLVEIARTLRA 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496892140 396 SLRQADILCRWGGEEFVVLLKDTELAKGMAVAEKIRQRTERSEFTFDASRVSLTASFGVTGL-ASGDTLRSLIARADQAL 474
Cdd:NF038266 162 ELREYDLCGRWGGEEFLLLLPETGLEEAQVVLERLREAVRALAVRVGDDVLSVTASAGLAEHrPPEEGLSATLSRADQAL 241
                        170
                 ....*....|.
gi 496892140 475 YRAKQSGRNRV 485
Cdd:NF038266 242 YQAKRAGRDRV 252
dCache_1 pfam02743
Cache domain; Double cache domain 1 covers the last three strands from the membrane distal ...
45-281 5.15e-12

Cache domain; Double cache domain 1 covers the last three strands from the membrane distal PAS-like domain, the first two strands of the membrane proximal domain, and the connecting elements between the two domains. This domain when present in chemoreceptors recognize several signals such as proteinogenic amino acids, GABA, Histamine and polyamines, decanoic acid, Autoinducer-2, purine derivatives, quaternary amines, citrate and taurine, among others. When associated with histidine kinases, it recognizes C3/C4-dicarboxylic acids, Spermine, guanosine and Autoinducer-2 (Mantilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1 https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 460673 [Multi-domain]  Cd Length: 237  Bit Score: 65.82  E-value: 5.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496892140   45 INTELPLTSDTVYSEIQKDLIRPIVVSSMLAQNTLLRDWTLAGEHDPEVmtrYLSEVERQQRAYTAFYVSEASGIYYQAK 124
Cdd:pfam02743   7 AEEQLLSLAKQLAENIESYLDSLEEILELLASNPDLQDLLSAPAEEELA---KLESLLRSNPGISSIYLVDADGRVLASS 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496892140  125 GILKKIDPSTPRDL-WYARVKQMQAPYE--INVDMDMANKDRMTVFINYKVLDEQNRFMGAAGVGLTVDAVVKLIDAYQL 201
Cdd:pfam02743  84 DESPSYPGLDVSERpWYKEALKGGGGIIwvFSSPYPSSESGEPVLTIARPIYDDDGEVIGVLVADLDLDTLQELLSQIKL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496892140  202 RYKRSVYFVDPRGQIVLtgstggpeGARPGTTLQSIPSLARLVERMPIPSTGSRE--YQRDDQLHFLNVRFIPELDWYLF 279
Cdd:pfam02743 164 GEGGYVFIVDSDGRILA--------HPLGKNLRSLLAPFLGKSLADALPGSGITEiaVDLDGEDYLVAYAPIPGTGWTLV 235

                  ..
gi 496892140  280 VE 281
Cdd:pfam02743 236 VV 237
 
Name Accession Description Interval E-value
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
263-486 2.54e-65

GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants [Signal transduction mechanisms];


Pssm-ID: 441801 [Multi-domain]  Cd Length: 275  Bit Score: 212.53  E-value: 2.54e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496892140 263 LHFLNVRFIPELDWYLFVEKPVGASLDGVKQSLYLNLAICAIISAVVLAMINGMVRRHQDgIQELATLDSLTHLHNRRAF 342
Cdd:COG2199   50 LLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLLLLALEDITELRRLEER-LRRLATHDPLTGLPNRRAF 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496892140 343 DLLAAQALLDAERGALPLTAVLIDLDHFKELNDTHGHLAGDEVLRQFARLLEGSLRQADILCRWGGEEFVVLLKDTELAK 422
Cdd:COG2199  129 EERLERELARARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEE 208
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496892140 423 GMAVAEKIRQRTERSEFTFDASRVSLTASFGVTGL-ASGDTLRSLIARADQALYRAKQSGRNRVC 486
Cdd:COG2199  209 AEALAERLREALEQLPFELEGKELRVTVSIGVALYpEDGDSAEELLRRADLALYRAKRAGRNRVV 273
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
331-486 4.37e-60

Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as a domain of unknown function 1 (DUF1). This domain is widely present in bacteria, linked to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain shows homology to the adenylyl cyclase catalytic domain. This correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesion in bacteria.


Pssm-ID: 143635 [Multi-domain]  Cd Length: 158  Bit Score: 194.31  E-value: 4.37e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496892140 331 DSLTHLHNRRAFDLLAAQALLDAERGALPLTAVLIDLDHFKELNDTHGHLAGDEVLRQFARLLEGSLRQADILCRWGGEE 410
Cdd:cd01949    3 DPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGDE 82
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496892140 411 FVVLLKDTELAKGMAVAEKIRQRTERSEFTFDASrVSLTASFGV-TGLASGDTLRSLIARADQALYRAKQSGRNRVC 486
Cdd:cd01949   83 FAILLPGTDLEEAEALAERLREAIEEPFFIDGQE-IRVTASIGIaTYPEDGEDAEELLRRADEALYRAKRSGRNRVV 158
pleD PRK09581
response regulator PleD; Reviewed
310-490 4.20e-54

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 188.19  E-value: 4.20e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496892140 310 LAMINGMVRR--HQDGIQ-------ELATLDSLTHLHNRRAFDLLAAQALLDAERGALPLTAVLIDLDHFKELNDTHGHL 380
Cdd:PRK09581 265 LARVRTQIRRkrYQDALRnnleqsiEMAVTDGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHD 344
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496892140 381 AGDEVLRQFARLLEGSLRQADILCRWGGEEFVVLLKDTELAKGMAVAEKIRQRTERSEFTF--DASRVSLTASFGVTGLA 458
Cdd:PRK09581 345 AGDEVLREFAKRLRNNIRGTDLIARYGGEEFVVVMPDTDIEDAIAVAERIRRKIAEEPFIIsdGKERLNVTVSIGVAELR 424
                        170       180       190
                 ....*....|....*....|....*....|...
gi 496892140 459 -SGDTLRSLIARADQALYRAKQSGRNRVCSEPA 490
Cdd:PRK09581 425 pSGDTIEALIKRADKALYEAKNTGRNRVVALAA 457
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
328-484 7.93e-52

Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of non-homologous domains in a variety of bacteria. It has been shown to be homologous to the adenylyl cyclase catalytic domain and has diguanylate cyclase activity. This observation correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. In the WspR protein of Pseudomonas aeruginosa, the GGDEF domain acts as a diguanylate cyclase, PDB:3bre, when the whole molecule appears to form a tetramer consisting of two symmetrically-related dimers representing a biological unit. The active site is the GGD/EF motif, buried in the structure, and the cyclic dimeric guanosine monophosphate (c-di-GMP) bind to the inhibitory-motif RxxD on the surface. The enzyme thus catalyzes the cyclization of two guanosine triphosphate (GTP) molecules to one c-di-GMP molecule.


Pssm-ID: 425976 [Multi-domain]  Cd Length: 160  Bit Score: 173.21  E-value: 7.93e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496892140  328 ATLDSLTHLHNRRAFDLLAAQALLDAERGALPLTAVLIDLDHFKELNDTHGHLAGDEVLRQFARLLEGSLRQADILCRWG 407
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496892140  408 GEEFVVLLKDTELAKGMAVAEKIRQRTERSEFTFDASRVS--LTASFGVTGLA-SGDTLRSLIARADQALYRAKQSGRNR 484
Cdd:pfam00990  81 GDEFAILLPETSLEGAQELAERIRRLLAKLKIPHTVSGLPlyVTISIGIAAYPnDGEDPEDLLKRADTALYQAKQAGRNR 160
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
326-486 4.49e-51

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 171.28  E-value: 4.49e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496892140   326 ELATLDSLTHLHNRRAFDLLAAQALLDAERGALPLTAVLIDLDHFKELNDTHGHLAGDEVLRQFARLLEGSLRQADILCR 405
Cdd:smart00267   1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496892140   406 WGGEEFVVLLKDTELAKGMAVAEKIRQRTERSeFTFDASRVSLTASFGV-TGLASGDTLRSLIARADQALYRAKQSGRNR 484
Cdd:smart00267  81 LGGDEFALLLPETSLEEAIALAERILQQLREP-IIIHGIPLYLTISIGVaAYPNPGEDAEDLLKRADTALYQAKKAGRNQ 159

                   ..
gi 496892140   485 VC 486
Cdd:smart00267 160 VA 161
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
327-485 1.30e-48

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: 164.82  E-value: 1.30e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496892140  327 LATLDSLTHLHNRRAFDLLAAQALLDAERGALPLTAVLIDLDHFKELNDTHGHLAGDEVLRQFARLLEGSLRQADILCRW 406
Cdd:TIGR00254   1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496892140  407 GGEEFVVLLKDTELAKGMAVAEKIRQRTERSEFTFDAS-RVSLTASFGVTGLAS-GDTLRSLIARADQALYRAKQSGRNR 484
Cdd:TIGR00254  81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSeTLTVTVSIGVACYPGhGLTLEELLKRADEALYQAKKAGRNR 160

                  .
gi 496892140  485 V 485
Cdd:TIGR00254 161 V 161
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
172-486 1.87e-47

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: 174.58  E-value: 1.87e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496892140 172 VLDEQNRFMGAAGVGLTVDAVVKLIDAYQLRYKRSVYFVDPRGQIVLTGSTGGPEGARPGTTLQSIPSLARLVERMPIPS 251
Cdd:COG5001   95 LLLALLVLLLLLLLLLALLALLAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARALLALLLLLLLALLL 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496892140 252 TGSREYQRDDQLHFLNVRFIPELDWYLFVEKPVGASLDGVKQSLYLNLAICAIISAVVLAMINGMVRRHQDGIQELATLD 331
Cdd:COG5001  175 LLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEERLRHLAYHD 254
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496892140 332 SLTHLHNRRAFDLLAAQALLDAERGALPLTAVLIDLDHFKELNDTHGHLAGDEVLRQFARLLEGSLRQADILCRWGGEEF 411
Cdd:COG5001  255 PLTGLPNRRLFLDRLEQALARARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEF 334
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496892140 412 VVLLKDTE-LAKGMAVAEKIRQRTERSeFTFDASRVSLTASFGVTGL-ASGDTLRSLIARADQALYRAKQSGRNRVC 486
Cdd:COG5001  335 AVLLPDLDdPEDAEAVAERILAALAEP-FELDGHELYVSASIGIALYpDDGADAEELLRNADLAMYRAKAAGRNRYR 410
diguan_SiaD NF038266
biofilm regulation diguanylate cyclase SiaD;
316-485 1.13e-45

biofilm regulation diguanylate cyclase SiaD;


Pssm-ID: 468439 [Multi-domain]  Cd Length: 252  Bit Score: 160.15  E-value: 1.13e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496892140 316 MVRRHQDGIQELATLDSLTHLHNRRAFDLLAAQALLDAERGALPLTAVLIDLDHFKELNDTHGHLAGDEVLRQFARLLEG 395
Cdd:NF038266  82 MMRDLNEALREASTRDPLTGLPNRRLLMERLREEVERARRSGRPFTLAMLDVDHFKRINDRYGHEVGDRVLVEIARTLRA 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496892140 396 SLRQADILCRWGGEEFVVLLKDTELAKGMAVAEKIRQRTERSEFTFDASRVSLTASFGVTGL-ASGDTLRSLIARADQAL 474
Cdd:NF038266 162 ELREYDLCGRWGGEEFLLLLPETGLEEAQVVLERLREAVRALAVRVGDDVLSVTASAGLAEHrPPEEGLSATLSRADQAL 241
                        170
                 ....*....|.
gi 496892140 475 YRAKQSGRNRV 485
Cdd:NF038266 242 YQAKRAGRDRV 252
PRK15426 PRK15426
cellulose biosynthesis regulator YedQ;
59-493 2.67e-45

cellulose biosynthesis regulator YedQ;


Pssm-ID: 237964 [Multi-domain]  Cd Length: 570  Bit Score: 166.73  E-value: 2.67e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496892140  59 EIQKDLIRPIV-VS-SMLAQNTLL--RDWTLAGEHDPEVMTRYLSEVERQQR--AYTAFYVSEAsGIY---YQAkgILKK 129
Cdd:PRK15426 117 ELPRRRTLPVNgVSdAFVSGLTLLsrDDEDLANELTAALELGYLLRLAHNSSslVERAMYVSRA-GFYvstYPT--LFPS 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496892140 130 IDPSTPRDL----WYARVKQMQAP-----YEINVDMDMANKDRM-TVFINykvLDEQNRFMGAAGVGLTVDAVVKLI-DA 198
Cdd:PRK15426 194 DVPTRYYQYvtqpWFIGQSQRRNPgrgvrWFTSQPDDASNTEPQvTASVP---VDAGNYWYGVLAMDIPVRSLQQFLrNA 270
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496892140 199 YQLRYKRSVYFVDPRGQiVLTGSTggpEGARPGTTL--QSIPSLARLVE-------RMpipstGSR--EYQRDDQLHFLN 267
Cdd:PRK15426 271 IDKDLDGEYQLYDSHLR-LLTSSA---PGVRTGNIFdpRELALLARAMEhdtrggiRM-----GSRyvSWERLDHFDGVL 341
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496892140 268 VRFIP--ELDWYLFvekpvgASLDGVKQSLYLNLAICAIISavvLAMINGMVRRH---QDGIQELATLDSLTHLHNRRAF 342
Cdd:PRK15426 342 VRVHTlrEGVRGDF------GSISIALTLLWALFTAMLLIS---WYVIRRMVSNMfvlQSSLQWQAWHDPLTRLYNRGAL 412
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496892140 343 DLLAAQALLDAERGALPLTAVLIDLDHFKELNDTHGHLAGDEVLRQFARLLEGSLRQADILCRWGGEEFVVLLKDTELAK 422
Cdd:PRK15426 413 FEKARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRVGGEEFCVVLPGASLAE 492
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496892140 423 GMAVAEKIRQRTERSEFTFDASR-VSLTASFGVTGLASGD--TLRSLIARADQALYRAKQSGRNRVCSEPASPE 493
Cdd:PRK15426 493 AAQVAERIRLRINEKEILVAKSTtIRISASLGVSSAEEDGdyDFEQLQSLADRRLYLAKQAGRNRVCASDNAHE 566
PRK09894 PRK09894
diguanylate cyclase; Provisional
327-485 7.31e-45

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 159.08  E-value: 7.31e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496892140 327 LATLDSLTHLHNRRAFDLLAAQALLDaeRGALPLTAVLIDLDHFKELNDTHGHLAGDEVLRQFARLLEGSLRQADILCRW 406
Cdd:PRK09894 128 RSNMDVLTGLPGRRVLDESFDHQLRN--REPQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRY 205
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496892140 407 GGEEFVVLLKDTELAKGMAVAEKIRQRTERSEFTFDASRVSLTASFGVTGLASGDTLRSLIARADQALYRAKQSGRNRV 485
Cdd:PRK09894 206 GGEEFIICLKAATDEEACRAGERIRQLIANHAITHSDGRINITATFGVSRAFPEETLDVVIGRADRAMYEGKQTGRNRV 284
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
328-485 5.37e-26

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 112.46  E-value: 5.37e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496892140  328 ATLDSLTHLHNRRAF----DLLAAQALLDAERGALpltaVLIDLDHFKELNDTHGHLAGDEVLRQFARLLEGSLRQADIL 403
Cdd:PRK09776  665 ASHDALTHLANRASFekqlRRLLQTVNSTHQRHAL----VFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSDVL 740
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496892140  404 CRWGGEEFVVLLKDTELAKGMAVAEKIRQRTERSEFTFDASRVSLTASFGVTGLASGDTLRS-LIARADQALYRAKQSGR 482
Cdd:PRK09776  741 ARLGGDEFGLLLPDCNVESARFIATRIISAINDYHFPWEGRVYRVGASAGITLIDANNHQASeVMSQADIACYAAKNAGR 820

                  ...
gi 496892140  483 NRV 485
Cdd:PRK09776  821 GRV 823
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
318-486 3.07e-22

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 100.14  E-value: 3.07e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496892140 318 RRHQDGIQELATLDSLTHLHNRRAFDLLAAQALLDAERGALPLtaVLIDLDHFKELNDTHGHLAGDEVLRQFARLLEGSL 397
Cdd:PRK10060 227 RRAQERLRILANTDSITGLPNRNAIQELIDHAINAADNNQVGI--VYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCL 304
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496892140 398 RQADILCRWGGEEFVVLLKDTELAKGMAVAEKIRQRTeRSEFTFDASRVSLTASFGVTgLAS--GDTLRSLIARADQALY 475
Cdd:PRK10060 305 EEDQTLARLGGDEFLVLASHTSQAALEAMASRILTRL-RLPFRIGLIEVYTGCSIGIA-LAPehGDDSESLIRSADTAMY 382
                        170
                 ....*....|.
gi 496892140 476 RAKQSGRNRVC 486
Cdd:PRK10060 383 TAKEGGRGQFC 393
adrA PRK10245
diguanylate cyclase AdrA; Provisional
320-484 5.66e-22

diguanylate cyclase AdrA; Provisional


Pssm-ID: 182329 [Multi-domain]  Cd Length: 366  Bit Score: 97.21  E-value: 5.66e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496892140 320 HQDGIQELATLDSLTHLHNRRAFDLLAAQALLDAERGALPLTAVLIDLDHFKELNDTHGHLAGDEVLRQFARLLEGSLRQ 399
Cdd:PRK10245 197 HKRRLQVMSTRDGMTGVYNRRHWETLLRNEFDNCRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRG 276
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496892140 400 ADILCRWGGEEFVVLLKDTELAKGMAVAEKIRQRTERSEFTfDASRVSLTASFGVTGLASG-DTLRSLIARADQALYRAK 478
Cdd:PRK10245 277 SDVIGRFGGDEFAVIMSGTPAESAITAMSRVHEGLNTLRLP-NAPQVTLRISVGVAPLNPQmSHYREWLKSADLALYKAK 355

                 ....*.
gi 496892140 479 QSGRNR 484
Cdd:PRK10245 356 NAGRNR 361
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
401-478 1.15e-14

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: 71.86  E-value: 1.15e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496892140 401 DILCRWGGEEFVVLLKDTELAKGMAVAEKIRQRTERSEftfdasRVSLTASFGVTGLasgdtlrSLIARADqALYRAK 478
Cdd:COG3706  116 DLVARYGGEEFAILLPGTDLEGALAVAERIREAVAELP------SLRVTVSIGVAGD-------SLLKRAD-ALYQAR 179
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
324-483 3.18e-13

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 72.11  E-value: 3.18e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496892140 324 IQELATLDSLTHLHNRRAFDLLAAQALLDaergALPLTAVLIDLDHFKELNDTHGHLAGDEVLRQFARLLEGSLRQADIL 403
Cdd:PRK11359 372 IEQLIQFDPLTGLPNRNNLHNYLDDLVDK----AVSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDQYL 447
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496892140 404 CRWGGEEFVVLLKDTELAKGMAVAEKIrQRTERSEFTFDASRVSLTASFGVTGLASGDTlRSLIARADQALYRAKQSGRN 483
Cdd:PRK11359 448 CRIEGTQFVLVSLENDVSNITQIADEL-RNVVSKPIMIDDKPFPLTLSIGISYDVGKNR-DYLLSTAHNAMDYIRKNGGN 525
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
359-478 4.23e-13

Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse group of nucleotidyl cyclases (NC's) containing prokaryotic and eukaryotic proteins. They can be divided into two major groups; the mononucleotidyl cyclases (MNC's) and the diguanylate cyclases (DGC's). The MNC's, which include the adenylate cyclases (AC's) and the guanylate cyclases (GC's), have a conserved cyclase homology domain (CHD), while the DGC's have a conserved GGDEF domain, named after a conserved motif within this subgroup. Their products, cyclic guanylyl and adenylyl nucleotides, are second messengers that play important roles in eukaryotic signal transduction and prokaryotic sensory pathways.


Pssm-ID: 143637 [Multi-domain]  Cd Length: 133  Bit Score: 66.23  E-value: 4.23e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496892140 359 PLTAVLIDLDHFKELNDTHGHLAGDEVLRQFARLL-EGSLRQADILCRWGGEEFVVLLKDTELAKGMAVAEKIRQRTERS 437
Cdd:cd07556    1 PVTILFADIVGFTSLADALGPDEGDELLNELAGRFdSLIRRSGDLKIKTIGDEFMVVSGLDHPAAAVAFAEDMREAVSAL 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 496892140 438 EFTfdaSRVSLTASFGV-TGLASG---------DTLRSLIARADQALYRAK 478
Cdd:cd07556   81 NQS---EGNPVRVRIGIhTGPVVVgvigsrpqyDVWGALVNLASRMESQAK 128
dCache_1 pfam02743
Cache domain; Double cache domain 1 covers the last three strands from the membrane distal ...
45-281 5.15e-12

Cache domain; Double cache domain 1 covers the last three strands from the membrane distal PAS-like domain, the first two strands of the membrane proximal domain, and the connecting elements between the two domains. This domain when present in chemoreceptors recognize several signals such as proteinogenic amino acids, GABA, Histamine and polyamines, decanoic acid, Autoinducer-2, purine derivatives, quaternary amines, citrate and taurine, among others. When associated with histidine kinases, it recognizes C3/C4-dicarboxylic acids, Spermine, guanosine and Autoinducer-2 (Mantilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1 https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 460673 [Multi-domain]  Cd Length: 237  Bit Score: 65.82  E-value: 5.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496892140   45 INTELPLTSDTVYSEIQKDLIRPIVVSSMLAQNTLLRDWTLAGEHDPEVmtrYLSEVERQQRAYTAFYVSEASGIYYQAK 124
Cdd:pfam02743   7 AEEQLLSLAKQLAENIESYLDSLEEILELLASNPDLQDLLSAPAEEELA---KLESLLRSNPGISSIYLVDADGRVLASS 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496892140  125 GILKKIDPSTPRDL-WYARVKQMQAPYE--INVDMDMANKDRMTVFINYKVLDEQNRFMGAAGVGLTVDAVVKLIDAYQL 201
Cdd:pfam02743  84 DESPSYPGLDVSERpWYKEALKGGGGIIwvFSSPYPSSESGEPVLTIARPIYDDDGEVIGVLVADLDLDTLQELLSQIKL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496892140  202 RYKRSVYFVDPRGQIVLtgstggpeGARPGTTLQSIPSLARLVERMPIPSTGSRE--YQRDDQLHFLNVRFIPELDWYLF 279
Cdd:pfam02743 164 GEGGYVFIVDSDGRILA--------HPLGKNLRSLLAPFLGKSLADALPGSGITEiaVDLDGEDYLVAYAPIPGTGWTLV 235

                  ..
gi 496892140  280 VE 281
Cdd:pfam02743 236 VV 237
PRK09966 PRK09966
diguanylate cyclase DgcN;
331-484 8.34e-09

diguanylate cyclase DgcN;


Pssm-ID: 182171 [Multi-domain]  Cd Length: 407  Bit Score: 57.32  E-value: 8.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496892140 331 DSLTHLHNRRAFDLLAAQALLdaERGALPLTAVL-IDLDHFKELNDTHGHLAGDEVLRQFARLLE---GSLRQAdilCRW 406
Cdd:PRK09966 251 DPLTGLANRAAFRSGINTLMN--NSDARKTSALLfLDGDNFKYINDTWGHATGDRVLIEIAKRLAefgGLRHKA---YRL 325
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496892140 407 GGEEFVVLLKDTELAKGMA-VAEKIRQRTERSEFTFDASRVSLTASFGVTGL---ASGDTLRSLiarADQALYRAKQSGR 482
Cdd:PRK09966 326 GGDEFAMVLYDVQSESEVQqICSALTQIFNLPFDLHNGHQTTMTLSIGYAMTiehASAEKLQEL---ADHNMYQAKHQRA 402

                 ..
gi 496892140 483 NR 484
Cdd:PRK09966 403 EK 404
 
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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