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Conserved domains on  [gi|406375330|gb|AFS38585|]
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diguanylate cyclase [Alteromonas macleodii ATCC 27126]

Protein Classification

diguanylate cyclase( domain architecture ID 10542681)

diguanylate cyclase containing the transmembrane region and the extracellular 2 domain of 7TM-DISM (7TM Receptors with Diverse Intracellular Signaling Modules), catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules and may function as a membrane-associated receptor for various signaling molecules such as carbohydrates and their derivatives

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 ...
 307-573 5.12e-61

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: 203.29  E-value: 5.12e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406375330 307 ALAVIIVLIGSRSFAVMSQLAVLTTIAIWMLLIGIFAYRNGDTLAKFFLPAILCGTGGAMVSSLATWGLIPYSKWAFRGI 386
Cdd:COG2199    2 LLLLLLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406375330 387 EIGMVLEMSLLSISLAFNYKQVQQARRNAERDARLDPLTSLYNRRAFEDLVYPIWEMGKRSNKFMSVMLIDIDWFKGIND 466
Cdd:COG2199   82 ELLLLLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRIND 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406375330 467 KYGHDMGDKVLKKVAEEIKGQVRGSDITFRWGGEEFLVFLPNTRVHYAKQIAENLRVHLFTHDI---NKFIRVTVSIGVA 543
Cdd:COG2199  162 TYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFeleGKELRVTVSIGVA 241

                        250       260       270
                 ....*....|....*....|....*....|
gi 406375330 544 GTSPGEEDINVLIKQSDQALYLAKAKGRNK 573
Cdd:COG2199  242 LYPEDGDSAEELLRRADLALYRAKRAGRNR 271
7TMR-DISM_7TM pfam07695
7TM diverse intracellular signalling; This entry represents the transmembrane region of the ...
 201-402 4.96e-29

7TM diverse intracellular signalling; This entry represents the transmembrane region of the 7TM-DISM (7TM Receptors with Diverse Intracellular Signalling Modules).


:

Pssm-ID: 429600 [Multi-domain]  Cd Length: 207  Bit Score: 114.29  E-value: 4.96e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406375330  201 YFYGALYGALVILLVYNLVLYSYLKERRYLLYSLYLLSFLLFNFTYTGHGFWWLWSESIF-LQQWLLPALMFLYL-FSAV 278
Cdd:pfam07695   3 LLLGLFYGILLALALYNLFLFFSLRDRSYLYYVLYLLSFLLYQLSLNGLGFQYLWPNAPPwLNNKLLYLSLLLLLpFFAL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406375330  279 RFTIEFLNTQLYLPTLYRCRKYIYGALGALAVIIVLIGSRSFAVMSQLAVLTTIaIWMLLIGIFAYRNGDTLAKFFLPAI 358
Cdd:pfam07695  83 LFARSFLELKKYLPRLLRLLLGLALLLALLLLLLPLFPYTLSLPLAQLLALLFI-LFLLLLGIIAWRKGYKPARYFLLAW 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 406375330  359 LCGTGGAMVSSLATWGLIPYSKWAFRGIEIGMVLEMSLLSISLA 402
Cdd:pfam07695 162 LLLLIGALIDILSLLGLLPSNFFTNYLLQIGSALEVLLLSLALA 205
7TMR-DISMED2 pfam07696
7TMR-DISM extracellular 2; This entry represents one of two distinct types of extracellular ...
 42-183 4.95e-15

7TMR-DISM extracellular 2; This entry represents one of two distinct types of extracellular domain found in the 7TM-DISM (7TM Receptors with Diverse Intracellular Signalling Modules) bacterial transmembrane proteins. It is possible that this domain adopts a jelly roll fold and acts as a receptor for carbohydrates and their derivatives. It can also recognize Ca(II) (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


:

Pssm-ID: 429601  Cd Length: 127  Bit Score: 71.99  E-value: 4.95e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406375330   42 WMYYEE-GSQLTAEDILTKYQQntLIKNTNGRVSYGFTGNTVWgvlaveldtygvLVTRIANNSPINVPFLplkIEIDNA 120
Cdd:pfam07696   1 VEYLEDpTGSLTIEDVLSADGR--FRPPEKGVPNFGYSSSAYW------------LRFTLENPTDAPKDWL---LELAYP 63

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 406375330  121 WLDDIDLYFFENGQRKRHVKLGDNQVHSARFEDARMPSVFYRFTQPETL-VVFRFSSEDPMTIP 183
Cdd:pfam07696  64 LLDEIDLYLPDGGGGYREQRLGDRLPFSQRPVAHRNFVFPLPLPPGETVtLYLRVKSSGSLLLP 127
 
Name Accession Description Interval E-value
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 307-573 5.12e-61

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: 203.29  E-value: 5.12e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406375330 307 ALAVIIVLIGSRSFAVMSQLAVLTTIAIWMLLIGIFAYRNGDTLAKFFLPAILCGTGGAMVSSLATWGLIPYSKWAFRGI 386
Cdd:COG2199    2 LLLLLLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406375330 387 EIGMVLEMSLLSISLAFNYKQVQQARRNAERDARLDPLTSLYNRRAFEDLVYPIWEMGKRSNKFMSVMLIDIDWFKGIND 466
Cdd:COG2199   82 ELLLLLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRIND 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406375330 467 KYGHDMGDKVLKKVAEEIKGQVRGSDITFRWGGEEFLVFLPNTRVHYAKQIAENLRVHLFTHDI---NKFIRVTVSIGVA 543
Cdd:COG2199  162 TYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFeleGKELRVTVSIGVA 241

                        250       260       270
                 ....*....|....*....|....*....|
gi 406375330 544 GTSPGEEDINVLIKQSDQALYLAKAKGRNK 573
Cdd:COG2199  242 LYPEDGDSAEELLRRADLALYRAKRAGRNR 271
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 422-573 7.34e-59

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: 193.54  E-value: 7.34e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406375330 422 DPLTSLYNRRAFEDLVYPIWEMGKRSNKFMSVMLIDIDWFKGINDKYGHDMGDKVLKKVAEEIKGQVRGSDITFRWGGEE 501
Cdd:cd01949    3 DPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGDE 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 406375330 502 FLVFLPNTRVHYAKQIAENLRVHLFTHDI--NKFIRVTVSIGVAGTSPGEEDINVLIKQSDQALYLAKAKGRNK 573
Cdd:cd01949   83 FAILLPGTDLEEAEALAERLREAIEEPFFidGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNR 156
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 419-573 2.39e-53

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: 178.99  E-value: 2.39e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406375330  419 ARLDPLTSLYNRRAFEDLVYPIWEMGKRSNKFMSVMLIDIDWFKGINDKYGHDMGDKVLKKVAEEIKGQVRGSDITFRWG 498
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406375330  499 GEEFLVFLPNTRVHYAKQIAENLRVHL----FTHDINKFIR-VTVSIGVAGTSPGEEDINVLIKQSDQALYLAKAKGRNK 573
Cdd:pfam00990  81 GDEFAILLPETSLEGAQELAERIRRLLaklkIPHTVSGLPLyVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGRNR 160
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 422-573 1.48e-51

diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by many proteins carrying the domain. There is evidence that the domain has diguanylate cyclase activity. Several proteins carrying this domain also carry domains with functions relating to environmental sensing. These include PleD, a response regulator protein involved in the swarmer-to-stalked cell transition in Caulobacter crescentus, and FixL, a heme-containing oxygen sensor protein. [Regulatory functions, Small molecule interactions, Signal transduction, Other]


Pssm-ID: 272984 [Multi-domain]  Cd Length: 165  Bit Score: 174.45  E-value: 1.48e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406375330  422 DPLTSLYNRRAFEDLVYPIWEMGKRSNKFMSVMLIDIDWFKGINDKYGHDMGDKVLKKVAEEIKGQVRGSDITFRWGGEE 501
Cdd:TIGR00254   5 DPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYGGEE 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 406375330  502 FLVFLPNTRVHYAKQIAENLRVHL----FTHDINKFIRVTVSIGVAGTSPGEEDINVLIKQSDQALYLAKAKGRNK 573
Cdd:TIGR00254  85 FVVILPGTPLEDALSKAERLRDAInskpIEVAGSETLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRNR 160
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 419-573 3.31e-50

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 170.89  E-value: 3.31e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406375330   419 ARLDPLTSLYNRRAFEDLVYPIWEMGKRSNKFMSVMLIDIDWFKGINDKYGHDMGDKVLKKVAEEIKGQVRGSDITFRWG 498
Cdd:smart00267   3 AFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARLG 82

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 406375330   499 GEEFLVFLPNTRVHYAKQIAENLRVHLFTHDINKFI--RVTVSIGVAGTSPGEEDINVLIKQSDQALYLAKAKGRNK 573
Cdd:smart00267  83 GDEFALLLPETSLEEAIALAERILQQLREPIIIHGIplYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQ 159
pleD PRK09581
response regulator PleD; Reviewed
 406-573 4.45e-48

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 173.93  E-value: 4.45e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406375330 406 KQVQQA-RRNAERDARL---DPLTSLYNRRAFEDLVYPIWEMGKRSNKFMSVMLIDIDWFKGINDKYGHDMGDKVLKKVA 481
Cdd:PRK09581 275 KRYQDAlRNNLEQSIEMavtDGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFA 354

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406375330 482 EEIKGQVRGSDITFRWGGEEFLVFLPNTRVHYAKQIAENLRVHL----F-THDINKFIRVTVSIGVAGTSPGEEDINVLI 556
Cdd:PRK09581 355 KRLRNNIRGTDLIARYGGEEFVVVMPDTDIEDAIAVAERIRRKIaeepFiISDGKERLNVTVSIGVAELRPSGDTIEALI 434

                        170
                 ....*....|....*..
gi 406375330 557 KQSDQALYLAKAKGRNK 573
Cdd:PRK09581 435 KRADKALYEAKNTGRNR 451
diguan_SiaD NF038266
biofilm regulation diguanylate cyclase SiaD;
419-573 2.05e-42

biofilm regulation diguanylate cyclase SiaD;


Pssm-ID: 468439 [Multi-domain]  Cd Length: 252  Bit Score: 152.83  E-value: 2.05e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406375330 419 ARLDPLTSLYNRRAFEDLVYPIWEMGKRSNKFMSVMLIDIDWFKGINDKYGHDMGDKVLKKVAEEIKGQVRGSDITFRWG 498
Cdd:NF038266  94 STRDPLTGLPNRRLLMERLREEVERARRSGRPFTLAMLDVDHFKRINDRYGHEVGDRVLVEIARTLRAELREYDLCGRWG 173

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 406375330 499 GEEFLVFLPNTRVHYAKQIAENLRVHLFTHDI---NKFIRVTVSIGVAGTSPGEEDINVLIKQSDQALYLAKAKGRNK 573
Cdd:NF038266 174 GEEFLLLLPETGLEEAQVVLERLREAVRALAVrvgDDVLSVTASAGLAEHRPPEEGLSATLSRADQALYQAKRAGRDR 251
7TMR-DISM_7TM pfam07695
7TM diverse intracellular signalling; This entry represents the transmembrane region of the ...
 201-402 4.96e-29

7TM diverse intracellular signalling; This entry represents the transmembrane region of the 7TM-DISM (7TM Receptors with Diverse Intracellular Signalling Modules).


Pssm-ID: 429600 [Multi-domain]  Cd Length: 207  Bit Score: 114.29  E-value: 4.96e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406375330  201 YFYGALYGALVILLVYNLVLYSYLKERRYLLYSLYLLSFLLFNFTYTGHGFWWLWSESIF-LQQWLLPALMFLYL-FSAV 278
Cdd:pfam07695   3 LLLGLFYGILLALALYNLFLFFSLRDRSYLYYVLYLLSFLLYQLSLNGLGFQYLWPNAPPwLNNKLLYLSLLLLLpFFAL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406375330  279 RFTIEFLNTQLYLPTLYRCRKYIYGALGALAVIIVLIGSRSFAVMSQLAVLTTIaIWMLLIGIFAYRNGDTLAKFFLPAI 358
Cdd:pfam07695  83 LFARSFLELKKYLPRLLRLLLGLALLLALLLLLLPLFPYTLSLPLAQLLALLFI-LFLLLLGIIAWRKGYKPARYFLLAW 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 406375330  359 LCGTGGAMVSSLATWGLIPYSKWAFRGIEIGMVLEMSLLSISLA 402
Cdd:pfam07695 162 LLLLIGALIDILSLLGLLPSNFFTNYLLQIGSALEVLLLSLALA 205
7TMR-DISMED2 pfam07696
7TMR-DISM extracellular 2; This entry represents one of two distinct types of extracellular ...
 42-183 4.95e-15

7TMR-DISM extracellular 2; This entry represents one of two distinct types of extracellular domain found in the 7TM-DISM (7TM Receptors with Diverse Intracellular Signalling Modules) bacterial transmembrane proteins. It is possible that this domain adopts a jelly roll fold and acts as a receptor for carbohydrates and their derivatives. It can also recognize Ca(II) (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 429601  Cd Length: 127  Bit Score: 71.99  E-value: 4.95e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406375330   42 WMYYEE-GSQLTAEDILTKYQQntLIKNTNGRVSYGFTGNTVWgvlaveldtygvLVTRIANNSPINVPFLplkIEIDNA 120
Cdd:pfam07696   1 VEYLEDpTGSLTIEDVLSADGR--FRPPEKGVPNFGYSSSAYW------------LRFTLENPTDAPKDWL---LELAYP 63

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 406375330  121 WLDDIDLYFFENGQRKRHVKLGDNQVHSARFEDARMPSVFYRFTQPETL-VVFRFSSEDPMTIP 183
Cdd:pfam07696  64 LLDEIDLYLPDGGGGYREQRLGDRLPFSQRPVAHRNFVFPLPLPPGETVtLYLRVKSSGSLLLP 127
 
Name Accession Description Interval E-value
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 307-573 5.12e-61

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: 203.29  E-value: 5.12e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406375330 307 ALAVIIVLIGSRSFAVMSQLAVLTTIAIWMLLIGIFAYRNGDTLAKFFLPAILCGTGGAMVSSLATWGLIPYSKWAFRGI 386
Cdd:COG2199    2 LLLLLLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406375330 387 EIGMVLEMSLLSISLAFNYKQVQQARRNAERDARLDPLTSLYNRRAFEDLVYPIWEMGKRSNKFMSVMLIDIDWFKGIND 466
Cdd:COG2199   82 ELLLLLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRIND 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406375330 467 KYGHDMGDKVLKKVAEEIKGQVRGSDITFRWGGEEFLVFLPNTRVHYAKQIAENLRVHLFTHDI---NKFIRVTVSIGVA 543
Cdd:COG2199  162 TYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFeleGKELRVTVSIGVA 241

                        250       260       270
                 ....*....|....*....|....*....|
gi 406375330 544 GTSPGEEDINVLIKQSDQALYLAKAKGRNK 573
Cdd:COG2199  242 LYPEDGDSAEELLRRADLALYRAKRAGRNR 271
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 422-573 7.34e-59

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: 193.54  E-value: 7.34e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406375330 422 DPLTSLYNRRAFEDLVYPIWEMGKRSNKFMSVMLIDIDWFKGINDKYGHDMGDKVLKKVAEEIKGQVRGSDITFRWGGEE 501
Cdd:cd01949    3 DPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGDE 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 406375330 502 FLVFLPNTRVHYAKQIAENLRVHLFTHDI--NKFIRVTVSIGVAGTSPGEEDINVLIKQSDQALYLAKAKGRNK 573
Cdd:cd01949   83 FAILLPGTDLEEAEALAERLREAIEEPFFidGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNR 156
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 419-573 2.39e-53

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: 178.99  E-value: 2.39e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406375330  419 ARLDPLTSLYNRRAFEDLVYPIWEMGKRSNKFMSVMLIDIDWFKGINDKYGHDMGDKVLKKVAEEIKGQVRGSDITFRWG 498
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406375330  499 GEEFLVFLPNTRVHYAKQIAENLRVHL----FTHDINKFIR-VTVSIGVAGTSPGEEDINVLIKQSDQALYLAKAKGRNK 573
Cdd:pfam00990  81 GDEFAILLPETSLEGAQELAERIRRLLaklkIPHTVSGLPLyVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGRNR 160
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 422-573 1.48e-51

diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by many proteins carrying the domain. There is evidence that the domain has diguanylate cyclase activity. Several proteins carrying this domain also carry domains with functions relating to environmental sensing. These include PleD, a response regulator protein involved in the swarmer-to-stalked cell transition in Caulobacter crescentus, and FixL, a heme-containing oxygen sensor protein. [Regulatory functions, Small molecule interactions, Signal transduction, Other]


Pssm-ID: 272984 [Multi-domain]  Cd Length: 165  Bit Score: 174.45  E-value: 1.48e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406375330  422 DPLTSLYNRRAFEDLVYPIWEMGKRSNKFMSVMLIDIDWFKGINDKYGHDMGDKVLKKVAEEIKGQVRGSDITFRWGGEE 501
Cdd:TIGR00254   5 DPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYGGEE 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 406375330  502 FLVFLPNTRVHYAKQIAENLRVHL----FTHDINKFIRVTVSIGVAGTSPGEEDINVLIKQSDQALYLAKAKGRNK 573
Cdd:TIGR00254  85 FVVILPGTPLEDALSKAERLRDAInskpIEVAGSETLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRNR 160
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 419-573 3.31e-50

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 170.89  E-value: 3.31e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406375330   419 ARLDPLTSLYNRRAFEDLVYPIWEMGKRSNKFMSVMLIDIDWFKGINDKYGHDMGDKVLKKVAEEIKGQVRGSDITFRWG 498
Cdd:smart00267   3 AFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARLG 82

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 406375330   499 GEEFLVFLPNTRVHYAKQIAENLRVHLFTHDINKFI--RVTVSIGVAGTSPGEEDINVLIKQSDQALYLAKAKGRNK 573
Cdd:smart00267  83 GDEFALLLPETSLEEAIALAERILQQLREPIIIHGIplYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQ 159
pleD PRK09581
response regulator PleD; Reviewed
 406-573 4.45e-48

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 173.93  E-value: 4.45e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406375330 406 KQVQQA-RRNAERDARL---DPLTSLYNRRAFEDLVYPIWEMGKRSNKFMSVMLIDIDWFKGINDKYGHDMGDKVLKKVA 481
Cdd:PRK09581 275 KRYQDAlRNNLEQSIEMavtDGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFA 354

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406375330 482 EEIKGQVRGSDITFRWGGEEFLVFLPNTRVHYAKQIAENLRVHL----F-THDINKFIRVTVSIGVAGTSPGEEDINVLI 556
Cdd:PRK09581 355 KRLRNNIRGTDLIARYGGEEFVVVMPDTDIEDAIAVAERIRRKIaeepFiISDGKERLNVTVSIGVAELRPSGDTIEALI 434

                        170
                 ....*....|....*..
gi 406375330 557 KQSDQALYLAKAKGRNK 573
Cdd:PRK09581 435 KRADKALYEAKNTGRNR 451
diguan_SiaD NF038266
biofilm regulation diguanylate cyclase SiaD;
419-573 2.05e-42

biofilm regulation diguanylate cyclase SiaD;


Pssm-ID: 468439 [Multi-domain]  Cd Length: 252  Bit Score: 152.83  E-value: 2.05e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406375330 419 ARLDPLTSLYNRRAFEDLVYPIWEMGKRSNKFMSVMLIDIDWFKGINDKYGHDMGDKVLKKVAEEIKGQVRGSDITFRWG 498
Cdd:NF038266  94 STRDPLTGLPNRRLLMERLREEVERARRSGRPFTLAMLDVDHFKRINDRYGHEVGDRVLVEIARTLRAELREYDLCGRWG 173

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 406375330 499 GEEFLVFLPNTRVHYAKQIAENLRVHLFTHDI---NKFIRVTVSIGVAGTSPGEEDINVLIKQSDQALYLAKAKGRNK 573
Cdd:NF038266 174 GEEFLLLLPETGLEEAQVVLERLREAVRALAVrvgDDVLSVTASAGLAEHRPPEEGLSATLSRADQALYQAKRAGRDR 251
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 307-577 4.18e-42

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: 161.10  E-value: 4.18e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406375330 307 ALAVIIVLIGSRSFAVMSQLAVLTTIAIWMLLIGIFAYRNGDTLAKFFLPAILCGTGGAMVSSLATWGLIPYSKWAFRGI 386
Cdd:COG5001  136 LLAAALGAALLAALALALLLALARALLALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLG 215

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406375330 387 EIGMVLEMSLLSISLAFNYKQVQQARRNAERDARL---DPLTSLYNRRAFEDLVYPIWEMGKRSNKFMSVMLIDIDWFKG 463
Cdd:COG5001  216 LLLLGLLLLLLLVAVLAIARLITERKRAEERLRHLayhDPLTGLPNRRLFLDRLEQALARARRSGRRLALLFIDLDRFKE 295

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406375330 464 INDKYGHDMGDKVLKKVAEEIKGQVRGSDITFRWGGEEFLVFLPNTR-VHYAKQIAENLRVHL---FTHDiNKFIRVTVS 539
Cdd:COG5001  296 INDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVLLPDLDdPEDAEAVAERILAALaepFELD-GHELYVSAS 374

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 406375330 540 IGVAGTSPGEEDINVLIKQSDQALYLAKAKGRNkKWCF 577
Cdd:COG5001  375 IGIALYPDDGADAEELLRNADLAMYRAKAAGRN-RYRF 411
PRK15426 PRK15426
cellulose biosynthesis regulator YedQ;
419-573 1.44e-38

cellulose biosynthesis regulator YedQ;


Pssm-ID: 237964 [Multi-domain]  Cd Length: 570  Bit Score: 149.78  E-value: 1.44e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406375330 419 ARLDPLTSLYNRRAFEDLVYPIWEMGKRSNKFMSVMLIDIDWFKGINDKYGHDMGDKVLKKVAEEIKGQVRGSDITFRWG 498
Cdd:PRK15426 398 AWHDPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRVG 477

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406375330 499 GEEFLVFLPNTRVHYAKQIAENLRVHLFTHDI----NKFIRVTVSIGVAGTSP-GEEDINVLIKQSDQALYLAKAKGRNK 573
Cdd:PRK15426 478 GEEFCVVLPGASLAEAAQVAERIRLRINEKEIlvakSTTIRISASLGVSSAEEdGDYDFEQLQSLADRRLYLAKQAGRNR 557
PRK09894 PRK09894
diguanylate cyclase; Provisional
 421-573 8.10e-30

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 119.02  E-value: 8.10e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406375330 421 LDPLTSLYNRRAF-EDLVYPIWEMGKRSnkfMSVMLIDIDWFKGINDKYGHDMGDKVLKKVAEEIKGQVRGSDITFRWGG 499
Cdd:PRK09894 131 MDVLTGLPGRRVLdESFDHQLRNREPQN---LYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGG 207

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 406375330 500 EEFLVFLPNTRVHYAKQIAENLRVHLFTHDI---NKFIRVTVSIGVAGTSPGEEdINVLIKQSDQALYLAKAKGRNK 573
Cdd:PRK09894 208 EEFIICLKAATDEEACRAGERIRQLIANHAIthsDGRINITATFGVSRAFPEET-LDVVIGRADRAMYEGKQTGRNR 283
7TMR-DISM_7TM pfam07695
7TM diverse intracellular signalling; This entry represents the transmembrane region of the ...
 201-402 4.96e-29

7TM diverse intracellular signalling; This entry represents the transmembrane region of the 7TM-DISM (7TM Receptors with Diverse Intracellular Signalling Modules).


Pssm-ID: 429600 [Multi-domain]  Cd Length: 207  Bit Score: 114.29  E-value: 4.96e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406375330  201 YFYGALYGALVILLVYNLVLYSYLKERRYLLYSLYLLSFLLFNFTYTGHGFWWLWSESIF-LQQWLLPALMFLYL-FSAV 278
Cdd:pfam07695   3 LLLGLFYGILLALALYNLFLFFSLRDRSYLYYVLYLLSFLLYQLSLNGLGFQYLWPNAPPwLNNKLLYLSLLLLLpFFAL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406375330  279 RFTIEFLNTQLYLPTLYRCRKYIYGALGALAVIIVLIGSRSFAVMSQLAVLTTIaIWMLLIGIFAYRNGDTLAKFFLPAI 358
Cdd:pfam07695  83 LFARSFLELKKYLPRLLRLLLGLALLLALLLLLLPLFPYTLSLPLAQLLALLFI-LFLLLLGIIAWRKGYKPARYFLLAW 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 406375330  359 LCGTGGAMVSSLATWGLIPYSKWAFRGIEIGMVLEMSLLSISLA 402
Cdd:pfam07695 162 LLLLIGALIDILSLLGLLPSNFFTNYLLQIGSALEVLLLSLALA 205
adrA PRK10245
diguanylate cyclase AdrA; Provisional
 382-573 9.87e-25

diguanylate cyclase AdrA; Provisional


Pssm-ID: 182329 [Multi-domain]  Cd Length: 366  Bit Score: 106.07  E-value: 9.87e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406375330 382 AFRGIEIGMVLEMSLLSI-SLAFNYKQVQQARRNAERDARL------DPLTSLYNRRAFEDLVYPIWEMGKRSNKFMSVM 454
Cdd:PRK10245 161 SFNSAPLEWWLSLPVIVIyPLLFAWVSYQTATKLAEHKRRLqvmstrDGMTGVYNRRHWETLLRNEFDNCRRHHRDATLL 240

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406375330 455 LIDIDWFKGINDKYGHDMGDKVLKKVAEEIKGQVRGSDITFRWGGEEFLVFLPNTRVHYAkqIAENLRVHlftHDINKF- 533
Cdd:PRK10245 241 IIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSDVIGRFGGDEFAVIMSGTPAESA--ITAMSRVH---EGLNTLr 315

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 406375330 534 ------IRVTVSIGVAGTSPGEEDINVLIKQSDQALYLAKAKGRNK 573
Cdd:PRK10245 316 lpnapqVTLRISVGVAPLNPQMSHYREWLKSADLALYKAKNAGRNR 361
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 384-573 8.95e-17

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 84.34  E-value: 8.95e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406375330  384 RGIEIGMVLEmsllsislafnYKQVQQAR---RNAERDARLDPLTSLYNRRAFED----LVYPIWEMGKRSnkfmSVMLI 456
Cdd:PRK09776  638 DGENIGSVLV-----------IQDVTESRkmlRQLSYSASHDALTHLANRASFEKqlrrLLQTVNSTHQRH----ALVFI 702

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406375330  457 DIDWFKGINDKYGHDMGDKVLKKVAEEIKGQVRGSDITFRWGGEEFLVFLPNTRVHYAKQIAENLrvhlfTHDIN--KFI 534
Cdd:PRK09776  703 DLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSDVLARLGGDEFGLLLPDCNVESARFIATRI-----ISAINdyHFP 777

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 406375330  535 ------RVTVSIGVAGTSPGEEDINVLIKQSDQALYLAKAKGRNK 573
Cdd:PRK09776  778 wegrvyRVGASAGITLIDANNHQASEVMSQADIACYAAKNAGRGR 822
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
412-573 6.13e-16

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 81.27  E-value: 6.13e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406375330 412 RRNAER---DARLDPLTSLYNRRAFEDLVYPIWEmgKRSNKFMSVMLIDIDWFKGINDKYGHDMGDKVLKKVAEEIKGQV 488
Cdd:PRK10060 227 RRAQERlriLANTDSITGLPNRNAIQELIDHAIN--AADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCL 304

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406375330 489 RGSDITFRWGGEEFLVFLPNTRVH----YAKQIAENLR-------VHLFThdinkfirvTVSIGVAGTSPGEEDINVLIK 557
Cdd:PRK10060 305 EEDQTLARLGGDEFLVLASHTSQAaleaMASRILTRLRlpfriglIEVYT---------GCSIGIALAPEHGDDSESLIR 375

                        170
                 ....*....|....*.
gi 406375330 558 QSDQALYLAKAKGRNK 573
Cdd:PRK10060 376 SADTAMYTAKEGGRGQ 391
7TMR-DISMED2 pfam07696
7TMR-DISM extracellular 2; This entry represents one of two distinct types of extracellular ...
 42-183 4.95e-15

7TMR-DISM extracellular 2; This entry represents one of two distinct types of extracellular domain found in the 7TM-DISM (7TM Receptors with Diverse Intracellular Signalling Modules) bacterial transmembrane proteins. It is possible that this domain adopts a jelly roll fold and acts as a receptor for carbohydrates and their derivatives. It can also recognize Ca(II) (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 429601  Cd Length: 127  Bit Score: 71.99  E-value: 4.95e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406375330   42 WMYYEE-GSQLTAEDILTKYQQntLIKNTNGRVSYGFTGNTVWgvlaveldtygvLVTRIANNSPINVPFLplkIEIDNA 120
Cdd:pfam07696   1 VEYLEDpTGSLTIEDVLSADGR--FRPPEKGVPNFGYSSSAYW------------LRFTLENPTDAPKDWL---LELAYP 63

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 406375330  121 WLDDIDLYFFENGQRKRHVKLGDNQVHSARFEDARMPSVFYRFTQPETL-VVFRFSSEDPMTIP 183
Cdd:pfam07696  64 LLDEIDLYLPDGGGGYREQRLGDRLPFSQRPVAHRNFVFPLPLPPGETVtLYLRVKSSGSLLLP 127
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 492-567 2.05e-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: 71.48  E-value: 2.05e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 406375330 492 DITFRWGGEEFLVFLPNTRVHYAKQIAENLRVHLFTHdinKFIRVTVSIGVAGTSpgeedinvLIKQSDqALYLAK 567
Cdd:COG3706  116 DLVARYGGEEFAILLPGTDLEGALAVAERIREAVAEL---PSLRVTVSIGVAGDS--------LLKRAD-ALYQAR 179
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
 452-568 2.46e-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: 2.46e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406375330 452 SVMLIDIDWFKGINDKYGHDMGDKVLKKVAEEIKGQV-RGSDITFRWGGEEFLVFLPNTRVHYAKQIAENLRVHLFTHDI 530
Cdd:cd07556    3 TILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIrRSGDLKIKTIGDEFMVVSGLDHPAAAVAFAEDMREAVSALNQ 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 406375330 531 NKFIRVTVSIGVA---------GTSPGEEDINVLIKQSDQALYLAKA 568
Cdd:cd07556   83 SEGNPVRVRIGIHtgpvvvgviGSRPQYDVWGALVNLASRMESQAKA 129
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 409-570 6.58e-12

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 68.64  E-value: 6.58e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406375330 409 QQARRNAERDARLDPLTSLYNR----RAFEDLVYPIWEMgkrsnkfmSVMLIDIDWFKGINDKYGHDMGDKVLKKVAEEI 484
Cdd:PRK11359 366 EKSRQHIEQLIQFDPLTGLPNRnnlhNYLDDLVDKAVSP--------VVYLIGVDHFQDVIDSLGYAWADQALLEVVNRF 437

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406375330 485 KGQVRGSDITFRWGGEEFLVFLPNTRVHYAKQIAENLRvHLFTHDI---NKFIRVTVSIGVAGTSPGEEDinVLIKQSDQ 561
Cdd:PRK11359 438 REKLKPDQYLCRIEGTQFVLVSLENDVSNITQIADELR-NVVSKPImidDKPFPLTLSIGISYDVGKNRD--YLLSTAHN 514

                        170
                 ....*....|
gi 406375330 562 AL-YLAKAKG 570
Cdd:PRK11359 515 AMdYIRKNGG 524
PRK09966 PRK09966
diguanylate cyclase DgcN;
407-567 2.19e-11

diguanylate cyclase DgcN;


Pssm-ID: 182171 [Multi-domain]  Cd Length: 407  Bit Score: 65.80  E-value: 2.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406375330 407 QVQQARRNAE--RDARLDPLTSLYNRRAFEDLVYPIweMGKRSNKFMSVML-IDIDWFKGINDKYGHDMGDKVLKKVAEE 483
Cdd:PRK09966 234 QLRLQAKNAQllRTALHDPLTGLANRAAFRSGINTL--MNNSDARKTSALLfLDGDNFKYINDTWGHATGDRVLIEIAKR 311

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406375330 484 IkGQVRGSDI-TFRWGGEEFLVFLPNTRVHY-AKQIAENLRVHL---FTHDINKFIRVTVSIGVAGT---SPGEEdinvL 555
Cdd:PRK09966 312 L-AEFGGLRHkAYRLGGDEFAMVLYDVQSESeVQQICSALTQIFnlpFDLHNGHQTTMTLSIGYAMTiehASAEK----L 386

                        170
                 ....*....|..
gi 406375330 556 IKQSDQALYLAK 567
Cdd:PRK09966 387 QELADHNMYQAK 398
PRK11829 PRK11829
biofilm formation regulator HmsP; Provisional
 393-577 4.16e-04

biofilm formation regulator HmsP; Provisional


Pssm-ID: 183329 [Multi-domain]  Cd Length: 660  Bit Score: 43.39  E-value: 4.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406375330 393 EMSLLSISLAFNYKQVQQARRNAERDARLDPLTSLYNRRAFEDLVYPIWEMGKRSNKFmSVMLIDIDWFK---GINDKYG 469
Cdd:PRK11829 206 ELGVLVRNYNRNQQLLADAYADMGRISHRFPVTELPNRSLFISLLEKEIASSTRTDHF-HLLVIGIETLQevsGAMSEAQ 284

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406375330 470 HDMgdkVLKKVAEEIKGQVRGSDITFRWGGEEFLVFLPNT-RVHYAKQIAENLrVHLFTHDI---NKFIRVTVSIGVAGT 545
Cdd:PRK11829 285 HQQ---LLLTIVQRIEQCIDDSDLLAQLSKTEFAVLARGTrRSFPAMQLARRI-MSQVTQPLffdEITLRPSASIGITRY 360

                        170       180       190
                 ....*....|....*....|....*....|..
gi 406375330 546 SPGEEDINVLIKQSDQALYLAKAKGRNKKWCF 577
Cdd:PRK11829 361 QAQQDTAESMMRNASTAMMAAHHEGRNQIMVF 392
 
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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