|
Name |
Accession |
Description |
Interval |
E-value |
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
112-378 |
6.41e-53 |
|
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: 177.09 E-value: 6.41e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670635 112 WWSRVMLGLQSLMIAALTLRASLLLRPHGASLSVGAVQLRFVLLIHGLFYVAKAVWALALGAFVDLAAFGGVLIQVSLVE 191
Cdd:COG2199 8 LLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670635 192 GSMAVMLIALSMTgTERHRREEHMGQLAARDPLTGLLNRRA-LLARAPALLAQASQAHPGALLLIDIDNFKQVNDLHGHA 270
Cdd:COG2199 88 LALLLLLLALEDI-TELRRLEERLRRLATHDPLTGLPNRRAfEERLERELARARREGRPLALLLIDLDHFKRINDTYGHA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670635 271 AGDKLLEALSTLLREVLPEDALAARLGGDEFVIVLRDVRPEQVEHLGEQLREAFAHVARKGVPTPDAVSLSVGVSLYSTP 350
Cdd:COG2199 167 AGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELEGKELRVTVSIGVALYPED 246
|
250 260
....*....|....*....|....*...
gi 2543670635 351 ALALESLLAMADAALYDAKRAGRNRLVV 378
Cdd:COG2199 247 GDSAEELLRRADLALYRAKRAGRNRVVV 274
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
221-377 |
5.23e-50 |
|
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: 165.42 E-value: 5.23e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670635 221 RDPLTGLLN-RRALLARAPALLAQASQAHPGALLLIDIDNFKQVNDLHGHAAGDKLLEALSTLLREVLPEDALAARLGGD 299
Cdd:cd01949 2 TDPLTGLPNrRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGD 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2543670635 300 EFVIVLRDVRPEQVEHLGEQLREAFAHVARKGVPTPDaVSLSVGVSLYSTPALALESLLAMADAALYDAKRAGRNRLV 377
Cdd:cd01949 82 EFAILLPGTDLEEAEALAERLREAIEEPFFIDGQEIR-VTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNRVV 158
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
217-378 |
7.01e-44 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 149.71 E-value: 7.01e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670635 217 QLAARDPLTGLLN-RRALLARAPALLAQASQAHPGALLLIDIDNFKQVNDLHGHAAGDKLLEALSTLLREVLPEDALAAR 295
Cdd:smart00267 1 RLAFRDPLTGLPNrRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670635 296 LGGDEFVIVLRDVRPEQVEHLGEQLREAFAHVARKGvPTPDAVSLSVGVSLYSTPALALESLLAMADAALYDAKRAGRNR 375
Cdd:smart00267 81 LGGDEFALLLPETSLEEAIALAERILQQLREPIIIH-GIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQ 159
|
...
gi 2543670635 376 LVV 378
Cdd:smart00267 160 VAV 162
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
219-375 |
1.40e-41 |
|
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: 143.55 E-value: 1.40e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670635 219 AARDPLTGLLN-RRALLARAPALLAQASQAHPGALLLIDIDNFKQVNDLHGHAAGDKLLEALSTLLREVLPEDALAARLG 297
Cdd:pfam00990 1 AAHDPLTGLPNrRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670635 298 GDEFVIVLRDVRPEQVEHLGEQLREAFAHVAR--KGVPTPDAVSLSVGVSLYSTPALALESLLAMADAALYDAKRAGRNR 375
Cdd:pfam00990 81 GDEFAILLPETSLEGAQELAERIRRLLAKLKIphTVSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGRNR 160
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
218-379 |
1.89e-33 |
|
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: 122.45 E-value: 1.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670635 218 LAARDPLTGLLN-RRALLARAPALLAQASQAHPGALLLIDIDNFKQVNDLHGHAAGDKLLEALSTLLREVLPEDALAARL 296
Cdd:TIGR00254 1 QAVRDPLTGLYNrRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670635 297 GGDEFVIVLRDVRPEQVEHLGEQLREAfAHVARKGVPTPDAVSL--SVGVSLYSTPALALESLLAMADAALYDAKRAGRN 374
Cdd:TIGR00254 81 GGEEFVVILPGTPLEDALSKAERLRDA-INSKPIEVAGSETLTVtvSIGVACYPGHGLTLEELLKRADEALYQAKKAGRN 159
|
....*
gi 2543670635 375 RLVVN 379
Cdd:TIGR00254 160 RVVVA 164
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
198-377 |
1.53e-31 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 124.24 E-value: 1.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670635 198 LIALSMTGTERHRREEHMGQ-------LAARDPLTGLLNRR-ALLARAPALLAQASQAHPGALLLIDIDNFKQVNDLHGH 269
Cdd:PRK09581 264 LLARVRTQIRRKRYQDALRNnleqsieMAVTDGLTGLHNRRyFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGH 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670635 270 AAGDKLLEALSTLLREVLPEDALAARLGGDEFVIVLRDVRPEQVEHLGEQLREAFA----HVARKGVPTPdaVSLSVGVS 345
Cdd:PRK09581 344 DAGDEVLREFAKRLRNNIRGTDLIARYGGEEFVVVMPDTDIEDAIAVAERIRRKIAeepfIISDGKERLN--VTVSIGVA 421
|
170 180 190
....*....|....*....|....*....|..
gi 2543670635 346 LYSTPALALESLLAMADAALYDAKRAGRNRLV 377
Cdd:PRK09581 422 ELRPSGDTIEALIKRADKALYEAKNTGRNRVV 453
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
112-378 |
6.41e-53 |
|
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: 177.09 E-value: 6.41e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670635 112 WWSRVMLGLQSLMIAALTLRASLLLRPHGASLSVGAVQLRFVLLIHGLFYVAKAVWALALGAFVDLAAFGGVLIQVSLVE 191
Cdd:COG2199 8 LLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670635 192 GSMAVMLIALSMTgTERHRREEHMGQLAARDPLTGLLNRRA-LLARAPALLAQASQAHPGALLLIDIDNFKQVNDLHGHA 270
Cdd:COG2199 88 LALLLLLLALEDI-TELRRLEERLRRLATHDPLTGLPNRRAfEERLERELARARREGRPLALLLIDLDHFKRINDTYGHA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670635 271 AGDKLLEALSTLLREVLPEDALAARLGGDEFVIVLRDVRPEQVEHLGEQLREAFAHVARKGVPTPDAVSLSVGVSLYSTP 350
Cdd:COG2199 167 AGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELEGKELRVTVSIGVALYPED 246
|
250 260
....*....|....*....|....*...
gi 2543670635 351 ALALESLLAMADAALYDAKRAGRNRLVV 378
Cdd:COG2199 247 GDSAEELLRRADLALYRAKRAGRNRVVV 274
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
221-377 |
5.23e-50 |
|
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: 165.42 E-value: 5.23e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670635 221 RDPLTGLLN-RRALLARAPALLAQASQAHPGALLLIDIDNFKQVNDLHGHAAGDKLLEALSTLLREVLPEDALAARLGGD 299
Cdd:cd01949 2 TDPLTGLPNrRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGD 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2543670635 300 EFVIVLRDVRPEQVEHLGEQLREAFAHVARKGVPTPDaVSLSVGVSLYSTPALALESLLAMADAALYDAKRAGRNRLV 377
Cdd:cd01949 82 EFAILLPGTDLEEAEALAERLREAIEEPFFIDGQEIR-VTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNRVV 158
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
1-378 |
1.35e-46 |
|
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: 169.18 E-value: 1.35e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670635 1 MALDPSTLLILTIALAASASLYLAIEWNSVRERSLLLWSSGFAIITIGSFLALLRSRGYLLVGIWFANGLLIAAHACFLA 80
Cdd:COG5001 33 LLALALLLLLLLLLLALLLAALLLLALLALLALLLLAAALLALALAALLLAALLAALLLLLLLLLALLVLLLLLLLLLAL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670635 81 GVAWFTRSRVSRGWWLIALLWVLMLLLPAHAWWSRVMLGLQSLMIAALTLRASLLLRPHGASLSVGAVQLRFVLLIHGLF 160
Cdd:COG5001 113 LALLAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARALLALLLLLLLALLLLLLLLLLLALLLLLLLAL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670635 161 YVAKAVWALALGAFVDLAAFGGVLIQVSLVEGSMAVMLIALSMTGTERHRREEHMGQLAARDPLTGLLN-RRALLARAPA 239
Cdd:COG5001 193 LLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEERLRHLAYHDPLTGLPNrRLFLDRLEQA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670635 240 LLAQASQAHPGALLLIDIDNFKQVNDLHGHAAGDKLLEALSTLLREVLPEDALAARLGGDEFVIVLRDVR-PEQVEHLGE 318
Cdd:COG5001 273 LARARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVLLPDLDdPEDAEAVAE 352
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2543670635 319 QLREAFA---HVARKGVptpdAVSLSVGVSLYSTPALALESLLAMADAALYDAKRAGRNRLVV 378
Cdd:COG5001 353 RILAALAepfELDGHEL----YVSASIGIALYPDDGADAEELLRNADLAMYRAKAAGRNRYRF 411
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
217-378 |
7.01e-44 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 149.71 E-value: 7.01e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670635 217 QLAARDPLTGLLN-RRALLARAPALLAQASQAHPGALLLIDIDNFKQVNDLHGHAAGDKLLEALSTLLREVLPEDALAAR 295
Cdd:smart00267 1 RLAFRDPLTGLPNrRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670635 296 LGGDEFVIVLRDVRPEQVEHLGEQLREAFAHVARKGvPTPDAVSLSVGVSLYSTPALALESLLAMADAALYDAKRAGRNR 375
Cdd:smart00267 81 LGGDEFALLLPETSLEEAIALAERILQQLREPIIIH-GIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQ 159
|
...
gi 2543670635 376 LVV 378
Cdd:smart00267 160 VAV 162
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
219-375 |
1.40e-41 |
|
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: 143.55 E-value: 1.40e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670635 219 AARDPLTGLLN-RRALLARAPALLAQASQAHPGALLLIDIDNFKQVNDLHGHAAGDKLLEALSTLLREVLPEDALAARLG 297
Cdd:pfam00990 1 AAHDPLTGLPNrRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670635 298 GDEFVIVLRDVRPEQVEHLGEQLREAFAHVAR--KGVPTPDAVSLSVGVSLYSTPALALESLLAMADAALYDAKRAGRNR 375
Cdd:pfam00990 81 GDEFAILLPETSLEGAQELAERIRRLLAKLKIphTVSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGRNR 160
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
218-379 |
1.89e-33 |
|
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: 122.45 E-value: 1.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670635 218 LAARDPLTGLLN-RRALLARAPALLAQASQAHPGALLLIDIDNFKQVNDLHGHAAGDKLLEALSTLLREVLPEDALAARL 296
Cdd:TIGR00254 1 QAVRDPLTGLYNrRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670635 297 GGDEFVIVLRDVRPEQVEHLGEQLREAfAHVARKGVPTPDAVSL--SVGVSLYSTPALALESLLAMADAALYDAKRAGRN 374
Cdd:TIGR00254 81 GGEEFVVILPGTPLEDALSKAERLRDA-INSKPIEVAGSETLTVtvSIGVACYPGHGLTLEELLKRADEALYQAKKAGRN 159
|
....*
gi 2543670635 375 RLVVN 379
Cdd:TIGR00254 160 RVVVA 164
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
198-377 |
1.53e-31 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 124.24 E-value: 1.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670635 198 LIALSMTGTERHRREEHMGQ-------LAARDPLTGLLNRR-ALLARAPALLAQASQAHPGALLLIDIDNFKQVNDLHGH 269
Cdd:PRK09581 264 LLARVRTQIRRKRYQDALRNnleqsieMAVTDGLTGLHNRRyFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGH 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670635 270 AAGDKLLEALSTLLREVLPEDALAARLGGDEFVIVLRDVRPEQVEHLGEQLREAFA----HVARKGVPTPdaVSLSVGVS 345
Cdd:PRK09581 344 DAGDEVLREFAKRLRNNIRGTDLIARYGGEEFVVVMPDTDIEDAIAVAERIRRKIAeepfIISDGKERLN--VTVSIGVA 421
|
170 180 190
....*....|....*....|....*....|..
gi 2543670635 346 LYSTPALALESLLAMADAALYDAKRAGRNRLV 377
Cdd:PRK09581 422 ELRPSGDTIEALIKRADKALYEAKNTGRNRVV 453
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
180-377 |
2.67e-26 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 110.49 E-value: 2.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670635 180 FGGVLIQV----SLVEGSMAVMLIALSM----------------TGTERHR--REEHMGQLAARDPLTGLLN-RRALLAR 236
Cdd:PRK15426 337 FDGVLVRVhtlrEGVRGDFGSISIALTLlwalftamlliswyviRRMVSNMfvLQSSLQWQAWHDPLTRLYNrGALFEKA 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670635 237 APALLAQASQAHPGALLLIDIDNFKQVNDLHGHAAGDKLLEALSTLLREVLPEDALAARLGGDEFVIVLRDVRPEQVEHL 316
Cdd:PRK15426 417 RALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRVGGEEFCVVLPGASLAEAAQV 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2543670635 317 GEQLREAFAH---VARKGvpTPDAVSLSVGVS-LYSTPALALESLLAMADAALYDAKRAGRNRLV 377
Cdd:PRK15426 497 AERIRLRINEkeiLVAKS--TTIRISASLGVSsAEEDGDYDFEQLQSLADRRLYLAKQAGRNRVC 559
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
201-378 |
6.52e-26 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 105.92 E-value: 6.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670635 201 LSMTgTERHRREEHMGQLAA-RDPLTGLLNRRALLARAPALLAQAsQAHPGALLLIDIDNFKQVNDLHGHAAGDKLLEAL 279
Cdd:PRK09894 111 LSFT-AALTDYKIYLLTIRSnMDVLTGLPGRRVLDESFDHQLRNR-EPQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670635 280 STLLREVLPEDALAARLGGDEFVIVLRDVRPEQVEHLGEQLREAfahVARKGVPTPDA---VSLSVGVSLySTPALALES 356
Cdd:PRK09894 189 ATYLASWTRDYETVYRYGGEEFIICLKAATDEEACRAGERIRQL---IANHAITHSDGrinITATFGVSR-AFPEETLDV 264
|
170 180
....*....|....*....|..
gi 2543670635 357 LLAMADAALYDAKRAGRNRLVV 378
Cdd:PRK09894 265 VIGRADRAMYEGKQTGRNRVMF 286
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
206-373 |
6.93e-24 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 103.61 E-value: 6.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670635 206 TERHRREEHMGQLAARDPLTGLLNRRALLARAPALLAQASQAHPGALLLiDIDNFKQVNDLHGHAAGDKLLEALSTLLRE 285
Cdd:PRK10060 224 TEERRAQERLRILANTDSITGLPNRNAIQELIDHAINAADNNQVGIVYL-DLDNFKKVNDAYGHMFGDQLLQDVSLAILS 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670635 286 VLPEDALAARLGGDEFvIVLrdvrpeqVEHLGEQLREAFAHVARKGVPTPDAVSL-------SVGVSLYSTPALALESLL 358
Cdd:PRK10060 303 CLEEDQTLARLGGDEF-LVL-------ASHTSQAALEAMASRILTRLRLPFRIGLievytgcSIGIALAPEHGDDSESLI 374
|
170
....*....|....*
gi 2543670635 359 AMADAALYDAKRAGR 373
Cdd:PRK10060 375 RSADTAMYTAKEGGR 389
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
219-378 |
6.77e-19 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 88.96 E-value: 6.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670635 219 AARDPLTGLLNRRA-LLARAPALLAQASQAHPGALLLIDIDNFKQVNDLHGHAAGDKLLEALSTLLREVLPEDALAARLG 297
Cdd:PRK09776 665 ASHDALTHLANRASfEKQLRRLLQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSDVLARLG 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670635 298 GDEFVIVLRDVRPEQVEHLGEQLREAFahvarKGVPTP-----DAVSLSVGVSLYSTPALALESLLAMADAALYDAKRAG 372
Cdd:PRK09776 745 GDEFGLLLPDCNVESARFIATRIISAI-----NDYHFPwegrvYRVGASAGITLIDANNHQASEVMSQADIACYAAKNAG 819
|
....*.
gi 2543670635 373 RNRLVV 378
Cdd:PRK09776 820 RGRVTV 825
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
219-377 |
7.01e-17 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 81.59 E-value: 7.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670635 219 AARDPLTGLLNRRALLARAPALLAQASQAHPGALLLIDIDNFKQVNDLHGHAAGDKLLEALSTLLREVLPEDALAARLGG 298
Cdd:PRK09966 248 ALHDPLTGLANRAAFRSGINTLMNNSDARKTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHKAYRLGG 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670635 299 DEFVIVLRDVRPE-QVEHLGEQLREAFAHVARKGVPTPDAVSLSVGVSLYSTPALAlESLLAMADAALYDAKRAGRNRLV 377
Cdd:PRK09966 328 DEFAMVLYDVQSEsEVQQICSALTQIFNLPFDLHNGHQTTMTLSIGYAMTIEHASA-EKLQELADHNMYQAKHQRAEKLV 406
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
195-387 |
5.89e-16 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 79.81 E-value: 5.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670635 195 AVMLIALSMtgtERHRREEHMGQLAARDPLTGLLNRRALLARAPALLaqaSQAHPGALLLIDIDNFKQVNDLHGHAAGDK 274
Cdd:PRK11359 355 SQHLAALAL---EQEKSRQHIEQLIQFDPLTGLPNRNNLHNYLDDLV---DKAVSPVVYLIGVDHFQDVIDSLGYAWADQ 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670635 275 LLEALSTLLREVLPEDALAARLGGDEFVIVLRDVRPEQVEHLGEQLRE-AFAHVARKGVPTPdaVSLSVGVSlYSTPAlA 353
Cdd:PRK11359 429 ALLEVVNRFREKLKPDQYLCRIEGTQFVLVSLENDVSNITQIADELRNvVSKPIMIDDKPFP--LTLSIGIS-YDVGK-N 504
|
170 180 190
....*....|....*....|....*....|....*
gi 2543670635 354 LESLLAMADAAL-YDAKRAGRNRLVVNPANVTAAS 387
Cdd:PRK11359 505 RDYLLSTAHNAMdYIRKNGGNGWQFFSPAMNEMVK 539
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
207-378 |
1.15e-14 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 74.48 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670635 207 ERHRREEHMgqlAARDPLTGLLNRRALLARAPALLAQASQAHPGA-LLLIDIDNFKQVNDLHGHAAGDKLLEALSTLLRE 285
Cdd:PRK10245 196 EHKRRLQVM---STRDGMTGVYNRRHWETLLRNEFDNCRRHHRDAtLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQI 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670635 286 VLPEDALAARLGGDEFVIVLRDVRPEQVEHLGEQLREAFAHVARKGVPTpDAVSLSVGVSLYSTPALALESLLAMADAAL 365
Cdd:PRK10245 273 TLRGSDVIGRFGGDEFAVIMSGTPAESAITAMSRVHEGLNTLRLPNAPQ-VTLRISVGVAPLNPQMSHYREWLKSADLAL 351
|
170
....*....|...
gi 2543670635 366 YDAKRAGRNRLVV 378
Cdd:PRK10245 352 YKAKNAGRNRTEV 364
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
292-369 |
2.27e-09 |
|
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: 56.46 E-value: 2.27e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2543670635 292 LAARLGGDEFVIVLRDVRPEQVEHLGEQLREAFAHvarkgvPTPDAVSLSVGVslystpalALESLLAMADaALYDAK 369
Cdd:COG3706 117 LVARYGGEEFAILLPGTDLEGALAVAERIREAVAE------LPSLRVTVSIGV--------AGDSLLKRAD-ALYQAR 179
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
252-345 |
2.90e-08 |
|
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: 51.97 E-value: 2.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670635 252 LLLIDIDNFKQVNDLHGHAAGDKLLEALSTLLREVLPEDA-LAARLGGDEFVIVLRDVRPEQVEHLGEQLREAFAHVARK 330
Cdd:cd07556 4 ILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSGdLKIKTIGDEFMVVSGLDHPAAAVAFAEDMREAVSALNQS 83
|
90
....*....|....*
gi 2543670635 331 GVPtpdAVSLSVGVS 345
Cdd:cd07556 84 EGN---PVRVRIGIH 95
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
210-386 |
1.51e-05 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 47.02 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670635 210 RREEHMGQLAARDPLTGLLNrraLLARAPALLAQASQAHPGALLLIDIDNFKQVNDLHGHAAGDKLLEALSTLLREVLPE 289
Cdd:PRK13561 222 RQYEEQSRNATRFPVSDLPN---KALLMALLEQVVARKQTTALMIITCETLRDTAGVLKEAQREILLLTLVEKLKSVLSP 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670635 290 DALAARLGGDEFVIVLRDV-RPEQVEHLGEQLREAFahvaRKGVPTPDAV---SLSVGVSLYSTpALALESLLAMADAAL 365
Cdd:PRK13561 299 RMVLAQISGYDFAIIANGVkEPWHAITLGQQVLTII----NERLPIQRIQlrpSCSIGIAMFYG-DLTAEQLYSRAISAA 373
|
170 180
....*....|....*....|..
gi 2543670635 366 YDAKRAGRNR-LVVNPANVTAA 386
Cdd:PRK13561 374 FTARRKGKNQiQFFDPQQMEAA 395
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
215-378 |
2.27e-05 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 46.47 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670635 215 MGQLAARDPLTGLLNRRALLARAPALLAQASQAHPGALLLIDIDNFKQVNDLHGHAAGDKLLEALSTLLREVLPEDALAA 294
Cdd:PRK11829 228 MGRISHRFPVTELPNRSLFISLLEKEIASSTRTDHFHLLVIGIETLQEVSGAMSEAQHQQLLLTIVQRIEQCIDDSDLLA 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670635 295 RLGGDEFVIVLRDV-RPEQVEHLGEQLREAFAHVArkgvpTPDAVSL----SVGVSLYSTPALALESLLAMADAALYDAK 369
Cdd:PRK11829 308 QLSKTEFAVLARGTrRSFPAMQLARRIMSQVTQPL-----FFDEITLrpsaSIGITRYQAQQDTAESMMRNASTAMMAAH 382
|
....*....
gi 2543670635 370 RAGRNRLVV 378
Cdd:PRK11829 383 HEGRNQIMV 391
|
|
| PI-PLC-C1 |
pfam16670 |
Phosphoinositide phospholipase C, Ca2+-dependent; PI-PLC-C1 is a family of calcium 2 ... |
245-338 |
7.39e-03 |
|
Phosphoinositide phospholipase C, Ca2+-dependent; PI-PLC-C1 is a family of calcium 2+-dependent phosphatidylinositol-specific phospholipase C1 enzymes from bacteria and fungi. The enzyme classification number is EC:3.1.4.11. This enzyme is involved in part of the myo-inositol phosphate metabolic pathway.
Pssm-ID: 435502 Cd Length: 330 Bit Score: 37.95 E-value: 7.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670635 245 SQAHPGAL-LLIDIdNFKQVNDLHGHAAG-------DKLLEALSTLLREVLPEDALaarlggdefvivlrdVRPEQVEHL 316
Cdd:pfam16670 123 SDAHPDHVpIFILL-ELKDGEPALALLGGveaepftAALLDALDAEIRSVFGPEKL---------------ITPDDVRGK 186
|
90 100
....*....|....*....|..
gi 2543670635 317 GEQLREAfahVARKGVPTPDAV 338
Cdd:pfam16670 187 YLTLEEA---VLAGGWPTLDAA 205
|
|
| |
