|
Name |
Accession |
Description |
Interval |
E-value |
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
416-571 |
1.12e-54 |
|
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: 182.37 E-value: 1.12e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896544729 416 TDQLTGLLNRRSLEERVRQ--RRAEGSTQAV-VILLDVDHFKAINDGQGHAAGDDVLVQVAQLLRSHLRRNDSIARYGGE 492
Cdd:cd01949 2 TDPLTGLPNRRAFEERLERllARARRSGRPLaLLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGD 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 896544729 493 EFLVLLADGDLASGRRLAESLRVALRAQDIVLGSRdiLRVTASFGVAQGALDPIGWHALVRAADAAMYEAKALGRDRVQ 571
Cdd:cd01949 82 EFAILLPGTDLEEAEALAERLREAIEEPFFIDGQE--IRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNRVV 158
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
326-572 |
2.57e-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: 182.87 E-value: 2.57e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896544729 326 AVRLTVLGATALGTLLLLALALRIAHVQILRPLLQAQAQVIQIASDTPGAEQHATHPMAEMQRLFDAIEVLRAKSH---Q 402
Cdd:COG2199 23 LLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLLLLALEditE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896544729 403 RSALTRELRELADTDQLTGLLNRRSLEERVRQ---RRAEGSTQAVVILLDVDHFKAINDGQGHAAGDDVLVQVAQLLRSH 479
Cdd:COG2199 103 LRRLEERLRRLATHDPLTGLPNRRAFEERLERelaRARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRAS 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896544729 480 LRRNDSIARYGGEEFLVLLADGDLASGRRLAESLRVALRAQDIVLGSRDIlRVTASFGVAQGALDPIGWHALVRAADAAM 559
Cdd:COG2199 183 LRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELEGKEL-RVTVSIGVALYPEDGDSAEELLRRADLAL 261
|
250
....*....|...
gi 896544729 560 YEAKALGRDRVQV 572
Cdd:COG2199 262 YRAKRAGRNRVVV 274
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
414-569 |
1.03e-44 |
|
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: 155.87 E-value: 1.03e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896544729 414 ADTDQLTGLLNRRSLEERVRQ--RRAEGSTQAV-VILLDVDHFKAINDGQGHAAGDDVLVQVAQLLRSHLRRNDSIARYG 490
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQelQRALREGSPVaVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896544729 491 GEEFLVLLADGDLASGRRLAESLRVALRAQDI-VLGSRDILRVTASFGVAQGALDPIGWHALVRAADAAMYEAKALGRDR 569
Cdd:pfam00990 81 GDEFAILLPETSLEGAQELAERIRRLLAKLKIpHTVSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGRNR 160
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
412-572 |
2.68e-44 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 154.71 E-value: 2.68e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896544729 412 ELADTDQLTGLLNRRSLEERVRQ---RRAEGSTQAVVILLDVDHFKAINDGQGHAAGDDVLVQVAQLLRSHLRRNDSIAR 488
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQelqRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896544729 489 YGGEEFLVLLADGDLASGRRLAESLRVALRAQDIVLGSRdiLRVTASFGVAQGALDPIGWHALVRAADAAMYEAKALGRD 568
Cdd:smart00267 81 LGGDEFALLLPETSLEEAIALAERILQQLREPIIIHGIP--LYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRN 158
|
....
gi 896544729 569 RVQV 572
Cdd:smart00267 159 QVAV 162
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
164-572 |
1.08e-43 |
|
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: 165.72 E-value: 1.08e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896544729 164 DRLQALTSVQISDLVAADREAAIPAMQGQILIDLREHGGRLASSVMAPLAVPGAWREPQVRAAQQTEGRLLELWRLAASH 243
Cdd:COG5001 1 LLALAALLLLLLALLLALLLLALLLLALLLAALLALALLLLLLLLLLALLLAALLLLALLALLALLLLAAALLALALAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896544729 244 ESVFRSEPALSLHWDMARRQFFGQSLPMVEKLIDDGRRGVPPPWTAAEFTARYVPTLQSLEALRDGYLGVSIARFQHTRS 323
Cdd:COG5001 81 LLAALLAALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896544729 324 KEAVRLTVLGATALGTLLLLALALRIAHVQILRPLLQAQAQVIQIASDTPGAEQHATHPMAEMQRLFDAIEVLRAKSHQR 403
Cdd:COG5001 161 LLALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITER 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896544729 404 SALTRELRELADTDQLTGLLNRRSLEERVRQ---RRAEGSTQAVVILLDVDHFKAINDGQGHAAGDDVLVQVAQLLRSHL 480
Cdd:COG5001 241 KRAEERLRHLAYHDPLTGLPNRRLFLDRLEQalaRARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896544729 481 RRNDSIARYGGEEFLVLLAD-GDLASGRRLAESLRVALrAQDIVLGSRDIlRVTASFGVAQGALDPIGWHALVRAADAAM 559
Cdd:COG5001 321 REGDTVARLGGDEFAVLLPDlDDPEDAEAVAERILAAL-AEPFELDGHEL-YVSASIGIALYPDDGADAEELLRNADLAM 398
|
410
....*....|...
gi 896544729 560 YEAKALGRDRVQV 572
Cdd:COG5001 399 YRAKAAGRNRYRF 411
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
413-573 |
3.66e-42 |
|
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: 149.02 E-value: 3.66e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896544729 413 LADTDQLTGLLNRRSLEERVRQRRAEGST---QAVVILLDVDHFKAINDGQGHAAGDDVLVQVAQLLRSHLRRNDSIARY 489
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRfqrSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896544729 490 GGEEFLVLLADGDLASGRRLAESLRVALRAQDIVLGSRDILRVTASFGVAQGALDPIGWHALVRAADAAMYEAKALGRDR 569
Cdd:TIGR00254 81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSETLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRNR 160
|
....
gi 896544729 570 VQVS 573
Cdd:TIGR00254 161 VVVA 164
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
412-575 |
1.11e-37 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 145.04 E-value: 1.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896544729 412 ELADTDQLTGLLNRRSLEERVRQ---RRAEGSTQAVVILLDVDHFKAINDGQGHAAGDDVLVQVAQLLRSHLRRNDSIAR 488
Cdd:PRK09581 290 EMAVTDGLTGLHNRRYFDMHLKNlieRANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIAR 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896544729 489 YGGEEFLVLLADGDLASGRRLAESLRVALRAQD-IVLGSRDILRVTASFGVA--QGALDPIGwhALVRAADAAMYEAKAL 565
Cdd:PRK09581 370 YGGEEFVVVMPDTDIEDAIAVAERIRRKIAEEPfIISDGKERLNVTVSIGVAelRPSGDTIE--ALIKRADKALYEAKNT 447
|
170
....*....|
gi 896544729 566 GRDRVQVSPA 575
Cdd:PRK09581 448 GRNRVVALAA 457
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
416-571 |
1.12e-54 |
|
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: 182.37 E-value: 1.12e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896544729 416 TDQLTGLLNRRSLEERVRQ--RRAEGSTQAV-VILLDVDHFKAINDGQGHAAGDDVLVQVAQLLRSHLRRNDSIARYGGE 492
Cdd:cd01949 2 TDPLTGLPNRRAFEERLERllARARRSGRPLaLLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGD 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 896544729 493 EFLVLLADGDLASGRRLAESLRVALRAQDIVLGSRdiLRVTASFGVAQGALDPIGWHALVRAADAAMYEAKALGRDRVQ 571
Cdd:cd01949 82 EFAILLPGTDLEEAEALAERLREAIEEPFFIDGQE--IRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNRVV 158
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
326-572 |
2.57e-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: 182.87 E-value: 2.57e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896544729 326 AVRLTVLGATALGTLLLLALALRIAHVQILRPLLQAQAQVIQIASDTPGAEQHATHPMAEMQRLFDAIEVLRAKSH---Q 402
Cdd:COG2199 23 LLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLLLLALEditE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896544729 403 RSALTRELRELADTDQLTGLLNRRSLEERVRQ---RRAEGSTQAVVILLDVDHFKAINDGQGHAAGDDVLVQVAQLLRSH 479
Cdd:COG2199 103 LRRLEERLRRLATHDPLTGLPNRRAFEERLERelaRARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRAS 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896544729 480 LRRNDSIARYGGEEFLVLLADGDLASGRRLAESLRVALRAQDIVLGSRDIlRVTASFGVAQGALDPIGWHALVRAADAAM 559
Cdd:COG2199 183 LRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELEGKEL-RVTVSIGVALYPEDGDSAEELLRRADLAL 261
|
250
....*....|...
gi 896544729 560 YEAKALGRDRVQV 572
Cdd:COG2199 262 YRAKRAGRNRVVV 274
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
414-569 |
1.03e-44 |
|
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: 155.87 E-value: 1.03e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896544729 414 ADTDQLTGLLNRRSLEERVRQ--RRAEGSTQAV-VILLDVDHFKAINDGQGHAAGDDVLVQVAQLLRSHLRRNDSIARYG 490
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQelQRALREGSPVaVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896544729 491 GEEFLVLLADGDLASGRRLAESLRVALRAQDI-VLGSRDILRVTASFGVAQGALDPIGWHALVRAADAAMYEAKALGRDR 569
Cdd:pfam00990 81 GDEFAILLPETSLEGAQELAERIRRLLAKLKIpHTVSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGRNR 160
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
412-572 |
2.68e-44 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 154.71 E-value: 2.68e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896544729 412 ELADTDQLTGLLNRRSLEERVRQ---RRAEGSTQAVVILLDVDHFKAINDGQGHAAGDDVLVQVAQLLRSHLRRNDSIAR 488
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQelqRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896544729 489 YGGEEFLVLLADGDLASGRRLAESLRVALRAQDIVLGSRdiLRVTASFGVAQGALDPIGWHALVRAADAAMYEAKALGRD 568
Cdd:smart00267 81 LGGDEFALLLPETSLEEAIALAERILQQLREPIIIHGIP--LYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRN 158
|
....
gi 896544729 569 RVQV 572
Cdd:smart00267 159 QVAV 162
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
164-572 |
1.08e-43 |
|
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: 165.72 E-value: 1.08e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896544729 164 DRLQALTSVQISDLVAADREAAIPAMQGQILIDLREHGGRLASSVMAPLAVPGAWREPQVRAAQQTEGRLLELWRLAASH 243
Cdd:COG5001 1 LLALAALLLLLLALLLALLLLALLLLALLLAALLALALLLLLLLLLLALLLAALLLLALLALLALLLLAAALLALALAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896544729 244 ESVFRSEPALSLHWDMARRQFFGQSLPMVEKLIDDGRRGVPPPWTAAEFTARYVPTLQSLEALRDGYLGVSIARFQHTRS 323
Cdd:COG5001 81 LLAALLAALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896544729 324 KEAVRLTVLGATALGTLLLLALALRIAHVQILRPLLQAQAQVIQIASDTPGAEQHATHPMAEMQRLFDAIEVLRAKSHQR 403
Cdd:COG5001 161 LLALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITER 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896544729 404 SALTRELRELADTDQLTGLLNRRSLEERVRQ---RRAEGSTQAVVILLDVDHFKAINDGQGHAAGDDVLVQVAQLLRSHL 480
Cdd:COG5001 241 KRAEERLRHLAYHDPLTGLPNRRLFLDRLEQalaRARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896544729 481 RRNDSIARYGGEEFLVLLAD-GDLASGRRLAESLRVALrAQDIVLGSRDIlRVTASFGVAQGALDPIGWHALVRAADAAM 559
Cdd:COG5001 321 REGDTVARLGGDEFAVLLPDlDDPEDAEAVAERILAAL-AEPFELDGHEL-YVSASIGIALYPDDGADAEELLRNADLAM 398
|
410
....*....|...
gi 896544729 560 YEAKALGRDRVQV 572
Cdd:COG5001 399 YRAKAAGRNRYRF 411
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
413-573 |
3.66e-42 |
|
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: 149.02 E-value: 3.66e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896544729 413 LADTDQLTGLLNRRSLEERVRQRRAEGST---QAVVILLDVDHFKAINDGQGHAAGDDVLVQVAQLLRSHLRRNDSIARY 489
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRfqrSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896544729 490 GGEEFLVLLADGDLASGRRLAESLRVALRAQDIVLGSRDILRVTASFGVAQGALDPIGWHALVRAADAAMYEAKALGRDR 569
Cdd:TIGR00254 81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSETLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRNR 160
|
....
gi 896544729 570 VQVS 573
Cdd:TIGR00254 161 VVVA 164
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
412-575 |
1.11e-37 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 145.04 E-value: 1.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896544729 412 ELADTDQLTGLLNRRSLEERVRQ---RRAEGSTQAVVILLDVDHFKAINDGQGHAAGDDVLVQVAQLLRSHLRRNDSIAR 488
Cdd:PRK09581 290 EMAVTDGLTGLHNRRYFDMHLKNlieRANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIAR 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896544729 489 YGGEEFLVLLADGDLASGRRLAESLRVALRAQD-IVLGSRDILRVTASFGVA--QGALDPIGwhALVRAADAAMYEAKAL 565
Cdd:PRK09581 370 YGGEEFVVVMPDTDIEDAIAVAERIRRKIAEEPfIISDGKERLNVTVSIGVAelRPSGDTIE--ALIKRADKALYEAKNT 447
|
170
....*....|
gi 896544729 566 GRDRVQVSPA 575
Cdd:PRK09581 448 GRNRVVALAA 457
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
404-570 |
1.77e-37 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 146.31 E-value: 1.77e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896544729 404 SALTRELRELADTDQLTGLLNRRSLEERVR---QRRAEGSTQAVVILLDVDHFKAINDGQGHAAGDDVLVQVAQLLRSHL 480
Cdd:PRK15426 388 FVLQSSLQWQAWHDPLTRLYNRGALFEKARalaKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSL 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896544729 481 RRNDSIARYGGEEFLVLLADGDLASGRRLAESLRVALRAQDIVLGSRDILRVTASFGVAQGALD-PIGWHALVRAADAAM 559
Cdd:PRK15426 468 RAQDVAGRVGGEEFCVVLPGASLAEAAQVAERIRLRINEKEILVAKSTTIRISASLGVSSAEEDgDYDFEQLQSLADRRL 547
|
170
....*....|.
gi 896544729 560 YEAKALGRDRV 570
Cdd:PRK15426 548 YLAKQAGRNRV 558
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
403-570 |
3.01e-37 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 139.82 E-value: 3.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896544729 403 RSALTRELRELADT----DQLTGLLNRRSLEERV-RQRRAEGSTQAVVILLDVDHFKAINDGQGHAAGDDVLVQVAQLLR 477
Cdd:PRK09894 114 TAALTDYKIYLLTIrsnmDVLTGLPGRRVLDESFdHQLRNREPQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLA 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896544729 478 SHLRRNDSIARYGGEEFLVLLADGDLASGRRLAESLRVALRAQDIVLGSRDIlRVTASFGVAQGALDPIGWHALVRaADA 557
Cdd:PRK09894 194 SWTRDYETVYRYGGEEFIICLKAATDEEACRAGERIRQLIANHAITHSDGRI-NITATFGVSRAFPEETLDVVIGR-ADR 271
|
170
....*....|...
gi 896544729 558 AMYEAKALGRDRV 570
Cdd:PRK09894 272 AMYEGKQTGRNRV 284
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
405-572 |
1.23e-26 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 115.54 E-value: 1.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896544729 405 ALTRELRELADTDQLTGLLNRRSLEERVR---QRRAEGSTQAVVILLDVDHFKAINDGQGHAAGDDVLVQVAQLLRSHLR 481
Cdd:PRK09776 656 KMLRQLSYSASHDALTHLANRASFEKQLRrllQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLR 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896544729 482 RNDSIARYGGEEFLVLLADGDLASGRRLAESLRVALRAQDIVLGSRdILRVTASFGVAQGALDPIGWHALVRAADAAMYE 561
Cdd:PRK09776 736 SSDVLARLGGDEFGLLLPDCNVESARFIATRIISAINDYHFPWEGR-VYRVGASAGITLIDANNHQASEVMSQADIACYA 814
|
170
....*....|.
gi 896544729 562 AKALGRDRVQV 572
Cdd:PRK09776 815 AKNAGRGRVTV 825
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
402-567 |
2.89e-24 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 107.46 E-value: 2.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896544729 402 QRSALTReLRELADTDQLTGLLNRRSLEERVRQR-RAEGSTQAVVILLDVDHFKAINDGQGHAAGDDVLVQVAQLLRSHL 480
Cdd:PRK10060 226 ERRAQER-LRILANTDSITGLPNRNAIQELIDHAiNAADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896544729 481 RRNDSIARYGGEEFLVLLADGDLASGRRLAESLRVALRaQDIVLGSRDILrVTASFGVAQGALDPIGWHALVRAADAAMY 560
Cdd:PRK10060 305 EEDQTLARLGGDEFLVLASHTSQAALEAMASRILTRLR-LPFRIGLIEVY-TGCSIGIALAPEHGDDSESLIRSADTAMY 382
|
....*..
gi 896544729 561 EAKALGR 567
Cdd:PRK10060 383 TAKEGGR 389
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
408-573 |
2.75e-20 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 92.97 E-value: 2.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896544729 408 RELRELADTDQLTGLLNRRSLEERVRQ-----RRaeGSTQAVVILLDVDHFKAINDGQGHAAGDDVLVQVAQLLRSHLRR 482
Cdd:PRK10245 199 RRLQVMSTRDGMTGVYNRRHWETLLRNefdncRR--HHRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRG 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896544729 483 NDSIARYGGEEFLVLL----ADGDLASGRRLAESLRvALRaqdIVLGSRDILRVtaSFGVAQGALDPIGWHALVRAADAA 558
Cdd:PRK10245 277 SDVIGRFGGDEFAVIMsgtpAESAITAMSRVHEGLN-TLR---LPNAPQVTLRI--SVGVAPLNPQMSHYREWLKSADLA 350
|
170
....*....|....*
gi 896544729 559 MYEAKALGRDRVQVS 573
Cdd:PRK10245 351 LYKAKNAGRNRTEVA 365
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
442-564 |
1.87e-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: 70.46 E-value: 1.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896544729 442 QAVVILLDVDHFKAINDGQGHAAGDDVLVQVAQLLRSHLRRN-DSIARYGGEEFLVLLADGDLASGRRLAESLRVALRAQ 520
Cdd:cd07556 1 PVTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSgDLKIKTIGDEFMVVSGLDHPAAAVAFAEDMREAVSAL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 896544729 521 DIVLGSrdilRVTASFGVAQGAL--DPIG-------WHALVRAADAAMYEAKA 564
Cdd:cd07556 81 NQSEGN----PVRVRIGIHTGPVvvGVIGsrpqydvWGALVNLASRMESQAKA 129
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
382-540 |
3.07e-13 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 72.88 E-value: 3.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896544729 382 PMAEMQRLFDAIEVLRAKSHQRSALTRELRELADTDQLTGLLNR----RSLEERVRQRRaegstQAVVILLDVDHFKAIN 457
Cdd:PRK11359 344 TSAFIERVADISQHLAALALEQEKSRQHIEQLIQFDPLTGLPNRnnlhNYLDDLVDKAV-----SPVVYLIGVDHFQDVI 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896544729 458 DGQGHAAGDDVLVQVAQLLRSHLRRNDSIARYGGEEFLVLLADGDLASGRRLAESLRVALRAQDIVLGSRdiLRVTASFG 537
Cdd:PRK11359 419 DSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGTQFVLVSLENDVSNITQIADELRNVVSKPIMIDDKP--FPLTLSIG 496
|
...
gi 896544729 538 VAQ 540
Cdd:PRK11359 497 ISY 499
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
484-563 |
2.18e-10 |
|
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: 59.92 E-value: 2.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896544729 484 DSIARYGGEEFLVLLADGDLASGRRLAESLRVALRAQDIVlgsrdilRVTASFGVAQgaldpigwHALVRAADaAMYEAK 563
Cdd:COG3706 116 DLVARYGGEEFAILLPGTDLEGALAVAERIREAVAELPSL-------RVTVSIGVAG--------DSLLKRAD-ALYQAR 179
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
389-563 |
1.68e-09 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 60.02 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896544729 389 LFDAIEVLRAKSHQRSAltrELRELADTDQLTGLLNRRSLEERVRQRRAEGSTQ--AVVILLDVDHFKAINDGQGHAAGD 466
Cdd:PRK09966 226 LLDEMEEWQLRLQAKNA---QLLRTALHDPLTGLANRAAFRSGINTLMNNSDARktSALLFLDGDNFKYINDTWGHATGD 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896544729 467 DVLVQVAQLLRSHLRRNDSIARYGGEEFLVLLADGDLASG-RRLAESLRVAL-RAQDIVLGSRdiLRVTASFGVAqgald 544
Cdd:PRK09966 303 RVLIEIAKRLAEFGGLRHKAYRLGGDEFAMVLYDVQSESEvQQICSALTQIFnLPFDLHNGHQ--TTMTLSIGYA----- 375
|
170 180
....*....|....*....|....
gi 896544729 545 pIGW-HA----LVRAADAAMYEAK 563
Cdd:PRK09966 376 -MTIeHAsaekLQELADHNMYQAK 398
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
60-579 |
4.37e-07 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 53.34 E-value: 4.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896544729 60 ANLVSAERGPANSLLGADSTDVQQQRRLAAQLAVA--------------RQRVDAATQHLQDVFQNDPRVVDETPRLHEA 125
Cdd:COG3321 809 QCLAAAGDAVVLPSLRRGEDELAQLLTALAQLWVAgvpvdwsalypgrgRRRVPLPTYPFQREDAAAALLAAALAAALAA 888
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896544729 126 RRRLQTARAAVDRVAALPRGERSAEEVEHAINNMFAVYDRLQALTSVQISDLVAADREAAIPAMQGQILIDLREHGGRLA 205
Cdd:COG3321 889 AAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLA 968
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896544729 206 SSVMAPLAVPGAWREPQVRAAQQTEGRLLELWRLAASHESVFRSEPALSLHWDMARRQFFGQSLPMVEKLIDDGRRGVPP 285
Cdd:COG3321 969 AAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAAL 1048
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896544729 286 PWTAAEFTARYVPTLQSLEALRDGYLGVSIARFQHTRSKEAVRLTVLGATALGTLLLLALALRIAHVQILRPLLQAQAQV 365
Cdd:COG3321 1049 AALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALAALAAALLLLALLAALALAAAAAALLALA 1128
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896544729 366 IQIASDTPGAEQHATHPMAEMQRLFDAIEVLRAKSHQRSALTRELRELADTDQLTGLLNRRSLEERVRQRRAEGSTQAVV 445
Cdd:COG3321 1129 ALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALAAALAAALAGLAALLLAALLAALLAAL 1208
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896544729 446 ILLDVDHFKAINDGQGHAAGDDVLVQVAQLLRSHLRRNDSIARYGGEEFLVLLADGDLASGRRLAESLRVALRAQDIVLG 525
Cdd:COG3321 1209 LALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAALAALALLAAAAGLAALAAAAAAAAAALALA 1288
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 896544729 526 SRDILRVTASFGVAQGALDPIGWHALVRAADAAMYEAKALGRDRVQVSPAGRAA 579
Cdd:COG3321 1289 AAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAVAAALA 1342
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
404-498 |
6.93e-05 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 45.62 E-value: 6.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896544729 404 SALTRELRELADT-----------------DQLTGLLNRRSLEER---VRQRRAEGSTQAVVILLDVDHFKAINDGQGHA 463
Cdd:PRK11059 201 RALDHLLSELQDAreersrfdtfirsnafqDAKTGLGNRLFFDNQlatLLEDQEMVGAHGVVMLIRLPDFDLLQEEWGES 280
|
90 100 110
....*....|....*....|....*....|....*..
gi 896544729 464 AGDDVLVQVAQLLRSHLRR-NDSI-ARYGGEEFLVLL 498
Cdd:PRK11059 281 QVEELLFELINLLSTFVMRyPGALlARYSRSDFAVLL 317
|
|
| |
