|
Name |
Accession |
Description |
Interval |
E-value |
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
85-294 |
1.23e-48 |
|
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: 163.23 E-value: 1.23e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434244458 85 RVLHVTSVPMDIEGAELVLELIKDVTDSLLVADIEVRDNIEITQMITKFNELAVRDGFTKLYNKTFINNELESLVQ-AAR 163
Cdd:COG2199 62 LLLLALGLLLLALLLLSLVLELLLLLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELArARR 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434244458 164 GGSPAgeaAVVLLDIDGFKQINDTYGHIAGDDALQYFASKMRSFSRSFDgWVGRFGGDEFVLCAPkGLSEDDLERLFAEI 243
Cdd:COG2199 142 EGRPL---ALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESD-LVARLGGDEFAVLLP-GTDLEEAEALAERL 216
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1434244458 244 -DAIERHVFQAEAGSFSLAASCGVCFVRPD-DTVRSLLDRADVAMYRAKESGR 294
Cdd:COG2199 217 rEALEQLPFELEGKELRVTVSIGVALYPEDgDSAEELLRRADLALYRAKRAGR 269
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
139-294 |
5.07e-45 |
|
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: 150.01 E-value: 5.07e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434244458 139 RDGFTKLYNKTFINNELESLV-QAARGGSPAgeaAVVLLDIDGFKQINDTYGHIAGDDALQYFASKMRSFSRSFDgWVGR 217
Cdd:cd01949 2 TDPLTGLPNRRAFEERLERLLaRARRSGRPL---ALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESD-LVAR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1434244458 218 FGGDEFVLCAPkGLSEDDLERLFAEI-DAIERHVFQAEaGSFSLAASCGVCFVRPD-DTVRSLLDRADVAMYRAKESGR 294
Cdd:cd01949 78 LGGDEFAILLP-GTDLEEAEALAERLrEAIEEPFFIDG-QEIRVTASIGIATYPEDgEDAEELLRRADEALYRAKRSGR 154
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
137-294 |
2.04e-37 |
|
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: 130.45 E-value: 2.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434244458 137 AVRDGFTKLYNKTFINNELESLVQ-AARGGSPAgeaAVVLLDIDGFKQINDTYGHIAGDDALQYFASKMRSFSRSFDgWV 215
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQrALREGSPV---AVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSD-LV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434244458 216 GRFGGDEFVLCapkgLSEDDLERLFAEIDAIERHV------FQAEAGSFSLAASCGVCFVRPD-DTVRSLLDRADVAMYR 288
Cdd:pfam00990 77 ARLGGDEFAIL----LPETSLEGAQELAERIRRLLaklkipHTVSGLPLYVTISIGIAAYPNDgEDPEDLLKRADTALYQ 152
|
....*.
gi 1434244458 289 AKESGR 294
Cdd:pfam00990 153 AKQAGR 158
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
135-294 |
1.01e-36 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 128.52 E-value: 1.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434244458 135 ELAVRDGFTKLYNKTFINNELESLVQAARggSPAGEAAVVLLDIDGFKQINDTYGHIAGDDALQYFASKMRSFSRSFDgW 214
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQ--RQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGD-L 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434244458 215 VGRFGGDEFVLCAPkGLSEDDLERLfAE--IDAIERHVFQAEaGSFSLAASCGVC-FVRPDDTVRSLLDRADVAMYRAKE 291
Cdd:smart00267 78 LARLGGDEFALLLP-ETSLEEAIAL-AEriLQQLREPIIIHG-IPLYLTISIGVAaYPNPGEDAEDLLKRADTALYQAKK 154
|
...
gi 1434244458 292 SGR 294
Cdd:smart00267 155 AGR 157
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
136-298 |
2.25e-35 |
|
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: 125.14 E-value: 2.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434244458 136 LAVRDGFTKLYNKTFINNELESLVQ-AARGGSPAgeaAVVLLDIDGFKQINDTYGHIAGDDALQYFASKMRSFSRSFDgW 214
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKrARRFQRSF---SVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSD-V 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434244458 215 VGRFGGDEFVLCAPKGLSEDDL---ERLFAEIDAIERHVFQAEAGsfSLAASCGV-CFVRPDDTVRSLLDRADVAMYRAK 290
Cdd:TIGR00254 77 VGRYGGEEFVVILPGTPLEDALskaERLRDAINSKPIEVAGSETL--TVTVSIGVaCYPGHGLTLEELLKRADEALYQAK 154
|
....*...
gi 1434244458 291 ESGRRWVE 298
Cdd:TIGR00254 155 KAGRNRVV 162
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
135-294 |
4.21e-30 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 118.08 E-value: 4.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434244458 135 ELAVRDGFTKLYNKTFINNELESLV-QAARGGSPAgeaAVVLLDIDGFKQINDTYGHIAGDDALQYFASKMRSFSRSFDg 213
Cdd:PRK09581 290 EMAVTDGLTGLHNRRYFDMHLKNLIeRANERGKPL---SLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTD- 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434244458 214 WVGRFGGDEFVLCAPkglsEDDLERLFAEIDAIERHV----FQAEAGS--FSLAASCGVCFVRP-DDTVRSLLDRADVAM 286
Cdd:PRK09581 366 LIARYGGEEFVVVMP----DTDIEDAIAVAERIRRKIaeepFIISDGKerLNVTVSIGVAELRPsGDTIEALIKRADKAL 441
|
....*...
gi 1434244458 287 YRAKESGR 294
Cdd:PRK09581 442 YEAKNTGR 449
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
85-294 |
1.23e-48 |
|
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: 163.23 E-value: 1.23e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434244458 85 RVLHVTSVPMDIEGAELVLELIKDVTDSLLVADIEVRDNIEITQMITKFNELAVRDGFTKLYNKTFINNELESLVQ-AAR 163
Cdd:COG2199 62 LLLLALGLLLLALLLLSLVLELLLLLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELArARR 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434244458 164 GGSPAgeaAVVLLDIDGFKQINDTYGHIAGDDALQYFASKMRSFSRSFDgWVGRFGGDEFVLCAPkGLSEDDLERLFAEI 243
Cdd:COG2199 142 EGRPL---ALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESD-LVARLGGDEFAVLLP-GTDLEEAEALAERL 216
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1434244458 244 -DAIERHVFQAEAGSFSLAASCGVCFVRPD-DTVRSLLDRADVAMYRAKESGR 294
Cdd:COG2199 217 rEALEQLPFELEGKELRVTVSIGVALYPEDgDSAEELLRRADLALYRAKRAGR 269
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
139-294 |
5.07e-45 |
|
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: 150.01 E-value: 5.07e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434244458 139 RDGFTKLYNKTFINNELESLV-QAARGGSPAgeaAVVLLDIDGFKQINDTYGHIAGDDALQYFASKMRSFSRSFDgWVGR 217
Cdd:cd01949 2 TDPLTGLPNRRAFEERLERLLaRARRSGRPL---ALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESD-LVAR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1434244458 218 FGGDEFVLCAPkGLSEDDLERLFAEI-DAIERHVFQAEaGSFSLAASCGVCFVRPD-DTVRSLLDRADVAMYRAKESGR 294
Cdd:cd01949 78 LGGDEFAILLP-GTDLEEAEALAERLrEAIEEPFFIDG-QEIRVTASIGIATYPEDgEDAEELLRRADEALYRAKRSGR 154
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
137-294 |
2.04e-37 |
|
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: 130.45 E-value: 2.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434244458 137 AVRDGFTKLYNKTFINNELESLVQ-AARGGSPAgeaAVVLLDIDGFKQINDTYGHIAGDDALQYFASKMRSFSRSFDgWV 215
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQrALREGSPV---AVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSD-LV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434244458 216 GRFGGDEFVLCapkgLSEDDLERLFAEIDAIERHV------FQAEAGSFSLAASCGVCFVRPD-DTVRSLLDRADVAMYR 288
Cdd:pfam00990 77 ARLGGDEFAIL----LPETSLEGAQELAERIRRLLaklkipHTVSGLPLYVTISIGIAAYPNDgEDPEDLLKRADTALYQ 152
|
....*.
gi 1434244458 289 AKESGR 294
Cdd:pfam00990 153 AKQAGR 158
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
135-294 |
1.01e-36 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 128.52 E-value: 1.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434244458 135 ELAVRDGFTKLYNKTFINNELESLVQAARggSPAGEAAVVLLDIDGFKQINDTYGHIAGDDALQYFASKMRSFSRSFDgW 214
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQ--RQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGD-L 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434244458 215 VGRFGGDEFVLCAPkGLSEDDLERLfAE--IDAIERHVFQAEaGSFSLAASCGVC-FVRPDDTVRSLLDRADVAMYRAKE 291
Cdd:smart00267 78 LARLGGDEFALLLP-ETSLEEAIAL-AEriLQQLREPIIIHG-IPLYLTISIGVAaYPNPGEDAEDLLKRADTALYQAKK 154
|
...
gi 1434244458 292 SGR 294
Cdd:smart00267 155 AGR 157
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
136-298 |
2.25e-35 |
|
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: 125.14 E-value: 2.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434244458 136 LAVRDGFTKLYNKTFINNELESLVQ-AARGGSPAgeaAVVLLDIDGFKQINDTYGHIAGDDALQYFASKMRSFSRSFDgW 214
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKrARRFQRSF---SVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSD-V 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434244458 215 VGRFGGDEFVLCAPKGLSEDDL---ERLFAEIDAIERHVFQAEAGsfSLAASCGV-CFVRPDDTVRSLLDRADVAMYRAK 290
Cdd:TIGR00254 77 VGRYGGEEFVVILPGTPLEDALskaERLRDAINSKPIEVAGSETL--TVTVSIGVaCYPGHGLTLEELLKRADEALYQAK 154
|
....*...
gi 1434244458 291 ESGRRWVE 298
Cdd:TIGR00254 155 KAGRNRVV 162
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
80-294 |
2.82e-35 |
|
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: 134.52 E-value: 2.82e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434244458 80 EYLDGRVLHVTSVPMDIEGAELVLELIKDVTDSLLVADIEVRDNIEITQMITKFNELAVRDGFTKLYNKTFINNELES-L 158
Cdd:COG5001 194 LRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEERLRHLAYHDPLTGLPNRRLFLDRLEQaL 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434244458 159 VQAARGGSPAgeaAVVLLDIDGFKQINDTYGHIAGDDALQYFASKMRSFSRSFDgWVGRFGGDEFVLCAPKGLSEDDLER 238
Cdd:COG5001 274 ARARRSGRRL---ALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGD-TVARLGGDEFAVLLPDLDDPEDAEA 349
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434244458 239 LfAE--IDAIERhVFQAEAGSFSLAASCGVCfVRPDD--TVRSLLDRADVAMYRAKESGR 294
Cdd:COG5001 350 V-AEriLAALAE-PFELDGHELYVSASIGIA-LYPDDgaDAEELLRNADLAMYRAKAAGR 406
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
135-294 |
4.21e-30 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 118.08 E-value: 4.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434244458 135 ELAVRDGFTKLYNKTFINNELESLV-QAARGGSPAgeaAVVLLDIDGFKQINDTYGHIAGDDALQYFASKMRSFSRSFDg 213
Cdd:PRK09581 290 EMAVTDGLTGLHNRRYFDMHLKNLIeRANERGKPL---SLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTD- 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434244458 214 WVGRFGGDEFVLCAPkglsEDDLERLFAEIDAIERHV----FQAEAGS--FSLAASCGVCFVRP-DDTVRSLLDRADVAM 286
Cdd:PRK09581 366 LIARYGGEEFVVVMP----DTDIEDAIAVAERIRRKIaeepFIISDGKerLNVTVSIGVAELRPsGDTIEALIKRADKAL 441
|
....*...
gi 1434244458 287 YRAKESGR 294
Cdd:PRK09581 442 YEAKNTGR 449
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
139-294 |
3.34e-28 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 110.16 E-value: 3.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434244458 139 RDGFTKLYNKTFINNELESLvQAARGGSPAgeaAVVLLDIDGFKQINDTYGHIAGDDALQYFASKMRSFSRSFDGwVGRF 218
Cdd:PRK09894 131 MDVLTGLPGRRVLDESFDHQ-LRNREPQNL---YLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYET-VYRY 205
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1434244458 219 GGDEFVLCAPKGLSEDD---LERLFAeidAIERHVFQAEAGSFSLAASCGVCFVRPDDTVRSLLDRADVAMYRAKESGR 294
Cdd:PRK09894 206 GGEEFIICLKAATDEEAcraGERIRQ---LIANHAITHSDGRINITATFGVSRAFPEETLDVVIGRADRAMYEGKQTGR 281
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
57-294 |
6.63e-22 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 95.89 E-value: 6.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434244458 57 QDDPCLNCSSRACLTMQDAVFKIEYLDGRVLhvtsvpmdieGAELVlelIKDVTDSllvadievrdnieiTQMITKFNEL 136
Cdd:PRK09776 612 EQDVVLHCRSGGSYDVHYSITPLSTLDGENI----------GSVLV---IQDVTES--------------RKMLRQLSYS 664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434244458 137 AVRDGFTKLYNKTFINNELESLVQAARggSPAGEAAVVLLDIDGFKQINDTYGHIAGDDALQYFASKMRSFSRSFDgWVG 216
Cdd:PRK09776 665 ASHDALTHLANRASFEKQLRRLLQTVN--STHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSD-VLA 741
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434244458 217 RFGGDEFVLCAPK---GLSEDDLERLfaeIDAIERHVFQAEAGSFSLAASCGVCFVrpDDTVRS---LLDRADVAMYRAK 290
Cdd:PRK09776 742 RLGGDEFGLLLPDcnvESARFIATRI---ISAINDYHFPWEGRVYRVGASAGITLI--DANNHQaseVMSQADIACYAAK 816
|
....
gi 1434244458 291 ESGR 294
Cdd:PRK09776 817 NAGR 820
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
82-298 |
2.32e-19 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 86.81 E-value: 2.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434244458 82 LDGRVLHVTSVPMdiegaELVLELIKDVTDSLLVADIEVRDNIEITQMITKFNELAVRDGFTKLYNK----TFINNELES 157
Cdd:PRK10245 155 LTGITVSFNSAPL-----EWWLSLPVIVIYPLLFAWVSYQTATKLAEHKRRLQVMSTRDGMTGVYNRrhweTLLRNEFDN 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434244458 158 LVQAARggspagEAAVVLLDIDGFKQINDTYGHIAGDDALQYFASKMRSFSRSFDgWVGRFGGDEF--VLCAPKGLSedd 235
Cdd:PRK10245 230 CRRHHR------DATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSD-VIGRFGGDEFavIMSGTPAES--- 299
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434244458 236 lerlfaEIDAIER------HVFQAEAGSFSLAASCGVCFVRPD-DTVRSLLDRADVAMYRAKESGRRWVE 298
Cdd:PRK10245 300 ------AITAMSRvheglnTLRLPNAPQVTLRISVGVAPLNPQmSHYREWLKSADLALYKAKNAGRNRTE 363
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
135-295 |
9.83e-19 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 86.27 E-value: 9.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434244458 135 ELAVRDGFTKLYNKtfinNELESLVQAARGGSPAGEAAVVLLDIDGFKQINDTYGHIAGDDALQYFASKMRSFSRSfDGW 214
Cdd:PRK10060 235 ILANTDSITGLPNR----NAIQELIDHAINAADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEE-DQT 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434244458 215 VGRFGGDEFVLCAPKGlSEDDLERLFAEIDAIERHVFQaeAGSFSLAASCGVCFVR-PD--DTVRSLLDRADVAMYRAKE 291
Cdd:PRK10060 310 LARLGGDEFLVLASHT-SQAALEAMASRILTRLRLPFR--IGLIEVYTGCSIGIALaPEhgDDSESLIRSADTAMYTAKE 386
|
....
gi 1434244458 292 SGRR 295
Cdd:PRK10060 387 GGRG 390
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
126-297 |
1.91e-15 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 76.21 E-value: 1.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434244458 126 ITQMI-------TKFNELAVRDGFTKLYNKTFINNELESLVQA-ARGGSPAgeaAVVLLDIDGFKQINDTYGHIAGDDAL 197
Cdd:PRK15426 380 IRRMVsnmfvlqSSLQWQAWHDPLTRLYNRGALFEKARALAKRcQRDQQPF---SVIQLDLDHFKSINDRFGHQAGDRVL 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434244458 198 QYFASKMRSFSRSFDgWVGRFGGDEFVLCAPKGLSEDDL---ERLFAEIDaiERHVFQAEAGSFSLAASCGVCFVRPDD- 273
Cdd:PRK15426 457 SHAAGLISSSLRAQD-VAGRVGGEEFCVVLPGASLAEAAqvaERIRLRIN--EKEILVAKSTTIRISASLGVSSAEEDGd 533
|
170 180
....*....|....*....|....*
gi 1434244458 274 -TVRSLLDRADVAMYRAKESGRRWV 297
Cdd:PRK15426 534 yDFEQLQSLADRRLYLAKQAGRNRV 558
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
96-296 |
5.73e-15 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 75.19 E-value: 5.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434244458 96 IEGAE--LVLELIKDVTDSLLVADIEVRDNieiTQMItkfNELAVRDGFTKLYNKTFINNELESLVQaarggsPAGEAAV 173
Cdd:PRK11359 339 SSGAEtsAFIERVADISQHLAALALEQEKS---RQHI---EQLIQFDPLTGLPNRNNLHNYLDDLVD------KAVSPVV 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434244458 174 VLLDIDGFKQINDTYGHIAGDDALQYFASKMRSFSRSfDGWVGRFGGDEFVLCAPKGlSEDDLERLFAEIDAIERHVFQA 253
Cdd:PRK11359 407 YLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKP-DQYLCRIEGTQFVLVSLEN-DVSNITQIADELRNVVSKPIMI 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1434244458 254 EAGSFSLAASCGVCFVRPDDTvRSLLDRADVAM-YRAKESGRRW 296
Cdd:PRK11359 485 DDKPFPLTLSIGISYDVGKNR-DYLLSTAHNAMdYIRKNGGNGW 527
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
170-290 |
8.74e-13 |
|
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse group of nucleotidyl cyclases (NC's) containing prokaryotic and eukaryotic proteins. They can be divided into two major groups; the mononucleotidyl cyclases (MNC's) and the diguanylate cyclases (DGC's). The MNC's, which include the adenylate cyclases (AC's) and the guanylate cyclases (GC's), have a conserved cyclase homology domain (CHD), while the DGC's have a conserved GGDEF domain, named after a conserved motif within this subgroup. Their products, cyclic guanylyl and adenylyl nucleotides, are second messengers that play important roles in eukaryotic signal transduction and prokaryotic sensory pathways.
Pssm-ID: 143637 [Multi-domain] Cd Length: 133 Bit Score: 64.30 E-value: 8.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434244458 170 EAAVVLLDIDGFKQINDTYGHIAGDDALQYFASKMRSFSRSFDGWVGRFGGDEFV----LCAPKGLSE--DDLERLFAEI 243
Cdd:cd07556 1 PVTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSGDLKIKTIGDEFMvvsgLDHPAAAVAfaEDMREAVSAL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1434244458 244 DAIERHVFQAEAGSFSLAASCGVCFVRPD-DTVRSLLDRADVAMYRAK 290
Cdd:cd07556 81 NQSEGNPVRVRIGIHTGPVVVGVIGSRPQyDVWGALVNLASRMESQAK 128
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
137-290 |
5.76e-12 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 65.41 E-value: 5.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434244458 137 AVRDGFTKLYNKTFINNELESLVQ--AARGGSpageaAVVLLDIDGFKQINDTYGHIAGDDALQYFASKMRSFSRSFDGw 214
Cdd:PRK09966 248 ALHDPLTGLANRAAFRSGINTLMNnsDARKTS-----ALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHK- 321
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1434244458 215 VGRFGGDEFVLCAPKGLSEDDLERLFAEIDAIERHVFQAEAGSF-SLAASCGVCFVRPDDTVRSLLDRADVAMYRAK 290
Cdd:PRK09966 322 AYRLGGDEFAMVLYDVQSESEVQQICSALTQIFNLPFDLHNGHQtTMTLSIGYAMTIEHASAEKLQELADHNMYQAK 398
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
215-290 |
8.45e-05 |
|
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: 42.59 E-value: 8.45e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1434244458 215 VGRFGGDEFVLCAPkglsEDDLERLFAEIDAIERHVfqAEAGSFSLAASCGVCFVrpddtvrSLLDRADvAMYRAK 290
Cdd:COG3706 118 VARYGGEEFAILLP----GTDLEGALAVAERIREAV--AELPSLRVTVSIGVAGD-------SLLKRAD-ALYQAR 179
|
|
| HUL4 |
COG5021 |
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones]; |
83-209 |
8.85e-03 |
|
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227354 [Multi-domain] Cd Length: 872 Bit Score: 37.82 E-value: 8.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434244458 83 DGRVLHVTSvpmdiegaELVLELIKDVTDSLLVADIEvrdnieitqmiTKFNelAVRDGFTKLYNKTFIN----NELESL 158
Cdd:COG5021 690 NGRNISVTN--------ENKKEYVKKVVDYKLNKRVE-----------KQFS--AFKSGFSEIIPPDLLQifdeSELELL 748
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1434244458 159 VqaarGGSPageaavVLLDIDGFKQINDTYGHIAGDDALQYFASKMRSFSR 209
Cdd:COG5021 749 I----GGIP------EDIDIDDWKSNTAYHGYTEDSPIIVWFWEIISEFDF 789
|
|
| |
