|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
1-296 |
1.10e-174 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 484.19 E-value: 1.10e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515511 1 MIKKTTEIDAILLNLNKAIDAHYQWLVSMFRSVVARDASKPEITDNHSYGLCQFGRWIDHLGPLDNDELPYVRLMDSAHQ 80
Cdd:PRK09894 1 MIKKTTEIDAILLNLNKAIDAHYQWLVSMFRSVVARDASKPEITDNHSHGLCQFGRWIDHLGPLDNDELPYVRLLDSAHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515511 81 HMHNCGRELMLAIVENHWQDAHFDAFQEGLLSFTAALTDYKIYLLTIRSNMDVLTGLPGRRVLDESFDHQLRNAEPLNLY 160
Cdd:PRK09894 81 HMHNCARELLLAIVEGHWQDAHFDAFQEGLLSFTAALTDYKIYLLTIRSNMDVLTGLPGRRVLDESFDHQLRNREPQNLY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515511 161 LMLLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGGEEFIIIVKAANDEEACRAGVRICQLVDNHAITH 240
Cdd:PRK09894 161 LALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGGEEFIICLKAATDEEACRAGERIRQLIANHAITH 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 446515511 241 SEGHINITVTAGVSRAFPEEPLDVVIGRADRAMYEGKQTGRNRCMFIDEQNVINRV 296
Cdd:PRK09894 241 SDGRINITATFGVSRAFPEETLDVVIGRADRAMYEGKQTGRNRVMFIDEQNVINRV 296
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
129-283 |
6.61e-59 |
|
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: 185.53 E-value: 6.61e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515511 129 SNMDVLTGLPGRRVLDESFDHQLRNA--EPLNLYLMLLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYG 206
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRAlrEGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515511 207 GEEFIIIVKAANDEEACRAGVRICQLVDNHAITHSEGHINITVTA--GVSRAFPE-EPLDVVIGRADRAMYEGKQTGRNR 283
Cdd:pfam00990 81 GDEFAILLPETSLEGAQELAERIRRLLAKLKIPHTVSGLPLYVTIsiGIAAYPNDgEDPEDLLKRADTALYQAKQAGRNR 160
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
128-286 |
8.54e-52 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 167.42 E-value: 8.54e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515511 128 RSNMDVLTGLPGRRVLDESFDHQLRNAEPLN--LYLMLLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRY 205
Cdd:smart00267 2 LAFRDPLTGLPNRRYFEEELEQELQRAQRQGspFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515511 206 GGEEFIIIVKAANDEEACRAGVRICQLVDNHAITHsEGHINITVTAGVSRA-FPEEPLDVVIGRADRAMYEGKQTGRNRC 284
Cdd:smart00267 82 GGDEFALLLPETSLEEAIALAERILQQLREPIIIH-GIPLYLTISIGVAAYpNPGEDAEDLLKRADTALYQAKKAGRNQV 160
|
..
gi 446515511 285 MF 286
Cdd:smart00267 161 AV 162
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
130-284 |
8.40e-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: 161.96 E-value: 8.40e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515511 130 NMDVLTGLPGRRVLDESFDHQLRNAEPLN--LYLMLLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGG 207
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLARARRSGrpLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446515511 208 EEFIIIVKAANDEEACRAGVRICQLVDNHAITHsEGHINITVTAGVSrAFPEEPLDV--VIGRADRAMYEGKQTGRNRC 284
Cdd:cd01949 81 DEFAILLPGTDLEEAEALAERLREAIEEPFFID-GQEIRVTASIGIA-TYPEDGEDAeeLLRRADEALYRAKRSGRNRV 157
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
86-286 |
1.94e-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: 162.46 E-value: 1.94e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515511 86 GRELMLAIVENHWQDAHFDAFQEGLLSFTAALTDYKIYLLTIR--SNMDVLTGLPGRRVLDESFDHQLRNA--EPLNLYL 161
Cdd:COG2199 69 LLLLALLLLSLVLELLLLLLALLLLLLALEDITELRRLEERLRrlATHDPLTGLPNRRAFEERLERELARArrEGRPLAL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515511 162 MLLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGGEEFIIIVKAANDEEACRAGVRICQLVDNHAITHS 241
Cdd:COG2199 149 LLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELE 228
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446515511 242 EGHINITVTAGVSRaFPE--EPLDVVIGRADRAMYEGKQTGRNRCMF 286
Cdd:COG2199 229 GKELRVTVSIGVAL-YPEdgDSAEELLRRADLALYRAKRAGRNRVVV 274
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
132-283 |
4.94e-40 |
|
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: 137.08 E-value: 4.94e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515511 132 DVLTGLPGRRVLDESFDHQLRNAEP--LNLYLMLLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGGEE 209
Cdd:TIGR00254 5 DPLTGLYNRRYLEEMLDSELKRARRfqRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYGGEE 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446515511 210 FIIIVKAANDEEACRAGVRICQLVDNHAITHSEGH-INITVTAGVSrAFPEEPLDVV--IGRADRAMYEGKQTGRNR 283
Cdd:TIGR00254 85 FVVILPGTPLEDALSKAERLRDAINSKPIEVAGSEtLTVTVSIGVA-CYPGHGLTLEelLKRADEALYQAKKAGRNR 160
|
|
| diguan_SiaD |
NF038266 |
biofilm regulation diguanylate cyclase SiaD; |
104-284 |
1.27e-34 |
|
biofilm regulation diguanylate cyclase SiaD;
Pssm-ID: 468439 [Multi-domain] Cd Length: 252 Bit Score: 125.86 E-value: 1.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515511 104 DAFQEGLLSFTAALTDYkiylltirSNMDVLTGLPGRRVLDESFDHQLRNAEPLN--LYLMLLDIDRFKLVNDTYGHLIG 181
Cdd:NF038266 77 DRYQRMMRDLNEALREA--------STRDPLTGLPNRRLLMERLREEVERARRSGrpFTLAMLDVDHFKRINDRYGHEVG 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515511 182 DVVLRTLATYLASWTRDYETVYRYGGEEFIIIVKAANDEEACRAGVRICQLVDNHAITHSEGHINITVTAGVSR-AFPEE 260
Cdd:NF038266 149 DRVLVEIARTLRAELREYDLCGRWGGEEFLLLLPETGLEEAQVVLERLREAVRALAVRVGDDVLSVTASAGLAEhRPPEE 228
|
170 180
....*....|....*....|....
gi 446515511 261 PLDVVIGRADRAMYEGKQTGRNRC 284
Cdd:NF038266 229 GLSATLSRADQALYQAKRAGRDRV 252
|
|
| dguan_cyc_DgcA |
NF041606 |
diguanylate cyclase DgcA; |
124-283 |
4.52e-33 |
|
diguanylate cyclase DgcA;
Pssm-ID: 469490 [Multi-domain] Cd Length: 340 Bit Score: 124.09 E-value: 4.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515511 124 LLTIRSNMDVLTGLPGRR----VLDESFDHQLRNAEPLNLylMLLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDY 199
Cdd:NF041606 173 LLLEMTTTDMMTHLKLKHyfytVLMEKLDTINSQGEPLSI--LMLDIDFFKQINDTYGHACGDLVLQMVASIIQSCTRTQ 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515511 200 ETVYRYGGEEFIIIVKAANDEEACRAGVRICQLVDNHAITHSEGHINITVTAGVSRAFPE-EPLDVVIGRADRAMYEGKQ 278
Cdd:NF041606 251 DMAARYGGEEFVVMLSNTSSKTAKKIAERIRKSIENLSILYDEQHIRVTISIGVAEYNFDvESAKSLVERADKALYESKQ 330
|
....*
gi 446515511 279 TGRNR 283
Cdd:NF041606 331 NGRNR 335
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
1-296 |
1.10e-174 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 484.19 E-value: 1.10e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515511 1 MIKKTTEIDAILLNLNKAIDAHYQWLVSMFRSVVARDASKPEITDNHSYGLCQFGRWIDHLGPLDNDELPYVRLMDSAHQ 80
Cdd:PRK09894 1 MIKKTTEIDAILLNLNKAIDAHYQWLVSMFRSVVARDASKPEITDNHSHGLCQFGRWIDHLGPLDNDELPYVRLLDSAHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515511 81 HMHNCGRELMLAIVENHWQDAHFDAFQEGLLSFTAALTDYKIYLLTIRSNMDVLTGLPGRRVLDESFDHQLRNAEPLNLY 160
Cdd:PRK09894 81 HMHNCARELLLAIVEGHWQDAHFDAFQEGLLSFTAALTDYKIYLLTIRSNMDVLTGLPGRRVLDESFDHQLRNREPQNLY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515511 161 LMLLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGGEEFIIIVKAANDEEACRAGVRICQLVDNHAITH 240
Cdd:PRK09894 161 LALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGGEEFIICLKAATDEEACRAGERIRQLIANHAITH 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 446515511 241 SEGHINITVTAGVSRAFPEEPLDVVIGRADRAMYEGKQTGRNRCMFIDEQNVINRV 296
Cdd:PRK09894 241 SDGRINITATFGVSRAFPEETLDVVIGRADRAMYEGKQTGRNRVMFIDEQNVINRV 296
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
129-283 |
6.61e-59 |
|
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: 185.53 E-value: 6.61e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515511 129 SNMDVLTGLPGRRVLDESFDHQLRNA--EPLNLYLMLLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYG 206
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRAlrEGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515511 207 GEEFIIIVKAANDEEACRAGVRICQLVDNHAITHSEGHINITVTA--GVSRAFPE-EPLDVVIGRADRAMYEGKQTGRNR 283
Cdd:pfam00990 81 GDEFAILLPETSLEGAQELAERIRRLLAKLKIPHTVSGLPLYVTIsiGIAAYPNDgEDPEDLLKRADTALYQAKQAGRNR 160
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
128-286 |
8.54e-52 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 167.42 E-value: 8.54e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515511 128 RSNMDVLTGLPGRRVLDESFDHQLRNAEPLN--LYLMLLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRY 205
Cdd:smart00267 2 LAFRDPLTGLPNRRYFEEELEQELQRAQRQGspFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515511 206 GGEEFIIIVKAANDEEACRAGVRICQLVDNHAITHsEGHINITVTAGVSRA-FPEEPLDVVIGRADRAMYEGKQTGRNRC 284
Cdd:smart00267 82 GGDEFALLLPETSLEEAIALAERILQQLREPIIIH-GIPLYLTISIGVAAYpNPGEDAEDLLKRADTALYQAKKAGRNQV 160
|
..
gi 446515511 285 MF 286
Cdd:smart00267 161 AV 162
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
130-284 |
8.40e-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: 161.96 E-value: 8.40e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515511 130 NMDVLTGLPGRRVLDESFDHQLRNAEPLN--LYLMLLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGG 207
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLARARRSGrpLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446515511 208 EEFIIIVKAANDEEACRAGVRICQLVDNHAITHsEGHINITVTAGVSrAFPEEPLDV--VIGRADRAMYEGKQTGRNRC 284
Cdd:cd01949 81 DEFAILLPGTDLEEAEALAERLREAIEEPFFID-GQEIRVTASIGIA-TYPEDGEDAeeLLRRADEALYRAKRSGRNRV 157
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
86-286 |
1.94e-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: 162.46 E-value: 1.94e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515511 86 GRELMLAIVENHWQDAHFDAFQEGLLSFTAALTDYKIYLLTIR--SNMDVLTGLPGRRVLDESFDHQLRNA--EPLNLYL 161
Cdd:COG2199 69 LLLLALLLLSLVLELLLLLLALLLLLLALEDITELRRLEERLRrlATHDPLTGLPNRRAFEERLERELARArrEGRPLAL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515511 162 MLLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGGEEFIIIVKAANDEEACRAGVRICQLVDNHAITHS 241
Cdd:COG2199 149 LLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELE 228
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446515511 242 EGHINITVTAGVSRaFPE--EPLDVVIGRADRAMYEGKQTGRNRCMF 286
Cdd:COG2199 229 GKELRVTVSIGVAL-YPEdgDSAEELLRRADLALYRAKRAGRNRVVV 274
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
132-283 |
4.94e-40 |
|
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: 137.08 E-value: 4.94e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515511 132 DVLTGLPGRRVLDESFDHQLRNAEP--LNLYLMLLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGGEE 209
Cdd:TIGR00254 5 DPLTGLYNRRYLEEMLDSELKRARRfqRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYGGEE 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446515511 210 FIIIVKAANDEEACRAGVRICQLVDNHAITHSEGH-INITVTAGVSrAFPEEPLDVV--IGRADRAMYEGKQTGRNR 283
Cdd:TIGR00254 85 FVVILPGTPLEDALSKAERLRDAINSKPIEVAGSEtLTVTVSIGVA-CYPGHGLTLEelLKRADEALYQAKKAGRNR 160
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
18-290 |
2.02e-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: 134.90 E-value: 2.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515511 18 AIDAHYQWLVSMFRSVVARDASKPEITDNHSYGLCQFGRWIDHLGPLDNDELPYVRLMDSAHQHMHNCGRELMLAIVENH 97
Cdd:COG5001 130 AAASAALLAAALGAALLAALALALLLALARALLALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLA 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515511 98 WQDAHFDAFQEGLLSFTAALTDYKIYLLTIR----------SNMDVLTGLPGRRVLDESFDHQLRNA--EPLNLYLMLLD 165
Cdd:COG5001 210 LRLLLGLLLLGLLLLLLLVAVLAIARLITERkraeerlrhlAYHDPLTGLPNRRLFLDRLEQALARArrSGRRLALLFID 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515511 166 IDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGGEEFIIIVKAANDEEACRA-GVRICQLVdNHAITHSEGH 244
Cdd:COG5001 290 LDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVLLPDLDDPEDAEAvAERILAAL-AEPFELDGHE 368
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 446515511 245 INITVTAGVSRaFPEEPLDV--VIGRADRAMYEGKQTGRNRCMFIDEQ 290
Cdd:COG5001 369 LYVSASIGIAL-YPDDGADAeeLLRNADLAMYRAKAAGRNRYRFFDPE 415
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
132-283 |
7.82e-35 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 130.79 E-value: 7.82e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515511 132 DVLTGLPGRRVLDESFDHQLR--NAEPLNLYLMLLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGGEE 209
Cdd:PRK09581 295 DGLTGLHNRRYFDMHLKNLIEraNERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARYGGEE 374
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446515511 210 FIIIVKAANDEEACRAGVRICQLVDNH--AITHSEGHINITVTAGVS-RAFPEEPLDVVIGRADRAMYEGKQTGRNR 283
Cdd:PRK09581 375 FVVVMPDTDIEDAIAVAERIRRKIAEEpfIISDGKERLNVTVSIGVAeLRPSGDTIEALIKRADKALYEAKNTGRNR 451
|
|
| diguan_SiaD |
NF038266 |
biofilm regulation diguanylate cyclase SiaD; |
104-284 |
1.27e-34 |
|
biofilm regulation diguanylate cyclase SiaD;
Pssm-ID: 468439 [Multi-domain] Cd Length: 252 Bit Score: 125.86 E-value: 1.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515511 104 DAFQEGLLSFTAALTDYkiylltirSNMDVLTGLPGRRVLDESFDHQLRNAEPLN--LYLMLLDIDRFKLVNDTYGHLIG 181
Cdd:NF038266 77 DRYQRMMRDLNEALREA--------STRDPLTGLPNRRLLMERLREEVERARRSGrpFTLAMLDVDHFKRINDRYGHEVG 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515511 182 DVVLRTLATYLASWTRDYETVYRYGGEEFIIIVKAANDEEACRAGVRICQLVDNHAITHSEGHINITVTAGVSR-AFPEE 260
Cdd:NF038266 149 DRVLVEIARTLRAELREYDLCGRWGGEEFLLLLPETGLEEAQVVLERLREAVRALAVRVGDDVLSVTASAGLAEhRPPEE 228
|
170 180
....*....|....*....|....
gi 446515511 261 PLDVVIGRADRAMYEGKQTGRNRC 284
Cdd:NF038266 229 GLSATLSRADQALYQAKRAGRDRV 252
|
|
| dguan_cyc_DgcA |
NF041606 |
diguanylate cyclase DgcA; |
124-283 |
4.52e-33 |
|
diguanylate cyclase DgcA;
Pssm-ID: 469490 [Multi-domain] Cd Length: 340 Bit Score: 124.09 E-value: 4.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515511 124 LLTIRSNMDVLTGLPGRR----VLDESFDHQLRNAEPLNLylMLLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDY 199
Cdd:NF041606 173 LLLEMTTTDMMTHLKLKHyfytVLMEKLDTINSQGEPLSI--LMLDIDFFKQINDTYGHACGDLVLQMVASIIQSCTRTQ 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515511 200 ETVYRYGGEEFIIIVKAANDEEACRAGVRICQLVDNHAITHSEGHINITVTAGVSRAFPE-EPLDVVIGRADRAMYEGKQ 278
Cdd:NF041606 251 DMAARYGGEEFVVMLSNTSSKTAKKIAERIRKSIENLSILYDEQHIRVTISIGVAEYNFDvESAKSLVERADKALYESKQ 330
|
....*
gi 446515511 279 TGRNR 283
Cdd:NF041606 331 NGRNR 335
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
132-283 |
1.21e-24 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 103.17 E-value: 1.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515511 132 DVLTGLPGRRVLDESFDH----QLRNAEPLNLylMLLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGG 207
Cdd:PRK15426 401 DPLTRLYNRGALFEKARAlakrCQRDQQPFSV--IQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRVGG 478
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446515511 208 EEFIIIVKAANDEEACRAGVRICQLVDNHAI-THSEGHINITVTAGVSRAFPEEP--LDVVIGRADRAMYEGKQTGRNR 283
Cdd:PRK15426 479 EEFCVVLPGASLAEAAQVAERIRLRINEKEIlVAKSTTIRISASLGVSSAEEDGDydFEQLQSLADRRLYLAKQAGRNR 557
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
125-291 |
1.91e-19 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 88.20 E-value: 1.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515511 125 LTIRSNMDVLTGLPGRRVLDESFDHQLRNAEPLNLYLMLLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYR 204
Cdd:PRK10060 233 LRILANTDSITGLPNRNAIQELIDHAINAADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQTLAR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515511 205 YGGEEFIIIVKAANDEEACRAGVRIC-QLVDNHAITHSEGHINITVtaGVSRAfPE--EPLDVVIGRADRAMYEGKQTGR 281
Cdd:PRK10060 313 LGGDEFLVLASHTSQAALEAMASRILtRLRLPFRIGLIEVYTGCSI--GIALA-PEhgDDSESLIRSADTAMYTAKEGGR 389
|
170
....*....|.
gi 446515511 282 NR-CMFIDEQN 291
Cdd:PRK10060 390 GQfCVFSPEMN 400
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
132-283 |
1.14e-16 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 80.10 E-value: 1.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515511 132 DVLTGLPGR--------RVLDESFDHQLRNAeplnlyLMLLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVY 203
Cdd:PRK09776 668 DALTHLANRasfekqlrRLLQTVNSTHQRHA------LVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSDVLA 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515511 204 RYGGEEFIIIVKAANDEEACRAGVRICQLVDN---------HAITHSEGhinITVTAGVSRAFPEepldvVIGRADRAMY 274
Cdd:PRK09776 742 RLGGDEFGLLLPDCNVESARFIATRIISAINDyhfpwegrvYRVGASAG---ITLIDANNHQASE-----VMSQADIACY 813
|
....*....
gi 446515511 275 EGKQTGRNR 283
Cdd:PRK09776 814 AAKNAGRGR 822
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
125-283 |
8.34e-14 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 71.01 E-value: 8.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515511 125 LTIRSNMDVLTGLPGRR----VLDESFDHQLRNAEplNLYLMLLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYE 200
Cdd:PRK10245 201 LQVMSTRDGMTGVYNRRhwetLLRNEFDNCRRHHR--DATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSD 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515511 201 TVYRYGGEEFIIIVKAANDEEACRAGVRICQLVdNHAITHSEGHINITVTAGVSrafpeePLDVVIGR-------ADRAM 273
Cdd:PRK10245 279 VIGRFGGDEFAVIMSGTPAESAITAMSRVHEGL-NTLRLPNAPQVTLRISVGVA------PLNPQMSHyrewlksADLAL 351
|
170
....*....|
gi 446515511 274 YEGKQTGRNR 283
Cdd:PRK10245 352 YKAKNAGRNR 361
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
132-278 |
1.33e-12 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 67.34 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515511 132 DVLTGLPGRRVLDESFDHQLRNAEPLNLY-LMLLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGGEEF 210
Cdd:PRK09966 251 DPLTGLANRAAFRSGINTLMNNSDARKTSaLLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHKAYRLGGDEF 330
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446515511 211 IIIVKAANDEEACRagvRIC----QLVDNHAITHSEGHINITVTAGVSRAFPEEPLDVVIGRADRAMYEGKQ 278
Cdd:PRK09966 331 AMVLYDVQSESEVQ---QICsaltQIFNLPFDLHNGHQTTMTLSIGYAMTIEHASAEKLQELADHNMYQAKH 399
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
132-283 |
1.16e-10 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 62.09 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515511 132 DVLTGLPGRRVLDESFDHQLRNAEPLNLYLmlLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGGEEFI 211
Cdd:PRK11359 379 DPLTGLPNRNNLHNYLDDLVDKAVSPVVYL--IGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGTQFV 456
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446515511 212 IIVkaandeEACRAgvricqlvdnHAITHSEGHINITVTAGVSRAFPEEPLDVVIGRAdramYEGkqtGRNR 283
Cdd:PRK11359 457 LVS------LENDV----------SNITQIADELRNVVSKPIMIDDKPFPLTLSIGIS----YDV---GKNR 505
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
200-275 |
8.03e-08 |
|
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: 51.06 E-value: 8.03e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446515511 200 ETVYRYGGEEFIIIVKAANDEEACRAGVRICQLVDNHAithsegHINITVTAGVSRafpeeplDVVIGRADrAMYE 275
Cdd:COG3706 116 DLVARYGGEEFAILLPGTDLEGALAVAERIREAVAELP------SLRVTVSIGVAG-------DSLLKRAD-ALYQ 177
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
161-277 |
1.47e-06 |
|
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: 46.58 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515511 161 LMLLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYE-TVYRYGGEEFIIIVKAANDEEACRAGVRI---CQLVDNH 236
Cdd:cd07556 4 ILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSGdLKIKTIGDEFMVVSGLDHPAAAVAFAEDMreaVSALNQS 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 446515511 237 AITHSEGHINITVTAGVSRAFPEEPLDVVIGR----ADRAMYEGK 277
Cdd:cd07556 84 EGNPVRVRIGIHTGPVVVGVIGSRPQYDVWGAlvnlASRMESQAK 128
|
|
| CZB |
pfam13682 |
Chemoreceptor zinc-binding domain; The chemoreceptor zinc-binding domain (CZB) is found in ... |
22-90 |
1.55e-06 |
|
Chemoreceptor zinc-binding domain; The chemoreceptor zinc-binding domain (CZB) is found in bacterial signal transduction proteins - most frequently receptors involved in chemotaxis and motility, but also in c-di-GMP signalling and nitrate/nitrite-sensing. Originally discovered in the cytoplasmic chemoreceptor TlpD from Helicobacter pylori, it is often found C-terminal to the MCPsignal domain in cytoplasmic chemoreceptor proteins. The CZB domain contains a core sequence motif, Hxx[WFYL]x21-28Cx[LFMVI]Gx[WFLVI]x18-27HxxxH. The highly-conserved H-C-H-H residues of this motif are believed to coordinate zinc; mutating the latter two histidines of the motif to alanines abolishes Zn binding. This domain binds zinc with high affinity, with a Kd in the femtomolar range. This domain has been shown in E. coli to be a zinc sensor that regulates the catalytic activity of pfam00990. This domain also binds the chemoattractant HOCl at a site very close to that of zinc. It has been shown that zinc participates in HOCl sensing by forming a redox 'Cys-Zn switch' that reacts towards HOCl (Matilla et. al.,FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 433401 Cd Length: 64 Bit Score: 44.81 E-value: 1.55e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446515511 22 HYQWLVSMFRSVVARDASKPEITDNHSyglCQFGRWIDHLGPLDNDELpyVRLMDSAHQHMHNCGRELM 90
Cdd:pfam13682 1 HLLWKNRLYKAIEGGEVDPEDLTDHHQ---CRLGKWYYGEGGERFGGA--FKELEEPHKELHESAAEII 64
|
|
| |
