|
Name |
Accession |
Description |
Interval |
E-value |
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
145-407 |
5.65e-67 |
|
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: 214.07 E-value: 5.65e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 145 IDPARDGQIVDANLAALNFYGYSHDDMCSKHTWEINTLGRDVMPIMTAIAALPGGHKPLNFVHRLADGSTRHVQTYAGPI 224
Cdd:COG2199 1 VLLLLLLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 225 -----EIYGDKLMLCIIHDITEQKRLEQELEHAALRDSMTGLLNRRQFYAITDQSNLNTLPAQQQFSLLLVDTDHFKNIN 299
Cdd:COG2199 81 lelllLLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 300 DLFGHLKGDEVLIALSRTLEACSREGDMVFRWGGEEFVILLPRTSLDTAMQIAESVRAAVAR--ITIPGLP-RFTVSIGV 376
Cdd:COG2199 161 DTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQlpFELEGKElRVTVSIGV 240
|
250 260 270
....*....|....*....|....*....|..
gi 1017925074 377 AR-HNQGESIDELFKRVDDALYRAKNDGRNKV 407
Cdd:COG2199 241 ALyPEDGDSAEELLRRADLALYRAKRAGRNRV 272
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
254-407 |
9.36e-60 |
|
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: 191.23 E-value: 9.36e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 254 LRDSMTGLLNRRQFYAITDQSNLNTLPAQQQFSLLLVDTDHFKNINDLFGHLKGDEVLIALSRTLEACSREGDMVFRWGG 333
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1017925074 334 EEFVILLPRTSLDTAMQIAESVRAAVARITIPGLPRF--TVSIGVAR-HNQGESIDELFKRVDDALYRAKNDGRNKV 407
Cdd:cd01949 81 DEFAILLPGTDLEEAEALAERLREAIEEPFFIDGQEIrvTASIGIATyPEDGEDAEELLRRADEALYRAKRSGRNRV 157
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
253-406 |
2.61e-58 |
|
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: 187.46 E-value: 2.61e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 253 ALRDSMTGLLNRRQFYAITDQSNLNTLPAQQQFSLLLVDTDHFKNINDLFGHLKGDEVLIALSRTLEACSREGDMVFRWG 332
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 333 GEEFVILLPRTSLDTAMQIAESVRAAVARITIP----GLPRF-TVSIGVAR-HNQGESIDELFKRVDDALYRAKNDGRNK 406
Cdd:pfam00990 81 GDEFAILLPETSLEGAQELAERIRRLLAKLKIPhtvsGLPLYvTISIGIAAyPNDGEDPEDLLKRADTALYQAKQAGRNR 160
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
251-407 |
5.48e-53 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 173.97 E-value: 5.48e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 251 HAALRDSMTGLLNRRQFYAITDQSNLNTLPAQQQFSLLLVDTDHFKNINDLFGHLKGDEVLIALSRTLEACSREGDMVFR 330
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 331 WGGEEFVILLPRTSLDTAMQIAESVRAAVARITIPGLPRF--TVSIGVAR-HNQGESIDELFKRVDDALYRAKNDGRNKV 407
Cdd:smart00267 81 LGGDEFALLLPETSLEEAIALAERILQQLREPIIIHGIPLylTISIGVAAyPNPGEDAEDLLKRADTALYQAKKAGRNQV 160
|
|
| diguan_SiaD |
NF038266 |
biofilm regulation diguanylate cyclase SiaD; |
245-407 |
1.29e-49 |
|
biofilm regulation diguanylate cyclase SiaD;
Pssm-ID: 468439 [Multi-domain] Cd Length: 252 Bit Score: 168.24 E-value: 1.29e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 245 LEQELEHAALRDSMTGLLNRRQFYAITDQSNLNTLPAQQQFSLLLVDTDHFKNINDLFGHLKGDEVLIALSRTLEACSRE 324
Cdd:NF038266 86 LNEALREASTRDPLTGLPNRRLLMERLREEVERARRSGRPFTLAMLDVDHFKRINDRYGHEVGDRVLVEIARTLRAELRE 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 325 GDMVFRWGGEEFVILLPRTSLDTAMQIAESVRAAVARITIP---GLPRFTVSIGVARHNQGES-IDELFKRVDDALYRAK 400
Cdd:NF038266 166 YDLCGRWGGEEFLLLLPETGLEEAQVVLERLREAVRALAVRvgdDVLSVTASAGLAEHRPPEEgLSATLSRADQALYQAK 245
|
....*..
gi 1017925074 401 NDGRNKV 407
Cdd:NF038266 246 RAGRDRV 252
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
253-410 |
4.30e-46 |
|
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: 156.34 E-value: 4.30e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 253 ALRDSMTGLLNRRQFYAITDQSNLNTLPAQQQFSLLLVDTDHFKNINDLFGHLKGDEVLIALSRTLEACSREGDMVFRWG 332
Cdd:TIGR00254 2 AVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 333 GEEFVILLPRTSLDTAMQIAESVRAAVA--RITIPGLP--RFTVSIGVARH-NQGESIDELFKRVDDALYRAKNDGRNKV 407
Cdd:TIGR00254 82 GEEFVVILPGTPLEDALSKAERLRDAINskPIEVAGSEtlTVTVSIGVACYpGHGLTLEELLKRADEALYQAKKAGRNRV 161
|
...
gi 1017925074 408 LAA 410
Cdd:TIGR00254 162 VVA 164
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
242-410 |
5.13e-44 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 158.91 E-value: 5.13e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 242 QKRLEQELEHA---ALRDSMTGLLNRRQFyaitdQSNLNTLPAQ-----QQFSLLLVDTDHFKNINDLFGHLKGDEVLIA 313
Cdd:PRK09581 278 QDALRNNLEQSiemAVTDGLTGLHNRRYF-----DMHLKNLIERanergKPLSLMMIDIDHFKKVNDTYGHDAGDEVLRE 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 314 LSRTLEACSREGDMVFRWGGEEFVILLPRTSLDTAMQIAESVRAAVAR--ITIPGLPRF---TVSIGVA-RHNQGESIDE 387
Cdd:PRK09581 353 FAKRLRNNIRGTDLIARYGGEEFVVVMPDTDIEDAIAVAERIRRKIAEepFIISDGKERlnvTVSIGVAeLRPSGDTIEA 432
|
170 180
....*....|....*....|...
gi 1017925074 388 LFKRVDDALYRAKNDGRNKVLAA 410
Cdd:PRK09581 433 LIKRADKALYEAKNTGRNRVVAL 455
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
25-249 |
2.15e-14 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 72.75 E-value: 2.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 25 KIIFANVSATQIMG-------DKTLDDLRKGIYSASAQTVLSMYVSELKTEQeiVEIWTTSRDGQDTPLSCRLSlAHYAP 97
Cdd:COG2202 32 RILYVNPAFERLTGysaeellGKTLRDLLPPEDDDEFLELLRAALAGGGVWR--GELRNRRKDGSLFWVELSIS-PVRDE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 98 WGDVIVFEGISQQIlSGLKASRSAnyRRKKQGFYARFFLTNSAPMLLIDParDGQIVDANLAALNFYGYSHDDMCSKHTW 177
Cdd:COG2202 109 DGEITGFVGIARDI-TERKRAEEA--LRESEERLRLLVENAPDGIFVLDL--DGRILYVNPAAEELLGYSPEELLGKSLL 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1017925074 178 EINTLGRDVMPIMTAIAALPGGHKPLNFVHRLADGSTRHVQTYAGPIEIYGD---KLMLCIIHDITEQKRLEQEL 249
Cdd:COG2202 184 DLLHPEDRERLLELLRRLLEGGRESYELELRLKDGDGRWVWVEASAVPLRDGgevIGVLGIVRDITERKRAEEAL 258
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
145-407 |
5.65e-67 |
|
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: 214.07 E-value: 5.65e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 145 IDPARDGQIVDANLAALNFYGYSHDDMCSKHTWEINTLGRDVMPIMTAIAALPGGHKPLNFVHRLADGSTRHVQTYAGPI 224
Cdd:COG2199 1 VLLLLLLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 225 -----EIYGDKLMLCIIHDITEQKRLEQELEHAALRDSMTGLLNRRQFYAITDQSNLNTLPAQQQFSLLLVDTDHFKNIN 299
Cdd:COG2199 81 lelllLLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 300 DLFGHLKGDEVLIALSRTLEACSREGDMVFRWGGEEFVILLPRTSLDTAMQIAESVRAAVAR--ITIPGLP-RFTVSIGV 376
Cdd:COG2199 161 DTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQlpFELEGKElRVTVSIGV 240
|
250 260 270
....*....|....*....|....*....|..
gi 1017925074 377 AR-HNQGESIDELFKRVDDALYRAKNDGRNKV 407
Cdd:COG2199 241 ALyPEDGDSAEELLRRADLALYRAKRAGRNRV 272
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
254-407 |
9.36e-60 |
|
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: 191.23 E-value: 9.36e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 254 LRDSMTGLLNRRQFYAITDQSNLNTLPAQQQFSLLLVDTDHFKNINDLFGHLKGDEVLIALSRTLEACSREGDMVFRWGG 333
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1017925074 334 EEFVILLPRTSLDTAMQIAESVRAAVARITIPGLPRF--TVSIGVAR-HNQGESIDELFKRVDDALYRAKNDGRNKV 407
Cdd:cd01949 81 DEFAILLPGTDLEEAEALAERLREAIEEPFFIDGQEIrvTASIGIATyPEDGEDAEELLRRADEALYRAKRSGRNRV 157
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
253-406 |
2.61e-58 |
|
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: 187.46 E-value: 2.61e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 253 ALRDSMTGLLNRRQFYAITDQSNLNTLPAQQQFSLLLVDTDHFKNINDLFGHLKGDEVLIALSRTLEACSREGDMVFRWG 332
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 333 GEEFVILLPRTSLDTAMQIAESVRAAVARITIP----GLPRF-TVSIGVAR-HNQGESIDELFKRVDDALYRAKNDGRNK 406
Cdd:pfam00990 81 GDEFAILLPETSLEGAQELAERIRRLLAKLKIPhtvsGLPLYvTISIGIAAyPNDGEDPEDLLKRADTALYQAKQAGRNR 160
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
251-407 |
5.48e-53 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 173.97 E-value: 5.48e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 251 HAALRDSMTGLLNRRQFYAITDQSNLNTLPAQQQFSLLLVDTDHFKNINDLFGHLKGDEVLIALSRTLEACSREGDMVFR 330
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 331 WGGEEFVILLPRTSLDTAMQIAESVRAAVARITIPGLPRF--TVSIGVAR-HNQGESIDELFKRVDDALYRAKNDGRNKV 407
Cdd:smart00267 81 LGGDEFALLLPETSLEEAIALAERILQQLREPIIIHGIPLylTISIGVAAyPNPGEDAEDLLKRADTALYQAKKAGRNQV 160
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
132-405 |
6.39e-51 |
|
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: 181.51 E-value: 6.39e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 132 ARFFLTNSAPMLLIDPARDGQIVDANLAALNFYGYSHDDMCSKHTWEINTLGRDVMPIMTAIAALPGGHKPLNFVHRLAD 211
Cdd:COG5001 125 AALLLAAASAALLAAALGAALLAALALALLLALARALLALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGR 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 212 GSTRHVQTYAGPIEIYGDKLMLCIIHD-----ITEQKRLEQELEHAALRDSMTGLLNRRQFYAITDQSNLNTLPAQQQFS 286
Cdd:COG5001 205 LLRLALRLLLGLLLLGLLLLLLLVAVLaiarlITERKRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRLA 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 287 LLLVDTDHFKNINDLFGHLKGDEVLIALSRTLEACSREGDMVFRWGGEEFVILLPR-TSLDTAMQIAESVRAAVAR-ITI 364
Cdd:COG5001 285 LLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVLLPDlDDPEDAEAVAERILAALAEpFEL 364
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1017925074 365 PGLP-RFTVSIGVA-RHNQGESIDELFKRVDDALYRAKNDGRN 405
Cdd:COG5001 365 DGHElYVSASIGIAlYPDDGADAEELLRNADLAMYRAKAAGRN 407
|
|
| diguan_SiaD |
NF038266 |
biofilm regulation diguanylate cyclase SiaD; |
245-407 |
1.29e-49 |
|
biofilm regulation diguanylate cyclase SiaD;
Pssm-ID: 468439 [Multi-domain] Cd Length: 252 Bit Score: 168.24 E-value: 1.29e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 245 LEQELEHAALRDSMTGLLNRRQFYAITDQSNLNTLPAQQQFSLLLVDTDHFKNINDLFGHLKGDEVLIALSRTLEACSRE 324
Cdd:NF038266 86 LNEALREASTRDPLTGLPNRRLLMERLREEVERARRSGRPFTLAMLDVDHFKRINDRYGHEVGDRVLVEIARTLRAELRE 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 325 GDMVFRWGGEEFVILLPRTSLDTAMQIAESVRAAVARITIP---GLPRFTVSIGVARHNQGES-IDELFKRVDDALYRAK 400
Cdd:NF038266 166 YDLCGRWGGEEFLLLLPETGLEEAQVVLERLREAVRALAVRvgdDVLSVTASAGLAEHRPPEEgLSATLSRADQALYQAK 245
|
....*..
gi 1017925074 401 NDGRNKV 407
Cdd:NF038266 246 RAGRDRV 252
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
253-410 |
4.30e-46 |
|
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: 156.34 E-value: 4.30e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 253 ALRDSMTGLLNRRQFYAITDQSNLNTLPAQQQFSLLLVDTDHFKNINDLFGHLKGDEVLIALSRTLEACSREGDMVFRWG 332
Cdd:TIGR00254 2 AVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 333 GEEFVILLPRTSLDTAMQIAESVRAAVA--RITIPGLP--RFTVSIGVARH-NQGESIDELFKRVDDALYRAKNDGRNKV 407
Cdd:TIGR00254 82 GEEFVVILPGTPLEDALSKAERLRDAINskPIEVAGSEtlTVTVSIGVACYpGHGLTLEELLKRADEALYQAKKAGRNRV 161
|
...
gi 1017925074 408 LAA 410
Cdd:TIGR00254 162 VVA 164
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
242-410 |
5.13e-44 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 158.91 E-value: 5.13e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 242 QKRLEQELEHA---ALRDSMTGLLNRRQFyaitdQSNLNTLPAQ-----QQFSLLLVDTDHFKNINDLFGHLKGDEVLIA 313
Cdd:PRK09581 278 QDALRNNLEQSiemAVTDGLTGLHNRRYF-----DMHLKNLIERanergKPLSLMMIDIDHFKKVNDTYGHDAGDEVLRE 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 314 LSRTLEACSREGDMVFRWGGEEFVILLPRTSLDTAMQIAESVRAAVAR--ITIPGLPRF---TVSIGVA-RHNQGESIDE 387
Cdd:PRK09581 353 FAKRLRNNIRGTDLIARYGGEEFVVVMPDTDIEDAIAVAERIRRKIAEepFIISDGKERlnvTVSIGVAeLRPSGDTIEA 432
|
170 180
....*....|....*....|...
gi 1017925074 388 LFKRVDDALYRAKNDGRNKVLAA 410
Cdd:PRK09581 433 LIKRADKALYEAKNTGRNRVVAL 455
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
247-407 |
2.06e-41 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 147.91 E-value: 2.06e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 247 QELEHAAL-----RDSMTGLLNRRQFYAITDQSNLNTLPaqQQFSLLLVDTDHFKNINDLFGHLKGDEVLIALSRTLEAC 321
Cdd:PRK09894 118 TDYKIYLLtirsnMDVLTGLPGRRVLDESFDHQLRNREP--QNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASW 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 322 SREGDMVFRWGGEEFVILLPRTSLDTAMQIAESVRAAVAR--ITIP-GLPRFTVSIGVARHNQGESIDELFKRVDDALYR 398
Cdd:PRK09894 196 TRDYETVYRYGGEEFIICLKAATDEEACRAGERIRQLIANhaITHSdGRINITATFGVSRAFPEETLDVVIGRADRAMYE 275
|
....*....
gi 1017925074 399 AKNDGRNKV 407
Cdd:PRK09894 276 GKQTGRNRV 284
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
231-409 |
3.57e-34 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 133.60 E-value: 3.57e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 231 LMLCII---------HDITEQKRLEQELEHaalrDSMTGLLNRRQFYAITdQSNLNTLPAQQQ-FSLLLVDTDHFKNIND 300
Cdd:PRK15426 371 AMLLISwyvirrmvsNMFVLQSSLQWQAWH----DPLTRLYNRGALFEKA-RALAKRCQRDQQpFSVIQLDLDHFKSIND 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 301 LFGHLKGDEVLIALSRTLEACSREGDMVFRWGGEEFVILLPRTSLDTAMQIAESVRAAVARITIPGLP----RFTVSIGV 376
Cdd:PRK15426 446 RFGHQAGDRVLSHAAGLISSSLRAQDVAGRVGGEEFCVVLPGASLAEAAQVAERIRLRINEKEILVAKsttiRISASLGV 525
|
170 180 190
....*....|....*....|....*....|....*
gi 1017925074 377 --ARHNQGESIDELFKRVDDALYRAKNDGRNKVLA 409
Cdd:PRK15426 526 ssAEEDGDYDFEQLQSLADRRLYLAKQAGRNRVCA 560
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
239-410 |
7.44e-30 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 118.39 E-value: 7.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 239 ITEQKRleqELEHAALRDSMTGLLNRRQFYAITDQSNLNTLPAQQQFSLLLVDTDHFKNINDLFGHLKGDEVLIALSRTL 318
Cdd:PRK10245 194 LAEHKR---RLQVMSTRDGMTGVYNRRHWETLLRNEFDNCRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQL 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 319 EACSREGDMVFRWGGEEFVILLPRTSLDTAMQIAESVRAAVARITIPGLP--RFTVSIGVARHN-QGESIDELFKRVDDA 395
Cdd:PRK10245 271 QITLRGSDVIGRFGGDEFAVIMSGTPAESAITAMSRVHEGLNTLRLPNAPqvTLRISVGVAPLNpQMSHYREWLKSADLA 350
|
170
....*....|....*
gi 1017925074 396 LYRAKNDGRNKVLAA 410
Cdd:PRK10245 351 LYKAKNAGRNRTEVA 365
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
217-406 |
3.52e-25 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 107.85 E-value: 3.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 217 VQTYAGPIEIYgdklMLCIIHDITEQKRLEQELEHAALRDSMTGLLNRrqfYAITDQSN--LNTLPaQQQFSLLLVDTDH 294
Cdd:PRK10060 205 VHSGSGKNEIF----LICSGTDITEERRAQERLRILANTDSITGLPNR---NAIQELIDhaINAAD-NNQVGIVYLDLDN 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 295 FKNINDLFGHLKGDEVLIALSRTLEACSREGDMVFRWGGEEFVILLPRTSLD----TAMQIAESVRAAVaRItipGLPR- 369
Cdd:PRK10060 277 FKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQTLARLGGDEFLVLASHTSQAaleaMASRILTRLRLPF-RI---GLIEv 352
|
170 180 190
....*....|....*....|....*....|....*....
gi 1017925074 370 FT-VSIGVARHNQ-GESIDELFKRVDDALYRAKNDGRNK 406
Cdd:PRK10060 353 YTgCSIGIALAPEhGDDSESLIRSADTAMYTAKEGGRGQ 391
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
235-407 |
8.66e-25 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 107.07 E-value: 8.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 235 IIHDITEQKRLEQELEHAALRDSMTGLLNRRQFYAITDQSNLNTLPAQQQFSLLLVDTDHFKNINDLFGHLKGDEVLIAL 314
Cdd:PRK09776 647 VIQDVTESRKMLRQLSYSASHDALTHLANRASFEKQLRRLLQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLREL 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 315 SRTLEACSREGDMVFRWGGEEFVILLPRTSLDTAMQIAESVRAAVARITIP---GLPRFTVSIGVAR-HNQGESIDELFK 390
Cdd:PRK09776 727 ASLMLSMLRSSDVLARLGGDEFGLLLPDCNVESARFIATRIISAINDYHFPwegRVYRVGASAGITLiDANNHQASEVMS 806
|
170
....*....|....*..
gi 1017925074 391 RVDDALYRAKNDGRNKV 407
Cdd:PRK09776 807 QADIACYAAKNAGRGRV 823
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
168-403 |
1.76e-18 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 87.90 E-value: 1.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 168 HDDMCSKHTWEINTLGRDVMPIMTAIAALPGGHKPLNFVHRLADGSTrHVQTYAgpieiygdklmlciihdiTEQKRLEQ 247
Cdd:PRK11359 310 GAEYQNAQSWSATIRQRDGAPAGTLQIKTSSGAETSAFIERVADISQ-HLAALA------------------LEQEKSRQ 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 248 ELEHAALRDSMTGLLNRRQFYAITDQSnlntLPAQQQFSLLLVDTDHFKNINDLFGHLKGDEVLIALSRTLEACSREGDM 327
Cdd:PRK11359 371 HIEQLIQFDPLTGLPNRNNLHNYLDDL----VDKAVSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDQY 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1017925074 328 VFRWGGEEFVILLPRTSLDTAMQIAESVRAAV-ARITIPGLP-RFTVSIGVArHNQGESIDELFKRVDDAL-YRAKNDG 403
Cdd:PRK11359 447 LCRIEGTQFVLVSLENDVSNITQIADELRNVVsKPIMIDDKPfPLTLSIGIS-YDVGKNRDYLLSTAHNAMdYIRKNGG 524
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
124-338 |
4.54e-17 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 80.45 E-value: 4.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 124 RRKKQGFYARFFLTNSAPMLLIDParDGQIVDANLAALNFYGYSHDDMCSKHTWEINTLG-RDVMPIMTAIAALPGGHKP 202
Cdd:COG2202 6 LEESERRLRALVESSPDAIIITDL--DGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEdDDEFLELLRAALAGGGVWR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 203 LNFVHRLADGSTRHVQTYAGPI-----EIYGdklMLCIIHDITEQKRLEQELEHAALRDSMTgLLNRRQFYAITDQSNLN 277
Cdd:COG2202 84 GELRNRRKDGSLFWVELSISPVrdedgEITG---FVGIARDITERKRAEEALRESEERLRLL-VENAPDGIFVLDLDGRI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1017925074 278 TL--PAQQQFSLLLVDTDHFKNINDLFGHLKGDEVLIALSRTLEACSREGDMVFRWGGEEFVI 338
Cdd:COG2202 160 LYvnPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLEGGRESYELELRLKDGDGRW 222
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
326-400 |
1.90e-16 |
|
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: 76.87 E-value: 1.90e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1017925074 326 DMVFRWGGEEFVILLPRTSLDTAMQIAESVRAAVARitiPGLPRFTVSIGVArhnqgesIDELFKRVdDALYRAK 400
Cdd:COG3706 116 DLVARYGGEEFAILLPGTDLEGALAVAERIREAVAE---LPSLRVTVSIGVA-------GDSLLKRA-DALYQAR 179
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
284-377 |
1.17e-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: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 284 QFSLLLVDTDHFKNINDLFGHLKGDEVLIALSRTL-EACSREGDMVFRWGGEEFVILLPRTSLDTAMQIAESVRAAVARI 362
Cdd:cd07556 1 PVTILFADIVGFTSLADALGPDEGDELLNELAGRFdSLIRRSGDLKIKTIGDEFMVVSGLDHPAAAVAFAEDMREAVSAL 80
|
90
....*....|....*
gi 1017925074 363 TIPGLPRFTVSIGVA 377
Cdd:cd07556 81 NQSEGNPVRVRIGIH 95
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
130-249 |
1.98e-14 |
|
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions]
Pssm-ID: 272971 [Multi-domain] Cd Length: 124 Bit Score: 69.24 E-value: 1.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 130 FYARFFLTNSAPMLLIDpaRDGQIVDANLAALNFYGYSHDDMCSKHTWEINT-LGRDVMPIMtAIAALPGGHKPLNFVHR 208
Cdd:TIGR00229 4 RYRAIFESSPDAIIVID--LEGNILYVNPAFEEIFGYSAEELIGRNVLELIPeEDREEVRER-IERRLEGEPEPVSEERR 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1017925074 209 L--ADGSTRHVQTYAGPIEIYGDKL-MLCIIHDITEQKRLEQEL 249
Cdd:TIGR00229 81 VrrKDGSEIWVEVSVSPIRTNGGELgVVGIVRDITERKEAEEAL 124
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
25-249 |
2.15e-14 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 72.75 E-value: 2.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 25 KIIFANVSATQIMG-------DKTLDDLRKGIYSASAQTVLSMYVSELKTEQeiVEIWTTSRDGQDTPLSCRLSlAHYAP 97
Cdd:COG2202 32 RILYVNPAFERLTGysaeellGKTLRDLLPPEDDDEFLELLRAALAGGGVWR--GELRNRRKDGSLFWVELSIS-PVRDE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 98 WGDVIVFEGISQQIlSGLKASRSAnyRRKKQGFYARFFLTNSAPMLLIDParDGQIVDANLAALNFYGYSHDDMCSKHTW 177
Cdd:COG2202 109 DGEITGFVGIARDI-TERKRAEEA--LRESEERLRLLVENAPDGIFVLDL--DGRILYVNPAAEELLGYSPEELLGKSLL 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1017925074 178 EINTLGRDVMPIMTAIAALPGGHKPLNFVHRLADGSTRHVQTYAGPIEIYGD---KLMLCIIHDITEQKRLEQEL 249
Cdd:COG2202 184 DLLHPEDRERLLELLRRLLEGGRESYELELRLKDGDGRWVWVEASAVPLRDGgevIGVLGIVRDITERKRAEEAL 258
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
242-401 |
4.31e-14 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 73.50 E-value: 4.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 242 QKRLE---QELEHAALRDSMTGLLNRRQFyaitdQSNLNTL----PAQQQFSLLLVDTDHFKNINDLFGHLKGDEVLIAL 314
Cdd:PRK09966 234 QLRLQaknAQLLRTALHDPLTGLANRAAF-----RSGINTLmnnsDARKTSALLFLDGDNFKYINDTWGHATGDRVLIEI 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 315 SRTLEACSREGDMVFRWGGEEFVILLPRTSLDTAMQ-IAESVRAAVAR---ITIPGLPRFTVSIGVA---RHNQGESIDE 387
Cdd:PRK09966 309 AKRLAEFGGLRHKAYRLGGDEFAMVLYDVQSESEVQqICSALTQIFNLpfdLHNGHQTTMTLSIGYAmtiEHASAEKLQE 388
|
170
....*....|....
gi 1017925074 388 LfkrVDDALYRAKN 401
Cdd:PRK09966 389 L---ADHNMYQAKH 399
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
125-253 |
8.92e-13 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 69.10 E-value: 8.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 125 RKKQGFYARFFLTNSAPMLLIDParDGQIVDANLAALNFYGYSHDDMCSKHTWEINTLGRDVMPIMTAIAALPGGHKPLN 204
Cdd:COG3852 3 RESEELLRAILDSLPDAVIVLDA--DGRITYVNPAAERLLGLSAEELLGRPLAELFPEDSPLRELLERALAEGQPVTERE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1017925074 205 FVHRLADGSTRHVQTYAGPIEIY-GDKLMLCIIHDITEQKRLEQELEHAA 253
Cdd:COG3852 81 VTLRRKDGEERPVDVSVSPLRDAeGEGGVLLVLRDITERKRLERELRRAE 130
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
25-261 |
1.64e-11 |
|
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 444511 [Multi-domain] Cd Length: 489 Bit Score: 65.77 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 25 KIIFANVSATQIMGDkTLDDLrkgIYSASAQTVLSMYVSELK------TEQEIVEIWTTS-RDGQDTPLSCRLSL-AHYA 96
Cdd:COG5809 36 KILKVNPAAERIFGY-TEDEL---LGTNILDFLHPDDEKELReilkllKEGESRDELEFElRHKNGKRLEFSSKLsPIFD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 97 PWGDVIVFEGISQQIlSGLKasRSANYRRKKQGFYARFFltNSAPMLLIDPARDGQIVDANLAALNFYGYSHDDMCSKHt 176
Cdd:COG5809 112 QNGDIEGMLAISRDI-TERK--RMEEALRESEEKFRLIF--NHSPDGIIVTDLDGRIIYANPAACKLLGISIEELIGKS- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 177 weINTLGR--DVMPIMTAIAALPGGHKPLN--FVHRLADGSTRHVQTYAGPI--EIYGDKLMLcIIHDITEQKRLEQELE 250
Cdd:COG5809 186 --ILELIHsdDQENVAAFISQLLKDGGIAQgeVRFWTKDGRWRLLEASGAPIkkNGEVDGIVI-IFRDITERKKLEELLR 262
|
250 260
....*....|....*....|....*.
gi 1017925074 251 H----------AA-----LRDSMTGL 261
Cdd:COG5809 263 KseklsvvgelAAgiaheIRNPLTSL 288
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
150-241 |
2.04e-08 |
|
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor domain. It recognizes FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 463873 [Multi-domain] Cd Length: 93 Bit Score: 51.31 E-value: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 150 DGQIVDANLAALNFYGYSHDDMCSKHTWEINTLGRDVMPIMTAIAALPGGHkPLNFVHRLADGSTRHVQTYAGPIEIYGD 229
Cdd:pfam13426 1 DGRIIYVNDAALRLLGYTREELLGKSITDLFAEPEDSERLREALREGKAVR-EFEVVLYRKDGEPFPVLVSLAPIRDDGG 79
|
90
....*....|....
gi 1017925074 230 KLML--CIIHDITE 241
Cdd:pfam13426 80 ELVGiiAILRDITE 93
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
223-408 |
1.70e-07 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 53.18 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 223 PIEIYGDKLMLCIIHDITE-----------QKRLEQ---ELEHAALRDSMTGLLNRRQFYAITDQsnlnTLPAQQQFSLL 288
Cdd:PRK13561 187 PQELVGHQLALPRLHQDDEigmlvrsynlnQQLLQRqyeEQSRNATRFPVSDLPNKALLMALLEQ----VVARKQTTALM 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 289 LVDTDHFKNINDLFGHLKGDEVLIALSRTLEACSREGDMVFRWGGEEFVILLPRTSLD-TAMQIAESVRAAV-ARITIPG 366
Cdd:PRK13561 263 IITCETLRDTAGVLKEAQREILLLTLVEKLKSVLSPRMVLAQISGYDFAIIANGVKEPwHAITLGQQVLTIInERLPIQR 342
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1017925074 367 LP-RFTVSIGVARHNQGESIDELFKRVDDALYRAKNDGRNKVL 408
Cdd:PRK13561 343 IQlRPSCSIGIAMFYGDLTAEQLYSRAISAAFTARRKGKNQIQ 385
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
140-239 |
1.71e-07 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.
Pssm-ID: 238075 [Multi-domain] Cd Length: 103 Bit Score: 49.17 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 140 APMLLIDPARDGQIVDANLAALNFYGYSHDDMCSKHTWEInTLGRDVMPIMTAIAALPGGHKPLNFVHRL--ADGSTRHV 217
Cdd:cd00130 1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDL-IHPEDREELRERLENLLSGGEPVTLEVRLrrKDGSVIWV 79
|
90 100
....*....|....*....|....
gi 1017925074 218 QTYAGPIEIYGDK--LMLCIIHDI 239
Cdd:cd00130 80 LVSLTPIRDEGGEviGLLGVVRDI 103
|
|
| PAS_4 |
pfam08448 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
138-244 |
1.87e-07 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain is associated to signalling systems and works as a signal sensor domain. It recognizes differently substituted aromatic hydrocarbons, oxygen, different dodecanoic acids, autoinducers, 3,5-dimethyl-pyrazin-2-ol and N-alanyl-aminoacetone (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 312075 [Multi-domain] Cd Length: 110 Bit Score: 49.33 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 138 NSAPMLLIDPARDGQIVDANLAALNFYGYSHDDMCSKHTWEI--NTLGRDVMPIMTAIAAlpgGHKPLNFVH-RLADGST 214
Cdd:pfam08448 2 DSLPDALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAELlpPEDAARLERALRRALE---GEEPIDFLEeLLLNGEE 78
|
90 100 110
....*....|....*....|....*....|..
gi 1017925074 215 RHVQTYAGPI-EIYGDKL-MLCIIHDITEQKR 244
Cdd:pfam08448 79 RHYELRLTPLrDPDGEVIgVLVISRDITERRR 110
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
242-408 |
3.02e-06 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 49.56 E-value: 3.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 242 QKRLE---QELEHAALRDSMTGLLNRRQFYAITDQSNLNTlPAQQQFSLLLVDTDHFKNINDLFGHLKGDEVLIALSRTL 318
Cdd:PRK11829 218 QQLLAdayADMGRISHRFPVTELPNRSLFISLLEKEIASS-TRTDHFHLLVIGIETLQEVSGAMSEAQHQQLLLTIVQRI 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 319 EACSREGDMVFRWGGEEFVIL---LPRTSldTAMQIAESVRAAVAR-ITIPGLP-RFTVSIGVARHN-QGESIDELFKRV 392
Cdd:PRK11829 297 EQCIDDSDLLAQLSKTEFAVLargTRRSF--PAMQLARRIMSQVTQpLFFDEITlRPSASIGITRYQaQQDTAESMMRNA 374
|
170
....*....|....*.
gi 1017925074 393 DDALYRAKNDGRNKVL 408
Cdd:PRK11829 375 STAMMAAHHEGRNQIM 390
|
|
| RocR |
COG3829 |
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ... |
141-255 |
5.59e-06 |
|
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis domains [Transcription, Signal transduction mechanisms];
Pssm-ID: 443041 [Multi-domain] Cd Length: 448 Bit Score: 48.23 E-value: 5.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 141 PMLLIDpaRDGQIVDANLAALNFYGYSHDDMCSKHTWeintlgrDVMPIMTAIAALPGGHKPLNFVHRLaDGSTRHVQTY 220
Cdd:COG3829 23 GIIVVD--ADGRITYVNRAAERILGLPREEVIGKNVT-------ELIPNSPLLEVLKTGKPVTGVIQKT-GGKGKTVIVT 92
|
90 100 110
....*....|....*....|....*....|....*.
gi 1017925074 221 AGPIEIYGD-KLMLCIIHDITEQKRLEQELEHAALR 255
Cdd:COG3829 93 AIPIFEDGEvIGAVETFRDITELKRLERKLREEELE 128
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
130-179 |
3.02e-04 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.
Pssm-ID: 214512 Cd Length: 67 Bit Score: 38.92 E-value: 3.02e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1017925074 130 FYARFFLTNSAPMLLIDpaRDGQIVDANLAALNFYGYSHDDMCSKHTWEI 179
Cdd:smart00091 2 RLRAILESLPDGIFVLD--LDGRILYANPAAEELLGYSPEELIGKSLLEL 49
|
|
| KinA |
COG5805 |
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ... |
6-249 |
1.27e-03 |
|
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 444507 [Multi-domain] Cd Length: 496 Bit Score: 40.87 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 6 FDALNVIKTPVWLVSpVSEKIIFANVSATQIMGDKTLDDLRKGIYSASAQTVLSMYVSELKTEQ--EIVEIWTTSRDGQD 83
Cdd:COG5805 37 ETILENLPDAIIAVN-REGKVIYINPAMEKLLGYTSEEIIGKTIFDFLEKEYHYRVKTRIERLQkgYDVVMIEQIYCKDG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 84 TPLSCRLSLAHYAPWGDVIVFEGISQqiLSGLKASRSANYRRKKQgFYArffLTNSAPMLLIDPARDGQIVDANLAALNF 163
Cdd:COG5805 116 ELIYVEVKLFPIYNQNGQAAILALRD--ITKKKKIEEILQEQEER-LQT---LIENSPDLICVIDTDGRILFINESIERL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 164 YGYSHDDMCSKHTWEINTLgRDVMPIMTAIAALPGGHKPLNFVHRL--ADGSTRHVQTYAGP-IEIYGD-KLMLCIIHDI 239
Cdd:COG5805 190 FGAPREELIGKNLLELLHP-CDKEEFKERIESITEVWQEFIIEREIitKDGRIRYFEAVIVPlIDTDGSvKGILVILRDI 268
|
250
....*....|
gi 1017925074 240 TEQKRLEQEL 249
Cdd:COG5805 269 TEKKEAEELM 278
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
251-399 |
2.83e-03 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 39.85 E-value: 2.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 251 HAALrDSMTGLLNRRQFyaitdQSNLNTLPAQQQF-----SLLLVDTDHFKNINDLFGHLKGDEVLIALSRTLEA-CSRE 324
Cdd:PRK11059 227 NAFQ-DAKTGLGNRLFF-----DNQLATLLEDQEMvgahgVVMLIRLPDFDLLQEEWGESQVEELLFELINLLSTfVMRY 300
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1017925074 325 GDMVF-RWGGEEFVILLPRTSLDTAMQIAESVRAAVARITIPG-LPRFT-VSIGVARHNQGESIDELFKRVDDALYRA 399
Cdd:PRK11059 301 PGALLaRYSRSDFAVLLPHRSLKEADSLASQLLKAVDALPPPKmLDRDDfLHIGICAYRSGQSTEQVMEEAEMALRSA 378
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
129-239 |
7.91e-03 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain can bind gases (O2, CO and NO), FAD, 4-hydroxycinnamic acid and NAD+ (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 395786 [Multi-domain] Cd Length: 113 Bit Score: 35.86 E-value: 7.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017925074 129 GFYARFFLTNSAPMLLIDpaRDGQIVDANLAALNFYGYSHDDMCSKHT---WEINTLGRDVMPIMTAIAAlpgGHKPLNF 205
Cdd:pfam00989 1 EDLRAILESLPDGIFVVD--EDGRILYVNAAAEELLGLSREEVIGKSLldlIPEEDDAEVAELLRQALLQ---GEESRGF 75
|
90 100 110
....*....|....*....|....*....|....*...
gi 1017925074 206 VHRL--ADGSTRHVQTYAGPIEIYGDKLM--LCIIHDI 239
Cdd:pfam00989 76 EVSFrvPDGRPRHVEVRASPVRDAGGEILgfLGVLRDI 113
|
|
| |
