|
Name |
Accession |
Description |
Interval |
E-value |
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
303-461 |
8.05e-55 |
|
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: 180.14 E-value: 8.05e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446480599 303 ADFDFLTQVYSRSGLYEALK---SPSLKQTQHLTVMLLDIDYFKSINDNYGHECGDKVLSVFAQHIQKIVGDKGLVARMG 379
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEqelQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446480599 380 GEEFAVAVPSVNPVDGLLMAEKIRKGVELQPFTWQQKT--LYLTVSIGVgsgcASYRTLTDDFNKLMVEADTCLYRSKKD 457
Cdd:pfam00990 81 GDEFAILLPETSLEGAQELAERIRRLLAKLKIPHTVSGlpLYVTISIGI----AAYPNDGEDPEDLLKRADTALYQAKQA 156
|
....
gi 446480599 458 GRNR 461
Cdd:pfam00990 157 GRNR 160
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
195-461 |
1.20e-52 |
|
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: 178.63 E-value: 1.20e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446480599 195 IPAIALIVSVIASVVIGGAGSLAFPLPALIWCAVRYTPQVTCLLTFVTGAVEVVLVANSVIDISVGSPFSIPQMFSARLG 274
Cdd:COG2199 9 LALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446480599 275 IATMAICPImvsFSVAAINSLMKQVALRADFDFLTQVYSRSGLYEALK---SPSLKQTQHLTVMLLDIDYFKSINDNYGH 351
Cdd:COG2199 89 ALLLLLLAL---EDITELRRLEERLRRLATHDPLTGLPNRRAFEERLErelARARREGRPLALLLIDLDHFKRINDTYGH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446480599 352 ECGDKVLSVFAQHIQKIVGDKGLVARMGGEEFAVAVPSVNPVDGLLMAEKIRKGVELQPFTWQQKTLYLTVSIGVgsgcA 431
Cdd:COG2199 166 AAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELEGKELRVTVSIGV----A 241
|
250 260 270
....*....|....*....|....*....|
gi 446480599 432 SYRTLTDDFNKLMVEADTCLYRSKKDGRNR 461
Cdd:COG2199 242 LYPEDGDSAEELLRRADLALYRAKRAGRNR 271
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
305-461 |
2.99e-52 |
|
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: 173.51 E-value: 2.99e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446480599 305 FDFLTQVYSRSGLYEALK---SPSLKQTQHLTVMLLDIDYFKSINDNYGHECGDKVLSVFAQHIQKIVGDKGLVARMGGE 381
Cdd:cd01949 2 TDPLTGLPNRRAFEERLErllARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446480599 382 EFAVAVPSVNPVDGLLMAEKIRKGVElQPFTWQQKTLYLTVSIGVgsgcASYRTLTDDFNKLMVEADTCLYRSKKDGRNR 461
Cdd:cd01949 82 EFAILLPGTDLEEAEALAERLREAIE-EPFFIDGQEIRVTASIGI----ATYPEDGEDAEELLRRADEALYRAKRSGRNR 156
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
301-463 |
1.03e-47 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 161.65 E-value: 1.03e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446480599 301 LRADFDFLTQVYSRSGLYEALK---SPSLKQTQHLTVMLLDIDYFKSINDNYGHECGDKVLSVFAQHIQKIVGDKGLVAR 377
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEqelQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446480599 378 MGGEEFAVAVPSVNPVDGLLMAEKIRKGVElQPFTWQQKTLYLTVSIGVgsgcASYRTLTDDFNKLMVEADTCLYRSKKD 457
Cdd:smart00267 81 LGGDEFALLLPETSLEEAIALAERILQQLR-EPIIIHGIPLYLTISIGV----AAYPNPGEDAEDLLKRADTALYQAKKA 155
|
....*.
gi 446480599 458 GRNRTS 463
Cdd:smart00267 156 GRNQVA 161
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
306-462 |
1.45e-36 |
|
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: 132.46 E-value: 1.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446480599 306 DFLTQVYSRSGLYEALKSPSLKQTQH---LTVMLLDIDYFKSINDNYGHECGDKVLSVFAQHIQKIVGDKGLVARMGGEE 382
Cdd:TIGR00254 5 DPLTGLYNRRYLEEMLDSELKRARRFqrsFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYGGEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446480599 383 FAVAVPSVNPVDGLLMAEKIRKGVELQPFTWQQK-TLYLTVSIGVgsgcASYRTLTDDFNKLMVEADTCLYRSKKDGRNR 461
Cdd:TIGR00254 85 FVVILPGTPLEDALSKAERLRDAINSKPIEVAGSeTLTVTVSIGV----ACYPGHGLTLEELLKRADEALYQAKKAGRNR 160
|
.
gi 446480599 462 T 462
Cdd:TIGR00254 161 V 161
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
325-461 |
6.12e-35 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 135.41 E-value: 6.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446480599 325 SLKQTQHLTVMLLDIDYFKSINDNYGHECGDKVLSVFAQHIQKIVGDKGLVARMGGEEFAVAVPSVNPVDGLLMAEKIRK 404
Cdd:PRK09581 317 ANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARYGGEEFVVVMPDTDIEDAIAVAERIRR 396
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 446480599 405 GVELQPFTWQQ--KTLYLTVSIGVgsgcASYRTLTDDFNKLMVEADTCLYRSKKDGRNR 461
Cdd:PRK09581 397 KIAEEPFIISDgkERLNVTVSIGV----AELRPSGDTIEALIKRADKALYEAKNTGRNR 451
|
|
| MASE1 |
COG3447 |
Integral membrane sensor domain MASE1 [Signal transduction mechanisms]; |
18-415 |
1.32e-34 |
|
Integral membrane sensor domain MASE1 [Signal transduction mechanisms];
Pssm-ID: 442670 [Multi-domain] Cd Length: 637 Bit Score: 136.86 E-value: 1.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446480599 18 LRNSIAIFVLTTLFYFIGAEL-RLVHELSLFWPLNGVMAGVFARYVWLNRLHYYAISYVAMLVYDaITTEWGLVSLAINF 96
Cdd:COG3447 14 LLRLLLLALLYFLLALLGLLLaRPPGGVSPIWPPAGVALAALLRFGRRAWPGILLGALLANLLAG-LTGDPLLLALLIAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446480599 97 SNMMFIVTVALLVARDKRLGKNKYEPVSALRLFNY-CLLAALLCAIVGAIGSV---SIDSLDFWPLLADWFSEQFSTGVL 172
Cdd:COG3447 93 GNTLEALLAAWLLRRLLGFSPPLQRLRDVLRFLLAaALLAPLISALLGALALAlagLLPGSPFLSSWLTWWLGDALGILL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446480599 173 IVPCMLTLAIPGvLPRFKAEQMIPAIALI---VSVIASVVIGGAGSLAF-PLPALIWCAVRYTPQVTCLLTFVTGAVEVV 248
Cdd:COG3447 173 VTPLLLAWRRPR-LRRLRRRRLLEALALLallLLVSWLVFGLLGYPLAFlLFPLLLWAALRFGLRGAALAVLLLALIAIL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446480599 249 LVANSVIDISVGSPFSipQMFSARLGIATMAICPIMVS----------------FSVAAINSLMKQVALRADFDFLTQVY 312
Cdd:COG3447 252 ATALGLGPFASLSPNQ--SLLLLQLFLAVLALTGLLLAaalaerrrqrlrerelALRAALELLALGLLLAALDDALLLLN 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446480599 313 SRSGLYEALKS-PSLKQTQHLTVMLLDIDYFKSINDNYGHECGDKVLSVFAQHIQKIVGDKGLVARMGGEEFAVAVPSVN 391
Cdd:COG3447 330 ARGLLLLALSLaALLLLRLALLLLLLALDALLLLLADDDRGELRGDLLRRRGATRLGAVVARLLRRSGGRGEEVVVLLVI 409
|
410 420
....*....|....*....|....
gi 446480599 392 PVDGLLMAEKIRKGVELQPFTWQQ 415
Cdd:COG3447 410 AQVEEALELALRERREERLLERLA 433
|
|
| diguan_SiaD |
NF038266 |
biofilm regulation diguanylate cyclase SiaD; |
293-461 |
3.53e-29 |
|
biofilm regulation diguanylate cyclase SiaD;
Pssm-ID: 468439 [Multi-domain] Cd Length: 252 Bit Score: 115.08 E-value: 3.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446480599 293 NSLMKQVALRadfDFLTQVYSRSGLYEALKSPSLKQTQH---LTVMLLDIDYFKSINDNYGHECGDKVLSVFAQHIQKIV 369
Cdd:NF038266 87 NEALREASTR---DPLTGLPNRRLLMERLREEVERARRSgrpFTLAMLDVDHFKRINDRYGHEVGDRVLVEIARTLRAEL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446480599 370 GDKGLVARMGGEEFAVAVPSVNPVDGLLMAEKIRKGVELQPFTWQQKTLYLTVSIGVgsgcASYRTLTDDFNKLMVEADT 449
Cdd:NF038266 164 REYDLCGRWGGEEFLLLLPETGLEEAQVVLERLREAVRALAVRVGDDVLSVTASAGL----AEHRPPEEGLSATLSRADQ 239
|
170
....*....|..
gi 446480599 450 CLYRSKKDGRNR 461
Cdd:NF038266 240 ALYQAKRAGRDR 251
|
|
| dguan_cyc_DgcA |
NF041606 |
diguanylate cyclase DgcA; |
283-463 |
6.48e-27 |
|
diguanylate cyclase DgcA;
Pssm-ID: 469490 [Multi-domain] Cd Length: 340 Bit Score: 110.99 E-value: 6.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446480599 283 IMVSFSVAAI---NSLMKQvalRADFDFLTQV----YSRSGLYEALKSpSLKQTQHLTVMLLDIDYFKSINDNYGHECGD 355
Cdd:NF041606 158 IMNIASLAAIainNALLLE---MTTTDMMTHLklkhYFYTVLMEKLDT-INSQGEPLSILMLDIDFFKQINDTYGHACGD 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446480599 356 KVLSVFAQHIQKIVGDKGLVARMGGEEFAVAVPSVNPVDGLLMAEKIRKGVELQPFTWQQKTLYLTVSIGVgsgcASYRT 435
Cdd:NF041606 234 LVLQMVASIIQSCTRTQDMAARYGGEEFVVMLSNTSSKTAKKIAERIRKSIENLSILYDEQHIRVTISIGV----AEYNF 309
|
170 180
....*....|....*....|....*...
gi 446480599 436 LTDDFNKLMVEADTCLYRSKKDGRNRTS 463
Cdd:NF041606 310 DVESAKSLVERADKALYESKQNGRNRVS 337
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
26-285 |
1.97e-03 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 40.81 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446480599 26 VLTTLFYFIGAELRLvhELSLF-------WPLNGVMAGVFAR-----YVWLnrlhyYAISYVAMLVYDAITTEWGLVSLA 93
Cdd:PRK09776 1 VSLGLVSFIFTLFSL--ELSRFpttlaplWFPTAIMMVAFYRhagrmWPGI-----LLSCSLGNIAANILLFSTSSLNLT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446480599 94 INFSNMMFIVTVALLVardkRLGKNKYEPV----SALRLfnyCLLAALLCAIVGAIGSVSI-DSLDFWPLLADWFSEQFS 168
Cdd:PRK09776 74 WTTINLVEAVVGAVLL----RKLLPWYNPLqnlaDWLRL---ALGSAIVPPLLGGVLVVLLtPGDDPLRAFLIWVLSEAI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446480599 169 TGVLIVPCMLTLAIPGVL----PRFKAEQmipAIALIVSVIASVV--IGGAGSLAFPLPALIWCAVRYTPQVTCLLTFVT 242
Cdd:PRK09776 147 GMLALVPLGLLFKPHYLLrhrnPRLLFES---LLTLAITLTLSWLalLYLPWPFTFIIVLLMWSAVRLPRMEAFLIFLTT 223
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 446480599 243 G-AVEVVLVANSVIDISVGSPFSIPQMFSARLGIATMAICPIMV 285
Cdd:PRK09776 224 VmMVSLMMAADPSLLATPRTYLMSHMPWLPFLLILLPANIMTMV 267
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
303-461 |
8.05e-55 |
|
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: 180.14 E-value: 8.05e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446480599 303 ADFDFLTQVYSRSGLYEALK---SPSLKQTQHLTVMLLDIDYFKSINDNYGHECGDKVLSVFAQHIQKIVGDKGLVARMG 379
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEqelQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446480599 380 GEEFAVAVPSVNPVDGLLMAEKIRKGVELQPFTWQQKT--LYLTVSIGVgsgcASYRTLTDDFNKLMVEADTCLYRSKKD 457
Cdd:pfam00990 81 GDEFAILLPETSLEGAQELAERIRRLLAKLKIPHTVSGlpLYVTISIGI----AAYPNDGEDPEDLLKRADTALYQAKQA 156
|
....
gi 446480599 458 GRNR 461
Cdd:pfam00990 157 GRNR 160
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
195-461 |
1.20e-52 |
|
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: 178.63 E-value: 1.20e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446480599 195 IPAIALIVSVIASVVIGGAGSLAFPLPALIWCAVRYTPQVTCLLTFVTGAVEVVLVANSVIDISVGSPFSIPQMFSARLG 274
Cdd:COG2199 9 LALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446480599 275 IATMAICPImvsFSVAAINSLMKQVALRADFDFLTQVYSRSGLYEALK---SPSLKQTQHLTVMLLDIDYFKSINDNYGH 351
Cdd:COG2199 89 ALLLLLLAL---EDITELRRLEERLRRLATHDPLTGLPNRRAFEERLErelARARREGRPLALLLIDLDHFKRINDTYGH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446480599 352 ECGDKVLSVFAQHIQKIVGDKGLVARMGGEEFAVAVPSVNPVDGLLMAEKIRKGVELQPFTWQQKTLYLTVSIGVgsgcA 431
Cdd:COG2199 166 AAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELEGKELRVTVSIGV----A 241
|
250 260 270
....*....|....*....|....*....|
gi 446480599 432 SYRTLTDDFNKLMVEADTCLYRSKKDGRNR 461
Cdd:COG2199 242 LYPEDGDSAEELLRRADLALYRAKRAGRNR 271
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
305-461 |
2.99e-52 |
|
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: 173.51 E-value: 2.99e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446480599 305 FDFLTQVYSRSGLYEALK---SPSLKQTQHLTVMLLDIDYFKSINDNYGHECGDKVLSVFAQHIQKIVGDKGLVARMGGE 381
Cdd:cd01949 2 TDPLTGLPNRRAFEERLErllARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446480599 382 EFAVAVPSVNPVDGLLMAEKIRKGVElQPFTWQQKTLYLTVSIGVgsgcASYRTLTDDFNKLMVEADTCLYRSKKDGRNR 461
Cdd:cd01949 82 EFAILLPGTDLEEAEALAERLREAIE-EPFFIDGQEIRVTASIGI----ATYPEDGEDAEELLRRADEALYRAKRSGRNR 156
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
301-463 |
1.03e-47 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 161.65 E-value: 1.03e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446480599 301 LRADFDFLTQVYSRSGLYEALK---SPSLKQTQHLTVMLLDIDYFKSINDNYGHECGDKVLSVFAQHIQKIVGDKGLVAR 377
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEqelQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446480599 378 MGGEEFAVAVPSVNPVDGLLMAEKIRKGVElQPFTWQQKTLYLTVSIGVgsgcASYRTLTDDFNKLMVEADTCLYRSKKD 457
Cdd:smart00267 81 LGGDEFALLLPETSLEEAIALAERILQQLR-EPIIIHGIPLYLTISIGV----AAYPNPGEDAEDLLKRADTALYQAKKA 155
|
....*.
gi 446480599 458 GRNRTS 463
Cdd:smart00267 156 GRNQVA 161
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
306-462 |
1.45e-36 |
|
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: 132.46 E-value: 1.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446480599 306 DFLTQVYSRSGLYEALKSPSLKQTQH---LTVMLLDIDYFKSINDNYGHECGDKVLSVFAQHIQKIVGDKGLVARMGGEE 382
Cdd:TIGR00254 5 DPLTGLYNRRYLEEMLDSELKRARRFqrsFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYGGEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446480599 383 FAVAVPSVNPVDGLLMAEKIRKGVELQPFTWQQK-TLYLTVSIGVgsgcASYRTLTDDFNKLMVEADTCLYRSKKDGRNR 461
Cdd:TIGR00254 85 FVVILPGTPLEDALSKAERLRDAINSKPIEVAGSeTLTVTVSIGV----ACYPGHGLTLEELLKRADEALYQAKKAGRNR 160
|
.
gi 446480599 462 T 462
Cdd:TIGR00254 161 V 161
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
298-461 |
1.83e-36 |
|
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: 142.61 E-value: 1.83e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446480599 298 QVALRADFDFLTQVYSRSGLYEALK---SPSLKQTQHLTVMLLDIDYFKSINDNYGHECGDKVLSVFAQHIQKIVGDKGL 374
Cdd:COG5001 246 RLRHLAYHDPLTGLPNRRLFLDRLEqalARARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDT 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446480599 375 VARMGGEEFAVAVPSVNPVDGLL-MAEKIRKGVElQPFTWQQKTLYLTVSIGVgsgcASYRTLTDDFNKLMVEADTCLYR 453
Cdd:COG5001 326 VARLGGDEFAVLLPDLDDPEDAEaVAERILAALA-EPFELDGHELYVSASIGI----ALYPDDGADAEELLRNADLAMYR 400
|
....*...
gi 446480599 454 SKKDGRNR 461
Cdd:COG5001 401 AKAAGRNR 408
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
325-461 |
6.12e-35 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 135.41 E-value: 6.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446480599 325 SLKQTQHLTVMLLDIDYFKSINDNYGHECGDKVLSVFAQHIQKIVGDKGLVARMGGEEFAVAVPSVNPVDGLLMAEKIRK 404
Cdd:PRK09581 317 ANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARYGGEEFVVVMPDTDIEDAIAVAERIRR 396
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 446480599 405 GVELQPFTWQQ--KTLYLTVSIGVgsgcASYRTLTDDFNKLMVEADTCLYRSKKDGRNR 461
Cdd:PRK09581 397 KIAEEPFIISDgkERLNVTVSIGV----AELRPSGDTIEALIKRADKALYEAKNTGRNR 451
|
|
| MASE1 |
COG3447 |
Integral membrane sensor domain MASE1 [Signal transduction mechanisms]; |
18-415 |
1.32e-34 |
|
Integral membrane sensor domain MASE1 [Signal transduction mechanisms];
Pssm-ID: 442670 [Multi-domain] Cd Length: 637 Bit Score: 136.86 E-value: 1.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446480599 18 LRNSIAIFVLTTLFYFIGAEL-RLVHELSLFWPLNGVMAGVFARYVWLNRLHYYAISYVAMLVYDaITTEWGLVSLAINF 96
Cdd:COG3447 14 LLRLLLLALLYFLLALLGLLLaRPPGGVSPIWPPAGVALAALLRFGRRAWPGILLGALLANLLAG-LTGDPLLLALLIAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446480599 97 SNMMFIVTVALLVARDKRLGKNKYEPVSALRLFNY-CLLAALLCAIVGAIGSV---SIDSLDFWPLLADWFSEQFSTGVL 172
Cdd:COG3447 93 GNTLEALLAAWLLRRLLGFSPPLQRLRDVLRFLLAaALLAPLISALLGALALAlagLLPGSPFLSSWLTWWLGDALGILL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446480599 173 IVPCMLTLAIPGvLPRFKAEQMIPAIALI---VSVIASVVIGGAGSLAF-PLPALIWCAVRYTPQVTCLLTFVTGAVEVV 248
Cdd:COG3447 173 VTPLLLAWRRPR-LRRLRRRRLLEALALLallLLVSWLVFGLLGYPLAFlLFPLLLWAALRFGLRGAALAVLLLALIAIL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446480599 249 LVANSVIDISVGSPFSipQMFSARLGIATMAICPIMVS----------------FSVAAINSLMKQVALRADFDFLTQVY 312
Cdd:COG3447 252 ATALGLGPFASLSPNQ--SLLLLQLFLAVLALTGLLLAaalaerrrqrlrerelALRAALELLALGLLLAALDDALLLLN 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446480599 313 SRSGLYEALKS-PSLKQTQHLTVMLLDIDYFKSINDNYGHECGDKVLSVFAQHIQKIVGDKGLVARMGGEEFAVAVPSVN 391
Cdd:COG3447 330 ARGLLLLALSLaALLLLRLALLLLLLALDALLLLLADDDRGELRGDLLRRRGATRLGAVVARLLRRSGGRGEEVVVLLVI 409
|
410 420
....*....|....*....|....
gi 446480599 392 PVDGLLMAEKIRKGVELQPFTWQQ 415
Cdd:COG3447 410 AQVEEALELALRERREERLLERLA 433
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
300-462 |
2.20e-30 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 119.40 E-value: 2.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446480599 300 ALRADFDFLTQVYSRSGLYEALKSpSLKQT--QHLTVMLLDIDYFKSINDNYGHECGDKVLSVFAQHIQKIVGDKGLVAR 377
Cdd:PRK09894 126 TIRSNMDVLTGLPGRRVLDESFDH-QLRNRepQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYR 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446480599 378 MGGEEFAVAVPSVNPVDGLLMAEKIRKGVELQPFTWQQKTLYLTVSIGVGSGCASyRTLTDdfnkLMVEADTCLYRSKKD 457
Cdd:PRK09894 205 YGGEEFIICLKAATDEEACRAGERIRQLIANHAITHSDGRINITATFGVSRAFPE-ETLDV----VIGRADRAMYEGKQT 279
|
....*
gi 446480599 458 GRNRT 462
Cdd:PRK09894 280 GRNRV 284
|
|
| diguan_SiaD |
NF038266 |
biofilm regulation diguanylate cyclase SiaD; |
293-461 |
3.53e-29 |
|
biofilm regulation diguanylate cyclase SiaD;
Pssm-ID: 468439 [Multi-domain] Cd Length: 252 Bit Score: 115.08 E-value: 3.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446480599 293 NSLMKQVALRadfDFLTQVYSRSGLYEALKSPSLKQTQH---LTVMLLDIDYFKSINDNYGHECGDKVLSVFAQHIQKIV 369
Cdd:NF038266 87 NEALREASTR---DPLTGLPNRRLLMERLREEVERARRSgrpFTLAMLDVDHFKRINDRYGHEVGDRVLVEIARTLRAEL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446480599 370 GDKGLVARMGGEEFAVAVPSVNPVDGLLMAEKIRKGVELQPFTWQQKTLYLTVSIGVgsgcASYRTLTDDFNKLMVEADT 449
Cdd:NF038266 164 REYDLCGRWGGEEFLLLLPETGLEEAQVVLERLREAVRALAVRVGDDVLSVTASAGL----AEHRPPEEGLSATLSRADQ 239
|
170
....*....|..
gi 446480599 450 CLYRSKKDGRNR 461
Cdd:NF038266 240 ALYQAKRAGRDR 251
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
282-461 |
2.19e-27 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 115.11 E-value: 2.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446480599 282 PIMVSFSVAAI-----NSLMKQVALR--ADFDFLTQVYSRSGLYE---ALKSPSLKQTQHLTVMLLDIDYFKSINDNYGH 351
Cdd:PRK15426 370 TAMLLISWYVIrrmvsNMFVLQSSLQwqAWHDPLTRLYNRGALFEkarALAKRCQRDQQPFSVIQLDLDHFKSINDRFGH 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446480599 352 ECGDKVLSVFAQHIQKIVGDKGLVARMGGEEFAVAVPSVNPVDGLLMAEKIRKGVELQP-FTWQQKTLYLTVSIGVGSgc 430
Cdd:PRK15426 450 QAGDRVLSHAAGLISSSLRAQDVAGRVGGEEFCVVLPGASLAEAAQVAERIRLRINEKEiLVAKSTTIRISASLGVSS-- 527
|
170 180 190
....*....|....*....|....*....|.
gi 446480599 431 aSYRTLTDDFNKLMVEADTCLYRSKKDGRNR 461
Cdd:PRK15426 528 -AEEDGDYDFEQLQSLADRRLYLAKQAGRNR 557
|
|
| dguan_cyc_DgcA |
NF041606 |
diguanylate cyclase DgcA; |
283-463 |
6.48e-27 |
|
diguanylate cyclase DgcA;
Pssm-ID: 469490 [Multi-domain] Cd Length: 340 Bit Score: 110.99 E-value: 6.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446480599 283 IMVSFSVAAI---NSLMKQvalRADFDFLTQV----YSRSGLYEALKSpSLKQTQHLTVMLLDIDYFKSINDNYGHECGD 355
Cdd:NF041606 158 IMNIASLAAIainNALLLE---MTTTDMMTHLklkhYFYTVLMEKLDT-INSQGEPLSILMLDIDFFKQINDTYGHACGD 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446480599 356 KVLSVFAQHIQKIVGDKGLVARMGGEEFAVAVPSVNPVDGLLMAEKIRKGVELQPFTWQQKTLYLTVSIGVgsgcASYRT 435
Cdd:NF041606 234 LVLQMVASIIQSCTRTQDMAARYGGEEFVVMLSNTSSKTAKKIAERIRKSIENLSILYDEQHIRVTISIGV----AEYNF 309
|
170 180
....*....|....*....|....*...
gi 446480599 436 LTDDFNKLMVEADTCLYRSKKDGRNRTS 463
Cdd:NF041606 310 DVESAKSLVERADKALYESKQNGRNRVS 337
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
283-470 |
8.14e-17 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 83.57 E-value: 8.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446480599 283 IMVSFSVAAINSLMKQVALRADFDFLTQVYSR----SGLYEALKSPSLKQTQHLTVmLLDIDYFKSINDNYGHECGDKVL 358
Cdd:PRK09776 645 VLVIQDVTESRKMLRQLSYSASHDALTHLANRasfeKQLRRLLQTVNSTHQRHALV-FIDLDRFKAVNDSAGHAAGDALL 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446480599 359 SVFAQHIQKIVGDKGLVARMGGEEFAVAVPSVNPVDGLLMAEKIRKGVELQPFTWQQKTLYLTVSIGVgsgcasyrTLTD 438
Cdd:PRK09776 724 RELASLMLSMLRSSDVLARLGGDEFGLLLPDCNVESARFIATRIISAINDYHFPWEGRVYRVGASAGI--------TLID 795
|
170 180 190
....*....|....*....|....*....|....*.
gi 446480599 439 DFN----KLMVEADTCLYRSKKDGRNRTSTMRYGEE 470
Cdd:PRK09776 796 ANNhqasEVMSQADIACYAAKNAGRGRVTVYEPQQA 831
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
306-462 |
1.48e-13 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 71.78 E-value: 1.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446480599 306 DFLTQVYSRSGLYEALKSP---SLKQTQHLTVMLLDIDYFKSINDNYGHECGDKVLSVFAQHIQKIVGDKGLVARMGGEE 382
Cdd:PRK10245 208 DGMTGVYNRRHWETLLRNEfdnCRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSDVIGRFGGDE 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446480599 383 FAV---AVPSVNPVDGLLMAEKIRKGVELqPFTWQQKtlyLTVSIGVgsgcASYRTLTDDFNKLMVEADTCLYRSKKDGR 459
Cdd:PRK10245 288 FAVimsGTPAESAITAMSRVHEGLNTLRL-PNAPQVT---LRISVGV----APLNPQMSHYREWLKSADLALYKAKNAGR 359
|
...
gi 446480599 460 NRT 462
Cdd:PRK10245 360 NRT 362
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
332-429 |
1.35e-12 |
|
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: 64.68 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446480599 332 LTVMLLDIDYFKSINDNYGHECGDKVLSVFAQHIQKIVGDKG-LVARMGGEEFAVAVPSVNPVDGLLMAEKIRKGVELQP 410
Cdd:cd07556 2 VTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSGdLKIKTIGDEFMVVSGLDHPAAAVAFAEDMREAVSALN 81
|
90
....*....|....*....
gi 446480599 411 ftwQQKTLYLTVSIGVGSG 429
Cdd:cd07556 82 ---QSEGNPVRVRIGIHTG 97
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
305-426 |
1.27e-11 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 67.10 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446480599 305 FDFLTQVYSRSGLYEALKSpSLKQTQHLTVMLLDIDYFKSINDNYGHECGDKVLSVFAQHIQKIVGDKGLVARMGGEEFA 384
Cdd:PRK11359 378 FDPLTGLPNRNNLHNYLDD-LVDKAVSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGTQFV 456
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 446480599 385 VAVPSVNPVDGLLMAEKIRKGVElQPFTWQQKTLYLTVSIGV 426
Cdd:PRK11359 457 LVSLENDVSNITQIADELRNVVS-KPIMIDDKPFPLTLSIGI 497
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
334-459 |
5.55e-11 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 64.70 E-value: 5.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446480599 334 VMLLDIDYFKSINDNYGHECGDKVLSVFAQHIQKIVGDKGLVARMGGEEFAVAVPsvNPVDGLL--MAEKIRKGVElQPF 411
Cdd:PRK10060 269 IVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQTLARLGGDEFLVLAS--HTSQAALeaMASRILTRLR-LPF 345
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 446480599 412 TWQQKTLYLTVSIGVgsgcASYRTLTDDFNKLMVEADTCLYRSKKDGR 459
Cdd:PRK10060 346 RIGLIEVYTGCSIGI----ALAPEHGDDSESLIRSADTAMYTAKEGGR 389
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
291-391 |
3.45e-08 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 55.40 E-value: 3.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446480599 291 AINSLMKQVALRADFdfltqvysRSGLYEALKSPSLKQTQHLtvMLLDIDYFKSINDNYGHECGDKVLSVFAQHIQKIVG 370
Cdd:PRK09966 248 ALHDPLTGLANRAAF--------RSGINTLMNNSDARKTSAL--LFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGG 317
|
90 100
....*....|....*....|.
gi 446480599 371 DKGLVARMGGEEFAVAVPSVN 391
Cdd:PRK09966 318 LRHKAYRLGGDEFAMVLYDVQ 338
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
374-426 |
1.01e-07 |
|
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: 51.83 E-value: 1.01e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 446480599 374 LVARMGGEEFAVAVPSVNPVDGLLMAEKIRKGVElqpftwQQKTLYLTVSIGV 426
Cdd:COG3706 117 LVARYGGEEFAILLPGTDLEGALAVAERIREAVA------ELPSLRVTVSIGV 163
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
325-461 |
1.02e-05 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 48.01 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446480599 325 SLKQTQHLTVMLLDIDYFKSINDNYGHECGDKVLSVFAQHIQKIVGDKGLVARMGGEEFAV-AVPSVNPVDGLLMAEKIR 403
Cdd:PRK11829 256 SSTRTDHFHLLVIGIETLQEVSGAMSEAQHQQLLLTIVQRIEQCIDDSDLLAQLSKTEFAVlARGTRRSFPAMQLARRIM 335
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 446480599 404 KGVElQPFTWQQKTLYLTVSIGVgsgcASYRTLTDDFNKLMVEADTCLYRSKKDGRNR 461
Cdd:PRK11829 336 SQVT-QPLFFDEITLRPSASIGI----TRYQAQQDTAESMMRNASTAMMAAHHEGRNQ 388
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
26-285 |
1.97e-03 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 40.81 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446480599 26 VLTTLFYFIGAELRLvhELSLF-------WPLNGVMAGVFAR-----YVWLnrlhyYAISYVAMLVYDAITTEWGLVSLA 93
Cdd:PRK09776 1 VSLGLVSFIFTLFSL--ELSRFpttlaplWFPTAIMMVAFYRhagrmWPGI-----LLSCSLGNIAANILLFSTSSLNLT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446480599 94 INFSNMMFIVTVALLVardkRLGKNKYEPV----SALRLfnyCLLAALLCAIVGAIGSVSI-DSLDFWPLLADWFSEQFS 168
Cdd:PRK09776 74 WTTINLVEAVVGAVLL----RKLLPWYNPLqnlaDWLRL---ALGSAIVPPLLGGVLVVLLtPGDDPLRAFLIWVLSEAI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446480599 169 TGVLIVPCMLTLAIPGVL----PRFKAEQmipAIALIVSVIASVV--IGGAGSLAFPLPALIWCAVRYTPQVTCLLTFVT 242
Cdd:PRK09776 147 GMLALVPLGLLFKPHYLLrhrnPRLLFES---LLTLAITLTLSWLalLYLPWPFTFIIVLLMWSAVRLPRMEAFLIFLTT 223
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 446480599 243 G-AVEVVLVANSVIDISVGSPFSIPQMFSARLGIATMAICPIMV 285
Cdd:PRK09776 224 VmMVSLMMAADPSLLATPRTYLMSHMPWLPFLLILLPANIMTMV 267
|
|
| |
