|
Name |
Accession |
Description |
Interval |
E-value |
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
6-370 |
0e+00 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 730.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446406229 6 MNDENFYRKAVEQAVAPPD-PPDDRQRSGLRFARRIRLPRAVGLGGMFLPVAAVLVSQPVFGGWWLLLVGWSFVWPHLAW 84
Cdd:PRK10245 1 MNDENFYKKAAAHGEEPPLtPQNEHQRSGLRFARRVRLPRAVGLAGMFLPIASTLVSHPPPGWWWLLLVGWAFVWPHLAW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446406229 85 QWAAKALDPLRQEIYNLKVDAILSGMWIALMGVNMLPAAALFMMMSMNLMGAGGRRLFTVGMGLLLASCLVTLQLTGLPV 164
Cdd:PRK10245 81 QIASRAVDPLSREIYNLKTDAVLAGMWVGVMGVNVLPSTAMLMIMCLNLMGAGGPRLFVAGLVLMVVSCLVTLELTGITV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446406229 165 AMRSSSLEVTLSLPVIMLYPLLFAWVSYQTAIKLAEHKRRLQAMSSRDGMTGVYNRRHWEILLRNEFDHSRRHHREATLL 244
Cdd:PRK10245 161 SFNSAPLEWWLSLPVIVIYPLLFAWVSYQTATKLAEHKRRLQVMSTRDGMTGVYNRRHWETLLRNEFDNCRRHHRDATLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446406229 245 IIDIDHFKSINDTWGHDVGDEAIIALTRQLQLTLRGSDIIGRFGGDEFAVIMCGTPADSAITAMSRVHERLNTLRLPGAP 324
Cdd:PRK10245 241 IIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSDVIGRFGGDEFAVIMSGTPAESAITAMSRVHEGLNTLRLPNAP 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 446406229 325 QVMLRISVGVAPLTPQIGHYREWLKSADMALYKAKNAGRNRTEVAA 370
Cdd:PRK10245 321 QVTLRISVGVAPLNPQMSHYREWLKSADLALYKAKNAGRNRTEVAA 366
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
208-370 |
2.38e-75 |
|
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: 230.30 E-value: 2.38e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446406229 208 MSSRDGMTGVYNRRHWEILLRNEFDHSRRHHREATLLIIDIDHFKSINDTWGHDVGDEAIIALTRQLQLTLRGSDIIGRF 287
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446406229 288 GGDEFAVIMCGTPADSAITAMSRVHERLNTLRLP--GAPQVMLRISVGVAPLTPQIGHYREWLKSADMALYKAKNAGRNR 365
Cdd:TIGR00254 81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPIEvaGSETLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRNR 160
|
....*
gi 446406229 366 TEVAA 370
Cdd:TIGR00254 161 VVVAD 165
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
211-365 |
8.01e-61 |
|
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: 192.77 E-value: 8.01e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446406229 211 RDGMTGVYNRRHWEILLRNEFDHSRRHHREATLLIIDIDHFKSINDTWGHDVGDEAIIALTRQLQLTLRGSDIIGRFGGD 290
Cdd:cd01949 2 TDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGD 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446406229 291 EFAVIMCGTPADSAITAMSRVHERLNTLRLPGAPQVMLRISVGVAPLTPQIGHYREWLKSADMALYKAKNAGRNR 365
Cdd:cd01949 82 EFAILLPGTDLEEAEALAERLREAIEEPFFIDGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNR 156
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
103-369 |
1.04e-59 |
|
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: 194.04 E-value: 1.04e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446406229 103 VDAILSGMWIALMGVNMLPAAALFMMMSMNLMGAGGRRLFTVGMGLLLASCLVTLQLTGLPVAMRSSSLEVTLSLPVIML 182
Cdd:COG2199 10 ALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446406229 183 YPLLFAWVSYQTAIKLAEhkRRLQAMSSRDGMTGVYNRRHWEILLRNEFDHSRRHHREATLLIIDIDHFKSINDTWGHDV 262
Cdd:COG2199 90 LLLLLLALEDITELRRLE--ERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTYGHAA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446406229 263 GDEAIIALTRQLQLTLRGSDIIGRFGGDEFAVIMCGTPADSAITAMSRVHERLNTLRLP-GAPQVMLRISVGVAPLTPQI 341
Cdd:COG2199 168 GDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFElEGKELRVTVSIGVALYPEDG 247
|
250 260
....*....|....*....|....*...
gi 446406229 342 GHYREWLKSADMALYKAKNAGRNRTEVA 369
Cdd:COG2199 248 DSAEELLRRADLALYRAKRAGRNRVVVY 275
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
209-365 |
1.19e-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: 1.19e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446406229 209 SSRDGMTGVYNRRHWEILLRNEFDHSRRHHREATLLIIDIDHFKSINDTWGHDVGDEAIIALTRQLQLTLRGSDIIGRFG 288
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446406229 289 GDEFAVIMCGTPADSAITAMSRVHERLNTLRLP---GAPQVMLRISVGVAPLTPQIGHYREWLKSADMALYKAKNAGRNR 365
Cdd:pfam00990 81 GDEFAILLPETSLEGAQELAERIRRLLAKLKIPhtvSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGRNR 160
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
208-369 |
7.19e-57 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 182.83 E-value: 7.19e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446406229 208 MSSRDGMTGVYNRRHWEILLRNEFDHSRRHHREATLLIIDIDHFKSINDTWGHDVGDEAIIALTRQLQLTLRGSDIIGRF 287
Cdd:smart00267 2 LAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446406229 288 GGDEFAVIMCGTPADSAITAMSRVHERLNTLRLPGAPQVMLRISVGVAPLTPQIGHYREWLKSADMALYKAKNAGRNRTE 367
Cdd:smart00267 82 GGDEFALLLPETSLEEAIALAERILQQLREPIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQVA 161
|
..
gi 446406229 368 VA 369
Cdd:smart00267 162 VY 163
|
|
| diguan_SiaD |
NF038266 |
biofilm regulation diguanylate cyclase SiaD; |
204-365 |
9.18e-43 |
|
biofilm regulation diguanylate cyclase SiaD;
Pssm-ID: 468439 [Multi-domain] Cd Length: 252 Bit Score: 149.36 E-value: 9.18e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446406229 204 RLQAMSSRDGMTGVYNRRHWEILLRNEFDHSRRHHREATLLIIDIDHFKSINDTWGHDVGDEAIIALTRQLQLTLRGSDI 283
Cdd:NF038266 89 ALREASTRDPLTGLPNRRLLMERLREEVERARRSGRPFTLAMLDVDHFKRINDRYGHEVGDRVLVEIARTLRAELREYDL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446406229 284 IGRFGGDEFAVIMCGTPADSAITAMSRVHERLNTLRLP-GAPQVMLRISVGVAPLTPQIGHYREWLKSADMALYKAKNAG 362
Cdd:NF038266 169 CGRWGGEEFLLLLPETGLEEAQVVLERLREAVRALAVRvGDDVLSVTASAGLAEHRPPEEGLSATLSRADQALYQAKRAG 248
|
...
gi 446406229 363 RNR 365
Cdd:NF038266 249 RDR 251
|
|
| diguan_DgcJ |
NF040885 |
diguanylate cyclase DgcJ; |
171-363 |
1.05e-19 |
|
diguanylate cyclase DgcJ;
Pssm-ID: 468821 [Multi-domain] Cd Length: 490 Bit Score: 90.02 E-value: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446406229 171 LEVTLSLPVimLYPLLFAW---VSY--QTAI--KLAEHKRRLQAMSSR----DGMTGVYNRRHWEILLRNEFDHSRRHHR 239
Cdd:NF040885 294 LHVELSLDV--LYFILSSWklfLFYllSTALllHLVRMHFRLYHNVSRenisDSMTGLYNRKILTPTLEQRLQRLTEKGI 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446406229 240 EATLLIIDIDHFKSINDTWGHDVGDEAIIALTRQLQLTLRGSDIIGRFGGDEFAVIMCGTPADSAITAMSRVHERLNTLr 319
Cdd:NF040885 372 PVTFIALDCDKLKHINDTLGHHEGDRAITLLAQAISASIRKSDYGIRLGGDEFCIILIDYEEAEAQNLIERIRQHLRTI- 450
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446406229 320 lpgAPQVMLRISVGVAPLTP--QIGHYrewLKSADMALYKAKNAGR 363
Cdd:NF040885 451 ---DPDKRVSFSWGAYQMQPgdTLDDA---YKAADERLYLNKKQKH 490
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
6-370 |
0e+00 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 730.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446406229 6 MNDENFYRKAVEQAVAPPD-PPDDRQRSGLRFARRIRLPRAVGLGGMFLPVAAVLVSQPVFGGWWLLLVGWSFVWPHLAW 84
Cdd:PRK10245 1 MNDENFYKKAAAHGEEPPLtPQNEHQRSGLRFARRVRLPRAVGLAGMFLPIASTLVSHPPPGWWWLLLVGWAFVWPHLAW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446406229 85 QWAAKALDPLRQEIYNLKVDAILSGMWIALMGVNMLPAAALFMMMSMNLMGAGGRRLFTVGMGLLLASCLVTLQLTGLPV 164
Cdd:PRK10245 81 QIASRAVDPLSREIYNLKTDAVLAGMWVGVMGVNVLPSTAMLMIMCLNLMGAGGPRLFVAGLVLMVVSCLVTLELTGITV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446406229 165 AMRSSSLEVTLSLPVIMLYPLLFAWVSYQTAIKLAEHKRRLQAMSSRDGMTGVYNRRHWEILLRNEFDHSRRHHREATLL 244
Cdd:PRK10245 161 SFNSAPLEWWLSLPVIVIYPLLFAWVSYQTATKLAEHKRRLQVMSTRDGMTGVYNRRHWETLLRNEFDNCRRHHRDATLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446406229 245 IIDIDHFKSINDTWGHDVGDEAIIALTRQLQLTLRGSDIIGRFGGDEFAVIMCGTPADSAITAMSRVHERLNTLRLPGAP 324
Cdd:PRK10245 241 IIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSDVIGRFGGDEFAVIMSGTPAESAITAMSRVHEGLNTLRLPNAP 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 446406229 325 QVMLRISVGVAPLTPQIGHYREWLKSADMALYKAKNAGRNRTEVAA 370
Cdd:PRK10245 321 QVTLRISVGVAPLNPQMSHYREWLKSADLALYKAKNAGRNRTEVAA 366
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
208-370 |
2.38e-75 |
|
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: 230.30 E-value: 2.38e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446406229 208 MSSRDGMTGVYNRRHWEILLRNEFDHSRRHHREATLLIIDIDHFKSINDTWGHDVGDEAIIALTRQLQLTLRGSDIIGRF 287
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446406229 288 GGDEFAVIMCGTPADSAITAMSRVHERLNTLRLP--GAPQVMLRISVGVAPLTPQIGHYREWLKSADMALYKAKNAGRNR 365
Cdd:TIGR00254 81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPIEvaGSETLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRNR 160
|
....*
gi 446406229 366 TEVAA 370
Cdd:TIGR00254 161 VVVAD 165
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
211-365 |
8.01e-61 |
|
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: 192.77 E-value: 8.01e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446406229 211 RDGMTGVYNRRHWEILLRNEFDHSRRHHREATLLIIDIDHFKSINDTWGHDVGDEAIIALTRQLQLTLRGSDIIGRFGGD 290
Cdd:cd01949 2 TDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGD 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446406229 291 EFAVIMCGTPADSAITAMSRVHERLNTLRLPGAPQVMLRISVGVAPLTPQIGHYREWLKSADMALYKAKNAGRNR 365
Cdd:cd01949 82 EFAILLPGTDLEEAEALAERLREAIEEPFFIDGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNR 156
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
103-369 |
1.04e-59 |
|
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: 194.04 E-value: 1.04e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446406229 103 VDAILSGMWIALMGVNMLPAAALFMMMSMNLMGAGGRRLFTVGMGLLLASCLVTLQLTGLPVAMRSSSLEVTLSLPVIML 182
Cdd:COG2199 10 ALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446406229 183 YPLLFAWVSYQTAIKLAEhkRRLQAMSSRDGMTGVYNRRHWEILLRNEFDHSRRHHREATLLIIDIDHFKSINDTWGHDV 262
Cdd:COG2199 90 LLLLLLALEDITELRRLE--ERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTYGHAA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446406229 263 GDEAIIALTRQLQLTLRGSDIIGRFGGDEFAVIMCGTPADSAITAMSRVHERLNTLRLP-GAPQVMLRISVGVAPLTPQI 341
Cdd:COG2199 168 GDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFElEGKELRVTVSIGVALYPEDG 247
|
250 260
....*....|....*....|....*...
gi 446406229 342 GHYREWLKSADMALYKAKNAGRNRTEVA 369
Cdd:COG2199 248 DSAEELLRRADLALYRAKRAGRNRVVVY 275
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
209-365 |
1.19e-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: 1.19e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446406229 209 SSRDGMTGVYNRRHWEILLRNEFDHSRRHHREATLLIIDIDHFKSINDTWGHDVGDEAIIALTRQLQLTLRGSDIIGRFG 288
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446406229 289 GDEFAVIMCGTPADSAITAMSRVHERLNTLRLP---GAPQVMLRISVGVAPLTPQIGHYREWLKSADMALYKAKNAGRNR 365
Cdd:pfam00990 81 GDEFAILLPETSLEGAQELAERIRRLLAKLKIPhtvSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGRNR 160
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
208-369 |
7.19e-57 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 182.83 E-value: 7.19e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446406229 208 MSSRDGMTGVYNRRHWEILLRNEFDHSRRHHREATLLIIDIDHFKSINDTWGHDVGDEAIIALTRQLQLTLRGSDIIGRF 287
Cdd:smart00267 2 LAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446406229 288 GGDEFAVIMCGTPADSAITAMSRVHERLNTLRLPGAPQVMLRISVGVAPLTPQIGHYREWLKSADMALYKAKNAGRNRTE 367
Cdd:smart00267 82 GGDEFALLLPETSLEEAIALAERILQQLREPIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQVA 161
|
..
gi 446406229 368 VA 369
Cdd:smart00267 162 VY 163
|
|
| diguan_SiaD |
NF038266 |
biofilm regulation diguanylate cyclase SiaD; |
204-365 |
9.18e-43 |
|
biofilm regulation diguanylate cyclase SiaD;
Pssm-ID: 468439 [Multi-domain] Cd Length: 252 Bit Score: 149.36 E-value: 9.18e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446406229 204 RLQAMSSRDGMTGVYNRRHWEILLRNEFDHSRRHHREATLLIIDIDHFKSINDTWGHDVGDEAIIALTRQLQLTLRGSDI 283
Cdd:NF038266 89 ALREASTRDPLTGLPNRRLLMERLREEVERARRSGRPFTLAMLDVDHFKRINDRYGHEVGDRVLVEIARTLRAELREYDL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446406229 284 IGRFGGDEFAVIMCGTPADSAITAMSRVHERLNTLRLP-GAPQVMLRISVGVAPLTPQIGHYREWLKSADMALYKAKNAG 362
Cdd:NF038266 169 CGRWGGEEFLLLLPETGLEEAQVVLERLREAVRALAVRvGDDVLSVTASAGLAEHRPPEEGLSATLSRADQALYQAKRAG 248
|
...
gi 446406229 363 RNR 365
Cdd:NF038266 249 RDR 251
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
15-365 |
1.89e-41 |
|
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: 154.16 E-value: 1.89e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446406229 15 AVEQAVAPPDPPDDRQRSGLRFARRIRLPRAVGLGGMFLPVAAVLVSQPVFGGWWLLLVGWSFVWPHLAWQWAAKALDPL 94
Cdd:COG5001 48 ALLLAALLLLALLALLALLLLAAALLALALAALLLAALLAALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALAAL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446406229 95 RQEIYNLKVDAILSGMWIALMGVNMLPAAALFMMMSMNLMGAGGRRLFTVGMGLLLASCLVTLQLTGLPVAMRSSSLEVT 174
Cdd:COG5001 128 LLAAASAALLAAALGAALLAALALALLLALARALLALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446406229 175 LSLPVIMLYPLLFAWVSY------QTAIKLAEHKR---RLQAMSSRDGMTGVYNRRHWEILLRNEFDHSRRHHREATLLI 245
Cdd:COG5001 208 LALRLLLGLLLLGLLLLLllvavlAIARLITERKRaeeRLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRLALLF 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446406229 246 IDIDHFKSINDTWGHDVGDEAIIALTRQLQLTLRGSDIIGRFGGDEFAVIMCGTPADSAITAM-SRVHERLNT-LRLPGA 323
Cdd:COG5001 288 IDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVLLPDLDDPEDAEAVaERILAALAEpFELDGH 367
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 446406229 324 pQVMLRISVGVApLTPQIGH-YREWLKSADMALYKAKNAGRNR 365
Cdd:COG5001 368 -ELYVSASIGIA-LYPDDGAdAEELLRNADLAMYRAKAAGRNR 408
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
208-365 |
1.02e-39 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 146.20 E-value: 1.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446406229 208 MSSRDGMTGVYNRRHWEILLRNEFDHSRRHHREATLLIIDIDHFKSINDTWGHDVGDEAIIALTRQLQLTLRGSDIIGRF 287
Cdd:PRK09581 291 MAVTDGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARY 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446406229 288 GGDEFAVIMCGTPADSAITAMSRVheRLNTLRLP-----GAPQVMLRISVGVAPLTPQIGHYREWLKSADMALYKAKNAG 362
Cdd:PRK09581 371 GGEEFVVVMPDTDIEDAIAVAERI--RRKIAEEPfiisdGKERLNVTVSIGVAELRPSGDTIEALIKRADKALYEAKNTG 448
|
...
gi 446406229 363 RNR 365
Cdd:PRK09581 449 RNR 451
|
|
| MASE2 |
pfam05230 |
MASE2 domain; Predicted integral membrane sensory domain found in histidine kinases, ... |
39-127 |
2.05e-31 |
|
MASE2 domain; Predicted integral membrane sensory domain found in histidine kinases, diguanylate cyclases and other bacterial signaling proteins.
Pssm-ID: 428382 Cd Length: 89 Bit Score: 114.23 E-value: 2.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446406229 39 RIRLPRAVGLGGMFLPVAAVLVSQPVFGGWWLLLVGWSFVWPHLAWQWAAKALDPLRQEIYNLKVDAILSGMWIALMGVN 118
Cdd:pfam05230 1 RIYLPRVLGYGLGALCIAAGLYEQHFSVWVWLLLVLNALLWPHLAYLLSRRSRDPYRTEQRLLLIDALLGGFWIALMGFS 80
|
....*....
gi 446406229 119 MLPAAALFM 127
Cdd:pfam05230 81 PLPSLVLLA 89
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
173-365 |
1.12e-29 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 119.73 E-value: 1.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446406229 173 VTLSLPVIMLYPLLFA--WVSYQTAIKLAEH----KRRLQAMSSRDGMTGVYNRRHWEILLRNEFDHSRRHHREATLLII 246
Cdd:PRK15426 356 GSISIALTLLWALFTAmlLISWYVIRRMVSNmfvlQSSLQWQAWHDPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQL 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446406229 247 DIDHFKSINDTWGHDVGDEAIIALTRQLQLTLRGSDIIGRFGGDEFAVIMCGTPADSAITAMSRVHERLNTLRLPGAPQV 326
Cdd:PRK15426 436 DLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRVGGEEFCVVLPGASLAEAAQVAERIRLRINEKEILVAKST 515
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446406229 327 MLRI--SVGVAPLTPQIGHYREWLKS-ADMALYKAKNAGRNR 365
Cdd:PRK15426 516 TIRIsaSLGVSSAEEDGDYDFEQLQSlADRRLYLAKQAGRNR 557
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
205-366 |
2.29e-25 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 103.99 E-value: 2.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446406229 205 LQAMSSRDGMTGVYNRRhweiLLRNEFDHSR--RHHREATLLIIDIDHFKSINDTWGHDVGDEAIIALTRQLQLTLRGSD 282
Cdd:PRK09894 125 LTIRSNMDVLTGLPGRR----VLDESFDHQLrnREPQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYE 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446406229 283 IIGRFGGDEFAVIMCGTPADSAITAMSRVHERLNTLRLPgAPQVMLRI--SVGVAPLTPQIgHYREWLKSADMALYKAKN 360
Cdd:PRK09894 201 TVYRYGGEEFIICLKAATDEEACRAGERIRQLIANHAIT-HSDGRINItaTFGVSRAFPEE-TLDVVIGRADRAMYEGKQ 278
|
....*.
gi 446406229 361 AGRNRT 366
Cdd:PRK09894 279 TGRNRV 284
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
203-368 |
8.17e-24 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 103.21 E-value: 8.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446406229 203 RRLQAMSSRDGMTGVYNRRHWEILLRNEFDHSRRHHREATLLIIDIDHFKSINDTWGHDVGDEAIIALTRQLQLTLRGSD 282
Cdd:PRK09776 659 RQLSYSASHDALTHLANRASFEKQLRRLLQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSD 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446406229 283 IIGRFGGDEFAVIMCGTPADSAITAMSRVHERLNTLRLPGAPQVMlRI--SVGVAPLTPQIGHYREWLKSADMALYKAKN 360
Cdd:PRK09776 739 VLARLGGDEFGLLLPDCNVESARFIATRIISAINDYHFPWEGRVY-RVgaSAGITLIDANNHQASEVMSQADIACYAAKN 817
|
....*...
gi 446406229 361 AGRNRTEV 368
Cdd:PRK09776 818 AGRGRVTV 825
|
|
| diguan_DgcJ |
NF040885 |
diguanylate cyclase DgcJ; |
171-363 |
1.05e-19 |
|
diguanylate cyclase DgcJ;
Pssm-ID: 468821 [Multi-domain] Cd Length: 490 Bit Score: 90.02 E-value: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446406229 171 LEVTLSLPVimLYPLLFAW---VSY--QTAI--KLAEHKRRLQAMSSR----DGMTGVYNRRHWEILLRNEFDHSRRHHR 239
Cdd:NF040885 294 LHVELSLDV--LYFILSSWklfLFYllSTALllHLVRMHFRLYHNVSRenisDSMTGLYNRKILTPTLEQRLQRLTEKGI 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446406229 240 EATLLIIDIDHFKSINDTWGHDVGDEAIIALTRQLQLTLRGSDIIGRFGGDEFAVIMCGTPADSAITAMSRVHERLNTLr 319
Cdd:NF040885 372 PVTFIALDCDKLKHINDTLGHHEGDRAITLLAQAISASIRKSDYGIRLGGDEFCIILIDYEEAEAQNLIERIRQHLRTI- 450
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446406229 320 lpgAPQVMLRISVGVAPLTP--QIGHYrewLKSADMALYKAKNAGR 363
Cdd:NF040885 451 ---DPDKRVSFSWGAYQMQPgdTLDDA---YKAADERLYLNKKQKH 490
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
204-363 |
1.48e-18 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 87.04 E-value: 1.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446406229 204 RLQAMSSRDGMTGVYNRRHWEILLRNEFDHSRRHhrEATLLIIDIDHFKSINDTWGHDVGDEAIIALTRQLQLTLRGSDI 283
Cdd:PRK10060 232 RLRILANTDSITGLPNRNAIQELIDHAINAADNN--QVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQT 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446406229 284 IGRFGGDEFAVIMCGTPADSAITAMSRVHERlntLRLP---GAPQVMLRISVGVApLTPQIGHYREWL-KSADMALYKAK 359
Cdd:PRK10060 310 LARLGGDEFLVLASHTSQAALEAMASRILTR---LRLPfriGLIEVYTGCSIGIA-LAPEHGDDSESLiRSADTAMYTAK 385
|
....
gi 446406229 360 NAGR 363
Cdd:PRK10060 386 EGGR 389
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
195-361 |
3.86e-13 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 70.57 E-value: 3.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446406229 195 AIKLAEHKRRLQAMSSRDGMTGVYNRRHweilLRNEFDHSRRHHREATLLIIDIDHFKSINDTWGHDVGDEAIIALTRQL 274
Cdd:PRK11359 362 ALEQEKSRQHIEQLIQFDPLTGLPNRNN----LHNYLDDLVDKAVSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRF 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446406229 275 QLTLRGSDIIGRFGGDEFAVIMcgtpADSAITAMSRVHERLNtlRLPGAPqvmLRISVGVAPLTPQIGHYREWLKSADMA 354
Cdd:PRK11359 438 REKLKPDQYLCRIEGTQFVLVS----LENDVSNITQIADELR--NVVSKP---IMIDDKPFPLTLSIGISYDVGKNRDYL 508
|
....*..
gi 446406229 355 LYKAKNA 361
Cdd:PRK11359 509 LSTAHNA 515
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
240-360 |
1.56e-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: 64.30 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446406229 240 EATLLIIDIDHFKSINDTWGHDVGDEAI-IALTRQLQLTLRGSDIIGRFGGDEFAVIMCGTPADSAITAMSRVHERLNTL 318
Cdd:cd07556 1 PVTILFADIVGFTSLADALGPDEGDELLnELAGRFDSLIRRSGDLKIKTIGDEFMVVSGLDHPAAAVAFAEDMREAVSAL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 446406229 319 RLPGAPQVMLRISV-------GVAPLTPQIGHYREWLKSADMALYKAKN 360
Cdd:cd07556 81 NQSEGNPVRVRIGIhtgpvvvGVIGSRPQYDVWGALVNLASRMESQAKA 129
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
197-360 |
1.79e-12 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 68.11 E-value: 1.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446406229 197 KLAEHKRRLQAMSSR-------DGMTGVYNRRHWEILLrNEFDHSRRHHREATLLIIDIDHFKSINDTWGHDVGDEAIIA 269
Cdd:PRK09966 229 EMEEWQLRLQAKNAQllrtalhDPLTGLANRAAFRSGI-NTLMNNSDARKTSALLFLDGDNFKYINDTWGHATGDRVLIE 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446406229 270 LTRQLQLTLRGSDIIGRFGGDEFAVIMCGTPADSAI----TAMSRVHERlnTLRLPGAPQVMLRISVGVApLTPQIGHYR 345
Cdd:PRK09966 308 IAKRLAEFGGLRHKAYRLGGDEFAMVLYDVQSESEVqqicSALTQIFNL--PFDLHNGHQTTMTLSIGYA-MTIEHASAE 384
|
170
....*....|....*
gi 446406229 346 EWLKSADMALYKAKN 360
Cdd:PRK09966 385 KLQELADHNMYQAKH 399
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
282-359 |
5.18e-10 |
|
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate cyclase (GGDEF) domain [Signal transduction mechanisms, Transcription];
Pssm-ID: 442920 [Multi-domain] Cd Length: 179 Bit Score: 58.00 E-value: 5.18e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446406229 282 DIIGRFGGDEFAVIMCGTPADSAITAMSRVHERLNTLrlpgaPQVMLRISVGVAPLTpqighyreWLKSADmALYKAK 359
Cdd:COG3706 116 DLVARYGGEEFAILLPGTDLEGALAVAERIREAVAEL-----PSLRVTVSIGVAGDS--------LLKRAD-ALYQAR 179
|
|
| |
