|
Name |
Accession |
Description |
Interval |
E-value |
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
121-399 |
9.48e-63 |
|
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: 203.29 E-value: 9.48e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698409 121 ILINVLENGQDNVLFHAAMMYAIVIIYGAVGMRFYTAIIAGWVGGLIGILVSTYLNGDIDWTFLNRTYTFSSFLGMTLAY 200
Cdd:COG2199 1 VLLLLLLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698409 201 ATDRQHRENYLQNCMIELNRIELMQQAQQLSLLSQQDALTGLANRRYLDETLDNEWRRALRHETPLTIMMVDIDFFKPYN 280
Cdd:COG2199 81 LELLLLLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698409 281 DSLGHLKGDQCLKDIATAISSiAARSGDLVARYGGEEFLLLFPMTNAQQAKIQAERLMNAIKKIAIVHPCSSVSpyVTIS 360
Cdd:COG2199 161 DTYGHAAGDEVLKEVARRLRA-SLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELEGKELR--VTVS 237
|
250 260 270
....*....|....*....|....*....|....*....
gi 446698409 361 VGVAtTIPRLNDSISAFVSRADHALYQAKTNGRNQYQIA 399
Cdd:COG2199 238 IGVA-LYPEDGDSAEELLRRADLALYRAKRAGRNRVVVY 275
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
235-397 |
2.85e-62 |
|
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: 197.78 E-value: 2.85e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698409 235 QQDALTGLANRRYLDETLDNEWRRALRHETPLTIMMVDIDFFKPYNDSLGHLKGDQCLKDIATAISSiAARSGDLVARYG 314
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRS-SLRESDLVARLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698409 315 GEEFLLLFPMTNAQQAKIQAERLMNAIKKIAIVHpcsSVSPYVTISVGVAtTIPRLNDSISAFVSRADHALYQAKTNGRN 394
Cdd:cd01949 80 GDEFAILLPGTDLEEAEALAERLREAIEEPFFID---GQEIRVTASIGIA-TYPEDGEDAEELLRRADEALYRAKRSGRN 155
|
...
gi 446698409 395 QYQ 397
Cdd:cd01949 156 RVV 158
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
234-395 |
2.73e-60 |
|
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: 192.85 E-value: 2.73e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698409 234 SQQDALTGLANRRYLDETLDNEWRRALRHETPLTIMMVDIDFFKPYNDSLGHLKGDQCLKDIATAISSiAARSGDLVARY 313
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSS-SLRRSDLVARL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698409 314 GGEEFLLLFPMTNAQQAKIQAERLMNAIKKIAIVHPCSSVSPYVTISVGVATTiPRLNDSISAFVSRADHALYQAKTNGR 393
Cdd:pfam00990 80 GGDEFAILLPETSLEGAQELAERIRRLLAKLKIPHTVSGLPLYVTISIGIAAY-PNDGEDPEDLLKRADTALYQAKQAGR 158
|
..
gi 446698409 394 NQ 395
Cdd:pfam00990 159 NR 160
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
232-399 |
2.07e-57 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 185.53 E-value: 2.07e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698409 232 LLSQQDALTGLANRRYLDETLDNEWRRALRHETPLTIMMVDIDFFKPYNDSLGHLKGDQCLKDIATAISSiAARSGDLVA 311
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSS-CLRPGDLLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698409 312 RYGGEEFLLLFPMTNAQQAKIQAERLMNAIKKIAIVHPcssVSPYVTISVGVATTiPRLNDSISAFVSRADHALYQAKTN 391
Cdd:smart00267 80 RLGGDEFALLLPETSLEEAIALAERILQQLREPIIIHG---IPLYLTISIGVAAY-PNPGEDAEDLLKRADTALYQAKKA 155
|
....*...
gi 446698409 392 GRNQYQIA 399
Cdd:smart00267 156 GRNQVAVY 163
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
233-399 |
1.65e-51 |
|
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: 170.21 E-value: 1.65e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698409 233 LSQQDALTGLANRRYLDETLDNEWRRALRHETPLTIMMVDIDFFKPYNDSLGHLKGDQCLKDIATAISSiAARSGDLVAR 312
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQS-SVRGSDVVGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698409 313 YGGEEFLLLFPMTNAQQAKIQAERLMNAIKKIAIVHPCSSVSpYVTISVGVATTIPRlNDSISAFVSRADHALYQAKTNG 392
Cdd:TIGR00254 80 YGGEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSETL-TVTVSIGVACYPGH-GLTLEELLKRADEALYQAKKAG 157
|
....*..
gi 446698409 393 RNQYQIA 399
Cdd:TIGR00254 158 RNRVVVA 164
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
233-395 |
6.48e-43 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 155.83 E-value: 6.48e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698409 233 LSQQDALTGLANRRYLDETLDNEWRRALRHETPLTIMMVDIDFFKPYNDSLGHLKGDQCLKDIATAISSiAARSGDLVAR 312
Cdd:PRK09581 291 MAVTDGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRN-NIRGTDLIAR 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698409 313 YGGEEFLLLFPMTNAQQAKIQAERLMNAIKKIAIVHPCSSVSPYVTISVGVATTIPRlNDSISAFVSRADHALYQAKTNG 392
Cdd:PRK09581 370 YGGEEFVVVMPDTDIEDAIAVAERIRRKIAEEPFIISDGKERLNVTVSIGVAELRPS-GDTIEALIKRADKALYEAKNTG 448
|
...
gi 446698409 393 RNQ 395
Cdd:PRK09581 449 RNR 451
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
121-399 |
9.48e-63 |
|
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: 203.29 E-value: 9.48e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698409 121 ILINVLENGQDNVLFHAAMMYAIVIIYGAVGMRFYTAIIAGWVGGLIGILVSTYLNGDIDWTFLNRTYTFSSFLGMTLAY 200
Cdd:COG2199 1 VLLLLLLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698409 201 ATDRQHRENYLQNCMIELNRIELMQQAQQLSLLSQQDALTGLANRRYLDETLDNEWRRALRHETPLTIMMVDIDFFKPYN 280
Cdd:COG2199 81 LELLLLLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698409 281 DSLGHLKGDQCLKDIATAISSiAARSGDLVARYGGEEFLLLFPMTNAQQAKIQAERLMNAIKKIAIVHPCSSVSpyVTIS 360
Cdd:COG2199 161 DTYGHAAGDEVLKEVARRLRA-SLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELEGKELR--VTVS 237
|
250 260 270
....*....|....*....|....*....|....*....
gi 446698409 361 VGVAtTIPRLNDSISAFVSRADHALYQAKTNGRNQYQIA 399
Cdd:COG2199 238 IGVA-LYPEDGDSAEELLRRADLALYRAKRAGRNRVVVY 275
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
235-397 |
2.85e-62 |
|
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: 197.78 E-value: 2.85e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698409 235 QQDALTGLANRRYLDETLDNEWRRALRHETPLTIMMVDIDFFKPYNDSLGHLKGDQCLKDIATAISSiAARSGDLVARYG 314
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRS-SLRESDLVARLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698409 315 GEEFLLLFPMTNAQQAKIQAERLMNAIKKIAIVHpcsSVSPYVTISVGVAtTIPRLNDSISAFVSRADHALYQAKTNGRN 394
Cdd:cd01949 80 GDEFAILLPGTDLEEAEALAERLREAIEEPFFID---GQEIRVTASIGIA-TYPEDGEDAEELLRRADEALYRAKRSGRN 155
|
...
gi 446698409 395 QYQ 397
Cdd:cd01949 156 RVV 158
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
234-395 |
2.73e-60 |
|
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: 192.85 E-value: 2.73e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698409 234 SQQDALTGLANRRYLDETLDNEWRRALRHETPLTIMMVDIDFFKPYNDSLGHLKGDQCLKDIATAISSiAARSGDLVARY 313
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSS-SLRRSDLVARL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698409 314 GGEEFLLLFPMTNAQQAKIQAERLMNAIKKIAIVHPCSSVSPYVTISVGVATTiPRLNDSISAFVSRADHALYQAKTNGR 393
Cdd:pfam00990 80 GGDEFAILLPETSLEGAQELAERIRRLLAKLKIPHTVSGLPLYVTISIGIAAY-PNDGEDPEDLLKRADTALYQAKQAGR 158
|
..
gi 446698409 394 NQ 395
Cdd:pfam00990 159 NR 160
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
232-399 |
2.07e-57 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 185.53 E-value: 2.07e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698409 232 LLSQQDALTGLANRRYLDETLDNEWRRALRHETPLTIMMVDIDFFKPYNDSLGHLKGDQCLKDIATAISSiAARSGDLVA 311
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSS-CLRPGDLLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698409 312 RYGGEEFLLLFPMTNAQQAKIQAERLMNAIKKIAIVHPcssVSPYVTISVGVATTiPRLNDSISAFVSRADHALYQAKTN 391
Cdd:smart00267 80 RLGGDEFALLLPETSLEEAIALAERILQQLREPIIIHG---IPLYLTISIGVAAY-PNPGEDAEDLLKRADTALYQAKKA 155
|
....*...
gi 446698409 392 GRNQYQIA 399
Cdd:smart00267 156 GRNQVAVY 163
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
233-399 |
1.65e-51 |
|
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: 170.21 E-value: 1.65e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698409 233 LSQQDALTGLANRRYLDETLDNEWRRALRHETPLTIMMVDIDFFKPYNDSLGHLKGDQCLKDIATAISSiAARSGDLVAR 312
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQS-SVRGSDVVGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698409 313 YGGEEFLLLFPMTNAQQAKIQAERLMNAIKKIAIVHPCSSVSpYVTISVGVATTIPRlNDSISAFVSRADHALYQAKTNG 392
Cdd:TIGR00254 80 YGGEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSETL-TVTVSIGVACYPGH-GLTLEELLKRADEALYQAKKAG 157
|
....*..
gi 446698409 393 RNQYQIA 399
Cdd:TIGR00254 158 RNRVVVA 164
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
114-398 |
9.50e-44 |
|
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: 161.87 E-value: 9.50e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698409 114 AAVAITFILINVLENGQDNVLFHAAMMYAIVIIYGAVGMRFYTAIIAGWVGGLIGILVSTYLNGDIDWTFLNRTYTFSSF 193
Cdd:COG5001 130 AAASAALLAAALGAALLAALALALLLALARALLALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLA 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698409 194 LGMTLAYATDRQHRENYLQNCMIELNRI-ELMQQAQQLSLLSQQDALTGLANRRYLDETLDNEWRRALRHETPLTIMMVD 272
Cdd:COG5001 210 LRLLLGLLLLGLLLLLLLVAVLAIARLItERKRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRLALLFID 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698409 273 IDFFKPYNDSLGHLKGDQCLKDIATAISSiAARSGDLVARYGGEEFLLLFP-MTNAQQAKIQAERLMNAIKK-IAIvhpc 350
Cdd:COG5001 290 LDRFKEINDTLGHAAGDELLREVARRLRA-CLREGDTVARLGGDEFAVLLPdLDDPEDAEAVAERILAALAEpFEL---- 364
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 446698409 351 SSVSPYVTISVGVATTiPRLNDSISAFVSRADHALYQAKTNGRNQYQI 398
Cdd:COG5001 365 DGHELYVSASIGIALY-PDDGADAEELLRNADLAMYRAKAAGRNRYRF 411
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
233-395 |
6.48e-43 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 155.83 E-value: 6.48e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698409 233 LSQQDALTGLANRRYLDETLDNEWRRALRHETPLTIMMVDIDFFKPYNDSLGHLKGDQCLKDIATAISSiAARSGDLVAR 312
Cdd:PRK09581 291 MAVTDGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRN-NIRGTDLIAR 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698409 313 YGGEEFLLLFPMTNAQQAKIQAERLMNAIKKIAIVHPCSSVSPYVTISVGVATTIPRlNDSISAFVSRADHALYQAKTNG 392
Cdd:PRK09581 370 YGGEEFVVVMPDTDIEDAIAVAERIRRKIAEEPFIISDGKERLNVTVSIGVAELRPS-GDTIEALIKRADKALYEAKNTG 448
|
...
gi 446698409 393 RNQ 395
Cdd:PRK09581 449 RNR 451
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
230-394 |
1.41e-35 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 132.50 E-value: 1.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698409 230 LSLLSQQDALTGLANRRYLDETLDNEwrRALRHETPLTIMMVDIDFFKPYNDSLGHLKGDQCLKDIATAISSiAARSGDL 309
Cdd:PRK09894 125 LTIRSNMDVLTGLPGRRVLDESFDHQ--LRNREPQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLAS-WTRDYET 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698409 310 VARYGGEEFLLLFPMTNAQQAKIQAERLMNAIKKIAIVHPCSSVSpyVTISVGVatTIPRLNDSISAFVSRADHALYQAK 389
Cdd:PRK09894 202 VYRYGGEEFIICLKAATDEEACRAGERIRQLIANHAITHSDGRIN--ITATFGV--SRAFPEETLDVVIGRADRAMYEGK 277
|
....*
gi 446698409 390 TNGRN 394
Cdd:PRK09894 278 QTGRN 282
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
227-395 |
8.51e-35 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 135.53 E-value: 8.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698409 227 AQQLSL--LSQQDALTGLANRRYLDETLDNEWRRALRHETPLTIMMVDIDFFKPYNDSLGHLKGDQCLKDIATAISSiAA 304
Cdd:PRK15426 389 VLQSSLqwQAWHDPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISS-SL 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698409 305 RSGDLVARYGGEEFLLLFPMTNAQQAKIQAERLMNAIK-KIAIVHPcsSVSPYVTISVGVATTIPRLNDSISAFVSRADH 383
Cdd:PRK15426 468 RAQDVAGRVGGEEFCVVLPGASLAEAAQVAERIRLRINeKEILVAK--STTIRISASLGVSSAEEDGDYDFEQLQSLADR 545
|
170
....*....|..
gi 446698409 384 ALYQAKTNGRNQ 395
Cdd:PRK15426 546 RLYLAKQAGRNR 557
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
221-399 |
9.12e-26 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 107.22 E-value: 9.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698409 221 IELMQQAQQLSLLSQQDALTGLANRRYLDETLDNEWRRALRHETPLTIMMVDIDFFKPYNDSLGHLKGDQCLKDIATAIs 300
Cdd:PRK10245 192 TKLAEHKRRLQVMSTRDGMTGVYNRRHWETLLRNEFDNCRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQL- 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698409 301 SIAARSGDLVARYGGEEFLLLFPMTNAQQAKIQAERLMNAIKKIAIvhPCssvSPYVT--ISVGVATTIPRLNdSISAFV 378
Cdd:PRK10245 271 QITLRGSDVIGRFGGDEFAVIMSGTPAESAITAMSRVHEGLNTLRL--PN---APQVTlrISVGVAPLNPQMS-HYREWL 344
|
170 180
....*....|....*....|.
gi 446698409 379 SRADHALYQAKTNGRNQYQIA 399
Cdd:PRK10245 345 KSADLALYKAKNAGRNRTEVA 365
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
227-398 |
1.95e-23 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 102.45 E-value: 1.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698409 227 AQQ-LSLLSQQDALTGLANRRYLDETLDNEWRRALRHETplTIMMVDIDFFKPYNDSLGHLKGDQCLKDIATAISSiAAR 305
Cdd:PRK10060 229 AQErLRILANTDSITGLPNRNAIQELIDHAINAADNNQV--GIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILS-CLE 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698409 306 SGDLVARYGGEEFLLLFPMTNAQQAKIQAERLMNAIKK-IAIvhpcSSVSPYVTISVGVATTiPRLNDSISAFVSRADHA 384
Cdd:PRK10060 306 EDQTLARLGGDEFLVLASHTSQAALEAMASRILTRLRLpFRI----GLIEVYTGCSIGIALA-PEHGDDSESLIRSADTA 380
|
170
....*....|....
gi 446698409 385 LYQAKTNGRNQYQI 398
Cdd:PRK10060 381 MYTAKEGGRGQFCV 394
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
224-396 |
1.56e-21 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 97.05 E-value: 1.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698409 224 MQQaqQLSLLSQQDALTGLANR----RYLDETLDNEWRRALRHetplTIMMVDIDFFKPYNDSLGHLKGDQCLKDIATAI 299
Cdd:PRK09776 657 MLR--QLSYSASHDALTHLANRasfeKQLRRLLQTVNSTHQRH----ALVFIDLDRFKAVNDSAGHAAGDALLRELASLM 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698409 300 SSIAaRSGDLVARYGGEEFLLLFPMTNAQQAKIQAERLMNAIKKIAI-----VHPcssvspyVTISVGVaTTIPRLNDSI 374
Cdd:PRK09776 731 LSML-RSSDVLARLGGDEFGLLLPDCNVESARFIATRIISAINDYHFpwegrVYR-------VGASAGI-TLIDANNHQA 801
|
170 180
....*....|....*....|..
gi 446698409 375 SAFVSRADHALYQAKTNGRNQY 396
Cdd:PRK09776 802 SEVMSQADIACYAAKNAGRGRV 823
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
265-391 |
2.08e-21 |
|
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: 89.34 E-value: 2.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698409 265 PLTIMMVDIDFFKPYNDSLGHLKGDQCLKDIATAISSIAARSGDLVARYGGEEFLLLFPMTNAQQAKIQAERLMNAIKKI 344
Cdd:cd07556 1 PVTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSGDLKIKTIGDEFMVVSGLDHPAAAVAFAEDMREAVSAL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 446698409 345 AIvhpcSSVSPyVTISVGVATTIP--------RLNDSISAFVSRADHALYQAKTN 391
Cdd:cd07556 81 NQ----SEGNP-VRVRIGIHTGPVvvgvigsrPQYDVWGALVNLASRMESQAKAG 130
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
221-402 |
1.89e-14 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 75.19 E-value: 1.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698409 221 IELMQQAQQLSLLSQQDALTGLANR----RYLDETLDNEwrralrheTPLTIMMVDIDFFKPYNDSLGHLKGDQCLKDIA 296
Cdd:PRK11359 363 LEQEKSRQHIEQLIQFDPLTGLPNRnnlhNYLDDLVDKA--------VSPVVYLIGVDHFQDVIDSLGYAWADQALLEVV 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698409 297 TAISSiAARSGDLVARYGGEEFLLLFPMTNAQQAKIQAERLMNAIKKiAIVHPCSSVSPyvTISVGVATTIPRLNDSIsa 376
Cdd:PRK11359 435 NRFRE-KLKPDQYLCRIEGTQFVLVSLENDVSNITQIADELRNVVSK-PIMIDDKPFPL--TLSIGISYDVGKNRDYL-- 508
|
170 180
....*....|....*....|....*....
gi 446698409 377 fVSRADHALYQAKTNGRNQYQI---ALNE 402
Cdd:PRK11359 509 -LSTAHNAMDYIRKNGGNGWQFfspAMNE 536
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
308-389 |
6.39e-14 |
|
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: 69.55 E-value: 6.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698409 308 DLVARYGGEEFLLLFPMTNAQQAKIQAERLMNAIKKIAivhpcssvSPYVTISVGVATTiprlndsisAFVSRADhALYQ 387
Cdd:COG3706 116 DLVARYGGEEFAILLPGTDLEGALAVAERIREAVAELP--------SLRVTVSIGVAGD---------SLLKRAD-ALYQ 177
|
..
gi 446698409 388 AK 389
Cdd:COG3706 178 AR 179
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
217-389 |
1.23e-08 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 56.55 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698409 217 ELNRIELMQQAQQLSLL--SQQDALTGLANRRYLDETLdNEWRRALRHETPLTIMMVDIDFFKPYNDSLGHLKGDQCLKD 294
Cdd:PRK09966 229 EMEEWQLRLQAKNAQLLrtALHDPLTGLANRAAFRSGI-NTLMNNSDARKTSALLFLDGDNFKYINDTWGHATGDRVLIE 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698409 295 IATAISSIAArSGDLVARYGGEEF-LLLFPMTNAQQAKIQAERLMNAIKKIAIVHPCSSVSpyVTISVGVATTIPrlNDS 373
Cdd:PRK09966 308 IAKRLAEFGG-LRHKAYRLGGDEFaMVLYDVQSESEVQQICSALTQIFNLPFDLHNGHQTT--MTLSIGYAMTIE--HAS 382
|
170
....*....|....*.
gi 446698409 374 ISAFVSRADHALYQAK 389
Cdd:PRK09966 383 AEKLQELADHNMYQAK 398
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
236-344 |
4.05e-05 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 45.62 E-value: 4.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446698409 236 QDALTGLANRRYLDETLDnewrrALRHE-----TPLTIMMVDIDFFKPYNDSLGHLKGDQCLKDIATAISSIAAR-SGDL 309
Cdd:PRK11059 230 QDAKTGLGNRLFFDNQLA-----TLLEDqemvgAHGVVMLIRLPDFDLLQEEWGESQVEELLFELINLLSTFVMRyPGAL 304
|
90 100 110
....*....|....*....|....*....|....*
gi 446698409 310 VARYGGEEFLLLFPMTNAQQAKIQAERLMNAIKKI 344
Cdd:PRK11059 305 LARYSRSDFAVLLPHRSLKEADSLASQLLKAVDAL 339
|
|
| |
