|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
1-407 |
0e+00 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 609.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462231119 1 MNKDFSQTPRPTFKRALRRISVISVVISMTLVWLLLSTASIFTLKQYAQKNLELTAATMGRSLEAALVFGDSAAAEETLA 80
Cdd:PRK09966 1 MDNDNSLNKRPTFKRALRNISMTSIFITMMLIWLLLSVTSVLTLKQYAQKNLALTAATMTYSLEAAVVFADGPAATETLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462231119 81 SLGKQGQISQAIVLNGQMQHFAAWRHEPLANKEQVSGLISKWLFPEPTVQPIWHQGKQIGELRLTALDELISHFLGISIL 160
Cdd:PRK09966 81 ALGQQGQFSTAEVRDKQQNILASWHYTRKDPGDTFSNFISHWLFPAPIIQPIRHNGETIGEVRLTARDSSISHFIWFSLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462231119 161 VLTGSILLASFIALLLTHSLHRGIVAALQSITEVVHDIRENRHFSRRVPEERIEEFHLFAQDFNSLLGEMEDWQRQLQAK 240
Cdd:PRK09966 161 VLTGCILLASGIAITLTRHLHNGLVEALKNITDVVHDVRSNRNFSRRVSEERIAEFHRFALDFNSLLDEMEEWQLRLQAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462231119 241 NAQLLRSSLHDPLTGLANRAAFRNALAELMQNEVDHQTSALLFLDGDNFKLINDNWGHAAGDKVLMEVASRLMTFAGKRH 320
Cdd:PRK09966 241 NAQLLRTALHDPLTGLANRAAFRSGINTLMNNSDARKTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462231119 321 LAWRLGGDEFAVLLREVRSEAEVQALCQALTEQFLPPFNLHNGHSATLSLSVGYALAWEHATAESLQELADQNMYRMKNQ 400
Cdd:PRK09966 321 KAYRLGGDEFAMVLYDVQSESEVQQICSALTQIFNLPFDLHNGHQTTMTLSIGYAMTIEHASAEKLQELADHNMYQAKHQ 400
|
....*..
gi 1462231119 401 RIQQTLK 407
Cdd:PRK09966 401 RAEKLVR 407
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
248-400 |
1.08e-47 |
|
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: 160.11 E-value: 1.08e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462231119 248 SLHDPLTGLANRAAFRNALAELMQNEVDHQTS-ALLFLDGDNFKLINDNWGHAAGDKVLMEVASRLMTFAGKRHLAWRLG 326
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPvAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1462231119 327 GDEFAVLLREVRSE--AEVQALCQALTEQFLPPFNlHNGHSATLSLSVGYALAWEHA-TAESLQELADQNMYRMKNQ 400
Cdd:pfam00990 81 GDEFAILLPETSLEgaQELAERIRRLLAKLKIPHT-VSGLPLYVTISIGIAAYPNDGeDPEDLLKRADTALYQAKQA 156
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
142-400 |
8.30e-46 |
|
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: 158.99 E-value: 8.30e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462231119 142 LRLTALDELISHFLGISILVLTGSILLASFIALLLTHSLHRGIVAALQSITEVVHDIRENRHFSRRVPEERIEEFHLFAQ 221
Cdd:COG2199 9 LALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462231119 222 DFNSLLGEMEDwQRQLQAKNAQLLRSSLHDPLTGLANRAAFRNALAELMQNEVDHQTS-ALLFLDGDNFKLINDNWGHAA 300
Cdd:COG2199 89 ALLLLLLALED-ITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPlALLLIDLDHFKRINDTYGHAA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462231119 301 GDKVLMEVASRLMTFAGKRHLAWRLGGDEFAVLLREVrSEAEVQALCQALTEQFL-PPFNlHNGHSATLSLSVGYALAWE 379
Cdd:COG2199 168 GDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGT-DLEEAEALAERLREALEqLPFE-LEGKELRVTVSIGVALYPE 245
|
250 260
....*....|....*....|..
gi 1462231119 380 HA-TAESLQELADQNMYRMKNQ 400
Cdd:COG2199 246 DGdSAEELLRRADLALYRAKRA 267
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
249-401 |
2.68e-45 |
|
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: 153.87 E-value: 2.68e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462231119 249 LHDPLTGLANRAAFRNALAELMQNEVDHQTS-ALLFLDGDNFKLINDNWGHAAGDKVLMEVASRLMTFAGKRHLAWRLGG 327
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLARARRSGRPlALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1462231119 328 DEFAVLLREVrSEAEVQALCQALTEQFLPPFNLHnGHSATLSLSVGYALAWEHA-TAESLQELADQNMYRMKNQR 401
Cdd:cd01949 81 DEFAILLPGT-DLEEAEALAERLREAIEEPFFID-GQEIRVTASIGIATYPEDGeDAEELLRRADEALYRAKRSG 153
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
246-400 |
1.39e-43 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 149.32 E-value: 1.39e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462231119 246 RSSLHDPLTGLANRAAFRNALAELMQNEVDHQTS-ALLFLDGDNFKLINDNWGHAAGDKVLMEVASRLMTFAGKRHLAWR 324
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPfALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1462231119 325 LGGDEFAVLLREVrSEAEVQALCQALTEQFLPPFNLHnGHSATLSLSVGYALAWEHA-TAESLQELADQNMYRMKNQ 400
Cdd:smart00267 81 LGGDEFALLLPET-SLEEAIALAERILQQLREPIIIH-GIPLYLTISIGVAAYPNPGeDAEDLLKRADTALYQAKKA 155
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
248-398 |
1.67e-28 |
|
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: 109.73 E-value: 1.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462231119 248 SLHDPLTGLANRAAFRNALAELMQNEVDHQTS-ALLFLDGDNFKLINDNWGHAAGDKVLMEVASRLMTFAGKRHLAWRLG 326
Cdd:TIGR00254 2 AVRDPLTGLYNRRYLEEMLDSELKRARRFQRSfSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYG 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1462231119 327 GDEFAVLLREVRSEAEV---QALCQALTEQflpPFNLHNGHSATLSLSVGYALAWEHA-TAESLQELADQNMYRMK 398
Cdd:TIGR00254 82 GEEFVVILPGTPLEDALskaERLRDAINSK---PIEVAGSETLTVTVSIGVACYPGHGlTLEELLKRADEALYQAK 154
|
|
| diguan_DgcJ |
NF040885 |
diguanylate cyclase DgcJ; |
240-401 |
1.65e-09 |
|
diguanylate cyclase DgcJ;
Pssm-ID: 468821 [Multi-domain] Cd Length: 490 Bit Score: 59.59 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462231119 240 KNAQLLRSSLHDPLTGLANRAAFRNALAELMQNEVDhQTSALLF--LDGDNFKLINDNWGHAAGDKVLMEVASRLMTFAG 317
Cdd:NF040885 333 LYHNVSRENISDSMTGLYNRKILTPTLEQRLQRLTE-KGIPVTFiaLDCDKLKHINDTLGHHEGDRAITLLAQAISASIR 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462231119 318 KRHLAWRLGGDEFAVLLREVrSEAEVQALCQALTEqflppfNLHN-GHSATLSLSVG-YALAWEHaTAESLQELADQNMY 395
Cdd:NF040885 412 KSDYGIRLGGDEFCIILIDY-EEAEAQNLIERIRQ------HLRTiDPDKRVSFSWGaYQMQPGD-TLDDAYKAADERLY 483
|
....*.
gi 1462231119 396 RMKNQR 401
Cdd:NF040885 484 LNKKQK 489
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
1-407 |
0e+00 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 609.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462231119 1 MNKDFSQTPRPTFKRALRRISVISVVISMTLVWLLLSTASIFTLKQYAQKNLELTAATMGRSLEAALVFGDSAAAEETLA 80
Cdd:PRK09966 1 MDNDNSLNKRPTFKRALRNISMTSIFITMMLIWLLLSVTSVLTLKQYAQKNLALTAATMTYSLEAAVVFADGPAATETLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462231119 81 SLGKQGQISQAIVLNGQMQHFAAWRHEPLANKEQVSGLISKWLFPEPTVQPIWHQGKQIGELRLTALDELISHFLGISIL 160
Cdd:PRK09966 81 ALGQQGQFSTAEVRDKQQNILASWHYTRKDPGDTFSNFISHWLFPAPIIQPIRHNGETIGEVRLTARDSSISHFIWFSLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462231119 161 VLTGSILLASFIALLLTHSLHRGIVAALQSITEVVHDIRENRHFSRRVPEERIEEFHLFAQDFNSLLGEMEDWQRQLQAK 240
Cdd:PRK09966 161 VLTGCILLASGIAITLTRHLHNGLVEALKNITDVVHDVRSNRNFSRRVSEERIAEFHRFALDFNSLLDEMEEWQLRLQAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462231119 241 NAQLLRSSLHDPLTGLANRAAFRNALAELMQNEVDHQTSALLFLDGDNFKLINDNWGHAAGDKVLMEVASRLMTFAGKRH 320
Cdd:PRK09966 241 NAQLLRTALHDPLTGLANRAAFRSGINTLMNNSDARKTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462231119 321 LAWRLGGDEFAVLLREVRSEAEVQALCQALTEQFLPPFNLHNGHSATLSLSVGYALAWEHATAESLQELADQNMYRMKNQ 400
Cdd:PRK09966 321 KAYRLGGDEFAMVLYDVQSESEVQQICSALTQIFNLPFDLHNGHQTTMTLSIGYAMTIEHASAEKLQELADHNMYQAKHQ 400
|
....*..
gi 1462231119 401 RIQQTLK 407
Cdd:PRK09966 401 RAEKLVR 407
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
248-400 |
1.08e-47 |
|
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: 160.11 E-value: 1.08e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462231119 248 SLHDPLTGLANRAAFRNALAELMQNEVDHQTS-ALLFLDGDNFKLINDNWGHAAGDKVLMEVASRLMTFAGKRHLAWRLG 326
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPvAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1462231119 327 GDEFAVLLREVRSE--AEVQALCQALTEQFLPPFNlHNGHSATLSLSVGYALAWEHA-TAESLQELADQNMYRMKNQ 400
Cdd:pfam00990 81 GDEFAILLPETSLEgaQELAERIRRLLAKLKIPHT-VSGLPLYVTISIGIAAYPNDGeDPEDLLKRADTALYQAKQA 156
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
142-400 |
8.30e-46 |
|
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: 158.99 E-value: 8.30e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462231119 142 LRLTALDELISHFLGISILVLTGSILLASFIALLLTHSLHRGIVAALQSITEVVHDIRENRHFSRRVPEERIEEFHLFAQ 221
Cdd:COG2199 9 LALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462231119 222 DFNSLLGEMEDwQRQLQAKNAQLLRSSLHDPLTGLANRAAFRNALAELMQNEVDHQTS-ALLFLDGDNFKLINDNWGHAA 300
Cdd:COG2199 89 ALLLLLLALED-ITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPlALLLIDLDHFKRINDTYGHAA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462231119 301 GDKVLMEVASRLMTFAGKRHLAWRLGGDEFAVLLREVrSEAEVQALCQALTEQFL-PPFNlHNGHSATLSLSVGYALAWE 379
Cdd:COG2199 168 GDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGT-DLEEAEALAERLREALEqLPFE-LEGKELRVTVSIGVALYPE 245
|
250 260
....*....|....*....|..
gi 1462231119 380 HA-TAESLQELADQNMYRMKNQ 400
Cdd:COG2199 246 DGdSAEELLRRADLALYRAKRA 267
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
249-401 |
2.68e-45 |
|
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: 153.87 E-value: 2.68e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462231119 249 LHDPLTGLANRAAFRNALAELMQNEVDHQTS-ALLFLDGDNFKLINDNWGHAAGDKVLMEVASRLMTFAGKRHLAWRLGG 327
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLARARRSGRPlALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1462231119 328 DEFAVLLREVrSEAEVQALCQALTEQFLPPFNLHnGHSATLSLSVGYALAWEHA-TAESLQELADQNMYRMKNQR 401
Cdd:cd01949 81 DEFAILLPGT-DLEEAEALAERLREAIEEPFFID-GQEIRVTASIGIATYPEDGeDAEELLRRADEALYRAKRSG 153
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
15-400 |
6.16e-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: 162.25 E-value: 6.16e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462231119 15 RALRRISVISVVISMTLVWLLLSTASIFTLKQYAQKNLELTAATMGRSLEAALVFGDSAAAEETLASLGKQGQISQAIVL 94
Cdd:COG5001 18 LLLLALLLLALLLAALLALALLLLLLLLLLALLLAALLLLALLALLALLLLAAALLALALAALLLAALLAALLLLLLLLL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462231119 95 NGQMQHFAAWRHEPLANKEQVSGLISKWLFPEPTVQPIWHQGKQIGELRLTALDELISHFLGISILVLTGSILLASFIAL 174
Cdd:COG5001 98 ALLVLLLLLLLLLALLALLAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARALLALLLLLLLALLLLLL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462231119 175 LLTHSLHRGIVAALQSITEVVHDIRENRHFSRRVPEERIEEFHLFAQDFNSLLGEMEDWQRQLQAKNAQLLRSSLHDPLT 254
Cdd:COG5001 178 LLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEERLRHLAYHDPLT 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462231119 255 GLANRAAFRNALAELMQNEVDHQTS-ALLFLDGDNFKLINDNWGHAAGDKVLMEVASRLMTFAGKRHLAWRLGGDEFAVL 333
Cdd:COG5001 258 GLPNRRLFLDRLEQALARARRSGRRlALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVL 337
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1462231119 334 LREVRSEAEVQALCQALTEQFLPPFNLhNGHSATLSLSVGYALAWEHA-TAESLQELADQNMYRMKNQ 400
Cdd:COG5001 338 LPDLDDPEDAEAVAERILAALAEPFEL-DGHELYVSASIGIALYPDDGaDAEELLRNADLAMYRAKAA 404
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
246-400 |
1.39e-43 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 149.32 E-value: 1.39e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462231119 246 RSSLHDPLTGLANRAAFRNALAELMQNEVDHQTS-ALLFLDGDNFKLINDNWGHAAGDKVLMEVASRLMTFAGKRHLAWR 324
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPfALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1462231119 325 LGGDEFAVLLREVrSEAEVQALCQALTEQFLPPFNLHnGHSATLSLSVGYALAWEHA-TAESLQELADQNMYRMKNQ 400
Cdd:smart00267 81 LGGDEFALLLPET-SLEEAIALAERILQQLREPIIIH-GIPLYLTISIGVAAYPNPGeDAEDLLKRADTALYQAKKA 155
|
|
| CHASE8 |
pfam17152 |
Periplasmic sensor domain; CHASE8 is a conserved periplasmic sensor domain found in histidine ... |
44-145 |
8.50e-38 |
|
Periplasmic sensor domain; CHASE8 is a conserved periplasmic sensor domain found in histidine kinases, diguanylate cyclases/phosphodiesterases and methyl-accepting chemotaxis proteins, including the diguanylate cyclase DgcN (YfiN) that regulates biofilm formation and motility in Escherichia coli. In Pseudomonas aeruginosa, CHASE8 is the sensor domain in the diguanylate cyclase TpbB that regulates biofilm formation by controlling the levels of extracellular DNA.
Pssm-ID: 435752 Cd Length: 102 Bit Score: 131.99 E-value: 8.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462231119 44 LKQYAQKNLELTAATMGRSLEAALVFGDSAAAEETLASLGKQGQISQAIVLNGQMQHFAAWRHEPLANKEQVSGLISKWL 123
Cdd:pfam17152 1 LRRYAQQNLELLARSIAYNVEAALVFGDPAAARETLAALGAQPQIASAAVYDAQGRLFASYARPGTDPPEPLEALLARWL 80
|
90 100
....*....|....*....|..
gi 1462231119 124 FPEPTVQPIWHQGKQIGELRLT 145
Cdd:pfam17152 81 LPAPVLQPIVHDGERIGSVVLA 102
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
248-398 |
1.67e-28 |
|
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: 109.73 E-value: 1.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462231119 248 SLHDPLTGLANRAAFRNALAELMQNEVDHQTS-ALLFLDGDNFKLINDNWGHAAGDKVLMEVASRLMTFAGKRHLAWRLG 326
Cdd:TIGR00254 2 AVRDPLTGLYNRRYLEEMLDSELKRARRFQRSfSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYG 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1462231119 327 GDEFAVLLREVRSEAEV---QALCQALTEQflpPFNLHNGHSATLSLSVGYALAWEHA-TAESLQELADQNMYRMK 398
Cdd:TIGR00254 82 GEEFVVILPGTPLEDALskaERLRDAINSK---PIEVAGSETLTVTVSIGVACYPGHGlTLEELLKRADEALYQAK 154
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
250-400 |
7.35e-23 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 100.47 E-value: 7.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462231119 250 HDPLTGLANRAAFRN---ALAELMQNevDHQTSALLFLDGDNFKLINDNWGHAAGDKVLMEVASRLMTFAGKRHLAWRLG 326
Cdd:PRK15426 400 HDPLTRLYNRGALFEkarALAKRCQR--DQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRVG 477
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1462231119 327 GDEFAVLLREVRSEAEVQA---LCQALTEQFLppfNLHNGHSATLSLSVGYALAWEHA--TAESLQELADQNMYRMKNQ 400
Cdd:PRK15426 478 GEEFCVVLPGASLAEAAQVaerIRLRINEKEI---LVAKSTTIRISASLGVSSAEEDGdyDFEQLQSLADRRLYLAKQA 553
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
243-353 |
3.75e-21 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 95.89 E-value: 3.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462231119 243 QLLRSSLHDPLTGLANRAAFRNALAELMQNEVDH-QTSALLFLDGDNFKLINDNWGHAAGDKVLMEVASRLMTFAGKRHL 321
Cdd:PRK09776 660 QLSYSASHDALTHLANRASFEKQLRRLLQTVNSThQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSDV 739
|
90 100 110
....*....|....*....|....*....|..
gi 1462231119 322 AWRLGGDEFAVLLREVrSEAEVQALCQALTEQ 353
Cdd:PRK09776 740 LARLGGDEFGLLLPDC-NVESARFIATRIISA 770
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
197-399 |
8.71e-21 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 91.67 E-value: 8.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462231119 197 DIRENRHFSRRVPEERIEEFHLFAQDFNSLLGEMEDWQRQLQAKNAQLL--RSSLhDPLTGLANRaafRNALAELMQNEV 274
Cdd:PRK09894 77 SAHQHMHNCARELLLAIVEGHWQDAHFDAFQEGLLSFTAALTDYKIYLLtiRSNM-DVLTGLPGR---RVLDESFDHQLR 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462231119 275 DH--QTSALLFLDGDNFKLINDNWGHAAGDKVLMEVASRLMTFAGKRHLAWRLGGDEFAVLLREVRSEAEVQA---LCQA 349
Cdd:PRK09894 153 NRepQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGGEEFIICLKAATDEEACRAgerIRQL 232
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1462231119 350 LTEQflpPFNLHNGHsATLSLSVGYALAWEHATAESLQELADQNMYRMKN 399
Cdd:PRK09894 233 IANH---AITHSDGR-INITATFGVSRAFPEETLDVVIGRADRAMYEGKQ 278
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
251-398 |
5.18e-20 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 92.05 E-value: 5.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462231119 251 DPLTGLANRAAFRNALAELMQNEVDHQTsALLFLDGDNFKLINDNWGHAAGDKVLMEVASRLMTFAGKRHLAWRLGGDEF 330
Cdd:PRK10060 240 DSITGLPNRNAIQELIDHAINAADNNQV-GIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQTLARLGGDEF 318
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1462231119 331 AVLLrEVRSEAEVQALCQALTEQFLPPFNLHNGHSATlSLSVGYALAWEHA-TAESLQELADQNMYRMK 398
Cdd:PRK10060 319 LVLA-SHTSQAALEAMASRILTRLRLPFRIGLIEVYT-GCSIGIALAPEHGdDSESLIRSADTAMYTAK 385
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
236-399 |
5.45e-20 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 91.50 E-value: 5.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462231119 236 QLQAKNAQ-LLRSSLH--------DPLTGLANRAAFRNALAELMQNEVDH-QTSALLFLDGDNFKLINDNWGHAAGDKVL 305
Cdd:PRK09581 271 QIRRKRYQdALRNNLEqsiemavtDGLTGLHNRRYFDMHLKNLIERANERgKPLSLMMIDIDHFKKVNDTYGHDAGDEVL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462231119 306 MEVASRLMTFAGKRHLAWRLGGDEFAVLLREV-RSEAEVQA--LCQALTEQflpPFNLHNG---HSATLSLSVGyALAWE 379
Cdd:PRK09581 351 REFAKRLRNNIRGTDLIARYGGEEFVVVMPDTdIEDAIAVAerIRRKIAEE---PFIISDGkerLNVTVSIGVA-ELRPS 426
|
170 180
....*....|....*....|
gi 1462231119 380 HATAESLQELADQNMYRMKN 399
Cdd:PRK09581 427 GDTIEALIKRADKALYEAKN 446
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
225-373 |
2.36e-14 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 74.81 E-value: 2.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462231119 225 SLLGEMEDWQRQLQaknaQLLRsslHDPLTGLANRAAFRNALAELMQNEvdhQTSALLFLDGDNFKLINDNWGHAAGDKV 304
Cdd:PRK11359 360 ALALEQEKSRQHIE----QLIQ---FDPLTGLPNRNNLHNYLDDLVDKA---VSPVVYLIGVDHFQDVIDSLGYAWADQA 429
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1462231119 305 LMEVASRLMTFAGKRHLAWRLGGDEFAVllreVRSEAEVQALCQaLTEQFL----PPFNLhNGHSATLSLSVG 373
Cdd:PRK11359 430 LLEVVNRFREKLKPDQYLCRIEGTQFVL----VSLENDVSNITQ-IADELRnvvsKPIMI-DDKPFPLTLSIG 496
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
248-399 |
2.14e-12 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 67.93 E-value: 2.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462231119 248 SLHDPLTGLANRAAFRnalaELMQNEVD-----HQTSALLFLDGDNFKLINDNWGHAAGDKVLMEVASRL-MTFAGKRHL 321
Cdd:PRK10245 205 STRDGMTGVYNRRHWE----TLLRNEFDncrrhHRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLqITLRGSDVI 280
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1462231119 322 AwRLGGDEFAVLLREVRSEAEVQALCQalTEQFLPPFNLHNGHSATLSLSVGYA-LAWEHATAESLQELADQNMYRMKN 399
Cdd:PRK10245 281 G-RFGGDEFAVIMSGTPAESAITAMSR--VHEGLNTLRLPNAPQVTLRISVGVApLNPQMSHYREWLKSADLALYKAKN 356
|
|
| diguan_DgcJ |
NF040885 |
diguanylate cyclase DgcJ; |
240-401 |
1.65e-09 |
|
diguanylate cyclase DgcJ;
Pssm-ID: 468821 [Multi-domain] Cd Length: 490 Bit Score: 59.59 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462231119 240 KNAQLLRSSLHDPLTGLANRAAFRNALAELMQNEVDhQTSALLF--LDGDNFKLINDNWGHAAGDKVLMEVASRLMTFAG 317
Cdd:NF040885 333 LYHNVSRENISDSMTGLYNRKILTPTLEQRLQRLTE-KGIPVTFiaLDCDKLKHINDTLGHHEGDRAITLLAQAISASIR 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462231119 318 KRHLAWRLGGDEFAVLLREVrSEAEVQALCQALTEqflppfNLHN-GHSATLSLSVG-YALAWEHaTAESLQELADQNMY 395
Cdd:NF040885 412 KSDYGIRLGGDEFCIILIDY-EEAEAQNLIERIRQ------HLRTiDPDKRVSFSWGaYQMQPGD-TLDDAYKAADERLY 483
|
....*.
gi 1462231119 396 RMKNQR 401
Cdd:NF040885 484 LNKKQK 489
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
36-392 |
7.42e-07 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 51.48 E-value: 7.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462231119 36 LSTASIFTLKQ-----------YAQKnLELTAATMGRSLEAALVFGDSAAAEETLASLGKQGQISQA-IVLNGQMQ---- 99
Cdd:PRK11829 9 LVTICIFIILQlfhfvqqrkddYANQ-LESIAYSVRQPLSEAILSVDIPQAKKILNSLLPIGILSRAeVILPNQIQvlha 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462231119 100 HFAAWRHEPLANKE------QVSGLISKWLFPEPTVQPIWHQGKQIGELR-----LTALDELISHFLgisILVLTGSILL 168
Cdd:PRK11829 88 NFPTERPIPHWAKRvfslpvQITVPLYALERVPANPQPLAHLVLRADSFRmyqfiLSALSAMLSTYL---LLALVLSVSI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462231119 169 ASFIALLLTHSLhRGIVAALQSI-TEVVHdirenRHFSRRVPEERIEEFHLFAQDFNSLlgemedwQRQLQAKNAQLLRS 247
Cdd:PRK11829 165 AWCINRLIIHPL-RAMAKELEDIgDHGVL-----HHQLTLPAHHQDDELGVLVRNYNRN-------QQLLADAYADMGRI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462231119 248 SLHDPLTGLANRAAFRNALAELMQNEVDHQTSALLFLDGDNFKLINDNWGHAAGDKVLMEVASRLMTFAGKRHLAWRLGG 327
Cdd:PRK11829 232 SHRFPVTELPNRSLFISLLEKEIASSTRTDHFHLLVIGIETLQEVSGAMSEAQHQQLLLTIVQRIEQCIDDSDLLAQLSK 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1462231119 328 DEFAVLLREVRSEAEVQALCQALTEQFLPPFNLHNghsATLSLSVGYALAWEHATAESLQELADQ 392
Cdd:PRK11829 312 TEFAVLARGTRRSFPAMQLARRIMSQVTQPLFFDE---ITLRPSASIGITRYQAQQDTAESMMRN 373
|
|
| NtrY |
COG5000 |
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ... |
159-244 |
1.63e-06 |
|
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism regulation [Signal transduction mechanisms];
Pssm-ID: 444024 [Multi-domain] Cd Length: 422 Bit Score: 49.96 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462231119 159 ILVLTGSILLASFIALLLTHSLHRGIVAALQSITEVVHDIRENrHFSRRVPEERIEEFHLFAQDFNSLLGEMEDWQRQLQ 238
Cdd:COG5000 8 LLLLLLIALLLLLLALWLALLLARRLTRPLRRLAEATRAVAAG-DLSVRLPVTGDDEIGELARAFNRMTDQLKEQREELE 86
|
....*.
gi 1462231119 239 AKNAQL 244
Cdd:COG5000 87 ERRRYL 92
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
23-406 |
6.27e-06 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 48.17 E-value: 6.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462231119 23 ISVVISMTLVWLLL-STASIFTLKQ-----YAQKnLELTAATMGRSLEAALVFGDSAAAEETLASLGKQGQISQA-IVLN 95
Cdd:PRK13561 1 MAMVAAVVLVFVFIfCTVLLFHLVQqnrynTATQ-LESIARSVREPLSSAILKADIPEAEAILASIKPAGVVSRAdVVLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462231119 96 GQMQHFaawrHEPLANKEQVSGLISKwLFPEPtVQ---PIWH-----QGKQIGELRLTALDELISHFL--GISILVlTGS 165
Cdd:PRK13561 80 NQFQAL----RKSFIPERPVPVMVTR-LFELP-VQislPVYSlerpaNPQPLAYLVLQADSFRMYKFVmsALSTLV-TIY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462231119 166 ILLASFIALLLTHSLHRGIVAALQSITEVVHDI--RENRHFSRRVPE-ERIEEFHLFAQDFNSLlgemedwQRQLQAKNA 242
Cdd:PRK13561 153 LLLSLILTVAISWCINRLIVHPLRNIARELNDIppQELVGHQLALPRlHQDDEIGMLVRSYNLN-------QQLLQRQYE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462231119 243 QLLRSSLHDPLTGLANRAAFrnaLAELMQNEVDHQTSALLFLDGDNFKLINDNWGHAAGDKVLMEVASRLMTFAGKRHLA 322
Cdd:PRK13561 226 EQSRNATRFPVSDLPNKALL---MALLEQVVARKQTTALMIITCETLRDTAGVLKEAQREILLLTLVEKLKSVLSPRMVL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462231119 323 WRLGGDEFAVLLREVRSEAEVQALCQALTEQFLPPFNLHnGHSATLSLSVGYALAWEHATAESLQELADQNMYRMKNQRI 402
Cdd:PRK13561 303 AQISGYDFAIIANGVKEPWHAITLGQQVLTIINERLPIQ-RIQLRPSCSIGIAMFYGDLTAEQLYSRAISAAFTARRKGK 381
|
....
gi 1462231119 403 QQTL 406
Cdd:PRK13561 382 NQIQ 385
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
33-334 |
2.58e-05 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 46.39 E-value: 2.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462231119 33 WLLLSTASIF--------TLKQYAQKNLELTAATMGRSLEAALVFGDSAAAEETLASLGKQGQISQAIVLNGQMQHFAAW 104
Cdd:PRK11059 15 VTLLVALAMFvtllgctlSFYQLTQEKQQHRVQALATAIDQHLLTQDAASLQRWLPELLQAANIVEVDLSQGDKPVYSFQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462231119 105 RHEPLANKEQVSGLISkwlfpepTVQPIWHQGKQigELRLTALDELISHFLGI-SILVLTGSILlasFIALLLTHSlHRG 183
Cdd:PRK11059 95 RPASYRPQGSSSLYRE-------LSLPLLKHPGM--SLRLKYVDPFGNYFYSLyATASLTLAIG---FIVLMLFLG-VRW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462231119 184 IVAALQSITEVvhDIRENRHFSRRVPEERIEEFHLFAQDFNS----LLGEMEDWQRQlQAKNAQLLRS-SLHDPLTGLAN 258
Cdd:PRK11059 162 LRRQLAGQELL--EERARRILNGEREQAVAGSGYEWPRTASRaldhLLSELQDAREE-RSRFDTFIRSnAFQDAKTGLGN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462231119 259 RAAFRNALAELMQNEVDHQT-SALLFLDGDNFKLINDNWGHAAGDKVLMEVASRLMTFAgKRH----LAwRLGGDEFAVL 333
Cdd:PRK11059 239 RLFFDNQLATLLEDQEMVGAhGVVMLIRLPDFDLLQEEWGESQVEELLFELINLLSTFV-MRYpgalLA-RYSRSDFAVL 316
|
.
gi 1462231119 334 L 334
Cdd:PRK11059 317 L 317
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
281-403 |
1.48e-04 |
|
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: 41.57 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462231119 281 LLFLDGDNFKLINDNWGHAAGDKVLMEVASRlMTFAGKRHLAW--RLGGDEFAVLL------REVRSEAEVQALCQALTE 352
Cdd:cd07556 4 ILFADIVGFTSLADALGPDEGDELLNELAGR-FDSLIRRSGDLkiKTIGDEFMVVSgldhpaAAVAFAEDMREAVSALNQ 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1462231119 353 QFLPPFNLHNGHSATLSLSVGYALAWEHATAESLQELADQNMYRMKNQRIQ 403
Cdd:cd07556 83 SEGNPVRVRIGIHTGPVVVGVIGSRPQYDVWGALVNLASRMESQAKAGQVL 133
|
|
| NarQ |
COG3850 |
Signal transduction histidine kinase NarQ, nitrate/nitrite-specific [Signal transduction ... |
61-342 |
3.83e-04 |
|
Signal transduction histidine kinase NarQ, nitrate/nitrite-specific [Signal transduction mechanisms];
Pssm-ID: 443059 [Multi-domain] Cd Length: 448 Bit Score: 42.56 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462231119 61 RSLEAALVFGDSAAAEETLASLGKQGQISQAIVLNGQMQHFAAWRHEPLANKEQVSGLISKWLFPEPTVQPIWHQGKQIG 140
Cdd:COG3850 19 LALLLLALLLLSLLALLLLLERTLLRLLSLLASAGLLAALLAALLLLLSLGLLALLLALLLLLLLLLLAALLSLLLLLLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462231119 141 ELRLTALDELISHFLGISILVLTGSILLASFIALLLTHSLHRGIVAALQSITEVVHDIREnRHFSRRVPEERIEEFHLFA 220
Cdd:COG3850 99 LLLLLLLLLLLLLAAAINRKLALLRLLLALLLALLLAYLLRRRIVRPLRRLTQAAERIAR-GDFDARVPVSGRDELGTLA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462231119 221 QDFNSLLGEMEDWQRQLQAKNAQLLRSSLHDPLTGLANRAAFRNALAELMQNEVDHQTSALLFLDGDNFKLINDNWGHAA 300
Cdd:COG3850 178 RAFNRMADELQELYAELEEEEELEAELELLALLDELLLLAALLLLLALLLALLLAALLAALLLLLLLQDALAESELLALN 257
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1462231119 301 GDKVLMEVASRLMTFAGKRHLAWRLGGDEFAVLLREVRSEAE 342
Cdd:COG3850 258 ILAGLLELLLALLLLLLASALLLLELELLALLLELVELLALA 299
|
|
| |
