|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
1-401 |
0e+00 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 630.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505183160 1 MNKDFSQAPRPTFKNALRRISMISVVISMTLVWLLLSAASVITLKQYAQKNLELTAATMGRSLEAALVFGDATAAEDTLA 80
Cdd:PRK09966 1 MDNDNSLNKRPTFKRALRNISMTSIFITMMLIWLLLSVTSVLTLKQYAQKNLALTAATMTYSLEAAVVFADGPAATETLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505183160 81 TLGRQGQFSEATLLDSHQRHFADWRNDALVKNEKFSGYISKWLFPEPTVQPIWHQGKIIGELRLKALDRLISHFLGTSLI 160
Cdd:PRK09966 81 ALGQQGQFSTAEVRDKQQNILASWHYTRKDPGDTFSNFISHWLFPAPIIQPIRHNGETIGEVRLTARDSSISHFIWFSLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505183160 161 VLTGSILLASVIALMLTHSLHRGIVAALQSITEVVHDIRENRHFSRRVPEERIEEFHLFAQDFNSLLGEMEDWQRQLQAK 240
Cdd:PRK09966 161 VLTGCILLASGIAITLTRHLHNGLVEALKNITDVVHDVRSNRNFSRRVSEERIAEFHRFALDFNSLLDEMEEWQLRLQAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505183160 241 NAQLLRSSLHDPLTGLANRAAFRNVIGKLMDDDAARHSSALLFLDGDNFKLINDNWGHAAGDKVLIEVASRLMAFVGDQH 320
Cdd:PRK09966 241 NAQLLRTALHDPLTGLANRAAFRSGINTLMNNSDARKTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505183160 321 QAWRLGGDEFAILLHDVHTETEVQALCATLSEQFLQPFNLHNGHTATLSLSIGYALTWEHTSVEELQELADQNMYRMKNQ 400
Cdd:PRK09966 321 KAYRLGGDEFAMVLYDVQSESEVQQICSALTQIFNLPFDLHNGHQTTMTLSIGYAMTIEHASAEKLQELADHNMYQAKHQ 400
|
.
gi 505183160 401 R 401
Cdd:PRK09966 401 R 401
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
146-400 |
4.36e-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: 159.76 E-value: 4.36e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505183160 146 ALDRLISHFLGTSLIVLTGSILLASVIALMLTHSLHRGIVAALQSITEVVHDIRENRHFSRRVPEERIEEFHLFAQDFNS 225
Cdd:COG2199 13 LLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505183160 226 LLGEMEDwQRQLQAKNAQLLRSSLHDPLTGLANRAAFRNVIGKLMDDDAARHSS-ALLFLDGDNFKLINDNWGHAAGDKV 304
Cdd:COG2199 93 LLLALED-ITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPlALLLIDLDHFKRINDTYGHAAGDEV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505183160 305 LIEVASRLMAFVGDQHQAWRLGGDEFAILLHDVHTEtEVQALCATLSEQFLQPFNLHNGHTATLSLSIGYALTWEH-TSV 383
Cdd:COG2199 172 LKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLE-EAEALAERLREALEQLPFELEGKELRVTVSIGVALYPEDgDSA 250
|
250
....*....|....*..
gi 505183160 384 EELQELADQNMYRMKNQ 400
Cdd:COG2199 251 EELLRRADLALYRAKRA 267
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
249-401 |
3.69e-44 |
|
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: 150.78 E-value: 3.69e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505183160 249 LHDPLTGLANRAAFRNVIGKLMDDDAARHSS-ALLFLDGDNFKLINDNWGHAAGDKVLIEVASRLMAFVGDQHQAWRLGG 327
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLARARRSGRPlALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505183160 328 DEFAILLHDVhTETEVQALCATLSEQFLQPFNLHnGHTATLSLSIGYALTWEH-TSVEELQELADQNMYRMKNQR 401
Cdd:cd01949 81 DEFAILLPGT-DLEEAEALAERLREAIEEPFFID-GQEIRVTASIGIATYPEDgEDAEELLRRADEALYRAKRSG 153
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
248-400 |
2.49e-42 |
|
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: 146.24 E-value: 2.49e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505183160 248 SLHDPLTGLANRAAFRNVIGKLMDDDAARHSS-ALLFLDGDNFKLINDNWGHAAGDKVLIEVASRLMAFVGDQHQAWRLG 326
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPvAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505183160 327 GDEFAILLHDVHTET--EVQALCATLSEQFLQPFNlHNGHTATLSLSIGYALTWEHT-SVEELQELADQNMYRMKNQ 400
Cdd:pfam00990 81 GDEFAILLPETSLEGaqELAERIRRLLAKLKIPHT-VSGLPLYVTISIGIAAYPNDGeDPEDLLKRADTALYQAKQA 156
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
246-406 |
7.07e-40 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 139.69 E-value: 7.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505183160 246 RSSLHDPLTGLANRAAFRNVIGKLMDD-DAARHSSALLFLDGDNFKLINDNWGHAAGDKVLIEVASRLMAFVGDQHQAWR 324
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRaQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505183160 325 LGGDEFAILLHDVHTEtEVQALCATLSEQFLQPFNLHnGHTATLSLSIGYALTWEHT-SVEELQELADQNMYRMKNQRFH 403
Cdd:smart00267 81 LGGDEFALLLPETSLE-EAIALAERILQQLREPIIIH-GIPLYLTISIGVAAYPNPGeDAEDLLKRADTALYQAKKAGRN 158
|
...
gi 505183160 404 HTQ 406
Cdd:smart00267 159 QVA 161
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
248-398 |
4.20e-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: 108.58 E-value: 4.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505183160 248 SLHDPLTGLANRAAFRNVIGKLMDDdAARH--SSALLFLDGDNFKLINDNWGHAAGDKVLIEVASRLMAFVGDQHQAWRL 325
Cdd:TIGR00254 2 AVRDPLTGLYNRRYLEEMLDSELKR-ARRFqrSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505183160 326 GGDEFAILLHDVHTETEVqalcaTLSEQFLQ-----PFNLHNGHTATLSLSIGYALTWEH-TSVEELQELADQNMYRMK 398
Cdd:TIGR00254 81 GGEEFVVILPGTPLEDAL-----SKAERLRDainskPIEVAGSETLTVTVSIGVACYPGHgLTLEELLKRADEALYQAK 154
|
|
| diguan_DgcJ |
NF040885 |
diguanylate cyclase DgcJ; |
240-401 |
2.25e-10 |
|
diguanylate cyclase DgcJ;
Pssm-ID: 468821 [Multi-domain] Cd Length: 490 Bit Score: 62.28 E-value: 2.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505183160 240 KNAQLLRSSLHDPLTGLANRAAFRNVIGKLMDDDAARHSS-ALLFLDGDNFKLINDNWGHAAGDKVLIEVASRLMAFVGD 318
Cdd:NF040885 333 LYHNVSRENISDSMTGLYNRKILTPTLEQRLQRLTEKGIPvTFIALDCDKLKHINDTLGHHEGDRAITLLAQAISASIRK 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505183160 319 QHQAWRLGGDEFAILLHDvHTETEVQALCATLsEQFLQpfnlHNGHTATLSLSIGYALTWEHTSVEELQELADQNMYRMK 398
Cdd:NF040885 413 SDYGIRLGGDEFCIILID-YEEAEAQNLIERI-RQHLR----TIDPDKRVSFSWGAYQMQPGDTLDDAYKAADERLYLNK 486
|
...
gi 505183160 399 NQR 401
Cdd:NF040885 487 KQK 489
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
1-401 |
0e+00 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 630.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505183160 1 MNKDFSQAPRPTFKNALRRISMISVVISMTLVWLLLSAASVITLKQYAQKNLELTAATMGRSLEAALVFGDATAAEDTLA 80
Cdd:PRK09966 1 MDNDNSLNKRPTFKRALRNISMTSIFITMMLIWLLLSVTSVLTLKQYAQKNLALTAATMTYSLEAAVVFADGPAATETLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505183160 81 TLGRQGQFSEATLLDSHQRHFADWRNDALVKNEKFSGYISKWLFPEPTVQPIWHQGKIIGELRLKALDRLISHFLGTSLI 160
Cdd:PRK09966 81 ALGQQGQFSTAEVRDKQQNILASWHYTRKDPGDTFSNFISHWLFPAPIIQPIRHNGETIGEVRLTARDSSISHFIWFSLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505183160 161 VLTGSILLASVIALMLTHSLHRGIVAALQSITEVVHDIRENRHFSRRVPEERIEEFHLFAQDFNSLLGEMEDWQRQLQAK 240
Cdd:PRK09966 161 VLTGCILLASGIAITLTRHLHNGLVEALKNITDVVHDVRSNRNFSRRVSEERIAEFHRFALDFNSLLDEMEEWQLRLQAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505183160 241 NAQLLRSSLHDPLTGLANRAAFRNVIGKLMDDDAARHSSALLFLDGDNFKLINDNWGHAAGDKVLIEVASRLMAFVGDQH 320
Cdd:PRK09966 241 NAQLLRTALHDPLTGLANRAAFRSGINTLMNNSDARKTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505183160 321 QAWRLGGDEFAILLHDVHTETEVQALCATLSEQFLQPFNLHNGHTATLSLSIGYALTWEHTSVEELQELADQNMYRMKNQ 400
Cdd:PRK09966 321 KAYRLGGDEFAMVLYDVQSESEVQQICSALTQIFNLPFDLHNGHQTTMTLSIGYAMTIEHASAEKLQELADHNMYQAKHQ 400
|
.
gi 505183160 401 R 401
Cdd:PRK09966 401 R 401
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
146-400 |
4.36e-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: 159.76 E-value: 4.36e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505183160 146 ALDRLISHFLGTSLIVLTGSILLASVIALMLTHSLHRGIVAALQSITEVVHDIRENRHFSRRVPEERIEEFHLFAQDFNS 225
Cdd:COG2199 13 LLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505183160 226 LLGEMEDwQRQLQAKNAQLLRSSLHDPLTGLANRAAFRNVIGKLMDDDAARHSS-ALLFLDGDNFKLINDNWGHAAGDKV 304
Cdd:COG2199 93 LLLALED-ITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPlALLLIDLDHFKRINDTYGHAAGDEV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505183160 305 LIEVASRLMAFVGDQHQAWRLGGDEFAILLHDVHTEtEVQALCATLSEQFLQPFNLHNGHTATLSLSIGYALTWEH-TSV 383
Cdd:COG2199 172 LKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLE-EAEALAERLREALEQLPFELEGKELRVTVSIGVALYPEDgDSA 250
|
250
....*....|....*..
gi 505183160 384 EELQELADQNMYRMKNQ 400
Cdd:COG2199 251 EELLRRADLALYRAKRA 267
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
16-400 |
2.63e-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: 163.41 E-value: 2.63e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505183160 16 ALRRISMISVVISMTLVWLLLSAASVITLKQYAQKNLELTAATMGRSLEAALVFGDATAAEDTLATLGRQGQFSEATLLD 95
Cdd:COG5001 19 LLLALLLLALLLAALLALALLLLLLLLLLALLLAALLLLALLALLALLLLAAALLALALAALLLAALLAALLLLLLLLLA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505183160 96 SHQRHFADWRNDALVKNEKFSGYISKWLFPEPTVQPIWHQGKIIGELRLKALDRLISHFLGTSLIVLTGSILLASVIALM 175
Cdd:COG5001 99 LLVLLLLLLLLLALLALLAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARALLALLLLLLLALLLLLLL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505183160 176 LTHSLHRGIVAALQSITEVVHDIRENRHFSRRVPEERIEEFHLFAQDFNSLLGEMEDWQRQLQAKNAQLLRSSLHDPLTG 255
Cdd:COG5001 179 LLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEERLRHLAYHDPLTG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505183160 256 LANRAAFRNVIGKLMDDDAARHSS-ALLFLDGDNFKLINDNWGHAAGDKVLIEVASRLMAFVGDQHQAWRLGGDEFAILL 334
Cdd:COG5001 259 LPNRRLFLDRLEQALARARRSGRRlALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVLL 338
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505183160 335 HDVHTETEVQALCATLSEQFLQPFNLhNGHTATLSLSIGYALTWEH-TSVEELQELADQNMYRMKNQ 400
Cdd:COG5001 339 PDLDDPEDAEAVAERILAALAEPFEL-DGHELYVSASIGIALYPDDgADAEELLRNADLAMYRAKAA 404
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
249-401 |
3.69e-44 |
|
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: 150.78 E-value: 3.69e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505183160 249 LHDPLTGLANRAAFRNVIGKLMDDDAARHSS-ALLFLDGDNFKLINDNWGHAAGDKVLIEVASRLMAFVGDQHQAWRLGG 327
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLARARRSGRPlALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505183160 328 DEFAILLHDVhTETEVQALCATLSEQFLQPFNLHnGHTATLSLSIGYALTWEH-TSVEELQELADQNMYRMKNQR 401
Cdd:cd01949 81 DEFAILLPGT-DLEEAEALAERLREAIEEPFFID-GQEIRVTASIGIATYPEDgEDAEELLRRADEALYRAKRSG 153
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
248-400 |
2.49e-42 |
|
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: 146.24 E-value: 2.49e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505183160 248 SLHDPLTGLANRAAFRNVIGKLMDDDAARHSS-ALLFLDGDNFKLINDNWGHAAGDKVLIEVASRLMAFVGDQHQAWRLG 326
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPvAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505183160 327 GDEFAILLHDVHTET--EVQALCATLSEQFLQPFNlHNGHTATLSLSIGYALTWEHT-SVEELQELADQNMYRMKNQ 400
Cdd:pfam00990 81 GDEFAILLPETSLEGaqELAERIRRLLAKLKIPHT-VSGLPLYVTISIGIAAYPNDGeDPEDLLKRADTALYQAKQA 156
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
246-406 |
7.07e-40 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 139.69 E-value: 7.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505183160 246 RSSLHDPLTGLANRAAFRNVIGKLMDD-DAARHSSALLFLDGDNFKLINDNWGHAAGDKVLIEVASRLMAFVGDQHQAWR 324
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRaQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505183160 325 LGGDEFAILLHDVHTEtEVQALCATLSEQFLQPFNLHnGHTATLSLSIGYALTWEHT-SVEELQELADQNMYRMKNQRFH 403
Cdd:smart00267 81 LGGDEFALLLPETSLE-EAIALAERILQQLREPIIIH-GIPLYLTISIGVAAYPNPGeDAEDLLKRADTALYQAKKAGRN 158
|
...
gi 505183160 404 HTQ 406
Cdd:smart00267 159 QVA 161
|
|
| CHASE8 |
pfam17152 |
Periplasmic sensor domain; CHASE8 is a conserved periplasmic sensor domain found in histidine ... |
44-144 |
1.53e-35 |
|
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: 126.22 E-value: 1.53e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505183160 44 LKQYAQKNLELTAATMGRSLEAALVFGDATAAEDTLATLGRQGQFSEATLLDSHQRHFADWRNDALVKNEKFSGYISKWL 123
Cdd:pfam17152 1 LRRYAQQNLELLARSIAYNVEAALVFGDPAAARETLAALGAQPQIASAAVYDAQGRLFASYARPGTDPPEPLEALLARWL 80
|
90 100
....*....|....*....|.
gi 505183160 124 FPEPTVQPIWHQGKIIGELRL 144
Cdd:pfam17152 81 LPAPVLQPIVHDGERIGSVVL 101
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
248-398 |
4.20e-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: 108.58 E-value: 4.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505183160 248 SLHDPLTGLANRAAFRNVIGKLMDDdAARH--SSALLFLDGDNFKLINDNWGHAAGDKVLIEVASRLMAFVGDQHQAWRL 325
Cdd:TIGR00254 2 AVRDPLTGLYNRRYLEEMLDSELKR-ARRFqrSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505183160 326 GGDEFAILLHDVHTETEVqalcaTLSEQFLQ-----PFNLHNGHTATLSLSIGYALTWEH-TSVEELQELADQNMYRMK 398
Cdd:TIGR00254 81 GGEEFVVILPGTPLEDAL-----SKAERLRDainskPIEVAGSETLTVTVSIGVACYPGHgLTLEELLKRADEALYQAK 154
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
250-400 |
2.68e-21 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 95.85 E-value: 2.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505183160 250 HDPLTGLANRAAFRNVIGKLMDD-DAARHSSALLFLDGDNFKLINDNWGHAAGDKVLIEVASRLMAFVGDQHQAWRLGGD 328
Cdd:PRK15426 400 HDPLTRLYNRGALFEKARALAKRcQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRVGGE 479
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505183160 329 EFAILLHDVhteTEVQAlcATLSEQFLQPFN-----LHNGHTATLSLSIGYALTWEHT--SVEELQELADQNMYRMKNQ 400
Cdd:PRK15426 480 EFCVVLPGA---SLAEA--AQVAERIRLRINekeilVAKSTTIRISASLGVSSAEEDGdyDFEQLQSLADRRLYLAKQA 553
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
236-399 |
5.01e-21 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 94.58 E-value: 5.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505183160 236 QLQAKNAQ-LLRSSLH--------DPLTGLANRAAFRNVIGKLMDDDAARHSS-ALLFLDGDNFKLINDNWGHAAGDKVL 305
Cdd:PRK09581 271 QIRRKRYQdALRNNLEqsiemavtDGLTGLHNRRYFDMHLKNLIERANERGKPlSLMMIDIDHFKKVNDTYGHDAGDEVL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505183160 306 IEVASRLMAFVGDQHQAWRLGGDEFAILLHDvhTETEVQALCAtlsEQFLQ-----PFNLHNG-HTATLSLSIGYA-LTW 378
Cdd:PRK09581 351 REFAKRLRNNIRGTDLIARYGGEEFVVVMPD--TDIEDAIAVA---ERIRRkiaeePFIISDGkERLNVTVSIGVAeLRP 425
|
170 180
....*....|....*....|.
gi 505183160 379 EHTSVEELQELADQNMYRMKN 399
Cdd:PRK09581 426 SGDTIEALIKRADKALYEAKN 446
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
197-399 |
1.37e-19 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 88.20 E-value: 1.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505183160 197 DIRENRHFSRRVPEERIEEFHLFAQDFNSLLGEMEDWQRQLQAKNAQLL--RSSLhDPLTGLANRaafrNVIGKLMDDDA 274
Cdd:PRK09894 77 SAHQHMHNCARELLLAIVEGHWQDAHFDAFQEGLLSFTAALTDYKIYLLtiRSNM-DVLTGLPGR----RVLDESFDHQL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505183160 275 ARHSS---ALLFLDGDNFKLINDNWGHAAGDKVLIEVASRLMAFVGDQHQAWRLGGDEFAILLHDvHTETEVQA----LC 347
Cdd:PRK09894 152 RNREPqnlYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGGEEFIICLKA-ATDEEACRagerIR 230
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 505183160 348 ATLSEqflQPFNLHNGH---TATLSLSIGYALtwehTSVEELQELADQNMYRMKN 399
Cdd:PRK09894 231 QLIAN---HAITHSDGRiniTATFGVSRAFPE----ETLDVVIGRADRAMYEGKQ 278
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
243-336 |
5.06e-18 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 86.26 E-value: 5.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505183160 243 QLLRSSLHDPLTGLANRAAFRNVIGKLMDDDAARHS-SALLFLDGDNFKLINDNWGHAAGDKVLIEVASRLMAFVGDQHQ 321
Cdd:PRK09776 660 QLSYSASHDALTHLANRASFEKQLRRLLQTVNSTHQrHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSDV 739
|
90
....*....|....*
gi 505183160 322 AWRLGGDEFAILLHD 336
Cdd:PRK09776 740 LARLGGDEFGLLLPD 754
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
225-373 |
2.24e-17 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 84.44 E-value: 2.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505183160 225 SLLGEMEDWQRQLQaknaQLLRsslHDPLTGLANRAAFRNVIGKLMDDDaarHSSALLFLDGDNFKLINDNWGHAAGDKV 304
Cdd:PRK11359 360 ALALEQEKSRQHIE----QLIQ---FDPLTGLPNRNNLHNYLDDLVDKA---VSPVVYLIGVDHFQDVIDSLGYAWADQA 429
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505183160 305 LIEVASRLMAFVGDQHQAWRLGGDEFAILLHD--VHTETEVQALcatLSEQFLQPFNLhNGHTATLSLSIG 373
Cdd:PRK11359 430 LLEVVNRFREKLKPDQYLCRIEGTQFVLVSLEndVSNITQIADE---LRNVVSKPIMI-DDKPFPLTLSIG 496
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
251-398 |
2.47e-17 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 83.96 E-value: 2.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505183160 251 DPLTGLANRAAFRNVIGKLMDDdAARHSSALLFLDGDNFKLINDNWGHAAGDKVLIEVASRLMAFVGDQHQAWRLGGDEF 330
Cdd:PRK10060 240 DSITGLPNRNAIQELIDHAINA-ADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQTLARLGGDEF 318
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505183160 331 aILLHDVHTETEVQALCATLSEQFLQPFNLHNGHTATlSLSIGYALTWEH-TSVEELQELADQNMYRMK 398
Cdd:PRK10060 319 -LVLASHTSQAALEAMASRILTRLRLPFRIGLIEVYT-GCSIGIALAPEHgDDSESLIRSADTAMYTAK 385
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
248-399 |
2.06e-11 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 64.85 E-value: 2.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505183160 248 SLHDPLTGLANRAAFRNVIGKLMDDDAARHSSA-LLFLDGDNFKLINDNWGHAAGDKVLIEVASRLMAFVGDQHQAWRLG 326
Cdd:PRK10245 205 STRDGMTGVYNRRHWETLLRNEFDNCRRHHRDAtLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSDVIGRFG 284
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505183160 327 GDEFAILLHDVHTETEVQALCATlsEQFLQPFNLHNGHTATLSLSIGYA-LTWEHTSVEELQELADQNMYRMKN 399
Cdd:PRK10245 285 GDEFAVIMSGTPAESAITAMSRV--HEGLNTLRLPNAPQVTLRISVGVApLNPQMSHYREWLKSADLALYKAKN 356
|
|
| diguan_DgcJ |
NF040885 |
diguanylate cyclase DgcJ; |
240-401 |
2.25e-10 |
|
diguanylate cyclase DgcJ;
Pssm-ID: 468821 [Multi-domain] Cd Length: 490 Bit Score: 62.28 E-value: 2.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505183160 240 KNAQLLRSSLHDPLTGLANRAAFRNVIGKLMDDDAARHSS-ALLFLDGDNFKLINDNWGHAAGDKVLIEVASRLMAFVGD 318
Cdd:NF040885 333 LYHNVSRENISDSMTGLYNRKILTPTLEQRLQRLTEKGIPvTFIALDCDKLKHINDTLGHHEGDRAITLLAQAISASIRK 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505183160 319 QHQAWRLGGDEFAILLHDvHTETEVQALCATLsEQFLQpfnlHNGHTATLSLSIGYALTWEHTSVEELQELADQNMYRMK 398
Cdd:NF040885 413 SDYGIRLGGDEFCIILID-YEEAEAQNLIERI-RQHLR----TIDPDKRVSFSWGAYQMQPGDTLDDAYKAADERLYLNK 486
|
...
gi 505183160 399 NQR 401
Cdd:NF040885 487 KQK 489
|
|
| NtrY |
COG5000 |
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ... |
159-285 |
1.42e-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: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505183160 159 LIVLTGSILLASVIALMLTHSLHRGIVAALQSITEVVHDIRENrHFSRRVPEERIEEFHLFAQDFNSLLGEMEDwQRQLQ 238
Cdd:COG5000 8 LLLLLLIALLLLLLALWLALLLARRLTRPLRRLAEATRAVAAG-DLSVRLPVTGDDEIGELARAFNRMTDQLKE-QREEL 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505183160 239 AKNAQLLRSSLHDPLTG-----------LANRAAFR-------NVIGKLMDDDAARHSSALLFLD 285
Cdd:COG5000 86 EERRRYLETILENLPAGvivldadgritLANPAAERllgipleELIGKPLEELLPELDLAELLRE 150
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
281-392 |
1.72e-05 |
|
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: 44.27 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505183160 281 LLFLDGDNFKLINDNWGHAAGDKVLIEVASRLMAFVgDQHQAW--RLGGDEFAILLHDVHTET------EVQALCATLSE 352
Cdd:cd07556 4 ILFADIVGFTSLADALGPDEGDELLNELAGRFDSLI-RRSGDLkiKTIGDEFMVVSGLDHPAAavafaeDMREAVSALNQ 82
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 505183160 353 QFLQPFNLHNGhTATLSLSIGYA-LTWEHTSVEELQELADQ 392
Cdd:cd07556 83 SEGNPVRVRIG-IHTGPVVVGVIgSRPQYDVWGALVNLASR 122
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
33-334 |
8.43e-05 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 44.85 E-value: 8.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505183160 33 WLLLSAA--------SVITLKQYAQKNLELTAATMGRSLEAALVFGDATAAEDTLATLGRQGQFSEATLLDSHQRHFADW 104
Cdd:PRK11059 15 VTLLVALamfvtllgCTLSFYQLTQEKQQHRVQALATAIDQHLLTQDAASLQRWLPELLQAANIVEVDLSQGDKPVYSFQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505183160 105 RNDALVKNEKFSGYISkwlfpepTVQPIWHQGKIigELRLKALDRLISHFLGT-SLIVLTGSILlasVIALMLTHSlHRG 183
Cdd:PRK11059 95 RPASYRPQGSSSLYRE-------LSLPLLKHPGM--SLRLKYVDPFGNYFYSLyATASLTLAIG---FIVLMLFLG-VRW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505183160 184 IVAALQSITEVvhdirENRhfSRRVPEERIEEF-----HLFAQDFNS----LLGEMEDWQRQlQAKNAQLLRS-SLHDPL 253
Cdd:PRK11059 162 LRRQLAGQELL-----EER--ARRILNGEREQAvagsgYEWPRTASRaldhLLSELQDAREE-RSRFDTFIRSnAFQDAK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505183160 254 TGLANRAAFRNVIGKLMDD--DAARHSSALLfLDGDNFKLINDNWGHAAGDKVLIEVASRLMAFVGDQHQAW--RLGGDE 329
Cdd:PRK11059 234 TGLGNRLFFDNQLATLLEDqeMVGAHGVVML-IRLPDFDLLQEEWGESQVEELLFELINLLSTFVMRYPGALlaRYSRSD 312
|
....*
gi 505183160 330 FAILL 334
Cdd:PRK11059 313 FAVLL 317
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
149-362 |
9.12e-04 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 41.47 E-value: 9.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505183160 149 RLISHFLGTSLIVLTGSILLASVIALMLTHSLHRGIVAALQSITEVVHDI-RENRHFSR--RVPEERIEEFHLFAQDFNS 225
Cdd:PRK11829 137 RMYQFILSALSAMLSTYLLLALVLSVSIAWCINRLIIHPLRAMAKELEDIgDHGVLHHQltLPAHHQDDELGVLVRNYNR 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505183160 226 LlgemedwQRQLQAKNAQLLRSSLHDPLTGLANRAAFRNVIGKLMDDDAARHSSALLFLDGDNFKLINDNWGHAAGDKVL 305
Cdd:PRK11829 217 N-------QQLLADAYADMGRISHRFPVTELPNRSLFISLLEKEIASSTRTDHFHLLVIGIETLQEVSGAMSEAQHQQLL 289
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 505183160 306 IEVASRLMAFVGDQHQAWRLGGDEFAILLHDVHTETEVQALCATLSEQFLQPFNLHN 362
Cdd:PRK11829 290 LTIVQRIEQCIDDSDLLAQLSKTEFAVLARGTRRSFPAMQLARRIMSQVTQPLFFDE 346
|
|
| NarQ |
COG3850 |
Signal transduction histidine kinase NarQ, nitrate/nitrite-specific [Signal transduction ... |
128-312 |
1.56e-03 |
|
Signal transduction histidine kinase NarQ, nitrate/nitrite-specific [Signal transduction mechanisms];
Pssm-ID: 443059 [Multi-domain] Cd Length: 448 Bit Score: 40.64 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505183160 128 TVQPIWHQGKIIGELRLKALDRLISHFLGTSLIVLTGSILLASVIALMLTHSLHRGIVAALQSITEVVHDIREnRHFSRR 207
Cdd:COG3850 86 LAALLSLLLLLLLLLLLLLLLLLLLLAAAINRKLALLRLLLALLLALLLAYLLRRRIVRPLRRLTQAAERIAR-GDFDAR 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505183160 208 VPEERIEEFHLFAQDFNSLLGEMEDWQRQLQAKNAQLLRSSLHDPLTGLANRAAFRNVIGKLMDDDAARHSSALLFLDGD 287
Cdd:COG3850 165 VPVSGRDELGTLARAFNRMADELQELYAELEEEEELEAELELLALLDELLLLAALLLLLALLLALLLAALLAALLLLLLL 244
|
170 180
....*....|....*....|....*
gi 505183160 288 NFKLINDNWGHAAGDKVLIEVASRL 312
Cdd:COG3850 245 QDALAESELLALNILAGLLELLLAL 269
|
|
| PRK10549 |
PRK10549 |
two-component system sensor histidine kinase BaeS; |
125-251 |
3.19e-03 |
|
two-component system sensor histidine kinase BaeS;
Pssm-ID: 182539 [Multi-domain] Cd Length: 466 Bit Score: 39.62 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505183160 125 PEPTVQPIWHQGKIIGELRLKALDRL-----IShF----LGTSLIVLTGSILLASVIALMLThslhRGIVAALQSITEVV 195
Cdd:PRK10549 125 PDGTRRPILVNGAEVGWVIASPVERLtrntdIN-FdkqqRRTSWLIVALSTLLAALATFLLA----RGLLAPVKRLVEGT 199
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 505183160 196 HDIRENrHFSRRVPEERIEEFHLFAQDFNSLLGEMEdwqrqlqaKNAQLLRSSLHD 251
Cdd:PRK10549 200 HKLAAG-DFTTRVTPTSRDELGRLAQDFNQLASTLE--------KNEQMRRDFMAD 246
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
162-386 |
6.52e-03 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 38.54 E-value: 6.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505183160 162 LTGSILLASVIALMLTHSLHRGIVAALQSITEVVHDI--RENRHFSRRVPE-ERIEEFHLFAQDFNSLlgemedwQRQLQ 238
Cdd:PRK13561 149 VTIYLLLSLILTVAISWCINRLIVHPLRNIARELNDIppQELVGHQLALPRlHQDDEIGMLVRSYNLN-------QQLLQ 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505183160 239 AKNAQLLRSSLHDPLTGLANRAAFRnvigKLMDDDAARHSS-ALLFLDGDNFKLINDNWGHAAGDKVLIEVASRLMAFVG 317
Cdd:PRK13561 222 RQYEEQSRNATRFPVSDLPNKALLM----ALLEQVVARKQTtALMIITCETLRDTAGVLKEAQREILLLTLVEKLKSVLS 297
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505183160 318 DQHQAWRLGGDEFAILLHDVhtETEVQALcaTLSEQFL----QPFNLHNGHTATlSLSIGYALTWEHTSVEEL 386
Cdd:PRK13561 298 PRMVLAQISGYDFAIIANGV--KEPWHAI--TLGQQVLtiinERLPIQRIQLRP-SCSIGIAMFYGDLTAEQL 365
|
|
| |
