|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
11-404 |
2.77e-96 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 294.22 E-value: 2.77e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167397 11 NARPTLGRVLQRVHLGLALIAVGTAGIFLTLVALFALRAYADHNLHLIARSISYTVEAAVVFEDGVAAREALMLIASNEE 90
Cdd:PRK09966 8 NKRPTFKRALRNISMTSIFITMMLIWLLLSVTSVLTLKQYAQKNLALTAATMTYSLEAAVVFADGPAATETLAALGQQGQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167397 91 ILEARILDNKGKMLASWRHPSDSPLHGLEQMVAHWALPEPVILPISHGGKQVGQVWLSGNGGSLLRFLLRGLVGMIACMV 170
Cdd:PRK09966 88 FSTAEVRDKQQNILASWHYTRKDPGDTFSNFISHWLFPAPIIQPIRHNGETIGEVRLTARDSSISHFIWFSLAVLTGCIL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167397 171 LSTLCALVLSRRMLVGIVSSLDDIANVAHAVRRDRTFGLRVPSAPIAELHELSNDFNGLLDELEAWQAHLKQENDSLAHR 250
Cdd:PRK09966 168 LASGIAITLTRHLHNGLVEALKNITDVVHDVRSNRNFSRRVSEERIAEFHRFALDFNSLLDEMEEWQLRLQAKNAQLLRT 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167397 251 ATHDSLTGLPNRAFFEGRLSRALGDIEPPAKLAVLFIDGDRFKEVNDSYGHAAGDAVLTTIAGRIRAQLRETDLVARLGG 330
Cdd:PRK09966 248 ALHDPLTGLANRAAFRSGINTLMNNSDARKTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHKAYRLGG 327
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 727167397 331 DEFAVLLAPVHGTEDVLQIADNIIDCMTQPVILPNDEAVITSLSIGIALYPDHASTpQGLLHEADDAMYQAKHR 404
Cdd:PRK09966 328 DEFAMVLYDVQSESEVQQICSALTQIFNLPFDLHNGHQTTMTLSIGYAMTIEHASA-EKLQELADHNMYQAKHQ 400
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
2-411 |
1.68e-65 |
|
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: 221.19 E-value: 1.68e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167397 2 RLLHRNRAGNARPTLGRVLQRVHLGLALIAVGTAGIFLTLVALFALRAYADHNLHLIARSISYTVEAAVVFEDGVAAREA 81
Cdd:COG5001 7 LLLLLLALLLALLLLALLLLALLLAALLALALLLLLLLLLLALLLAALLLLALLALLALLLLAAALLALALAALLLAALL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167397 82 LMLIASNEEILEARILDNKGKMLASWRHPSDSPLHGLEQMVAHWALPEPVILPISHGGKQVGQVWLSGNGGSLLRFLLRG 161
Cdd:COG5001 87 AALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARALLALLL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167397 162 LVGMIACMVLSTLCALVLSRRMLVGIVSSLDDIANVAHAVRRDRTFGLRVPSAPIAELHELSNDFNGLLDELEawqahLK 241
Cdd:COG5001 167 LLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITE-----RK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167397 242 QENDSLAHRATHDSLTGLPNRAFFEGRLSRALGDIE-PPAKLAVLFIDGDRFKEVNDSYGHAAGDAVLTTIAGRIRAQLR 320
Cdd:COG5001 242 RAEERLRHLAYHDPLTGLPNRRLFLDRLEQALARARrSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167397 321 ETDLVARLGGDEFAVLLAPVHGTEDVLQIADNIIDCMTQPVILpNDEAVITSLSIGIALYPDHASTPQGLLHEADDAMYQ 400
Cdd:COG5001 322 EGDTVARLGGDEFAVLLPDLDDPEDAEAVAERILAALAEPFEL-DGHELYVSASIGIALYPDDGADAEELLRNADLAMYR 400
|
410
....*....|.
gi 727167397 401 AKHRYNGGWRL 411
Cdd:COG5001 401 AKAAGRNRYRF 411
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
252-410 |
4.11e-58 |
|
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: 187.38 E-value: 4.11e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167397 252 THDSLTGLPNRAFFEGRLSRALGDIEPPAK-LAVLFIDGDRFKEVNDSYGHAAGDAVLTTIAGRIRAQLRETDLVARLGG 330
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLARARRSGRpLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167397 331 DEFAVLLaPVHGTEDVLQIADNIIDCMTQPVILPNDEAVITsLSIGIALYPDHASTPQGLLHEADDAMYQAKHRYNGGWR 410
Cdd:cd01949 81 DEFAILL-PGTDLEEAEALAERLREAIEEPFFIDGQEIRVT-ASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNRVV 158
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
251-404 |
3.66e-53 |
|
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: 174.36 E-value: 3.66e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167397 251 ATHDSLTGLPNRAFFEGRLSRALGDIEP-PAKLAVLFIDGDRFKEVNDSYGHAAGDAVLTTIAGRIRAQLRETDLVARLG 329
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALReGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 727167397 330 GDEFAVLL--APVHGTEDVLQIADNIIDCMTQPVILpNDEAVITSLSIGIALYPDHASTPQGLLHEADDAMYQAKHR 404
Cdd:pfam00990 81 GDEFAILLpeTSLEGAQELAERIRRLLAKLKIPHTV-SGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQA 156
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
249-404 |
7.04e-50 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 165.88 E-value: 7.04e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167397 249 HRATHDSLTGLPNRAFFEGRLSRALGDIEPPAK-LAVLFIDGDRFKEVNDSYGHAAGDAVLTTIAGRIRAQLRETDLVAR 327
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSpFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 727167397 328 LGGDEFAVLLaPVHGTEDVLQIADNIIDCMTQPvILPNDEAVITSLSIGIALYPDHASTPQGLLHEADDAMYQAKHR 404
Cdd:smart00267 81 LGGDEFALLL-PETSLEEAIALAERILQQLREP-IIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKA 155
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
250-412 |
2.62e-44 |
|
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: 151.72 E-value: 2.62e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167397 250 RATHDSLTGLPNRAFFEGRLSRALGDIEPPAK-LAVLFIDGDRFKEVNDSYGHAAGDAVLTTIAGRIRAQLRETDLVARL 328
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRsFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167397 329 GGDEFAVLLaPVHGTEDVLQIADNIIDCM-TQPVILPNDEAVITSLSIGIALYPDHASTPQGLLHEADDAMYQAKHRYNG 407
Cdd:TIGR00254 81 GGEEFVVIL-PGTPLEDALSKAERLRDAInSKPIEVAGSETLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRN 159
|
....*
gi 727167397 408 GWRLA 412
Cdd:TIGR00254 160 RVVVA 164
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
11-404 |
2.77e-96 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 294.22 E-value: 2.77e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167397 11 NARPTLGRVLQRVHLGLALIAVGTAGIFLTLVALFALRAYADHNLHLIARSISYTVEAAVVFEDGVAAREALMLIASNEE 90
Cdd:PRK09966 8 NKRPTFKRALRNISMTSIFITMMLIWLLLSVTSVLTLKQYAQKNLALTAATMTYSLEAAVVFADGPAATETLAALGQQGQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167397 91 ILEARILDNKGKMLASWRHPSDSPLHGLEQMVAHWALPEPVILPISHGGKQVGQVWLSGNGGSLLRFLLRGLVGMIACMV 170
Cdd:PRK09966 88 FSTAEVRDKQQNILASWHYTRKDPGDTFSNFISHWLFPAPIIQPIRHNGETIGEVRLTARDSSISHFIWFSLAVLTGCIL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167397 171 LSTLCALVLSRRMLVGIVSSLDDIANVAHAVRRDRTFGLRVPSAPIAELHELSNDFNGLLDELEAWQAHLKQENDSLAHR 250
Cdd:PRK09966 168 LASGIAITLTRHLHNGLVEALKNITDVVHDVRSNRNFSRRVSEERIAEFHRFALDFNSLLDEMEEWQLRLQAKNAQLLRT 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167397 251 ATHDSLTGLPNRAFFEGRLSRALGDIEPPAKLAVLFIDGDRFKEVNDSYGHAAGDAVLTTIAGRIRAQLRETDLVARLGG 330
Cdd:PRK09966 248 ALHDPLTGLANRAAFRSGINTLMNNSDARKTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHKAYRLGG 327
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 727167397 331 DEFAVLLAPVHGTEDVLQIADNIIDCMTQPVILPNDEAVITSLSIGIALYPDHASTpQGLLHEADDAMYQAKHR 404
Cdd:PRK09966 328 DEFAMVLYDVQSESEVQQICSALTQIFNLPFDLHNGHQTTMTLSIGYAMTIEHASA-EKLQELADHNMYQAKHQ 400
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
2-411 |
1.68e-65 |
|
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: 221.19 E-value: 1.68e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167397 2 RLLHRNRAGNARPTLGRVLQRVHLGLALIAVGTAGIFLTLVALFALRAYADHNLHLIARSISYTVEAAVVFEDGVAAREA 81
Cdd:COG5001 7 LLLLLLALLLALLLLALLLLALLLAALLALALLLLLLLLLLALLLAALLLLALLALLALLLLAAALLALALAALLLAALL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167397 82 LMLIASNEEILEARILDNKGKMLASWRHPSDSPLHGLEQMVAHWALPEPVILPISHGGKQVGQVWLSGNGGSLLRFLLRG 161
Cdd:COG5001 87 AALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARALLALLL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167397 162 LVGMIACMVLSTLCALVLSRRMLVGIVSSLDDIANVAHAVRRDRTFGLRVPSAPIAELHELSNDFNGLLDELEawqahLK 241
Cdd:COG5001 167 LLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITE-----RK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167397 242 QENDSLAHRATHDSLTGLPNRAFFEGRLSRALGDIE-PPAKLAVLFIDGDRFKEVNDSYGHAAGDAVLTTIAGRIRAQLR 320
Cdd:COG5001 242 RAEERLRHLAYHDPLTGLPNRRLFLDRLEQALARARrSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167397 321 ETDLVARLGGDEFAVLLAPVHGTEDVLQIADNIIDCMTQPVILpNDEAVITSLSIGIALYPDHASTPQGLLHEADDAMYQ 400
Cdd:COG5001 322 EGDTVARLGGDEFAVLLPDLDDPEDAEAVAERILAALAEPFEL-DGHELYVSASIGIALYPDDGADAEELLRNADLAMYR 400
|
410
....*....|.
gi 727167397 401 AKHRYNGGWRL 411
Cdd:COG5001 401 AKAAGRNRYRF 411
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
252-410 |
4.11e-58 |
|
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: 187.38 E-value: 4.11e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167397 252 THDSLTGLPNRAFFEGRLSRALGDIEPPAK-LAVLFIDGDRFKEVNDSYGHAAGDAVLTTIAGRIRAQLRETDLVARLGG 330
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLARARRSGRpLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167397 331 DEFAVLLaPVHGTEDVLQIADNIIDCMTQPVILPNDEAVITsLSIGIALYPDHASTPQGLLHEADDAMYQAKHRYNGGWR 410
Cdd:cd01949 81 DEFAILL-PGTDLEEAEALAERLREAIEEPFFIDGQEIRVT-ASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNRVV 158
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
142-412 |
8.41e-58 |
|
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: 190.57 E-value: 8.41e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167397 142 VGQVWLSGNGGSLLRFLLRGLVGMIACMVLSTLCALVLSRRMLVGIVSSLDDIANVAHAVRRDRTFGLRVPSAPIAELHE 221
Cdd:COG2199 6 LLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167397 222 LSNDFNGLLDELEAwQAHLKQENDSLAHRATHDSLTGLPNRAFFEGRLSRALGDIE-PPAKLAVLFIDGDRFKEVNDSYG 300
Cdd:COG2199 86 LLLALLLLLLALED-ITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARrEGRPLALLLIDLDHFKRINDTYG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167397 301 HAAGDAVLTTIAGRIRAQLRETDLVARLGGDEFAVLLaPVHGTEDVLQIADNIIDCMTQPVILPNDEAVITSLSIGIALY 380
Cdd:COG2199 165 HAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLL-PGTDLEEAEALAERLREALEQLPFELEGKELRVTVSIGVALY 243
|
250 260 270
....*....|....*....|....*....|..
gi 727167397 381 PDHASTPQGLLHEADDAMYQAKHRYNGGWRLA 412
Cdd:COG2199 244 PEDGDSAEELLRRADLALYRAKRAGRNRVVVY 275
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
251-404 |
3.66e-53 |
|
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: 174.36 E-value: 3.66e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167397 251 ATHDSLTGLPNRAFFEGRLSRALGDIEP-PAKLAVLFIDGDRFKEVNDSYGHAAGDAVLTTIAGRIRAQLRETDLVARLG 329
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALReGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 727167397 330 GDEFAVLL--APVHGTEDVLQIADNIIDCMTQPVILpNDEAVITSLSIGIALYPDHASTPQGLLHEADDAMYQAKHR 404
Cdd:pfam00990 81 GDEFAILLpeTSLEGAQELAERIRRLLAKLKIPHTV-SGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQA 156
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
249-404 |
7.04e-50 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 165.88 E-value: 7.04e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167397 249 HRATHDSLTGLPNRAFFEGRLSRALGDIEPPAK-LAVLFIDGDRFKEVNDSYGHAAGDAVLTTIAGRIRAQLRETDLVAR 327
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSpFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 727167397 328 LGGDEFAVLLaPVHGTEDVLQIADNIIDCMTQPvILPNDEAVITSLSIGIALYPDHASTPQGLLHEADDAMYQAKHR 404
Cdd:smart00267 81 LGGDEFALLL-PETSLEEAIALAERILQQLREP-IIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKA 155
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
250-412 |
2.62e-44 |
|
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: 151.72 E-value: 2.62e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167397 250 RATHDSLTGLPNRAFFEGRLSRALGDIEPPAK-LAVLFIDGDRFKEVNDSYGHAAGDAVLTTIAGRIRAQLRETDLVARL 328
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRsFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167397 329 GGDEFAVLLaPVHGTEDVLQIADNIIDCM-TQPVILPNDEAVITSLSIGIALYPDHASTPQGLLHEADDAMYQAKHRYNG 407
Cdd:TIGR00254 81 GGEEFVVIL-PGTPLEDALSKAERLRDAInSKPIEVAGSETLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRN 159
|
....*
gi 727167397 408 GWRLA 412
Cdd:TIGR00254 160 RVVVA 164
|
|
| CHASE8 |
pfam17152 |
Periplasmic sensor domain; CHASE8 is a conserved periplasmic sensor domain found in histidine ... |
47-148 |
3.63e-40 |
|
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: 138.54 E-value: 3.63e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167397 47 LRAYADHNLHLIARSISYTVEAAVVFEDGVAAREALMLIASNEEILEARILDNKGKMLASWRHPSDSPLHGLEQMVAHWA 126
Cdd:pfam17152 1 LRRYAQQNLELLARSIAYNVEAALVFGDPAAARETLAALGAQPQIASAAVYDAQGRLFASYARPGTDPPEPLEALLARWL 80
|
90 100
....*....|....*....|..
gi 727167397 127 LPEPVILPISHGGKQVGQVWLS 148
Cdd:pfam17152 81 LPAPVLQPIVHDGERIGSVVLA 102
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
236-403 |
1.03e-32 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 128.09 E-value: 1.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167397 236 WQAHLKQENDSLAHRATHDSLTGLPNRAFFEGRLS----RALGDIEPpakLAVLFIDGDRFKEVNDSYGHAAGDAVLTTI 311
Cdd:PRK09581 277 YQDALRNNLEQSIEMAVTDGLTGLHNRRYFDMHLKnlieRANERGKP---LSLMMIDIDHFKKVNDTYGHDAGDEVLREF 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167397 312 AGRIRAQLRETDLVARLGGDEFAVLLaPVHGTEDVLQIADNI-IDCMTQPVILPNDEAVIT-SLSIGIALYPDHASTPQG 389
Cdd:PRK09581 354 AKRLRNNIRGTDLIARYGGEEFVVVM-PDTDIEDAIAVAERIrRKIAEEPFIISDGKERLNvTVSIGVAELRPSGDTIEA 432
|
170
....*....|....
gi 727167397 390 LLHEADDAMYQAKH 403
Cdd:PRK09581 433 LIKRADKALYEAKN 446
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
251-402 |
1.96e-31 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 126.33 E-value: 1.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167397 251 ATHDSLTGLPNRAFFEGRLSRALgDIEPPAKLAVLFIDGDRFKEVNDSYGHAAGDAVLTTIAGRIRAQLRETDLVARLGG 330
Cdd:PRK10060 237 ANTDSITGLPNRNAIQELIDHAI-NAADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQTLARLGG 315
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 727167397 331 DEFAVLLApvHGTEDVLQ-IADNIIDCMTQPVILPNDEaVITSLSIGIALYPDHASTPQGLLHEADDAMYQAK 402
Cdd:PRK10060 316 DEFLVLAS--HTSQAALEaMASRILTRLRLPFRIGLIE-VYTGCSIGIALAPEHGDDSESLIRSADTAMYTAK 385
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
247-403 |
3.00e-31 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 126.71 E-value: 3.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167397 247 LAHRATHDSLTGLPNRAFFEGRLSRALGD-IEPPAKLAVLFIDGDRFKEVNDSYGHAAGDAVLTTIAGRIRAQLRETDLV 325
Cdd:PRK09776 661 LSYSASHDALTHLANRASFEKQLRRLLQTvNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSDVL 740
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 727167397 326 ARLGGDEFAVLLaPVHGTEDVLQIADNIIDCMTQPVILPNDEAVITSLSIGIALYPDHASTPQGLLHEADDAMYQAKH 403
Cdd:PRK09776 741 ARLGGDEFGLLL-PDCNVESARFIATRIISAINDYHFPWEGRVYRVGASAGITLIDANNHQASEVMSQADIACYAAKN 817
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
216-402 |
8.43e-28 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 111.31 E-value: 8.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167397 216 IAELHELSNDFNGLLDELEAWQAHLKQ-ENDSLAHRATHDSLTGLPNRAFFEGRLSRALGDIEPpAKLAVLFIDGDRFKE 294
Cdd:PRK09894 93 IVEGHWQDAHFDAFQEGLLSFTAALTDyKIYLLTIRSNMDVLTGLPGRRVLDESFDHQLRNREP-QNLYLALLDIDRFKL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167397 295 VNDSYGHAAGDAVLTTIAGRIRAQLRETDLVARLGGDEFAVLLaPVHGTEDVLQIADNI-IDCMTQPVILPNDEAVITSl 373
Cdd:PRK09894 172 VNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGGEEFIICL-KAATDEEACRAGERIrQLIANHAITHSDGRINITA- 249
|
170 180 190
....*....|....*....|....*....|
gi 727167397 374 SIGIA-LYPDHasTPQGLLHEADDAMYQAK 402
Cdd:PRK09894 250 TFGVSrAFPEE--TLDVVIGRADRAMYEGK 277
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
246-404 |
9.37e-27 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 112.42 E-value: 9.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167397 246 SLAHRATHDSLTGLPNR-AFFEgrLSRALG-----DIEPpakLAVLFIDGDRFKEVNDSYGHAAGDAVLTTIAGRIRAQL 319
Cdd:PRK15426 393 SLQWQAWHDPLTRLYNRgALFE--KARALAkrcqrDQQP---FSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSL 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167397 320 RETDLVARLGGDEFAVLLaPVHGTEDVLQIADNI---IDCmtQPVILPNDEAVITSLSIGIA-LYPDHASTPQGLLHEAD 395
Cdd:PRK15426 468 RAQDVAGRVGGEEFCVVL-PGASLAEAAQVAERIrlrINE--KEILVAKSTTIRISASLGVSsAEEDGDYDFEQLQSLAD 544
|
....*....
gi 727167397 396 DAMYQAKHR 404
Cdd:PRK15426 545 RRLYLAKQA 553
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
254-409 |
4.90e-21 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 95.61 E-value: 4.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167397 254 DSLTGLPNRAFFEGRLSRALGdiePPAKLAVLFIDGDRFKEVNDSYGHAAGDAVLTTIAGRIRAQLRETDLVARLGGDEF 333
Cdd:PRK11359 379 DPLTGLPNRNNLHNYLDDLVD---KAVSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGTQF 455
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 727167397 334 aVLLAPVHGTEDVLQIADNIIDCMTQPVILpNDEAVITSLSIGIALypDHASTPQGLLHEADDAMYQAKHRYNGGW 409
Cdd:PRK11359 456 -VLVSLENDVSNITQIADELRNVVSKPIMI-DDKPFPLTLSIGISY--DVGKNRDYLLSTAHNAMDYIRKNGGNGW 527
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
233-402 |
1.08e-14 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 74.87 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167397 233 LEAWQAH-----LKQENDSLAHRATHDSLTGLPNRAFFEGRLSRALGDIEPPAKLA-VLFIDGDRFKEVNDSYGHAAGDA 306
Cdd:PRK10245 182 LFAWVSYqtatkLAEHKRRLQVMSTRDGMTGVYNRRHWETLLRNEFDNCRRHHRDAtLLIIDIDHFKSINDTWGHDVGDE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167397 307 VLTTIAGRIRAQLRETDLVARLGGDEFAVLLApvhGTEdvlqiADNIIDCMTQ------PVILPNDEAVITSLSIGIALY 380
Cdd:PRK10245 262 AIVALTRQLQITLRGSDVIGRFGGDEFAVIMS---GTP-----AESAITAMSRvheglnTLRLPNAPQVTLRISVGVAPL 333
|
170 180
....*....|....*....|..
gi 727167397 381 PDHASTPQGLLHEADDAMYQAK 402
Cdd:PRK10245 334 NPQMSHYREWLKSADLALYKAK 355
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
113-403 |
2.31e-12 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 68.82 E-value: 2.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167397 113 SPLHGLEQMVAHwalPEPVilpishggkqvGQVWLSGNGGSLLRFLLRGLVGMIAC-MVLSTLCALVLSRRMLVGIVSSL 191
Cdd:PRK11829 111 VPLYALERVPAN---PQPL-----------AHLVLRADSFRMYQFILSALSAMLSTyLLLALVLSVSIAWCINRLIIHPL 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167397 192 DDIANVAHAVRRDRTFGLRVPSAPiaelHELSNDFNGLLDELEAWQAHLKQENDSLAHRATHDSLTGLPNRAFFEGRLSR 271
Cdd:PRK11829 177 RAMAKELEDIGDHGVLHHQLTLPA----HHQDDELGVLVRNYNRNQQLLADAYADMGRISHRFPVTELPNRSLFISLLEK 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167397 272 ALGDIEPPAKLAVLFIDGDRFKEVNDSYGHAAGDAVLTTIAGRIRAQLRETDLVARLGGDEFAVLLAPVHGTEDVLQIAD 351
Cdd:PRK11829 253 EIASSTRTDHFHLLVIGIETLQEVSGAMSEAQHQQLLLTIVQRIEQCIDDSDLLAQLSKTEFAVLARGTRRSFPAMQLAR 332
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 727167397 352 NIIDCMTQPVILPNdEAVITSLSIGIALYPDHASTPQGLLHEADDAMYQAKH 403
Cdd:PRK11829 333 RIMSQVTQPLFFDE-ITLRPSASIGITRYQAQQDTAESMMRNASTAMMAAHH 383
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
237-404 |
7.49e-12 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 67.05 E-value: 7.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167397 237 QAHLKQENDSLAHRATHDSLTGLPNRAFFEGRLSRALGDiepPAKLAVLFIDGDRFKEVNDSYGHAAGDAVLTTIAGRIR 316
Cdd:PRK13561 217 QQLLQRQYEEQSRNATRFPVSDLPNKALLMALLEQVVAR---KQTTALMIITCETLRDTAGVLKEAQREILLLTLVEKLK 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167397 317 AQLRETDLVARLGGDEFAVLLAPVHGTEDVLQIADNIIDCMTQPVILPnDEAVITSLSIGIALYPDHASTPQgLLHEADD 396
Cdd:PRK13561 294 SVLSPRMVLAQISGYDFAIIANGVKEPWHAITLGQQVLTIINERLPIQ-RIQLRPSCSIGIAMFYGDLTAEQ-LYSRAIS 371
|
....*...
gi 727167397 397 AMYQAKHR 404
Cdd:PRK13561 372 AAFTARRK 379
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
284-402 |
1.69e-10 |
|
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: 58.52 E-value: 1.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167397 284 VLFIDGDRFKEVNDSYGHAAGDAVLTTIAGRIRAQLRET-DLVARLGGDEFAVLLAPVHgTEDVLQIADNIIDCMTQpvi 362
Cdd:cd07556 4 ILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSgDLKIKTIGDEFMVVSGLDH-PAAAVAFAEDMREAVSA--- 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 727167397 363 LPNDEAVITSLSIGIALYPDHA----STPQG-----LLHEADDAMYQAK 402
Cdd:cd07556 80 LNQSEGNPVRVRIGIHTGPVVVgvigSRPQYdvwgaLVNLASRMESQAK 128
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
323-402 |
1.65e-07 |
|
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate cyclase (GGDEF) domain [Signal transduction mechanisms, Transcription];
Pssm-ID: 442920 [Multi-domain] Cd Length: 179 Bit Score: 51.06 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167397 323 DLVARLGGDEFAVLLaPVHGTEDVLQIADNIIDCMTQPvilpndEAVITSLSIGIAlypdhastPQGLLHEAdDAMYQAK 402
Cdd:COG3706 116 DLVARYGGEEFAILL-PGTDLEGALAVAERIREAVAEL------PSLRVTVSIGVA--------GDSLLKRA-DALYQAR 179
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
251-409 |
5.85e-07 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 51.79 E-value: 5.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167397 251 ATHDSLTGLPNRAFFEGRLSRALGDIEPPAKLAVLF-IDGDRFKEVNDSYGHAAGDAVLTTIAGRIRAQL-RETD-LVAR 327
Cdd:PRK11059 228 AFQDAKTGLGNRLFFDNQLATLLEDQEMVGAHGVVMlIRLPDFDLLQEEWGESQVEELLFELINLLSTFVmRYPGaLLAR 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167397 328 LGGDEFAVLLaPVHGTEDVLQIAD---NIIDCMTQPVILPNDEAvitsLSIGIALYPDHASTPQgLLHEADDAMYQAKHR 404
Cdd:PRK11059 308 YSRSDFAVLL-PHRSLKEADSLASqllKAVDALPPPKMLDRDDF----LHIGICAYRSGQSTEQ-VMEEAEMALRSAQLQ 381
|
....*
gi 727167397 405 YNGGW 409
Cdd:PRK11059 382 GGNGW 386
|
|
| NtrY |
COG5000 |
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ... |
155-244 |
4.40e-04 |
|
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: 42.26 E-value: 4.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167397 155 LRFLLRGLVGMIAcmVLSTLCALVLSRRMLVGIVSSLDDIANVAHAVRRDRtFGLRVPSAPIAELHELSNDFNGLLDELE 234
Cdd:COG5000 3 LQILFLLLLLLIA--LLLLLLALWLALLLARRLTRPLRRLAEATRAVAAGD-LSVRLPVTGDDEIGELARAFNRMTDQLK 79
|
90
....*....|
gi 727167397 235 AWQAHLKQEN 244
Cdd:COG5000 80 EQREELEERR 89
|
|
| NarQ |
COG3850 |
Signal transduction histidine kinase NarQ, nitrate/nitrite-specific [Signal transduction ... |
165-354 |
3.27e-03 |
|
Signal transduction histidine kinase NarQ, nitrate/nitrite-specific [Signal transduction mechanisms];
Pssm-ID: 443059 [Multi-domain] Cd Length: 448 Bit Score: 39.48 E-value: 3.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167397 165 MIACMVLSTLCALVLSRRMLVGIVSSLDDIANVAHAVRRdRTFGLRVPSAPIAELHELSNDFNGLLDELEAWQAHLKQEN 244
Cdd:COG3850 120 ALLRLLLALLLALLLAYLLRRRIVRPLRRLTQAAERIAR-GDFDARVPVSGRDELGTLARAFNRMADELQELYAELEEEE 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167397 245 DSLAHRATHDSLTGLPNRAFFEGRLSRALGDIEPPAKLAVLFIDGDRFKEVNDSYGHAAGDAVLTTIAGRIRAQLRETDL 324
Cdd:COG3850 199 ELEAELELLALLDELLLLAALLLLLALLLALLLAALLAALLLLLLLQDALAESELLALNILAGLLELLLALLLLLLASAL 278
|
170 180 190
....*....|....*....|....*....|
gi 727167397 325 VARLGGDEFAVLLAPVHGTEDVLQIADNII 354
Cdd:COG3850 279 LLLELELLALLLELVELLALAAAEEALLLL 308
|
|
| |
