|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
2-408 |
0e+00 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 806.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891751 2 MDNDNSLHKRPTFKRALRNISMTSIFITMTLIWLLLSVTSVLTLKQYAQKNLALTAATMTYSLEAAVVFADGPAATETLA 81
Cdd:PRK09966 1 MDNDNSLNKRPTFKRALRNISMTSIFITMMLIWLLLSVTSVLTLKQYAQKNLALTAATMTYSLEAAVVFADGPAATETLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891751 82 ALGQQGQFSTAEVRDKQQNILASWHYTHKEPGDTFSNFISHWLFPAPIIQPIRHNGETIGEVRLTARDSSISHFIWFSLA 161
Cdd:PRK09966 81 ALGQQGQFSTAEVRDKQQNILASWHYTRKDPGDTFSNFISHWLFPAPIIQPIRHNGETIGEVRLTARDSSISHFIWFSLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891751 162 VLTGCILLASGIAITLTRHLHNGLVEALKNITDVVHDVRSNRNFSRRVSEERIAEFHRFALDFNSLLDEMEEWQLRLQAK 241
Cdd:PRK09966 161 VLTGCILLASGIAITLTRHLHNGLVEALKNITDVVHDVRSNRNFSRRVSEERIAEFHRFALDFNSLLDEMEEWQLRLQAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891751 242 NAQLLRTALHDPLTGLANRAAFRSGINTLMNNSDARKTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRH 321
Cdd:PRK09966 241 NAQLLRTALHDPLTGLANRAAFRSGINTLMNNSDARKTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891751 322 KAYRLGGDEFAMVLYDVQSESEVQQICSALTQIFNLPFDLHNGHQTTMTLSIGYAMTIEHASAENLQELADHNMYQAKHQ 401
Cdd:PRK09966 321 KAYRLGGDEFAMVLYDVQSESEVQQICSALTQIFNLPFDLHNGHQTTMTLSIGYAMTIEHASAEKLQELADHNMYQAKHQ 400
|
....*..
gi 446891751 402 RAEKLVR 408
Cdd:PRK09966 401 RAEKLVR 407
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
249-401 |
2.38e-50 |
|
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: 167.04 E-value: 2.38e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891751 249 ALHDPLTGLANRAAFRSGINTLMNNSDARKTS-ALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHKAYRLG 327
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPvAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446891751 328 GDEFAMVLYDVQSES--EVQQICSALTQIFNLPFDlHNGHQTTMTLSIGYAMTIEHA-SAENLQELADHNMYQAKHQ 401
Cdd:pfam00990 81 GDEFAILLPETSLEGaqELAERIRRLLAKLKIPHT-VSGLPLYVTISIGIAAYPNDGeDPEDLLKRADTALYQAKQA 156
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
247-401 |
1.41e-45 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 154.71 E-value: 1.41e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891751 247 RTALHDPLTGLANRAAFRSGINTLMNNSDARKTS-ALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHKAYR 325
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPfALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446891751 326 LGGDEFAMVLYDVqSESEVQQICSALTQIFNLPFDLHnGHQTTMTLSIGYAMTIEHA-SAENLQELADHNMYQAKHQ 401
Cdd:smart00267 81 LGGDEFALLLPET-SLEEAIALAERILQQLREPIIIH-GIPLYLTISIGVAAYPNPGeDAEDLLKRADTALYQAKKA 155
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
134-401 |
2.33e-45 |
|
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: 166.10 E-value: 2.33e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891751 134 RHNGETIGEVRLTARDSSISHFIWFSLAVLTGCILLASGIAITLTRHLHNGLVEALKNITDVVHDVRSNRNFSRRVSEER 213
Cdd:COG5001 133 SAALLAAALGAALLAALALALLLALARALLALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRL 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891751 214 IAEFHRFALDFNSLL---DEMEEWQLRLQAKNAQLLRTALHDPLTGLANRAAFRSGINTLMNNSDARKTS-ALLFLDGDN 289
Cdd:COG5001 213 LLGLLLLGLLLLLLLvavLAIARLITERKRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRlALLFIDLDR 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891751 290 FKYINDTWGHATGDRVLIEIAKRLAEfgGLRHKA--YRLGGDEFAMVLYDVQSESEVQQICSALTQIFNLPFDLhNGHQT 367
Cdd:COG5001 293 FKEINDTLGHAAGDELLREVARRLRA--CLREGDtvARLGGDEFAVLLPDLDDPEDAEAVAERILAALAEPFEL-DGHEL 369
|
250 260 270
....*....|....*....|....*....|....*
gi 446891751 368 TMTLSIGYAMTIEHA-SAENLQELADHNMYQAKHQ 401
Cdd:COG5001 370 YVSASIGIALYPDDGaDAEELLRNADLAMYRAKAA 404
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
250-402 |
6.55e-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: 152.71 E-value: 6.55e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891751 250 LHDPLTGLANRAAFRSGINTLMNNSDARKTS-ALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHKAYRLGG 328
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLARARRSGRPlALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446891751 329 DEFAMVLYDVqSESEVQQICSALTQIFNLPFDLHnGHQTTMTLSIGYAMTIEHA-SAENLQELADHNMYQAKHQR 402
Cdd:cd01949 81 DEFAILLPGT-DLEEAEALAERLREAIEEPFFID-GQEIRVTASIGIATYPEDGeDAEELLRRADEALYRAKRSG 153
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
249-399 |
4.25e-29 |
|
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: 111.27 E-value: 4.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891751 249 ALHDPLTGLANRAAFRSGINTLMNNSDA-RKTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEfgGLRHKAY--R 325
Cdd:TIGR00254 2 AVRDPLTGLYNRRYLEEMLDSELKRARRfQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQS--SVRGSDVvgR 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446891751 326 LGGDEFAMVLYDVQSESEVQQICSALTQIFNLPFDLHNGHQTTMTLSIGYAMTIEHA-SAENLQELADHNMYQAK 399
Cdd:TIGR00254 80 YGGEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSETLTVTVSIGVACYPGHGlTLEELLKRADEALYQAK 154
|
|
| diguan_DgcJ |
NF040885 |
diguanylate cyclase DgcJ; |
227-402 |
3.06e-11 |
|
diguanylate cyclase DgcJ;
Pssm-ID: 468821 [Multi-domain] Cd Length: 490 Bit Score: 64.98 E-value: 3.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891751 227 LLDEMEEWQLRLqakNAQLLRTALHDPLTGLANR----AAFRSGINTLMnnsdaRKTSALLF--LDGDNFKYINDTWGHA 300
Cdd:NF040885 322 LLLHLVRMHFRL---YHNVSRENISDSMTGLYNRkiltPTLEQRLQRLT-----EKGIPVTFiaLDCDKLKHINDTLGHH 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891751 301 TGDRVLIEIAKRLAEfgGLRHKAY--RLGGDEFAMVLYDVqSESEVQQ----ICSALTQIfnlpfdlhnGHQTTMTLSIG 374
Cdd:NF040885 394 EGDRAITLLAQAISA--SIRKSDYgiRLGGDEFCIILIDY-EEAEAQNlierIRQHLRTI---------DPDKRVSFSWG 461
|
170 180 190
....*....|....*....|....*....|...
gi 446891751 375 -YAM----TIEHAsaenlQELADHNMYQAKHQR 402
Cdd:NF040885 462 aYQMqpgdTLDDA-----YKAADERLYLNKKQK 489
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
2-408 |
0e+00 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 806.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891751 2 MDNDNSLHKRPTFKRALRNISMTSIFITMTLIWLLLSVTSVLTLKQYAQKNLALTAATMTYSLEAAVVFADGPAATETLA 81
Cdd:PRK09966 1 MDNDNSLNKRPTFKRALRNISMTSIFITMMLIWLLLSVTSVLTLKQYAQKNLALTAATMTYSLEAAVVFADGPAATETLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891751 82 ALGQQGQFSTAEVRDKQQNILASWHYTHKEPGDTFSNFISHWLFPAPIIQPIRHNGETIGEVRLTARDSSISHFIWFSLA 161
Cdd:PRK09966 81 ALGQQGQFSTAEVRDKQQNILASWHYTRKDPGDTFSNFISHWLFPAPIIQPIRHNGETIGEVRLTARDSSISHFIWFSLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891751 162 VLTGCILLASGIAITLTRHLHNGLVEALKNITDVVHDVRSNRNFSRRVSEERIAEFHRFALDFNSLLDEMEEWQLRLQAK 241
Cdd:PRK09966 161 VLTGCILLASGIAITLTRHLHNGLVEALKNITDVVHDVRSNRNFSRRVSEERIAEFHRFALDFNSLLDEMEEWQLRLQAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891751 242 NAQLLRTALHDPLTGLANRAAFRSGINTLMNNSDARKTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRH 321
Cdd:PRK09966 241 NAQLLRTALHDPLTGLANRAAFRSGINTLMNNSDARKTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891751 322 KAYRLGGDEFAMVLYDVQSESEVQQICSALTQIFNLPFDLHNGHQTTMTLSIGYAMTIEHASAENLQELADHNMYQAKHQ 401
Cdd:PRK09966 321 KAYRLGGDEFAMVLYDVQSESEVQQICSALTQIFNLPFDLHNGHQTTMTLSIGYAMTIEHASAEKLQELADHNMYQAKHQ 400
|
....*..
gi 446891751 402 RAEKLVR 408
Cdd:PRK09966 401 RAEKLVR 407
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
249-401 |
2.38e-50 |
|
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: 167.04 E-value: 2.38e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891751 249 ALHDPLTGLANRAAFRSGINTLMNNSDARKTS-ALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHKAYRLG 327
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPvAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446891751 328 GDEFAMVLYDVQSES--EVQQICSALTQIFNLPFDlHNGHQTTMTLSIGYAMTIEHA-SAENLQELADHNMYQAKHQ 401
Cdd:pfam00990 81 GDEFAILLPETSLEGaqELAERIRRLLAKLKIPHT-VSGLPLYVTISIGIAAYPNDGeDPEDLLKRADTALYQAKQA 156
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
247-401 |
1.41e-45 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 154.71 E-value: 1.41e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891751 247 RTALHDPLTGLANRAAFRSGINTLMNNSDARKTS-ALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHKAYR 325
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPfALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446891751 326 LGGDEFAMVLYDVqSESEVQQICSALTQIFNLPFDLHnGHQTTMTLSIGYAMTIEHA-SAENLQELADHNMYQAKHQ 401
Cdd:smart00267 81 LGGDEFALLLPET-SLEEAIALAERILQQLREPIIIH-GIPLYLTISIGVAAYPNPGeDAEDLLKRADTALYQAKKA 155
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
134-401 |
2.33e-45 |
|
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: 166.10 E-value: 2.33e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891751 134 RHNGETIGEVRLTARDSSISHFIWFSLAVLTGCILLASGIAITLTRHLHNGLVEALKNITDVVHDVRSNRNFSRRVSEER 213
Cdd:COG5001 133 SAALLAAALGAALLAALALALLLALARALLALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRL 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891751 214 IAEFHRFALDFNSLL---DEMEEWQLRLQAKNAQLLRTALHDPLTGLANRAAFRSGINTLMNNSDARKTS-ALLFLDGDN 289
Cdd:COG5001 213 LLGLLLLGLLLLLLLvavLAIARLITERKRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRlALLFIDLDR 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891751 290 FKYINDTWGHATGDRVLIEIAKRLAEfgGLRHKA--YRLGGDEFAMVLYDVQSESEVQQICSALTQIFNLPFDLhNGHQT 367
Cdd:COG5001 293 FKEINDTLGHAAGDELLREVARRLRA--CLREGDtvARLGGDEFAVLLPDLDDPEDAEAVAERILAALAEPFEL-DGHEL 369
|
250 260 270
....*....|....*....|....*....|....*
gi 446891751 368 TMTLSIGYAMTIEHA-SAENLQELADHNMYQAKHQ 401
Cdd:COG5001 370 YVSASIGIALYPDDGaDAEELLRNADLAMYRAKAA 404
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
143-401 |
5.10e-45 |
|
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: 157.06 E-value: 5.10e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891751 143 VRLTARDSSISHFIWFSLAVLTGCILLASGIAITLTRHLHNGLVEALKNITDVVHDVRSNRNFSRRVSEERIAEFHRFAL 222
Cdd:COG2199 9 LALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891751 223 DFNSLLDEMEEwQLRLQAKNAQLLRTALHDPLTGLANRAAFRSGINTLMNNSDARKTS-ALLFLDGDNFKYINDTWGHAT 301
Cdd:COG2199 89 ALLLLLLALED-ITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPlALLLIDLDHFKRINDTYGHAA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891751 302 GDRVLIEIAKRLAEFGGLRHKAYRLGGDEFAMVLYDVqSESEVQQICSALTQIF-NLPFDlHNGHQTTMTLSIGYAMTIE 380
Cdd:COG2199 168 GDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGT-DLEEAEALAERLREALeQLPFE-LEGKELRVTVSIGVALYPE 245
|
250 260
....*....|....*....|..
gi 446891751 381 HA-SAENLQELADHNMYQAKHQ 401
Cdd:COG2199 246 DGdSAEELLRRADLALYRAKRA 267
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
250-402 |
6.55e-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: 152.71 E-value: 6.55e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891751 250 LHDPLTGLANRAAFRSGINTLMNNSDARKTS-ALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHKAYRLGG 328
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLARARRSGRPlALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446891751 329 DEFAMVLYDVqSESEVQQICSALTQIFNLPFDLHnGHQTTMTLSIGYAMTIEHA-SAENLQELADHNMYQAKHQR 402
Cdd:cd01949 81 DEFAILLPGT-DLEEAEALAERLREAIEEPFFID-GQEIRVTASIGIATYPEDGeDAEELLRRADEALYRAKRSG 153
|
|
| CHASE8 |
pfam17152 |
Periplasmic sensor domain; CHASE8 is a conserved periplasmic sensor domain found in histidine ... |
45-146 |
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 446891751 45 LKQYAQKNLALTAATMTYSLEAAVVFADGPAATETLAALGQQGQFSTAEVRDKQQNILASWHYTHKEPGDTFSNFISHWL 124
Cdd:pfam17152 1 LRRYAQQNLELLARSIAYNVEAALVFGDPAAARETLAALGAQPQIASAAVYDAQGRLFASYARPGTDPPEPLEALLARWL 80
|
90 100
....*....|....*....|..
gi 446891751 125 FPAPIIQPIRHNGETIGEVRLT 146
Cdd:pfam17152 81 LPAPVLQPIVHDGERIGSVVLA 102
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
249-399 |
4.25e-29 |
|
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: 111.27 E-value: 4.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891751 249 ALHDPLTGLANRAAFRSGINTLMNNSDA-RKTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEfgGLRHKAY--R 325
Cdd:TIGR00254 2 AVRDPLTGLYNRRYLEEMLDSELKRARRfQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQS--SVRGSDVvgR 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446891751 326 LGGDEFAMVLYDVQSESEVQQICSALTQIFNLPFDLHNGHQTTMTLSIGYAMTIEHA-SAENLQELADHNMYQAK 399
Cdd:TIGR00254 80 YGGEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSETLTVTVSIGVACYPGHGlTLEELLKRADEALYQAK 154
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
249-400 |
3.94e-23 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 100.75 E-value: 3.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891751 249 ALHDPLTGLANRAAFRSGINTLMNNSDAR-KTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEfgGLR--HKAYR 325
Cdd:PRK09581 292 AVTDGLTGLHNRRYFDMHLKNLIERANERgKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRN--NIRgtDLIAR 369
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446891751 326 LGGDEFAMVLYDVQSESEVQQICSALTQIFNLPFDLHNG-HQTTMTLSIGYA-MTIEHASAENLQELADHNMYQAKH 400
Cdd:PRK09581 370 YGGEEFVVVMPDTDIEDAIAVAERIRRKIAEEPFIISDGkERLNVTVSIGVAeLRPSGDTIEALIKRADKALYEAKN 446
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
249-401 |
1.85e-20 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 93.54 E-value: 1.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891751 249 ALHDPLTGLANRAAFRSGINTLMNNSDARKTS-ALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAefGGLRHK--AYR 325
Cdd:PRK15426 398 AWHDPLTRLYNRGALFEKARALAKRCQRDQQPfSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLIS--SSLRAQdvAGR 475
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446891751 326 LGGDEFAMVLYDVQSEsEVQQICSALTQIFNLPF-DLHNGHQTTMTLSIGYAMTIEHA--SAENLQELADHNMYQAKHQ 401
Cdd:PRK15426 476 VGGEEFCVVLPGASLA-EAAQVAERIRLRINEKEiLVAKSTTIRISASLGVSSAEEDGdyDFEQLQSLADRRLYLAKQA 553
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
241-399 |
2.27e-18 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 87.04 E-value: 2.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891751 241 KNAQ--LLRTALHDPLTGLANRAAFRSGINTLMNnSDARKTSALLFLDGDNFKYINDTWGHATGDRVLIEIAkrLAEFGG 318
Cdd:PRK10060 227 RRAQerLRILANTDSITGLPNRNAIQELIDHAIN-AADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVS--LAILSC 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891751 319 LRHKAY--RLGGDEFaMVLYDVQSESEVQQICSALTQIFNLPFdlHNGHQTTMT-LSIGYAMTIEHA-SAENLQELADHN 394
Cdd:PRK10060 304 LEEDQTlaRLGGDEF-LVLASHTSQAALEAMASRILTRLRLPF--RIGLIEVYTgCSIGIALAPEHGdDSESLIRSADTA 380
|
....*
gi 446891751 395 MYQAK 399
Cdd:PRK10060 381 MYTAK 385
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
212-399 |
1.11e-17 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 82.81 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891751 212 ERIAEFHRFALDFNSLLDEMEEWQLRLQAKNAQLLRTALH-DPLTGLANRAAFRSGINtlMNNSDARK-TSALLFLDGDN 289
Cdd:PRK09894 91 LAIVEGHWQDAHFDAFQEGLLSFTAALTDYKIYLLTIRSNmDVLTGLPGRRVLDESFD--HQLRNREPqNLYLALLDIDR 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891751 290 FKYINDTWGHATGDRVLIEIAKRLAEfgGLRH--KAYRLGGDEFAMVL---YDVQSESEVQQICSAltqIFNLPFdLHNG 364
Cdd:PRK09894 169 FKLVNDTYGHLIGDVVLRTLATYLAS--WTRDyeTVYRYGGEEFIICLkaaTDEEACRAGERIRQL---IANHAI-THSD 242
|
170 180 190
....*....|....*....|....*....|....*
gi 446891751 365 HQTTMTLSIGYAMTIEHASAENLQELADHNMYQAK 399
Cdd:PRK09894 243 GRINITATFGVSRAFPEETLDVVIGRADRAMYEGK 277
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
212-393 |
2.32e-17 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 84.44 E-value: 2.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891751 212 ERIAEF--HRFALDFnslldEMEEWQLRLQaknaQLLRtalHDPLTGLANRAAFRSGINTLMNNSdarKTSALLFLDGDN 289
Cdd:PRK11359 349 ERVADIsqHLAALAL-----EQEKSRQHIE----QLIQ---FDPLTGLPNRNNLHNYLDDLVDKA---VSPVVYLIGVDH 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891751 290 FKYINDTWGHATGDRVLIEIAKRLAEFGGLRHKAYRLGGDEFAMVLYDvQSESEVQQICSALTQIFNLPFDLhNGHQTTM 369
Cdd:PRK11359 414 FQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGTQFVLVSLE-NDVSNITQIADELRNVVSKPIMI-DDKPFPL 491
|
170 180
....*....|....*....|....
gi 446891751 370 TLSIGyamtIEHASAENLQELADH 393
Cdd:PRK11359 492 TLSIG----ISYDVGKNRDYLLST 511
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
244-351 |
9.55e-17 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 82.41 E-value: 9.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891751 244 QLLRTALHDPLTGLANRAAFRSGINTLMNNS-DARKTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFggLRHK 322
Cdd:PRK09776 660 QLSYSASHDALTHLANRASFEKQLRRLLQTVnSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSM--LRSS 737
|
90 100 110
....*....|....*....|....*....|.
gi 446891751 323 AY--RLGGDEFAMVLYDVQSESeVQQICSAL 351
Cdd:PRK09776 738 DVlaRLGGDEFGLLLPDCNVES-ARFIATRI 767
|
|
| diguan_DgcJ |
NF040885 |
diguanylate cyclase DgcJ; |
227-402 |
3.06e-11 |
|
diguanylate cyclase DgcJ;
Pssm-ID: 468821 [Multi-domain] Cd Length: 490 Bit Score: 64.98 E-value: 3.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891751 227 LLDEMEEWQLRLqakNAQLLRTALHDPLTGLANR----AAFRSGINTLMnnsdaRKTSALLF--LDGDNFKYINDTWGHA 300
Cdd:NF040885 322 LLLHLVRMHFRL---YHNVSRENISDSMTGLYNRkiltPTLEQRLQRLT-----EKGIPVTFiaLDCDKLKHINDTLGHH 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891751 301 TGDRVLIEIAKRLAEfgGLRHKAY--RLGGDEFAMVLYDVqSESEVQQ----ICSALTQIfnlpfdlhnGHQTTMTLSIG 374
Cdd:NF040885 394 EGDRAITLLAQAISA--SIRKSDYgiRLGGDEFCIILIDY-EEAEAQNlierIRQHLRTI---------DPDKRVSFSWG 461
|
170 180 190
....*....|....*....|....*....|...
gi 446891751 375 -YAM----TIEHAsaenlQELADHNMYQAKHQR 402
Cdd:NF040885 462 aYQMqpgdTLDDA-----YKAADERLYLNKKQK 489
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
231-399 |
1.29e-10 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 62.54 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891751 231 MEEWQLRLQAKNAQllrtalhDPLTGLANRaafRSGINTLMNNSDA----RKTSALLFLDGDNFKYINDTWGHATGDRVL 306
Cdd:PRK10245 194 LAEHKRRLQVMSTR-------DGMTGVYNR---RHWETLLRNEFDNcrrhHRDATLLIIDIDHFKSINDTWGHDVGDEAI 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891751 307 IEIAKRLAEfgGLRHKAY--RLGGDEFAMVLYDVQSESEVQQICSALTQIFNLpfDLHNGHQTTMTLSIGYA-MTIEHAS 383
Cdd:PRK10245 264 VALTRQLQI--TLRGSDVigRFGGDEFAVIMSGTPAESAITAMSRVHEGLNTL--RLPNAPQVTLRISVGVApLNPQMSH 339
|
170
....*....|....*.
gi 446891751 384 AENLQELADHNMYQAK 399
Cdd:PRK10245 340 YREWLKSADLALYKAK 355
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
282-399 |
7.87e-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: 42.34 E-value: 7.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891751 282 LLFLDGDNFKYINDTWGHATGDRVLIEIAKR----LAEFGGLRhkaYRLGGDEFAMVLYDVQSES------EVQQICSAL 351
Cdd:cd07556 4 ILFADIVGFTSLADALGPDEGDELLNELAGRfdslIRRSGDLK---IKTIGDEFMVVSGLDHPAAavafaeDMREAVSAL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 446891751 352 TQIFNLPFDLHNGHQTTMTLSIGYAMTIEHASAENLQELADHNMYQAK 399
Cdd:cd07556 81 NQSEGNPVRVRIGIHTGPVVVGVIGSRPQYDVWGALVNLASRMESQAK 128
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
323-399 |
2.29e-04 |
|
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: 41.82 E-value: 2.29e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446891751 323 AYRLGGDEFAMVLYDVqSESEVQQICSALTQIFNLPFDLHnghqttMTLSIGYAmtiehasAENLQELADhNMYQAK 399
Cdd:COG3706 118 VARYGGEEFAILLPGT-DLEGALAVAERIREAVAELPSLR------VTVSIGVA-------GDSLLKRAD-ALYQAR 179
|
|
| NtrY |
COG5000 |
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ... |
160-334 |
5.10e-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: 41.87 E-value: 5.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891751 160 LAVLTGCILLASGIAITLTRHLHNGLVEALKNITDVVHDVRSNrNFSRRVSEERIAEFHRFALDFNSLLDEMEEWQLRLQ 239
Cdd:COG5000 8 LLLLLLIALLLLLLALWLALLLARRLTRPLRRLAEATRAVAAG-DLSVRLPVTGDDEIGELARAFNRMTDQLKEQREELE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891751 240 AKNaQLLRTALHDPLTGLAnrAAFRSGINTLMNNsdarktSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGL 319
Cdd:COG5000 87 ERR-RYLETILENLPAGVI--VLDADGRITLANP------AAERLLGIPLEELIGKPLEELLPELDLAELLREALERGWQ 157
|
170
....*....|....*
gi 446891751 320 RHKAYRLGGDEFAMV 334
Cdd:COG5000 158 EEIELTRDGRRTLLV 172
|
|
| NarQ |
COG3850 |
Signal transduction histidine kinase NarQ, nitrate/nitrite-specific [Signal transduction ... |
129-315 |
7.94e-04 |
|
Signal transduction histidine kinase NarQ, nitrate/nitrite-specific [Signal transduction mechanisms];
Pssm-ID: 443059 [Multi-domain] Cd Length: 448 Bit Score: 41.41 E-value: 7.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891751 129 IIQPIRHNGETIGEVRLTARDSSISHFIWFSLAVLTGCILLASGIAITLTRHLHNGLVEALKNITDVVHDVrSNRNFSRR 208
Cdd:COG3850 86 LAALLSLLLLLLLLLLLLLLLLLLLLAAAINRKLALLRLLLALLLALLLAYLLRRRIVRPLRRLTQAAERI-ARGDFDAR 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891751 209 VSEERIAEFHRFALDFNSLLDEMEEWQLRLQAKNAQLLRTALHDPLTGLANRAAFRSGINTLMNNSDARKTSALLFLDGD 288
Cdd:COG3850 165 VPVSGRDELGTLARAFNRMADELQELYAELEEEEELEAELELLALLDELLLLAALLLLLALLLALLLAALLAALLLLLLL 244
|
170 180
....*....|....*....|....*..
gi 446891751 289 NFKYINDTWGHATGDRVLIEIAKRLAE 315
Cdd:COG3850 245 QDALAESELLALNILAGLLELLLALLL 271
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
235-401 |
4.59e-03 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 39.31 E-value: 4.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891751 235 QLRLQAKNAQLLRTALHDPLTGLANRAAFRSgintLMNNSDARK-TSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRL 313
Cdd:PRK13561 217 QQLLQRQYEEQSRNATRFPVSDLPNKALLMA----LLEQVVARKqTTALMIITCETLRDTAGVLKEAQREILLLTLVEKL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891751 314 AEFGGLRHKAYRLGGDEFAMVLYDVQSESEVQQICSALTQIFNLPFDLHnGHQTTMTLSIGYAMTIEHASAENLQELADH 393
Cdd:PRK13561 293 KSVLSPRMVLAQISGYDFAIIANGVKEPWHAITLGQQVLTIINERLPIQ-RIQLRPSCSIGIAMFYGDLTAEQLYSRAIS 371
|
....*...
gi 446891751 394 NMYQAKHQ 401
Cdd:PRK13561 372 AAFTARRK 379
|
|
| |
