|
Name |
Accession |
Description |
Interval |
E-value |
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
60-331 |
3.63e-68 |
|
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: 214.46 E-value: 3.63e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492150616 60 WETQRMIYVSPAYEHIFGRSAGLLLADYSEWRDSIYPDDLNYAERSLSEVIEKGAVEDREYRIIRADGEVRWLSDKCFVS 139
Cdd:COG2199 1 VLLLLLLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492150616 140 HRADASQRLIVVGIA--EDITDKKHLEDELQRLATTDVLTQSSNRRHFFECAQREFELARLNGTPLAFLLLDIDDFKLVN 217
Cdd:COG2199 81 LELLLLLLALLLLLLalEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492150616 218 DTYGHQEGDTVLQRIAESGRSALRRGDLFGRIGGEEFAAVFPGCAPEMAMQIAERLQREIQRQNFQANGSTFSITASQGL 297
Cdd:COG2199 161 DTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELEGKELRVTVSIGV 240
|
250 260 270
....*....|....*....|....*....|....
gi 492150616 298 TNLGPEDQGLEALYGRADAAMYQAKRQGKNQIVL 331
Cdd:COG2199 241 ALYPEDGDSAEELLRRADLALYRAKRAGRNRVVV 274
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
172-330 |
1.69e-59 |
|
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: 188.15 E-value: 1.69e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492150616 172 TTDVLTQSSNRRHFFECAQREFELARLNGTPLAFLLLDIDDFKLVNDTYGHQEGDTVLQRIAESGRSALRRGDLFGRIGG 251
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492150616 252 EEFAAVFPGCAPEMAMQIAERLQREIqRQNFQANGSTFSITASQGLTNLGPEDQGLEALYGRADAAMYQAKRQGKNQIV 330
Cdd:cd01949 81 DEFAILLPGTDLEEAEALAERLREAI-EEPFFIDGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNRVV 158
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
171-328 |
2.04e-52 |
|
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: 170.13 E-value: 2.04e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492150616 171 ATTDVLTQSSNRRHFFECAQREFELARLNGTPLAFLLLDIDDFKLVNDTYGHQEGDTVLQRIAESGRSALRRGDLFGRIG 250
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492150616 251 GEEFAAVFPGCAPEMAMQIAERLQREIQRQN--FQANGSTFSITASQGLTNLGPEDQGLEALYGRADAAMYQAKRQGKNQ 328
Cdd:pfam00990 81 GDEFAILLPETSLEGAQELAERIRRLLAKLKipHTVSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGRNR 160
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
169-331 |
2.24e-49 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 162.42 E-value: 2.24e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492150616 169 RLATTDVLTQSSNRRHFFECAQREFELARLNGTPLAFLLLDIDDFKLVNDTYGHQEGDTVLQRIAESGRSALRRGDLFGR 248
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492150616 249 IGGEEFAAVFPGCAPEMAMQIAERLQREIqRQNFQANGSTFSITASQGLTNLGPEDQGLEALYGRADAAMYQAKRQGKNQ 328
Cdd:smart00267 81 LGGDEFALLLPETSLEEAIALAERILQQL-REPIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQ 159
|
...
gi 492150616 329 IVL 331
Cdd:smart00267 160 VAV 162
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
170-331 |
3.60e-45 |
|
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: 3.60e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492150616 170 LATTDVLTQSSNRRHFFECAQREFELARLNGTPLAFLLLDIDDFKLVNDTYGHQEGDTVLQRIAESGRSALRRGDLFGRI 249
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492150616 250 GGEEFAAVFPGCAPEMAMQIAERLQREIQRQNFQ-ANGSTFSITASQGLTNLGPEDQGLEALYGRADAAMYQAKRQGKNQ 328
Cdd:TIGR00254 81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPIEvAGSETLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRNR 160
|
...
gi 492150616 329 IVL 331
Cdd:TIGR00254 161 VVV 163
|
|
| diguan_SiaD |
NF038266 |
biofilm regulation diguanylate cyclase SiaD; |
163-329 |
1.48e-42 |
|
biofilm regulation diguanylate cyclase SiaD;
Pssm-ID: 468439 [Multi-domain] Cd Length: 252 Bit Score: 147.82 E-value: 1.48e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492150616 163 LEDELQRLATTDVLTQSSNRRHFFECAQREFELARLNGTPLAFLLLDIDDFKLVNDTYGHQEGDTVLQRIAESGRSALRR 242
Cdd:NF038266 86 LNEALREASTRDPLTGLPNRRLLMERLREEVERARRSGRPFTLAMLDVDHFKRINDRYGHEVGDRVLVEIARTLRAELRE 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492150616 243 GDLFGRIGGEEFAAVFPGCAPEMAMQIAERLQREIQRQNFQANGSTFSITASQGLTNLGPEDQGLEALYGRADAAMYQAK 322
Cdd:NF038266 166 YDLCGRWGGEEFLLLLPETGLEEAQVVLERLREAVRALAVRVGDDVLSVTASAGLAEHRPPEEGLSATLSRADQALYQAK 245
|
....*..
gi 492150616 323 RQGKNQI 329
Cdd:NF038266 246 RAGRDRV 252
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
163-330 |
3.73e-42 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 153.63 E-value: 3.73e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492150616 163 LEDELQRLATTDVLTQSSNRRHFFECAQREFELARLNGTPLAFLLLDIDDFKLVNDTYGHQEGDTVLQRIAESGRSALRR 242
Cdd:PRK15426 390 LQSSLQWQAWHDPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRA 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492150616 243 GDLFGRIGGEEFAAVFPGCAPEMAMQIAERLQREIQRQN-FQANGSTFSITASQGLTNLGPE-DQGLEALYGRADAAMYQ 320
Cdd:PRK15426 470 QDVAGRVGGEEFCVVLPGASLAEAAQVAERIRLRINEKEiLVAKSTTIRISASLGVSSAEEDgDYDFEQLQSLADRRLYL 549
|
170
....*....|
gi 492150616 321 AKRQGKNQIV 330
Cdd:PRK15426 550 AKQAGRNRVC 559
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
60-331 |
3.63e-68 |
|
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: 214.46 E-value: 3.63e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492150616 60 WETQRMIYVSPAYEHIFGRSAGLLLADYSEWRDSIYPDDLNYAERSLSEVIEKGAVEDREYRIIRADGEVRWLSDKCFVS 139
Cdd:COG2199 1 VLLLLLLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492150616 140 HRADASQRLIVVGIA--EDITDKKHLEDELQRLATTDVLTQSSNRRHFFECAQREFELARLNGTPLAFLLLDIDDFKLVN 217
Cdd:COG2199 81 LELLLLLLALLLLLLalEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492150616 218 DTYGHQEGDTVLQRIAESGRSALRRGDLFGRIGGEEFAAVFPGCAPEMAMQIAERLQREIQRQNFQANGSTFSITASQGL 297
Cdd:COG2199 161 DTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELEGKELRVTVSIGV 240
|
250 260 270
....*....|....*....|....*....|....
gi 492150616 298 TNLGPEDQGLEALYGRADAAMYQAKRQGKNQIVL 331
Cdd:COG2199 241 ALYPEDGDSAEELLRRADLALYRAKRAGRNRVVV 274
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
172-330 |
1.69e-59 |
|
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: 188.15 E-value: 1.69e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492150616 172 TTDVLTQSSNRRHFFECAQREFELARLNGTPLAFLLLDIDDFKLVNDTYGHQEGDTVLQRIAESGRSALRRGDLFGRIGG 251
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492150616 252 EEFAAVFPGCAPEMAMQIAERLQREIqRQNFQANGSTFSITASQGLTNLGPEDQGLEALYGRADAAMYQAKRQGKNQIV 330
Cdd:cd01949 81 DEFAILLPGTDLEEAEALAERLREAI-EEPFFIDGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNRVV 158
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
14-331 |
2.19e-56 |
|
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: 193.84 E-value: 2.19e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492150616 14 ITDMPAAAETLLALMHAQAEVARLSEREQLFSSLLVSVNAVLWAFDWETQRMIYVSPAYEHIFGRSAGLLLADYSEWRDS 93
Cdd:COG5001 94 LLLLALLVLLLLLLLLLALLALLAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARALLALLLLLLLALL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492150616 94 IYPDDLNYAERSLSEVIEKGAVEDREYRIIRADGEVRWLSDKCFVSHRADASQRLIVVGIAEDITDKKHLEDELQRLATT 173
Cdd:COG5001 174 LLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEERLRHLAYH 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492150616 174 DVLTQSSNRRHFFECAQREFELARLNGTPLAFLLLDIDDFKLVNDTYGHQEGDTVLQRIAESGRSALRRGDLFGRIGGEE 253
Cdd:COG5001 254 DPLTGLPNRRLFLDRLEQALARARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDE 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492150616 254 FAAVFPGCA-PEMAMQIAERLQREIqRQNFQANGSTFSITASQGLTnLGPED-QGLEALYGRADAAMYQAKRQGKNQIVL 331
Cdd:COG5001 334 FAVLLPDLDdPEDAEAVAERILAAL-AEPFELDGHELYVSASIGIA-LYPDDgADAEELLRNADLAMYRAKAAGRNRYRF 411
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
171-328 |
2.04e-52 |
|
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: 170.13 E-value: 2.04e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492150616 171 ATTDVLTQSSNRRHFFECAQREFELARLNGTPLAFLLLDIDDFKLVNDTYGHQEGDTVLQRIAESGRSALRRGDLFGRIG 250
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492150616 251 GEEFAAVFPGCAPEMAMQIAERLQREIQRQN--FQANGSTFSITASQGLTNLGPEDQGLEALYGRADAAMYQAKRQGKNQ 328
Cdd:pfam00990 81 GDEFAILLPETSLEGAQELAERIRRLLAKLKipHTVSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGRNR 160
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
169-331 |
2.24e-49 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 162.42 E-value: 2.24e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492150616 169 RLATTDVLTQSSNRRHFFECAQREFELARLNGTPLAFLLLDIDDFKLVNDTYGHQEGDTVLQRIAESGRSALRRGDLFGR 248
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492150616 249 IGGEEFAAVFPGCAPEMAMQIAERLQREIqRQNFQANGSTFSITASQGLTNLGPEDQGLEALYGRADAAMYQAKRQGKNQ 328
Cdd:smart00267 81 LGGDEFALLLPETSLEEAIALAERILQQL-REPIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQ 159
|
...
gi 492150616 329 IVL 331
Cdd:smart00267 160 VAV 162
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
170-331 |
3.60e-45 |
|
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: 3.60e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492150616 170 LATTDVLTQSSNRRHFFECAQREFELARLNGTPLAFLLLDIDDFKLVNDTYGHQEGDTVLQRIAESGRSALRRGDLFGRI 249
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492150616 250 GGEEFAAVFPGCAPEMAMQIAERLQREIQRQNFQ-ANGSTFSITASQGLTNLGPEDQGLEALYGRADAAMYQAKRQGKNQ 328
Cdd:TIGR00254 81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPIEvAGSETLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRNR 160
|
...
gi 492150616 329 IVL 331
Cdd:TIGR00254 161 VVV 163
|
|
| diguan_SiaD |
NF038266 |
biofilm regulation diguanylate cyclase SiaD; |
163-329 |
1.48e-42 |
|
biofilm regulation diguanylate cyclase SiaD;
Pssm-ID: 468439 [Multi-domain] Cd Length: 252 Bit Score: 147.82 E-value: 1.48e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492150616 163 LEDELQRLATTDVLTQSSNRRHFFECAQREFELARLNGTPLAFLLLDIDDFKLVNDTYGHQEGDTVLQRIAESGRSALRR 242
Cdd:NF038266 86 LNEALREASTRDPLTGLPNRRLLMERLREEVERARRSGRPFTLAMLDVDHFKRINDRYGHEVGDRVLVEIARTLRAELRE 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492150616 243 GDLFGRIGGEEFAAVFPGCAPEMAMQIAERLQREIQRQNFQANGSTFSITASQGLTNLGPEDQGLEALYGRADAAMYQAK 322
Cdd:NF038266 166 YDLCGRWGGEEFLLLLPETGLEEAQVVLERLREAVRALAVRVGDDVLSVTASAGLAEHRPPEEGLSATLSRADQALYQAK 245
|
....*..
gi 492150616 323 RQGKNQI 329
Cdd:NF038266 246 RAGRDRV 252
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
163-330 |
3.73e-42 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 153.63 E-value: 3.73e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492150616 163 LEDELQRLATTDVLTQSSNRRHFFECAQREFELARLNGTPLAFLLLDIDDFKLVNDTYGHQEGDTVLQRIAESGRSALRR 242
Cdd:PRK15426 390 LQSSLQWQAWHDPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRA 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492150616 243 GDLFGRIGGEEFAAVFPGCAPEMAMQIAERLQREIQRQN-FQANGSTFSITASQGLTNLGPE-DQGLEALYGRADAAMYQ 320
Cdd:PRK15426 470 QDVAGRVGGEEFCVVLPGASLAEAAQVAERIRLRINEKEiLVAKSTTIRISASLGVSSAEEDgDYDFEQLQSLADRRLYL 549
|
170
....*....|
gi 492150616 321 AKRQGKNQIV 330
Cdd:PRK15426 550 AKQAGRNRVC 559
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
162-330 |
4.05e-42 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 151.59 E-value: 4.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492150616 162 HLEDELQR---LATTDVLTQSSNRRHFFECAQREFELARLNGTPLAFLLLDIDDFKLVNDTYGHQEGDTVLQRIAESGRS 238
Cdd:PRK09581 280 ALRNNLEQsieMAVTDGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRN 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492150616 239 ALRRGDLFGRIGGEEFAAVFPGCAPEMAMQIAERLQREIQRQNFQ-ANGST-FSITASQGLTNLGPEDQGLEALYGRADA 316
Cdd:PRK09581 360 NIRGTDLIARYGGEEFVVVMPDTDIEDAIAVAERIRRKIAEEPFIiSDGKErLNVTVSIGVAELRPSGDTIEALIKRADK 439
|
170
....*....|....
gi 492150616 317 AMYQAKRQGKNQIV 330
Cdd:PRK09581 440 ALYEAKNTGRNRVV 453
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
167-331 |
3.06e-37 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 134.81 E-value: 3.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492150616 167 LQRLATTDVLTQSSNRRHFFECAQREfeLARLNGTPLAFLLLDIDDFKLVNDTYGHQEGDTVLQRIAESGRSALRRGDLF 246
Cdd:PRK09894 125 LTIRSNMDVLTGLPGRRVLDESFDHQ--LRNREPQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETV 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492150616 247 GRIGGEEFAAVFPGCAPEMAMQIAERLQREIQRQNFQANGSTFSITASQGLTNLGPeDQGLEALYGRADAAMYQAKRQGK 326
Cdd:PRK09894 203 YRYGGEEFIICLKAATDEEACRAGERIRQLIANHAITHSDGRINITATFGVSRAFP-EETLDVVIGRADRAMYEGKQTGR 281
|
....*
gi 492150616 327 NQIVL 331
Cdd:PRK09894 282 NRVMF 286
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
155-329 |
3.58e-25 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 106.30 E-value: 3.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492150616 155 EDITDKKHLEDELQRLATTDVLTQSSNRRHFFECAQREFELARLNGTPLAFLLLDIDDFKLVNDTYGHQEGDTVLQRIAE 234
Cdd:PRK09776 649 QDVTESRKMLRQLSYSASHDALTHLANRASFEKQLRRLLQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELAS 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492150616 235 SGRSALRRGDLFGRIGGEEFAAVFPGCAPEMAMQIAERLQREIQRQNFQANGSTFSITASQGLTNLGPEDQGLEALYGRA 314
Cdd:PRK09776 729 LMLSMLRSSDVLARLGGDEFGLLLPDCNVESARFIATRIISAINDYHFPWEGRVYRVGASAGITLIDANNHQASEVMSQA 808
|
170
....*....|....*
gi 492150616 315 DAAMYQAKRQGKNQI 329
Cdd:PRK09776 809 DIACYAAKNAGRGRV 823
|
|
| PAS_3 |
pfam08447 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
66-154 |
8.24e-22 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.
Pssm-ID: 430001 [Multi-domain] Cd Length: 89 Bit Score: 87.78 E-value: 8.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492150616 66 IYVSPAYEHIFGRSAGLLLADYSEWRDSIYPDDLNYAERSLSEVIEKGAVEDREYRIIRADGEVRWLSDKCFVsHRADAS 145
Cdd:pfam08447 2 IYWSPRFEEILGYTPEELLGKGESWLDLVHPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARP-IRDENG 80
|
....*....
gi 492150616 146 QRLIVVGIA 154
Cdd:pfam08447 81 KPVRVIGVA 89
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
167-328 |
2.64e-21 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 92.97 E-value: 2.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492150616 167 LQRLATTDVLTQSSNRRHFFECAQREFELARLNGTPLAFLLLDIDDFKLVNDTYGHQEGDTVLQRIAESGRSALRRGDLF 246
Cdd:PRK10245 201 LQVMSTRDGMTGVYNRRHWETLLRNEFDNCRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSDVI 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492150616 247 GRIGGEEFAAVFPGCAPEMAMQIAERLQREIQRQNFqANGSTFSITASQGLTNLGPEDQGLEALYGRADAAMYQAKRQGK 326
Cdd:PRK10245 281 GRFGGDEFAVIMSGTPAESAITAMSRVHEGLNTLRL-PNAPQVTLRISVGVAPLNPQMSHYREWLKSADLALYKAKNAGR 359
|
..
gi 492150616 327 NQ 328
Cdd:PRK10245 360 NR 361
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
146-328 |
4.37e-20 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 90.90 E-value: 4.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492150616 146 QRLIVVGIaeDITDKKHLEDELQRLATTDVLTQSSNRRHFFECAQREfeLARLNGTPLAFLLLDIDDFKLVNDTYGHQEG 225
Cdd:PRK10060 214 IFLICSGT--DITEERRAQERLRILANTDSITGLPNRNAIQELIDHA--INAADNNQVGIVYLDLDNFKKVNDAYGHMFG 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492150616 226 DTVLQRIAESGRSALRRGDLFGRIGGEEFAAVFP-GCAPE---MAMQIAERLqreiqRQNFQANGSTFSITASQGLTnLG 301
Cdd:PRK10060 290 DQLLQDVSLAILSCLEEDQTLARLGGDEFLVLAShTSQAAleaMASRILTRL-----RLPFRIGLIEVYTGCSIGIA-LA 363
|
170 180
....*....|....*....|....*...
gi 492150616 302 PED-QGLEALYGRADAAMYQAKRQGKNQ 328
Cdd:PRK10060 364 PEHgDDSESLIRSADTAMYTAKEGGRGQ 391
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
202-330 |
7.74e-19 |
|
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: 81.25 E-value: 7.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492150616 202 PLAFLLLDIDDFKLVNDTYGHQEGDTVLQRIAESGRSALRR-GDLFGRIGGEEFAAVFPGCAPEMAMQIAERLQREIQRQ 280
Cdd:cd07556 1 PVTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRsGDLKIKTIGDEFMVVSGLDHPAAAVAFAEDMREAVSAL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 492150616 281 NFQA-NGSTFSITASQGLTNLG-----PEDQGLEALYGRADAAMYQAKrqgKNQIV 330
Cdd:cd07556 81 NQSEgNPVRVRIGIHTGPVVVGvigsrPQYDVWGALVNLASRMESQAK---AGQVL 133
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
137-327 |
5.91e-16 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 78.66 E-value: 5.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492150616 137 FVSHRADASQRLIVVGIaEDITDKKHLEdelqRLATTDVLTQSSNRRHFfecaQREFELARLNGTPLAFLLLDIDDFKLV 216
Cdd:PRK11359 347 FIERVADISQHLAALAL-EQEKSRQHIE----QLIQFDPLTGLPNRNNL----HNYLDDLVDKAVSPVVYLIGVDHFQDV 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492150616 217 NDTYGHQEGDTVLQRIAESGRSALRRGDLFGRIGGEEFAAVFPGCAPEMAMQIAERLQReIQRQNFQANGSTFSITASQG 296
Cdd:PRK11359 418 IDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGTQFVLVSLENDVSNITQIADELRN-VVSKPIMIDDKPFPLTLSIG 496
|
170 180 190
....*....|....*....|....*....|.
gi 492150616 297 LTNLGPEDQglEALYGRADAAMYQAKRQGKN 327
Cdd:PRK11359 497 ISYDVGKNR--DYLLSTAHNAMDYIRKNGGN 525
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
32-254 |
1.50e-15 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 75.06 E-value: 1.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492150616 32 AEVARLSEREQLFSSLLVSVNAVLWAFDwETQRMIYVSPAYEHIFGRSAGLLLAdySEWRDSIYPDDLNYAERSLSEVIE 111
Cdd:COG2202 1 TAEEALEESERRLRALVESSPDAIIITD-LDGRILYVNPAFERLTGYSAEELLG--KTLRDLLPPEDDDEFLELLRAALA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492150616 112 KGAVEDREYRIIRADGEVRWLSDKcfVSHRADASQRLI-VVGIAEDITDKKHLEDELQRLATTDVLTQSSNRRHFFECAq 190
Cdd:COG2202 78 GGGVWRGELRNRRKDGSLFWVELS--ISPVRDEDGEITgFVGIARDITERKRAEEALRESEERLRLLVENAPDGIFVLD- 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492150616 191 REFELARLNGTPLAFLLLDIDDF--KLVNDTYGHQEGDTVLQRIAESGRSALRRGDLFGRIGGEEF 254
Cdd:COG2202 155 LDGRILYVNPAAEELLGYSPEELlgKSLLDLLHPEDRERLLELLRRLLEGGRESYELELRLKDGDG 220
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
166-324 |
1.88e-15 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 76.58 E-value: 1.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492150616 166 ELQRLATTDVLTQSSNRRHFFECAQREFELARLNGTPlAFLLLDIDDFKLVNDTYGHQEGDTVL----QRIAESGRSalr 241
Cdd:PRK09966 243 QLLRTALHDPLTGLANRAAFRSGINTLMNNSDARKTS-ALLFLDGDNFKYINDTWGHATGDRVLieiaKRLAEFGGL--- 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492150616 242 RGDLFgRIGGEEFAAVFPGCAPEMAMQ-IAERLQREIQRQNFQANGSTFSITASQGLTnLGPEDQGLEALYGRADAAMYQ 320
Cdd:PRK09966 319 RHKAY-RLGGDEFAMVLYDVQSESEVQqICSALTQIFNLPFDLHNGHQTTMTLSIGYA-MTIEHASAEKLQELADHNMYQ 396
|
....
gi 492150616 321 AKRQ 324
Cdd:PRK09966 397 AKHQ 400
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
31-167 |
2.42e-12 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 65.82 E-value: 2.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492150616 31 QAEvARLSEREQLFSSLLVSVNAVLWAFDwETQRMIYVSPAYEHIFGRSAGLLLAdySEWRDSIYPDDLNYAERSLSEVI 110
Cdd:COG2202 127 RAE-EALRESEERLRLLVENAPDGIFVLD-LDGRILYVNPAAEELLGYSPEELLG--KSLLDLLHPEDRERLLELLRRLL 202
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 492150616 111 EKGA-VEDREYRIIRADGEVRWLSDKcfVSHRADASQRLIVVGIAEDITDKKHLEDEL 167
Cdd:COG2202 203 EGGReSYELELRLKDGDGRWVWVEAS--AVPLRDGGEVIGVLGIVRDITERKRAEEAL 258
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
244-322 |
1.58e-11 |
|
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: 62.23 E-value: 1.58e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492150616 244 DLFGRIGGEEFAAVFPGCAPEMAMQIAERLQREIQRQNfqangsTFSITASQGLTNlgpedqglEALYGRADaAMYQAK 322
Cdd:COG3706 116 DLVARYGGEEFAILLPGTDLEGALAVAERIREAVAELP------SLRVTVSIGVAG--------DSLLKRAD-ALYQAR 179
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
37-178 |
1.76e-11 |
|
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 444511 [Multi-domain] Cd Length: 489 Bit Score: 64.61 E-value: 1.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492150616 37 LSEREQLFSSLLVSVNAVLWAFDwETQRMIYVSPAYEHIFGRSAGLLLADYSEwrDSIYPDDLNYAERSLSEVIEKGAVE 116
Cdd:COG5809 136 LRESEEKFRLIFNHSPDGIIVTD-LDGRIIYANPAACKLLGISIEELIGKSIL--ELIHSDDQENVAAFISQLLKDGGIA 212
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492150616 117 DREYRIIRADGEVRWLSDKCFVSHraDASQRLIVVGIAEDITDKKHLEDELQRLATTDVLTQ 178
Cdd:COG5809 213 QGEVRFWTKDGRWRLLEASGAPIK--KNGEVDGIVIIFRDITERKKLEELLRKSEKLSVVGE 272
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
40-167 |
4.32e-11 |
|
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions]
Pssm-ID: 272971 [Multi-domain] Cd Length: 124 Bit Score: 59.61 E-value: 4.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492150616 40 REQLFSSLLVSVNAVLWAFDWETqRMIYVSPAYEHIFGRSAGLLLAdySEWRDSIYPDDLNYAERSLSEVIEKGAVEDR- 118
Cdd:TIGR00229 1 SEERYRAIFESSPDAIIVIDLEG-NILYVNPAFEEIFGYSAEELIG--RNVLELIPEEDREEVRERIERRLEGEPEPVSe 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 492150616 119 EYRIIRADGEVRWLSDkcFVSHRADASQRLIVVGIAEDITDKKHLEDEL 167
Cdd:TIGR00229 78 ERRVRRKDGSEIWVEV--SVSPIRTNGGELGVVGIVRDITERKEAEEAL 124
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
36-171 |
8.31e-11 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 62.17 E-value: 8.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492150616 36 RLSEREQLFSSLLVSVNAVLWAFDwETQRMIYVSPAYEHIFGRSAGLLL-ADYSEwrdsIYPDDLNYAERsLSEVIEKG- 113
Cdd:COG3852 1 ALRESEELLRAILDSLPDAVIVLD-ADGRITYVNPAAERLLGLSAEELLgRPLAE----LFPEDSPLREL-LERALAEGq 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 492150616 114 AVEDREYRIIRADGEVRWLSdkCFVSHRADASQRLIVVGIAEDITDKKHLEDELQRLA 171
Cdd:COG3852 75 PVTEREVTLRRKDGEERPVD--VSVSPLRDAEGEGGVLLVLRDITERKRLERELRRAE 130
|
|
| KinA |
COG5805 |
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ... |
37-178 |
4.60e-09 |
|
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 444507 [Multi-domain] Cd Length: 496 Bit Score: 57.43 E-value: 4.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492150616 37 LSEREQLFSSLLVSVNAVLWAFDWEtQRMIYVSPAYEHIFGRSAGLLLAD-YSEWRDSIYPDDLNYAERSLSEVIEKGAV 115
Cdd:COG5805 152 LQEQEERLQTLIENSPDLICVIDTD-GRILFINESIERLFGAPREELIGKnLLELLHPCDKEEFKERIESITEVWQEFII 230
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492150616 116 EdreYRIIRADGEVRWLSDKCfVSHRADASQRLIVVGIAEDITDKKHLEDELQRLATTDVLTQ 178
Cdd:COG5805 231 E---REIITKDGRIRYFEAVI-VPLIDTDGSVKGILVILRDITEKKEAEELMARSEKLSIAGQ 289
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
64-157 |
2.91e-07 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.
Pssm-ID: 238075 [Multi-domain] Cd Length: 103 Bit Score: 48.01 E-value: 2.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492150616 64 RMIYVSPAYEHIFGRSAGLLLAdySEWRDSIYPDDLNYAERSLSEVIEKGAVEDREYRIIRADGEVRWLSDkCFVSHRAD 143
Cdd:cd00130 13 RILYANPAAEQLLGYSPEELIG--KSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLV-SLTPIRDE 89
|
90
....*....|....
gi 492150616 144 ASQRLIVVGIAEDI 157
Cdd:cd00130 90 GGEVIGLLGVVRDI 103
|
|
| PRK13560 |
PRK13560 |
hypothetical protein; Provisional |
27-168 |
1.62e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 106506 [Multi-domain] Cd Length: 807 Bit Score: 49.67 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492150616 27 LMHAQAEVARLSEREQLFSSL----LVSVNAVLWAFDWETQRMIYVSPAYEHI--FGRSAGLLLADYSEWRDSIYPDDLN 100
Cdd:PRK13560 452 IIGAIALLVDITERKQVEEQLllanLIVENSPLVLFRWKAEEGWPVELVSKNItqFGYEPDEFISGKRMFAAIIHPADLE 531
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492150616 101 YAERSLSEVIEKGAveDR---EYRIIRADGEVRWLSDKCFVsHRADASQRLIVVGIAEDITDKKHLEDELQ 168
Cdd:PRK13560 532 QVAAEVAEFAAQGV--DRfeqEYRILGKGGAVCWIDDQSAA-ERDEEGQISHFEGIVIDISERKHAEEKIK 599
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
165-329 |
8.17e-06 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 47.40 E-value: 8.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492150616 165 DELQRLATTDVLTQSSNRRHFFecAQREFELARlnGTPLAFLLLDIDDFKLVNDTYGHQEGDTVLQRIAESGRSALRRGD 244
Cdd:PRK13561 225 EEQSRNATRFPVSDLPNKALLM--ALLEQVVAR--KQTTALMIITCETLRDTAGVLKEAQREILLLTLVEKLKSVLSPRM 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492150616 245 LFGRIGGEEFAAVFPGCA-PEMAMQIAERLQREI-QRQNFQanGSTFSITASQGLTnLGPEDQGLEALYGRADAAMYQAK 322
Cdd:PRK13561 301 VLAQISGYDFAIIANGVKePWHAITLGQQVLTIInERLPIQ--RIQLRPSCSIGIA-MFYGDLTAEQLYSRAISAAFTAR 377
|
....*..
gi 492150616 323 RQGKNQI 329
Cdd:PRK13561 378 RKGKNQI 384
|
|
| PAC |
smart00086 |
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ... |
117-160 |
1.08e-03 |
|
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif occurs C-terminal to a subset of all known PAS motifs. It is proposed to contribute to the PAS domain fold.
Pssm-ID: 197509 Cd Length: 43 Bit Score: 36.39 E-value: 1.08e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 492150616 117 DREYRIIRADGEVRWLsDKCFVSHRADASQRLIVVGIAEDITDK 160
Cdd:smart00086 1 TVEYRLRRKDGSYIWV-LVSASPIRDEDGEVEGILGVVRDITER 43
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
227-331 |
2.22e-03 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 39.93 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492150616 227 TVLQRIAESGRSAlrrgDLFGRIGGEEFAAVFPGCA-PEMAMQIAERLQREIQRQNFQANgSTFSITASQGLTNLGPEDQ 305
Cdd:PRK11829 291 TIVQRIEQCIDDS----DLLAQLSKTEFAVLARGTRrSFPAMQLARRIMSQVTQPLFFDE-ITLRPSASIGITRYQAQQD 365
|
90 100
....*....|....*....|....*.
gi 492150616 306 GLEALYGRADAAMYQAKRQGKNQIVL 331
Cdd:PRK11829 366 TAESMMRNASTAMMAAHHEGRNQIMV 391
|
|
| |
