|
Name |
Accession |
Description |
Interval |
E-value |
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
71-322 |
2.26e-57 |
|
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: 186.72 E-value: 2.26e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490585942 71 AALLLADYGEWRNSIYPDDLDYAAESMAKVLETGAVESREYRIIRADGQLRWLSDKCFVSPLPGVDKGSVIVGIAEDITE 150
Cdd:COG2199 23 LLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLLLLALEDITE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490585942 151 KKRLEGELHRLATTDVLTQSSNRRHFFECARREFEHARKFGSPLTFLLLDLDDFKKINDQYGHQTGDEVLRRLAQCGSNA 230
Cdd:COG2199 103 LRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRAS 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490585942 231 LRRGDLFGRIGGEEFAALFPGCEQDVALQVAERLQREVQRLSFQHEGSSFGITVSQGLTSLLATDVSLDALYARAGAAMY 310
Cdd:COG2199 183 LRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELEGKELRVTVSIGVALYPEDGDSAEELLRRADLALY 262
|
250
....*....|..
gi 2490585942 311 LAKRQGKNQIVL 322
Cdd:COG2199 263 RAKRAGRNRVVV 274
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
163-321 |
3.57e-49 |
|
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: 161.57 E-value: 3.57e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490585942 163 TTDVLTQSSNRRHFFECARREFEHARKFGSPLTFLLLDLDDFKKINDQYGHQTGDEVLRRLAQCGSNALRRGDLFGRIGG 242
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2490585942 243 EEFAALFPGCEQDVALQVAERLQREVQRLSFQHeGSSFGITVSQGLTSLLATDVSLDALYARAGAAMYLAKRQGKNQIV 321
Cdd:cd01949 81 DEFAILLPGTDLEEAEALAERLREAIEEPFFID-GQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNRVV 158
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
162-319 |
6.20e-43 |
|
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: 145.47 E-value: 6.20e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490585942 162 ATTDVLTQSSNRRHFFECARREFEHARKFGSPLTFLLLDLDDFKKINDQYGHQTGDEVLRRLAQCGSNALRRGDLFGRIG 241
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490585942 242 GEEFAALFPGCEQDVALQVAERLQREVQRLSFQHEGS--------SFGITVSQGLTSllatdvSLDALYARAGAAMYLAK 313
Cdd:pfam00990 81 GDEFAILLPETSLEGAQELAERIRRLLAKLKIPHTVSglplyvtiSIGIAAYPNDGE------DPEDLLKRADTALYQAK 154
|
....*.
gi 2490585942 314 RQGKNQ 319
Cdd:pfam00990 155 QAGRNR 160
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
160-322 |
6.00e-41 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 140.46 E-value: 6.00e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490585942 160 RLATTDVLTQSSNRRHFFECARREFEHARKFGSPLTFLLLDLDDFKKINDQYGHQTGDEVLRRLAQCGSNALRRGDLFGR 239
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490585942 240 IGGEEFAALFPGCEQDVALQVAERLQREVQRLSFQHeGSSFGITVSQGLTSLLATDVSLDALYARAGAAMYLAKRQGKNQ 319
Cdd:smart00267 81 LGGDEFALLLPETSLEEAIALAERILQQLREPIIIH-GIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQ 159
|
...
gi 2490585942 320 IVL 322
Cdd:smart00267 160 VAV 162
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
161-322 |
3.63e-37 |
|
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: 130.53 E-value: 3.63e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490585942 161 LATTDVLTQSSNRRHFFECARREFEHARKFGSPLTFLLLDLDDFKKINDQYGHQTGDEVLRRLAQCGSNALRRGDLFGRI 240
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490585942 241 GGEEFAALFPGCEQDVALQVAERLQREVQRLSFQHEGSSFG-ITVSQGLTSLLATDVSLDALYARAGAAMYLAKRQGKNQ 319
Cdd:TIGR00254 81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSETLtVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRNR 160
|
...
gi 2490585942 320 IVL 322
Cdd:TIGR00254 161 VVV 163
|
|
| diguan_SiaD |
NF038266 |
biofilm regulation diguanylate cyclase SiaD; |
158-320 |
2.90e-35 |
|
biofilm regulation diguanylate cyclase SiaD;
Pssm-ID: 468439 [Multi-domain] Cd Length: 252 Bit Score: 128.18 E-value: 2.90e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490585942 158 LHRLATTDVLTQSSNRRHFFECARREFEHARKFGSPLTFLLLDLDDFKKINDQYGHQTGDEVLRRLAQCGSNALRRGDLF 237
Cdd:NF038266 90 LREASTRDPLTGLPNRRLLMERLREEVERARRSGRPFTLAMLDVDHFKRINDRYGHEVGDRVLVEIARTLRAELREYDLC 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490585942 238 GRIGGEEFAALFPGCEQDVALQVAERLQREVQRLSFQHEGSSFGITVSQGLTSLLATDVSLDALYARAGAAMYLAKRQGK 317
Cdd:NF038266 170 GRWGGEEFLLLLPETGLEEAQVVLERLREAVRALAVRVGDDVLSVTASAGLAEHRPPEEGLSATLSRADQALYQAKRAGR 249
|
...
gi 2490585942 318 NQI 320
Cdd:NF038266 250 DRV 252
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
158-321 |
2.33e-34 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 131.68 E-value: 2.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490585942 158 LHRLATTDVLTQSSNRRHFFECARREFEHARKFGSPLTFLLLDLDDFKKINDQYGHQTGDEVLRRLAQCGSNALRRGDLF 237
Cdd:PRK15426 394 LQWQAWHDPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVA 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490585942 238 GRIGGEEFAALFPGCEQDVALQVAERLQREVQ-RLSFQHEGSSFGITVSQGLTSLLAT-DVSLDALYARAGAAMYLAKRQ 315
Cdd:PRK15426 474 GRVGGEEFCVVLPGASLAEAAQVAERIRLRINeKEILVAKSTTIRISASLGVSSAEEDgDYDFEQLQSLADRRLYLAKQA 553
|
....*.
gi 2490585942 316 GKNQIV 321
Cdd:PRK15426 554 GRNRVC 559
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
71-322 |
2.26e-57 |
|
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: 186.72 E-value: 2.26e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490585942 71 AALLLADYGEWRNSIYPDDLDYAAESMAKVLETGAVESREYRIIRADGQLRWLSDKCFVSPLPGVDKGSVIVGIAEDITE 150
Cdd:COG2199 23 LLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLLLLALEDITE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490585942 151 KKRLEGELHRLATTDVLTQSSNRRHFFECARREFEHARKFGSPLTFLLLDLDDFKKINDQYGHQTGDEVLRRLAQCGSNA 230
Cdd:COG2199 103 LRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRAS 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490585942 231 LRRGDLFGRIGGEEFAALFPGCEQDVALQVAERLQREVQRLSFQHEGSSFGITVSQGLTSLLATDVSLDALYARAGAAMY 310
Cdd:COG2199 183 LRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELEGKELRVTVSIGVALYPEDGDSAEELLRRADLALY 262
|
250
....*....|..
gi 2490585942 311 LAKRQGKNQIVL 322
Cdd:COG2199 263 RAKRAGRNRVVV 274
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
163-321 |
3.57e-49 |
|
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: 161.57 E-value: 3.57e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490585942 163 TTDVLTQSSNRRHFFECARREFEHARKFGSPLTFLLLDLDDFKKINDQYGHQTGDEVLRRLAQCGSNALRRGDLFGRIGG 242
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2490585942 243 EEFAALFPGCEQDVALQVAERLQREVQRLSFQHeGSSFGITVSQGLTSLLATDVSLDALYARAGAAMYLAKRQGKNQIV 321
Cdd:cd01949 81 DEFAILLPGTDLEEAEALAERLREAIEEPFFID-GQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNRVV 158
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
162-319 |
6.20e-43 |
|
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: 145.47 E-value: 6.20e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490585942 162 ATTDVLTQSSNRRHFFECARREFEHARKFGSPLTFLLLDLDDFKKINDQYGHQTGDEVLRRLAQCGSNALRRGDLFGRIG 241
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490585942 242 GEEFAALFPGCEQDVALQVAERLQREVQRLSFQHEGS--------SFGITVSQGLTSllatdvSLDALYARAGAAMYLAK 313
Cdd:pfam00990 81 GDEFAILLPETSLEGAQELAERIRRLLAKLKIPHTVSglplyvtiSIGIAAYPNDGE------DPEDLLKRADTALYQAK 154
|
....*.
gi 2490585942 314 RQGKNQ 319
Cdd:pfam00990 155 QAGRNR 160
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
22-322 |
1.47e-42 |
|
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: 155.70 E-value: 1.47e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490585942 22 RAEVERLGEREQLFSSLLGSVNAVLWAFDWHEQRMIYVSPAYERIFGRSAALLLADYGEWRNSIYPDDLDYAAESMAKVL 101
Cdd:COG5001 111 ALLALLAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARALLALLLLLLLALLLLLLLLLLLALLLLLLL 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490585942 102 ETGAVESREYRIIRADGQLRWLSDKCFVSPLPGVDKGSVIVGIAEDITEKKRLEGELHRLATTDVLTQSSNRRHFFECAR 181
Cdd:COG5001 191 ALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEERLRHLAYHDPLTGLPNRRLFLDRLE 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490585942 182 REFEHARKFGSPLTFLLLDLDDFKKINDQYGHQTGDEVLRRLAQCGSNALRRGDLFGRIGGEEFAALFPGCEQ-DVALQV 260
Cdd:COG5001 271 QALARARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVLLPDLDDpEDAEAV 350
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2490585942 261 AERLQREVQRlSFQHEGSSFGITVSQGLTSLLATDVSLDALYARAGAAMYLAKRQGKNQIVL 322
Cdd:COG5001 351 AERILAALAE-PFELDGHELYVSASIGIALYPDDGADAEELLRNADLAMYRAKAAGRNRYRF 411
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
160-322 |
6.00e-41 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 140.46 E-value: 6.00e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490585942 160 RLATTDVLTQSSNRRHFFECARREFEHARKFGSPLTFLLLDLDDFKKINDQYGHQTGDEVLRRLAQCGSNALRRGDLFGR 239
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490585942 240 IGGEEFAALFPGCEQDVALQVAERLQREVQRLSFQHeGSSFGITVSQGLTSLLATDVSLDALYARAGAAMYLAKRQGKNQ 319
Cdd:smart00267 81 LGGDEFALLLPETSLEEAIALAERILQQLREPIIIH-GIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQ 159
|
...
gi 2490585942 320 IVL 322
Cdd:smart00267 160 VAV 162
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
161-322 |
3.63e-37 |
|
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: 130.53 E-value: 3.63e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490585942 161 LATTDVLTQSSNRRHFFECARREFEHARKFGSPLTFLLLDLDDFKKINDQYGHQTGDEVLRRLAQCGSNALRRGDLFGRI 240
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490585942 241 GGEEFAALFPGCEQDVALQVAERLQREVQRLSFQHEGSSFG-ITVSQGLTSLLATDVSLDALYARAGAAMYLAKRQGKNQ 319
Cdd:TIGR00254 81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSETLtVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRNR 160
|
...
gi 2490585942 320 IVL 322
Cdd:TIGR00254 161 VVV 163
|
|
| diguan_SiaD |
NF038266 |
biofilm regulation diguanylate cyclase SiaD; |
158-320 |
2.90e-35 |
|
biofilm regulation diguanylate cyclase SiaD;
Pssm-ID: 468439 [Multi-domain] Cd Length: 252 Bit Score: 128.18 E-value: 2.90e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490585942 158 LHRLATTDVLTQSSNRRHFFECARREFEHARKFGSPLTFLLLDLDDFKKINDQYGHQTGDEVLRRLAQCGSNALRRGDLF 237
Cdd:NF038266 90 LREASTRDPLTGLPNRRLLMERLREEVERARRSGRPFTLAMLDVDHFKRINDRYGHEVGDRVLVEIARTLRAELREYDLC 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490585942 238 GRIGGEEFAALFPGCEQDVALQVAERLQREVQRLSFQHEGSSFGITVSQGLTSLLATDVSLDALYARAGAAMYLAKRQGK 317
Cdd:NF038266 170 GRWGGEEFLLLLPETGLEEAQVVLERLREAVRALAVRVGDDVLSVTASAGLAEHRPPEEGLSATLSRADQALYQAKRAGR 249
|
...
gi 2490585942 318 NQI 320
Cdd:NF038266 250 DRV 252
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
158-321 |
2.33e-34 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 131.68 E-value: 2.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490585942 158 LHRLATTDVLTQSSNRRHFFECARREFEHARKFGSPLTFLLLDLDDFKKINDQYGHQTGDEVLRRLAQCGSNALRRGDLF 237
Cdd:PRK15426 394 LQWQAWHDPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVA 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490585942 238 GRIGGEEFAALFPGCEQDVALQVAERLQREVQ-RLSFQHEGSSFGITVSQGLTSLLAT-DVSLDALYARAGAAMYLAKRQ 315
Cdd:PRK15426 474 GRVGGEEFCVVLPGASLAEAAQVAERIRLRINeKEILVAKSTTIRISASLGVSSAEEDgDYDFEQLQSLADRRLYLAKQA 553
|
....*.
gi 2490585942 316 GKNQIV 321
Cdd:PRK15426 554 GRNRVC 559
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
161-321 |
2.20e-31 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 122.32 E-value: 2.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490585942 161 LATTDVLTQSSNRRHFFECARREFEHARKFGSPLTFLLLDLDDFKKINDQYGHQTGDEVLRRLAQCGSNALRRGDLFGRI 240
Cdd:PRK09581 291 MAVTDGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARY 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490585942 241 GGEEFAALFPGCEQDVALQVAERLQREVQRLSFQHEGSSFGI--TVSQGLTSLLATDVSLDALYARAGAAMYLAKRQGKN 318
Cdd:PRK09581 371 GGEEFVVVMPDTDIEDAIAVAERIRRKIAEEPFIISDGKERLnvTVSIGVAELRPSGDTIEALIKRADKALYEAKNTGRN 450
|
...
gi 2490585942 319 QIV 321
Cdd:PRK09581 451 RVV 453
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
153-322 |
6.43e-27 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 107.07 E-value: 6.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490585942 153 RLEGELHRLATT-DVLTQSSNRRHFFEcarrEFEHARKFGSPLTFLLLDLD--DFKKINDQYGHQTGDEVLRRLAQCGSN 229
Cdd:PRK09894 119 DYKIYLLTIRSNmDVLTGLPGRRVLDE----SFDHQLRNREPQNLYLALLDidRFKLVNDTYGHLIGDVVLRTLATYLAS 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490585942 230 ALRRGDLFGRIGGEEFAALFPGCEQDVALQVAERLQREVQRLSFQHEGSSFGITVSQGLTSLLAtDVSLDALYARAGAAM 309
Cdd:PRK09894 195 WTRDYETVYRYGGEEFIICLKAATDEEACRAGERIRQLIANHAITHSDGRINITATFGVSRAFP-EETLDVVIGRADRAM 273
|
170
....*....|...
gi 2490585942 310 YLAKRQGKNQIVL 322
Cdd:PRK09894 274 YEGKQTGRNRVMF 286
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
129-320 |
1.20e-24 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 104.75 E-value: 1.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490585942 129 VSPLPGVDKGSVIVgiAEDITEKKRLEGELHRLATTDVLTQSSNRRHFFECARREFEHARKFGSPLTFLLLDLDDFKKIN 208
Cdd:PRK09776 634 LSTLDGENIGSVLV--IQDVTESRKMLRQLSYSASHDALTHLANRASFEKQLRRLLQTVNSTHQRHALVFIDLDRFKAVN 711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490585942 209 DQYGHQTGDEVLRRLAQCGSNALRRGDLFGRIGGEEFAALFPGCEQDVALQVAERLQREVQRLSFQHEGSSFGITVSQGL 288
Cdd:PRK09776 712 DSAGHAAGDALLRELASLMLSMLRSSDVLARLGGDEFGLLLPDCNVESARFIATRIISAINDYHFPWEGRVYRVGASAGI 791
|
170 180 190
....*....|....*....|....*....|..
gi 2490585942 289 TSLLATDVSLDALYARAGAAMYLAKRQGKNQI 320
Cdd:PRK09776 792 TLIDANNHQASEVMSQADIACYAAKNAGRGRV 823
|
|
| PAS_3 |
pfam08447 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
57-129 |
1.07e-19 |
|
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: 82.00 E-value: 1.07e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2490585942 57 IYVSPAYERIFGRSAALLLADYGEWRNSIYPDDLDYAAESMAKVLETGAVESREYRIIRADGQLRWLSDKCFV 129
Cdd:pfam08447 2 IYWSPRFEEILGYTPEELLGKGESWLDLVHPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARP 74
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
147-319 |
4.59e-16 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 78.96 E-value: 4.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490585942 147 DITEKKRLEGELHRLATTDVLTQSSNRRHFFECARREFEHARkfGSPLTFLLLDLDDFKKINDQYGHQTGDEVLRRLAQC 226
Cdd:PRK10060 222 DITEERRAQERLRILANTDSITGLPNRNAIQELIDHAINAAD--NNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLA 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490585942 227 GSNALRRGDLFGRIGGEEFAALFPGCEQDVALQVAER-LQRevQRLSFQ------HEGSSFGITVS--QGltsllatdVS 297
Cdd:PRK10060 300 ILSCLEEDQTLARLGGDEFLVLASHTSQAALEAMASRiLTR--LRLPFRiglievYTGCSIGIALApeHG--------DD 369
|
170 180
....*....|....*....|..
gi 2490585942 298 LDALYARAGAAMYLAKRQGKNQ 319
Cdd:PRK10060 370 SESLIRSADTAMYTAKEGGRGQ 391
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
144-319 |
1.75e-15 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 76.02 E-value: 1.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490585942 144 IAEDITEKKRlegELHRLATTDVLTQSSNRRHFFECARREFEHARKFGSPLTFLLLDLDDFKKINDQYGHQTGDEVLRRL 223
Cdd:PRK10245 190 TATKLAEHKR---RLQVMSTRDGMTGVYNRRHWETLLRNEFDNCRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAIVAL 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490585942 224 AQCGSNALRRGDLFGRIGGEEFAALFPGCEQDVALQVAERLQREVQRLSFQHeGSSFGITVSQGLTSLLATDVSLDALYA 303
Cdd:PRK10245 267 TRQLQITLRGSDVIGRFGGDEFAVIMSGTPAESAITAMSRVHEGLNTLRLPN-APQVTLRISVGVAPLNPQMSHYREWLK 345
|
170
....*....|....*.
gi 2490585942 304 RAGAAMYLAKRQGKNQ 319
Cdd:PRK10245 346 SADLALYKAKNAGRNR 361
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
31-158 |
9.52e-15 |
|
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: 69.63 E-value: 9.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490585942 31 REQLFSSLLGSVNAVLWAFDwHEQRMIYVSPAYERIFGRSAALLLADYgeWRNSIYPDDLDYAAESMAKVLE-TGAVESR 109
Cdd:TIGR00229 1 SEERYRAIFESSPDAIIVID-LEGNILYVNPAFEEIFGYSAEELIGRN--VLELIPEEDREEVRERIERRLEgEPEPVSE 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2490585942 110 EYRIIRADGQLRWLSDkcFVSPLPGVDKGSVIVGIAEDITEKKRLEGEL 158
Cdd:TIGR00229 78 ERRVRRKDGSEIWVEV--SVSPIRTNGGELGVVGIVRDITERKEAEEAL 124
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
23-160 |
1.12e-14 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 72.75 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490585942 23 AEVERLGEREQLFSSLLGSVNAVLWAFDwHEQRMIYVSPAYERIFGRSAALLLAdyGEWRNSIYPDDLDYAAESMAKVLE 102
Cdd:COG2202 1 TAEEALEESERRLRALVESSPDAIIITD-LDGRILYVNPAFERLTGYSAEELLG--KTLRDLLPPEDDDEFLELLRAALA 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490585942 103 TGAVESREYRIIRADGQLRWLSDKcfVSPLPGvDKGSV--IVGIAEDITEKKRLEGELHR 160
Cdd:COG2202 78 GGGVWRGELRNRRKDGSLFWVELS--ISPVRD-EDGEItgFVGIARDITERKRAEEALRE 134
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
22-158 |
2.29e-14 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 71.59 E-value: 2.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490585942 22 RAEvERLGEREQLFSSLLGSVNAVLWAFDwHEQRMIYVSPAYERIFGRSAALLLAdyGEWRNSIYPDDLDYAAESMAKVL 101
Cdd:COG2202 127 RAE-EALRESEERLRLLVENAPDGIFVLD-LDGRILYVNPAAEELLGYSPEELLG--KSLLDLLHPEDRERLLELLRRLL 202
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2490585942 102 ETGAVESR-EYRIIRADGQLRWLSDKcfVSPLPGVDKGSVIVGIAEDITEKKRLEGEL 158
Cdd:COG2202 203 EGGRESYElELRLKDGDGRWVWVEAS--AVPLRDGGEVIGVLGIVRDITERKRAEEAL 258
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
27-162 |
1.00e-13 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 71.03 E-value: 1.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490585942 27 RLGEREQLFSSLLGSVNAVLWAFDwHEQRMIYVSPAYERIFGRSAALLLadyGEWRNSIYPDDLDYAaESMAKVLETG-A 105
Cdd:COG3852 1 ALRESEELLRAILDSLPDAVIVLD-ADGRITYVNPAAERLLGLSAEELL---GRPLAELFPEDSPLR-ELLERALAEGqP 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2490585942 106 VESREYRIIRADGQLRWLSdkCFVSPLPGVDKGSVIVGIAEDITEKKRLEGELHRLA 162
Cdd:COG3852 76 VTEREVTLRRKDGEERPVD--VSVSPLRDAEGEGGVLLVLRDITERKRLERELRRAE 130
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
204-321 |
1.55e-13 |
|
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: 66.61 E-value: 1.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490585942 204 FKKINDQYGHQTGDEVLRRLAQCGSNALRR-GDLFGRIGGEEFAALFPGCEQDVALQVAERLQREVQRLSfQHEGSsfGI 282
Cdd:cd07556 12 FTSLADALGPDEGDELLNELAGRFDSLIRRsGDLKIKTIGDEFMVVSGLDHPAAAVAFAEDMREAVSALN-QSEGN--PV 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2490585942 283 TVSQGLTSLL--ATDVSLDALYARAGAAMYLAKR---QGK-NQIV 321
Cdd:cd07556 89 RVRIGIHTGPvvVGVIGSRPQYDVWGALVNLASRmesQAKaGQVL 133
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
26-169 |
4.05e-12 |
|
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: 66.54 E-value: 4.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490585942 26 ERLGEREQLFSSLLGSVNAVLWAFDwHEQRMIYVSPAYERIFGRSAALLLADYGEwrNSIYPDDLDYAAESMAKVLETGA 105
Cdd:COG5809 134 EALRESEEKFRLIFNHSPDGIIVTD-LDGRIIYANPAACKLLGISIEELIGKSIL--ELIHSDDQENVAAFISQLLKDGG 210
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2490585942 106 VESREYRIIRADGQLRWLSDKCfvSPLPGVDKGSVIVGIAEDITEKKRLEGELHRLATTDVLTQ 169
Cdd:COG5809 211 IAQGEVRFWTKDGRWRLLEASG--APIKKNGEVDGIVIIFRDITERKKLEELLRKSEKLSVVGE 272
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
235-313 |
1.14e-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: 62.62 E-value: 1.14e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2490585942 235 DLFGRIGGEEFAALFPGCEQDVALQVAERLQREVQRLsfqhegSSFGITVSQGltsllatdVSLDALYARAgAAMYLAK 313
Cdd:COG3706 116 DLVARYGGEEFAILLPGTDLEGALAVAERIREAVAEL------PSLRVTVSIG--------VAGDSLLKRA-DALYQAR 179
|
|
| KinA |
COG5805 |
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ... |
20-169 |
1.34e-10 |
|
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: 62.06 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490585942 20 HSRAEVERLGEREQLFSSLLGSVNAVLWAFDwHEQRMIYVSPAYERIFGRSAALLLADygEWRNSIYPDDLDYAAESMAK 99
Cdd:COG5805 144 KKKKIEEILQEQEERLQTLIENSPDLICVID-TDGRILFINESIERLFGAPREELIGK--NLLELLHPCDKEEFKERIES 220
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2490585942 100 VLETGAVESREYRIIRADGQLRWLSDKCfvSPLPGVDKGSV-IVGIAEDITEKKRLEGELHRLATTDVLTQ 169
Cdd:COG5805 221 ITEVWQEFIIEREIITKDGRIRYFEAVI--VPLIDTDGSVKgILVILRDITEKKEAEELMARSEKLSIAGQ 289
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
157-315 |
3.06e-09 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 57.71 E-value: 3.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490585942 157 ELHRLATTDVLTQSSNRRHFFEC--ARREFEHARKfGSPLTFLLLDLddFKKINDQYGHQTGDEVL----RRLAQCGSNa 230
Cdd:PRK09966 243 QLLRTALHDPLTGLANRAAFRSGinTLMNNSDARK-TSALLFLDGDN--FKYINDTWGHATGDRVLieiaKRLAEFGGL- 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490585942 231 lrRGDLFgRIGGEEFAALFPGCEQDVALQ-VAERLQREVQRLSFQHEGSSFGITVSQGLtSLLATDVSLDALYARAGAAM 309
Cdd:PRK09966 319 --RHKAY-RLGGDEFAMVLYDVQSESEVQqICSALTQIFNLPFDLHNGHQTTMTLSIGY-AMTIEHASAEKLQELADHNM 394
|
....*.
gi 2490585942 310 YLAKRQ 315
Cdd:PRK09966 395 YQAKHQ 400
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
150-318 |
3.06e-07 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 51.69 E-value: 3.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490585942 150 EKKRLEGELHRLATTDVLTQSSNRRHFfecaRREFEHARKFGSPLTFLLLDLDDFKKINDQYGHQTGDEVLRRLAQCGSN 229
Cdd:PRK11359 364 EQEKSRQHIEQLIQFDPLTGLPNRNNL----HNYLDDLVDKAVSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFRE 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490585942 230 ALRRGDLFGRIGGEEFAALFPGCEQDVALQVAERLQREV-QRLSFqhEGSSFGITVSQGLTSLLATDvsLDALYARAGAA 308
Cdd:PRK11359 440 KLKPDQYLCRIEGTQFVLVSLENDVSNITQIADELRNVVsKPIMI--DDKPFPLTLSIGISYDVGKN--RDYLLSTAHNA 515
|
170
....*....|
gi 2490585942 309 MYLAKRQGKN 318
Cdd:PRK11359 516 MDYIRKNGGN 525
|
|
| RocR |
COG3829 |
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ... |
23-158 |
4.61e-07 |
|
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis domains [Transcription, Signal transduction mechanisms];
Pssm-ID: 443041 [Multi-domain] Cd Length: 448 Bit Score: 50.93 E-value: 4.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490585942 23 AEVERLGEREQLFSSLLGSVNAVLWAFDwHEQRMIYVSPAYERIFGRSAALLLadyGEWRNSIYPDDLdyaaesMAKVLE 102
Cdd:COG3829 1 AEELELKELEEELEAILDSLDDGIIVVD-ADGRITYVNRAAERILGLPREEVI---GKNVTELIPNSP------LLEVLK 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2490585942 103 TGavESREYRIIRADGQLRwlsdKCFVSPLPGVDKGSVI--VGIAEDITEKKRLEGEL 158
Cdd:COG3829 71 TG--KPVTGVIQKTGGKGK----TVIVTAIPIFEDGEVIgaVETFRDITELKRLERKL 122
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
46-148 |
6.90e-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: 46.86 E-value: 6.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490585942 46 LWAFDwHEQRMIYVSPAYERIFGRSAALLLAdyGEWRNSIYPDDLDYAAESMAKVLETGAVESREYRIIRADGQLRWLSd 125
Cdd:cd00130 5 VIVLD-LDGRILYANPAAEQLLGYSPEELIG--KSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVL- 80
|
90 100
....*....|....*....|....
gi 2490585942 126 kCFVSPLPGVDKGSV-IVGIAEDI 148
Cdd:cd00130 81 -VSLTPIRDEGGEVIgLLGVVRDI 103
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
55-150 |
1.38e-05 |
|
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor domain. It recognizes FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 463873 [Multi-domain] Cd Length: 93 Bit Score: 43.22 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490585942 55 RMIYVSPAYERIFGRSAALLLAdyGEWRNSIYPDDldyAAESMAKVLETG-AVESREYRIIRADGQLRWLsdKCFVSPLP 133
Cdd:pfam13426 3 RIIYVNDAALRLLGYTREELLG--KSITDLFAEPE---DSERLREALREGkAVREFEVVLYRKDGEPFPV--LVSLAPIR 75
|
90
....*....|....*...
gi 2490585942 134 GVDKGSV-IVGIAEDITE 150
Cdd:pfam13426 76 DDGGELVgIIAILRDITE 93
|
|
| PAS_4 |
pfam08448 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
39-153 |
4.36e-05 |
|
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. This domain is associated to signalling systems and works as a signal sensor domain. It recognizes differently substituted aromatic hydrocarbons, oxygen, different dodecanoic acids, autoinducers, 3,5-dimethyl-pyrazin-2-ol and N-alanyl-aminoacetone (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 312075 [Multi-domain] Cd Length: 110 Bit Score: 42.02 E-value: 4.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490585942 39 LGSVNAVLWAFDwHEQRMIYVSPAYERIFGRSAALLLadyGEWRNSIYPDDlDYAAES--MAKVLETGAVESREyRIIRA 116
Cdd:pfam08448 1 LDSLPDALAVLD-PDGRVRYANAAAAELFGLPPEELL---GKTLAELLPPE-DAARLEraLRRALEGEEPIDFL-EELLL 74
|
90 100 110
....*....|....*....|....*....|....*....
gi 2490585942 117 DGQLRWLSdkCFVSPLPGVDkGSVI--VGIAEDITEKKR 153
Cdd:pfam08448 75 NGEERHYE--LRLTPLRDPD-GEVIgvLVISRDITERRR 110
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
236-320 |
1.30e-04 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 43.55 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490585942 236 LFGRIGGEEFAALFPGCEQDV-ALQVAER-LQREVQRLSFQH----EGSSFGITVSQGltsllatDVSLDALYARAGAAM 309
Cdd:PRK13561 301 VLAQISGYDFAIIANGVKEPWhAITLGQQvLTIINERLPIQRiqlrPSCSIGIAMFYG-------DLTAEQLYSRAISAA 373
|
90
....*....|.
gi 2490585942 310 YLAKRQGKNQI 320
Cdd:PRK13561 374 FTARRKGKNQI 384
|
|
| PRK13558 |
PRK13558 |
bacterio-opsin activator; Provisional |
56-160 |
2.81e-04 |
|
bacterio-opsin activator; Provisional
Pssm-ID: 237426 [Multi-domain] Cd Length: 665 Bit Score: 42.52 E-value: 2.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490585942 56 MIYVSPAYERIFGRSAALLLAdygewRNSIYPDDLDYAAESMAKVLEtgAVESR-----EYRIIRADGQLRWlsDKCFVS 130
Cdd:PRK13558 173 LIYINDAFERITGYSPDEVLG-----RNCRFLQGEDTNEERVAELRE--AIDEErptsvELRNYRKDGSTFW--NQVDIA 243
|
90 100 110
....*....|....*....|....*....|..
gi 2490585942 131 PLPGVDkGSV--IVGIAEDITEKKRLEGELHR 160
Cdd:PRK13558 244 PIRDED-GTVthYVGFQTDVTERKEAELALQR 274
|
|
| PRK13560 |
PRK13560 |
hypothetical protein; Provisional |
23-158 |
1.35e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 106506 [Multi-domain] Cd Length: 807 Bit Score: 40.43 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490585942 23 AEVERLGEREQLFSSLLGSVNAVLWAFDWHEQRMIY---VSPAYERIFGRSAALLLADYGEWRNSIYPDDLDY------- 92
Cdd:PRK13560 58 AEAEAQDCREQCERNLKANIPGGMFLFALDGDGTFSfpsLLDANGELAAIAKHDLMADKGLLAMLIGGDDGDFffanpfr 137
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2490585942 93 AAESMAKVLETGAVESREYRIIRADGqlRWLSdkCFVSPLPGVDKGSVIVGIAEDITEKKRLEGEL 158
Cdd:PRK13560 138 SAETIAMALQSDDWQEEEGHFRCGDG--RFID--CCLRFERHAHADDQVDGFAEDITERKRAEERI 199
|
|
| |
