|
Name |
Accession |
Description |
Interval |
E-value |
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
71-322 |
4.07e-67 |
|
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: 211.76 E-value: 4.07e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595487 71 AALLLADYEEWRNSIYPDDLDYADSSLLQVLERGAVEQREYRIVRGDGEVRWLNDKCFVSRQGEAGLPLMVVGIAEDITD 150
Cdd:COG2199 23 LLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLLLLALEDITE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595487 151 KKHMESELQRLATTDVLTQSSNRRYFFDSAEAAFKECRREGIPLAFLLLDVDDFKKINDRFGHQVGDQVLQRIAQSGSAA 230
Cdd:COG2199 103 LRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRAS 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595487 231 LRRGDLFGRIGGEEFAVLLPGCDEQTARQIGERLQREVQRLRFQEGEHSFGITVSQGLTVLQADDEGLGALYSRADAAMY 310
Cdd:COG2199 183 LRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELEGKELRVTVSIGVALYPEDGDSAEELLRRADLALY 262
|
250
....*....|..
gi 15595487 311 SAKRQGKDCIVV 322
Cdd:COG2199 263 RAKRAGRNRVVV 274
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
163-321 |
1.24e-60 |
|
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: 190.85 E-value: 1.24e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595487 163 TTDVLTQSSNRRYFFDSAEAAFKECRREGIPLAFLLLDVDDFKKINDRFGHQVGDQVLQRIAQSGSAALRRGDLFGRIGG 242
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15595487 243 EEFAVLLPGCDEQTARQIGERLQREVQRLRFQEGeHSFGITVSQGLTVLQADDEGLGALYSRADAAMYSAKRQGKDCIV 321
Cdd:cd01949 81 DEFAILLPGTDLEEAEALAERLREAIEEPFFIDG-QEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNRVV 158
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
162-319 |
2.74e-54 |
|
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of non-homologous domains in a variety of bacteria. It has been shown to be homologous to the adenylyl cyclase catalytic domain and has diguanylate cyclase activity. This observation correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. In the WspR protein of Pseudomonas aeruginosa, the GGDEF domain acts as a diguanylate cyclase, PDB:3bre, when the whole molecule appears to form a tetramer consisting of two symmetrically-related dimers representing a biological unit. The active site is the GGD/EF motif, buried in the structure, and the cyclic dimeric guanosine monophosphate (c-di-GMP) bind to the inhibitory-motif RxxD on the surface. The enzyme thus catalyzes the cyclization of two guanosine triphosphate (GTP) molecules to one c-di-GMP molecule.
Pssm-ID: 425976 [Multi-domain] Cd Length: 160 Bit Score: 174.75 E-value: 2.74e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595487 162 ATTDVLTQSSNRRYFFDSAEAAFKECRREGIPLAFLLLDVDDFKKINDRFGHQVGDQVLQRIAQSGSAALRRGDLFGRIG 241
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595487 242 GEEFAVLLPGCDEQTARQIGERLQREVQRLR--FQEGEHSFGITVSQGLTVLQADDEGLGALYSRADAAMYSAKRQGKDC 319
Cdd:pfam00990 81 GDEFAILLPETSLEGAQELAERIRRLLAKLKipHTVSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGRNR 160
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
160-322 |
3.01e-50 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 164.34 E-value: 3.01e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595487 160 RLATTDVLTQSSNRRYFFDSAEAAFKECRREGIPLAFLLLDVDDFKKINDRFGHQVGDQVLQRIAQSGSAALRRGDLFGR 239
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595487 240 IGGEEFAVLLPGCDEQTARQIGERLQREVQRLRFQEGEHSFgITVSQGLTVLQADDEGLGALYSRADAAMYSAKRQGKDC 319
Cdd:smart00267 81 LGGDEFALLLPETSLEEAIALAERILQQLREPIIIHGIPLY-LTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQ 159
|
...
gi 15595487 320 IVV 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 |
1.54e-41 |
|
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: 142.09 E-value: 1.54e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595487 161 LATTDVLTQSSNRRYFFDSAEAAFKECRREGIPLAFLLLDVDDFKKINDRFGHQVGDQVLQRIAQSGSAALRRGDLFGRI 240
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595487 241 GGEEFAVLLPGCDEQTARQIGERLQREVQRLRFQ-EGEHSFGITVSQGLTVLQADDEGLGALYSRADAAMYSAKRQGKDC 319
Cdd:TIGR00254 81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPIEvAGSETLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRNR 160
|
...
gi 15595487 320 IVV 322
Cdd:TIGR00254 161 VVV 163
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
154-321 |
2.11e-41 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 151.32 E-value: 2.11e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595487 154 MESELQRLATTDVLTQSSNRRYFFDSAEAAFKECRREGIPLAFLLLDVDDFKKINDRFGHQVGDQVLQRIAQSGSAALRR 233
Cdd:PRK15426 390 LQSSLQWQAWHDPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRA 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595487 234 GDLFGRIGGEEFAVLLPGCDEQTARQIGERLqrevqRLRFQEGE------HSFGITVSQGLTVLQADDEG-LGALYSRAD 306
Cdd:PRK15426 470 QDVAGRVGGEEFCVVLPGASLAEAAQVAERI-----RLRINEKEilvaksTTIRISASLGVSSAEEDGDYdFEQLQSLAD 544
|
170
....*....|....*
gi 15595487 307 AAMYSAKRQGKDCIV 321
Cdd:PRK15426 545 RRLYLAKQAGRNRVC 559
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
71-322 |
4.07e-67 |
|
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: 211.76 E-value: 4.07e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595487 71 AALLLADYEEWRNSIYPDDLDYADSSLLQVLERGAVEQREYRIVRGDGEVRWLNDKCFVSRQGEAGLPLMVVGIAEDITD 150
Cdd:COG2199 23 LLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLLLLALEDITE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595487 151 KKHMESELQRLATTDVLTQSSNRRYFFDSAEAAFKECRREGIPLAFLLLDVDDFKKINDRFGHQVGDQVLQRIAQSGSAA 230
Cdd:COG2199 103 LRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRAS 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595487 231 LRRGDLFGRIGGEEFAVLLPGCDEQTARQIGERLQREVQRLRFQEGEHSFGITVSQGLTVLQADDEGLGALYSRADAAMY 310
Cdd:COG2199 183 LRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELEGKELRVTVSIGVALYPEDGDSAEELLRRADLALY 262
|
250
....*....|..
gi 15595487 311 SAKRQGKDCIVV 322
Cdd:COG2199 263 RAKRAGRNRVVV 274
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
163-321 |
1.24e-60 |
|
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: 190.85 E-value: 1.24e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595487 163 TTDVLTQSSNRRYFFDSAEAAFKECRREGIPLAFLLLDVDDFKKINDRFGHQVGDQVLQRIAQSGSAALRRGDLFGRIGG 242
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15595487 243 EEFAVLLPGCDEQTARQIGERLQREVQRLRFQEGeHSFGITVSQGLTVLQADDEGLGALYSRADAAMYSAKRQGKDCIV 321
Cdd:cd01949 81 DEFAILLPGTDLEEAEALAERLREAIEEPFFIDG-QEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNRVV 158
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
14-322 |
4.76e-55 |
|
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: 189.99 E-value: 4.76e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595487 14 AALALLHSRAEVARLKEREQLFSALLASVNSVLWAYDWQNRRMVYVSPAYEKIFGRSAALLLADYEEWRNSIYPDDLDYA 93
Cdd:COG5001 103 LLLLLLLLALLALLAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARALLALLLLLLLALLLLLLLLLLL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595487 94 DSSLLQVLERGAVEQREYRIVRGDGEVRWLNDKCFVSRQGEAGLPLMVVGIAEDITDKKHMESELQRLATTDVLTQSSNR 173
Cdd:COG5001 183 ALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEERLRHLAYHDPLTGLPNR 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595487 174 RYFFDSAEAAFKECRREGIPLAFLLLDVDDFKKINDRFGHQVGDQVLQRIAQSGSAALRRGDLFGRIGGEEFAVLLPGC- 252
Cdd:COG5001 263 RLFLDRLEQALARARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVLLPDLd 342
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595487 253 DEQTARQIGERLQREVQRlRFQEGEHSFGITVSQGLTVLQADDEGLGALYSRADAAMYSAKRQGKDCIVV 322
Cdd:COG5001 343 DPEDAEAVAERILAALAE-PFELDGHELYVSASIGIALYPDDGADAEELLRNADLAMYRAKAAGRNRYRF 411
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
162-319 |
2.74e-54 |
|
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of non-homologous domains in a variety of bacteria. It has been shown to be homologous to the adenylyl cyclase catalytic domain and has diguanylate cyclase activity. This observation correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. In the WspR protein of Pseudomonas aeruginosa, the GGDEF domain acts as a diguanylate cyclase, PDB:3bre, when the whole molecule appears to form a tetramer consisting of two symmetrically-related dimers representing a biological unit. The active site is the GGD/EF motif, buried in the structure, and the cyclic dimeric guanosine monophosphate (c-di-GMP) bind to the inhibitory-motif RxxD on the surface. The enzyme thus catalyzes the cyclization of two guanosine triphosphate (GTP) molecules to one c-di-GMP molecule.
Pssm-ID: 425976 [Multi-domain] Cd Length: 160 Bit Score: 174.75 E-value: 2.74e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595487 162 ATTDVLTQSSNRRYFFDSAEAAFKECRREGIPLAFLLLDVDDFKKINDRFGHQVGDQVLQRIAQSGSAALRRGDLFGRIG 241
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595487 242 GEEFAVLLPGCDEQTARQIGERLQREVQRLR--FQEGEHSFGITVSQGLTVLQADDEGLGALYSRADAAMYSAKRQGKDC 319
Cdd:pfam00990 81 GDEFAILLPETSLEGAQELAERIRRLLAKLKipHTVSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGRNR 160
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
160-322 |
3.01e-50 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 164.34 E-value: 3.01e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595487 160 RLATTDVLTQSSNRRYFFDSAEAAFKECRREGIPLAFLLLDVDDFKKINDRFGHQVGDQVLQRIAQSGSAALRRGDLFGR 239
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595487 240 IGGEEFAVLLPGCDEQTARQIGERLQREVQRLRFQEGEHSFgITVSQGLTVLQADDEGLGALYSRADAAMYSAKRQGKDC 319
Cdd:smart00267 81 LGGDEFALLLPETSLEEAIALAERILQQLREPIIIHGIPLY-LTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQ 159
|
...
gi 15595487 320 IVV 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 |
1.54e-41 |
|
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: 142.09 E-value: 1.54e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595487 161 LATTDVLTQSSNRRYFFDSAEAAFKECRREGIPLAFLLLDVDDFKKINDRFGHQVGDQVLQRIAQSGSAALRRGDLFGRI 240
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595487 241 GGEEFAVLLPGCDEQTARQIGERLQREVQRLRFQ-EGEHSFGITVSQGLTVLQADDEGLGALYSRADAAMYSAKRQGKDC 319
Cdd:TIGR00254 81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPIEvAGSETLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRNR 160
|
...
gi 15595487 320 IVV 322
Cdd:TIGR00254 161 VVV 163
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
154-321 |
2.11e-41 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 151.32 E-value: 2.11e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595487 154 MESELQRLATTDVLTQSSNRRYFFDSAEAAFKECRREGIPLAFLLLDVDDFKKINDRFGHQVGDQVLQRIAQSGSAALRR 233
Cdd:PRK15426 390 LQSSLQWQAWHDPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRA 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595487 234 GDLFGRIGGEEFAVLLPGCDEQTARQIGERLqrevqRLRFQEGE------HSFGITVSQGLTVLQADDEG-LGALYSRAD 306
Cdd:PRK15426 470 QDVAGRVGGEEFCVVLPGASLAEAAQVAERI-----RLRINEKEilvaksTTIRISASLGVSSAEEDGDYdFEQLQSLAD 544
|
170
....*....|....*
gi 15595487 307 AAMYSAKRQGKDCIV 321
Cdd:PRK15426 545 RRLYLAKQAGRNRVC 559
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
161-321 |
7.81e-38 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 140.04 E-value: 7.81e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595487 161 LATTDVLTQSSNRRYFFDSAEAAFKECRREGIPLAFLLLDVDDFKKINDRFGHQVGDQVLQRIAQSGSAALRRGDLFGRI 240
Cdd:PRK09581 291 MAVTDGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARY 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595487 241 GGEEFAVLLPGCDEQTARQIGERLQREVQRLRFQ--EGEHSFGITVSQGLTVLQADDEGLGALYSRADAAMYSAKRQGKD 318
Cdd:PRK09581 371 GGEEFVVVMPDTDIEDAIAVAERIRRKIAEEPFIisDGKERLNVTVSIGVAELRPSGDTIEALIKRADKALYEAKNTGRN 450
|
...
gi 15595487 319 CIV 321
Cdd:PRK09581 451 RVV 453
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
154-322 |
6.06e-33 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 123.25 E-value: 6.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595487 154 MESELQRLATT-DVLTQSSNRRYFFDSAEAAFKecRREGIPLAFLLLDVDDFKKINDRFGHQVGDQVLQRIAQSGSAALR 232
Cdd:PRK09894 120 YKIYLLTIRSNmDVLTGLPGRRVLDESFDHQLR--NREPQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTR 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595487 233 RGDLFGRIGGEEFAVLLPGCDEQTARQIGERLQREVQRLRFQEGEHSFGITVSQGLTVLQAdDEGLGALYSRADAAMYSA 312
Cdd:PRK09894 198 DYETVYRYGGEEFIICLKAATDEEACRAGERIRQLIANHAITHSDGRINITATFGVSRAFP-EETLDVVIGRADRAMYEG 276
|
170
....*....|
gi 15595487 313 KRQGKDCIVV 322
Cdd:PRK09894 277 KQTGRNRVMF 286
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
146-317 |
2.56e-24 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 103.60 E-value: 2.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595487 146 EDITDKKHMESELQRLATTDVLTQSSNRRYFFDSAEAAFKECRREGIPLAFLLLDVDDFKKINDRFGHQVGDQVLQRIAQ 225
Cdd:PRK09776 649 QDVTESRKMLRQLSYSASHDALTHLANRASFEKQLRRLLQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELAS 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595487 226 SGSAALRRGDLFGRIGGEEFAVLLPGCDEQTARQIGERLQREVQRLRFQEGEHSFGITVSQGLTVLQADDEGLGALYSRA 305
Cdd:PRK09776 729 LMLSMLRSSDVLARLGGDEFGLLLPDCNVESARFIATRIISAINDYHFPWEGRVYRVGASAGITLIDANNHQASEVMSQA 808
|
170
....*....|..
gi 15595487 306 DAAMYSAKRQGK 317
Cdd:PRK09776 809 DIACYAAKNAGR 820
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
147-317 |
1.85e-21 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 94.75 E-value: 1.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595487 147 DITDKKHMESELQRLATTDVLTQSSNRRYFFDSAEAAFKecRREGIPLAFLLLDVDDFKKINDRFGHQVGDQVLQRIAQS 226
Cdd:PRK10060 222 DITEERRAQERLRILANTDSITGLPNRNAIQELIDHAIN--AADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLA 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595487 227 GSAALRRGDLFGRIGGEEFAVLLPGCD----EQTARQIGERLqrevqRLRFQEG--EHSFGITVSQGLTVLQADDegLGA 300
Cdd:PRK10060 300 ILSCLEEDQTLARLGGDEFLVLASHTSqaalEAMASRILTRL-----RLPFRIGliEVYTGCSIGIALAPEHGDD--SES 372
|
170
....*....|....*..
gi 15595487 301 LYSRADAAMYSAKRQGK 317
Cdd:PRK10060 373 LIRSADTAMYTAKEGGR 389
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
158-318 |
6.35e-19 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 86.04 E-value: 6.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595487 158 LQRLATTDVLTQSSNRRYFFDSAEAAFKECRREGIPLAFLLLDVDDFKKINDRFGHQVGDQVLQRIAQSGSAALRRGDLF 237
Cdd:PRK10245 201 LQVMSTRDGMTGVYNRRHWETLLRNEFDNCRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSDVI 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595487 238 GRIGGEEFAVLLPGCDEQTARQIGERLQREVQRLRFqEGEHSFGITVSQGLTVLQADDEGLGALYSRADAAMYSAKRQGK 317
Cdd:PRK10245 281 GRFGGDEFAVIMSGTPAESAITAMSRVHEGLNTLRL-PNAPQVTLRISVGVAPLNPQMSHYREWLKSADLALYKAKNAGR 359
|
.
gi 15595487 318 D 318
Cdd:PRK10245 360 N 360
|
|
| PAS_3 |
pfam08447 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
57-145 |
3.75e-18 |
|
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: 77.76 E-value: 3.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595487 57 VYVSPAYEKIFGRSAALLLADYEEWRNSIYPDDLDYADSSLLQVLERGAVEQREYRIVRGDGEVRWLNDKCFVsRQGEAG 136
Cdd:pfam08447 2 IYWSPRFEEILGYTPEELLGKGESWLDLVHPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARP-IRDENG 80
|
....*....
gi 15595487 137 LPLMVVGIA 145
Cdd:pfam08447 81 KPVRVIGVA 89
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
193-313 |
4.41e-17 |
|
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: 76.24 E-value: 4.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595487 193 PLAFLLLDVDDFKKINDRFGHQVGDQVLQRIAQSGSAALRR-GDLFGRIGGEEFAVLLPGCDEQTARQIGERLQREVQRL 271
Cdd:cd07556 1 PVTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRsGDLKIKTIGDEFMVVSGLDHPAAAVAFAEDMREAVSAL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 15595487 272 RFQEGEH-SFGITVSQGLTV-----LQADDEGLGALYSRADAAMYSAK 313
Cdd:cd07556 81 NQSEGNPvRVRIGIHTGPVVvgvigSRPQYDVWGALVNLASRMESQAK 128
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
23-245 |
3.43e-16 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 76.99 E-value: 3.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595487 23 AEVARLKEREQLFSALLASVNSVLWAYDwQNRRMVYVSPAYEKIFGRSAALLLAdyEEWRNSIYPDDLDYADSSLLQVLE 102
Cdd:COG2202 1 TAEEALEESERRLRALVESSPDAIIITD-LDGRILYVNPAFERLTGYSAEELLG--KTLRDLLPPEDDDEFLELLRAALA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595487 103 RGAVEQREYRIVRGDGEVRWLNDKCFVSRqGEAGLPLMVVGIAEDITDKKHMESELQRlattdvltqsSNRRY--FFDSA 180
Cdd:COG2202 78 GGGVWRGELRNRRKDGSLFWVELSISPVR-DEDGEITGFVGIARDITERKRAEEALRE----------SEERLrlLVENA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15595487 181 EAAFKECRREGIPL-------AFLLLDVDDF--KKINDRFGHQVGDQVLQRIAQSGSAALRRGDLFGRIGGEEF 245
Cdd:COG2202 147 PDGIFVLDLDGRILyvnpaaeELLGYSPEELlgKSLLDLLHPEDRERLLELLRRLLEGGRESYELELRLKDGDG 220
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
156-315 |
3.27e-13 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 69.65 E-value: 3.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595487 156 SELQRLATTDVLTQSSNRRYFFDSAEAAFKECRREGIPlAFLLLDVDDFKKINDRFGHQVGDQVLQRIAqsgsaalRRGD 235
Cdd:PRK09966 242 AQLLRTALHDPLTGLANRAAFRSGINTLMNNSDARKTS-ALLFLDGDNFKYINDTWGHATGDRVLIEIA-------KRLA 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595487 236 LFG-------RIGGEEFAVLLPGC-DEQTARQIGERLQREVQRLRFQEGEHSFGITVSQG--LTVLQADDEGLGALysrA 305
Cdd:PRK09966 314 EFGglrhkayRLGGDEFAMVLYDVqSESEVQQICSALTQIFNLPFDLHNGHQTTMTLSIGyaMTIEHASAEKLQEL---A 390
|
170
....*....|
gi 15595487 306 DAAMYSAKRQ 315
Cdd:PRK09966 391 DHNMYQAKHQ 400
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
27-162 |
2.98e-12 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 66.41 E-value: 2.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595487 27 RLKEREQLFSALLASVNSVLWAYDwQNRRMVYVSPAYEKIFGRSAALLL-ADYEEwrnsIYPDDLDYADSsLLQVLERG- 104
Cdd:COG3852 1 ALRESEELLRAILDSLPDAVIVLD-ADGRITYVNPAAERLLGLSAEELLgRPLAE----LFPEDSPLREL-LERALAEGq 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 15595487 105 AVEQREYRIVRGDGEVRWLNdkCFVSRQGEAGLPLMVVGIAEDITDKKHMESELQRLA 162
Cdd:COG3852 75 PVTEREVTLRRKDGEERPVD--VSVSPLRDAEGEGGVLLVLRDITERKRLERELRRAE 130
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
235-313 |
3.11e-12 |
|
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: 64.16 E-value: 3.11e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15595487 235 DLFGRIGGEEFAVLLPGCDEQTARQIGERLQREVQRLRfqegehSFGITVSQGLtvlqADDEglgaLYSRADaAMYSAK 313
Cdd:COG3706 116 DLVARYGGEEFAILLPGTDLEGALAVAERIREAVAELP------SLRVTVSIGV----AGDS----LLKRAD-ALYQAR 179
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
31-158 |
4.66e-12 |
|
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: 62.31 E-value: 4.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595487 31 REQLFSALLASVNSVLWAYDwQNRRMVYVSPAYEKIFGRSAALLLADYeeWRNSIYPDDLDYADSSLLQVLE-RGAVEQR 109
Cdd:TIGR00229 1 SEERYRAIFESSPDAIIVID-LEGNILYVNPAFEEIFGYSAEELIGRN--VLELIPEEDREEVRERIERRLEgEPEPVSE 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 15595487 110 EYRIVRGDGEVRWLNDkcFVSRQGEAGLPLMVVGIAEDITDKKHMESEL 158
Cdd:TIGR00229 78 ERRVRRKDGSEIWVEV--SVSPIRTNGGELGVVGIVRDITERKEAEEAL 124
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
158-316 |
1.24e-11 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 65.56 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595487 158 LQRLATTDVLTQSSNRRYFfdsaEAAFKECRREGIPLAFLLLDVDDFKKINDRFGHQVGDQVLQRIAQSGSAALRRGDLF 237
Cdd:PRK11359 372 IEQLIQFDPLTGLPNRNNL----HNYLDDLVDKAVSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDQYL 447
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15595487 238 GRIGGEEFAVLLPGCDEQTARQIGERLQREVQRLRFQEGeHSFGITVSQGLTVLQADDEglGALYSRADAAMYSAKRQG 316
Cdd:PRK11359 448 CRIEGTQFVLVSLENDVSNITQIADELRNVVSKPIMIDD-KPFPLTLSIGISYDVGKNR--DYLLSTAHNAMDYIRKNG 523
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
28-169 |
3.63e-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: 63.84 E-value: 3.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595487 28 LKEREQLFSALLASVNS--VLWAYDWqnrRMVYVSPAYEKIFGRSAALLL--ADYEEWRnsiyPDDLDYADSSLLQVLER 103
Cdd:COG5809 136 LRESEEKFRLIFNHSPDgiIVTDLDG---RIIYANPAACKLLGISIEELIgkSILELIH----SDDQENVAAFISQLLKD 208
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15595487 104 GAVEQREYRIVRGDGEVRWLNDKCfvSRQGEAGLPLMVVGIAEDITDKKHMESELQRLATTDVLTQ 169
Cdd:COG5809 209 GGIAQGEVRFWTKDGRWRLLEASG--APIKKNGEVDGIVIIFRDITERKKLEELLRKSEKLSVVGE 272
|
|
| KinA |
COG5805 |
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ... |
4-169 |
1.46e-08 |
|
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: 55.89 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595487 4 LTGIPEDPQEAALALL------HSRAEVARLKEREQLFSALLASVNSVLWAYDwQNRRMVYVSPAYEKIFGRSAALLLAD 77
Cdd:COG5805 122 VKLFPIYNQNGQAAILalrditKKKKIEEILQEQEERLQTLIENSPDLICVID-TDGRILFINESIERLFGAPREELIGK 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595487 78 yeEWRNSIYPDDLDYADSSLLQVLERGAVEQREYRIVRGDGEVRWLNDKCfVSRQGEAGLPLMVVGIAEDITDKKHMESE 157
Cdd:COG5805 201 --NLLELLHPCDKEEFKERIESITEVWQEFIIEREIITKDGRIRYFEAVI-VPLIDTDGSVKGILVILRDITEKKEAEEL 277
|
170
....*....|..
gi 15595487 158 LQRLATTDVLTQ 169
Cdd:COG5805 278 MARSEKLSIAGQ 289
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
26-159 |
1.66e-08 |
|
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: 55.37 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595487 26 ARLKEREQLFSALLASVNSVLWAYDwQNRRMVYVSPAYEKIFGRSAALLLADyeEWRNSIYPDDLDYADSSLLQVLERGA 105
Cdd:COG5809 8 LQLRKSEQRFRSLFENAPDAILILD-LEGKILKVNPAAERIFGYTEDELLGT--NILDFLHPDDEKELREILKLLKEGES 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 15595487 106 VEQREYRIVRGDGEVRWLNDKCFVSRqGEAGLPLMVVGIAEDITDKKHMESELQ 159
Cdd:COG5809 85 RDELEFELRHKNGKRLEFSSKLSPIF-DQNGDIEGMLAISRDITERKRMEEALR 137
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
86-162 |
3.91e-07 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 51.60 E-value: 3.91e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15595487 86 YPDDLdYADSSLLQVLERGAVE--QREYRIVRGDGEVRWLNDKCFVSRQgEAGLPLMVVGIAEDITDKKHMESELQRLA 162
Cdd:PRK09776 333 WPEDL-NKDLQQVEKLLSGEINsySMEKRYYRRDGEVVWALLAVSLVRD-TDGTPLYFIAQIEDINELKRTEQVNERLM 409
|
|
| RocR |
COG3829 |
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ... |
23-179 |
6.08e-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: 50.54 E-value: 6.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595487 23 AEVARLKEREQLFSALLASVNSVLWAYDwQNRRMVYVSPAYEKIFGRSAALLLAdyeewRNSiypDDLdYADSSLLQVLE 102
Cdd:COG3829 1 AEELELKELEEELEAILDSLDDGIIVVD-ADGRITYVNRAAERILGLPREEVIG-----KNV---TEL-IPNSPLLEVLK 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15595487 103 RGAVEQREYRIVRGDGEvrwlndKCFVSRQG--EAGLPLMVVGIAEDITDKKHMESELQRlattDVLTQSSNRRYFFDS 179
Cdd:COG3829 71 TGKPVTGVIQKTGGKGK------TVIVTAIPifEDGEVIGAVETFRDITELKRLERKLRE----EELERGLSAKYTFDD 139
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
55-148 |
7.18e-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: 7.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595487 55 RMVYVSPAYEKIFGRSAALLLAdyEEWRNSIYPDDLDYADSSLLQVLERGAVEQREYRIVRGDGEVRWLNDkCFVSRQGE 134
Cdd:cd00130 13 RILYANPAAEQLLGYSPEELIG--KSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLV-SLTPIRDE 89
|
90
....*....|....
gi 15595487 135 AGLPLMVVGIAEDI 148
Cdd:cd00130 90 GGEVIGLLGVVRDI 103
|
|
| PRK13560 |
PRK13560 |
hypothetical protein; Provisional |
15-159 |
7.96e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 106506 [Multi-domain] Cd Length: 807 Bit Score: 47.36 E-value: 7.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595487 15 ALALLHSRAEvaRLKEREQLFSALLASVNSVLWAYDWQNRR---MVYVSPAYEKiFGRSAALLLADYEEWRNSIYPDDLD 91
Cdd:PRK13560 455 AIALLVDITE--RKQVEEQLLLANLIVENSPLVLFRWKAEEgwpVELVSKNITQ-FGYEPDEFISGKRMFAAIIHPADLE 531
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15595487 92 YADSSLLQVLERGAVE-QREYRIVRGDGEVRWLNDKCFVSRQGEaGLPLMVVGIAEDITDKKHMESELQ 159
Cdd:PRK13560 532 QVAAEVAEFAAQGVDRfEQEYRILGKGGAVCWIDDQSAAERDEE-GQISHFEGIVIDISERKHAEEKIK 599
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
53-148 |
9.48e-06 |
|
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 can bind gases (O2, CO and NO), FAD, 4-hydroxycinnamic acid and NAD+ (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 395786 [Multi-domain] Cd Length: 113 Bit Score: 43.95 E-value: 9.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595487 53 NRRMVYVSPAYEKIFGRSAallladyEEWRNSIYPDDLDYADSSLLQVLERGAVEQR------EYRIVRGDGEVRWLNDK 126
Cdd:pfam00989 20 DGRILYVNAAAEELLGLSR-------EEVIGKSLLDLIPEEDDAEVAELLRQALLQGeesrgfEVSFRVPDGRPRHVEVR 92
|
90 100
....*....|....*....|..
gi 15595487 127 CfVSRQGEAGLPLMVVGIAEDI 148
Cdd:pfam00989 93 A-SPVRDAGGEILGFLGVLRDI 113
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
165-271 |
2.82e-04 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 42.54 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595487 165 DVLTQSSNRrYFFDSA-EAAFKECRREGIPLAFLLLDVDDFKKINDRFGHQVGDQVLQRIAQSGSAALRR--GDLFGRIG 241
Cdd:PRK11059 231 DAKTGLGNR-LFFDNQlATLLEDQEMVGAHGVVMLIRLPDFDLLQEEWGESQVEELLFELINLLSTFVMRypGALLARYS 309
|
90 100 110
....*....|....*....|....*....|
gi 15595487 242 GEEFAVLLPGCDEQTARQIGERLQREVQRL 271
Cdd:PRK11059 310 RSDFAVLLPHRSLKEADSLASQLLKAVDAL 339
|
|
| PAC |
smart00086 |
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ... |
108-151 |
1.03e-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: 1.03e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 15595487 108 QREYRIVRGDGEVRWLNDKCFVsRQGEAGLPLMVVGIAEDITDK 151
Cdd:smart00086 1 TVEYRLRRKDGSYIWVLVSASP-IRDEDGEVEGILGVVRDITER 43
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
236-320 |
7.71e-03 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 38.16 E-value: 7.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595487 236 LFGRIGGEEFAVLLPGCDE-----QTARQIgerLQREVQRLRFQEGE----HSFGITVSQGltvlqadDEGLGALYSRAD 306
Cdd:PRK13561 301 VLAQISGYDFAIIANGVKEpwhaiTLGQQV---LTIINERLPIQRIQlrpsCSIGIAMFYG-------DLTAEQLYSRAI 370
|
90
....*....|....
gi 15595487 307 AAMYSAKRQGKDCI 320
Cdd:PRK13561 371 SAAFTARRKGKNQI 384
|
|
| |
