|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
1-556 |
0e+00 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 889.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565651138 1 MPDKLLISRWRTKNPIRVVNFCFCAVFIFSTLLTWREGVILQDAFISAQRNQLDSTATAMDRNLQYSVDKLLFYRAGMRY 80
Cdd:PRK15426 8 ENQSWLKKLARRLGPGHVVNLCFIVVLLFSTLLTWREVVVLEDAYISSQRNHLENVANALDAQLQYNVDKLIFLRNGMRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565651138 81 AMHNLLEGPQTDALIDGFKAERDKPEWTLPTGRELAPEIQGVSDAFIGQSTLLERNDALLYSELNATLALGHMLSIAdAR 160
Cdd:PRK15426 88 ALVAPLDFPALDAAVTQFEQHRDEHVWQLELPRRRTLPVNGVSDAFVSGLTLLSRDDEDLANELTAALELGYLLRLA-HN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565651138 161 SERPEVRTFYVSRAGFYLTNLPFFDHGSIPELYYQQVSSRWFIDQSQRRNPGRGVRWLHGR-DLSMPSGQRVTASIPVDD 239
Cdd:PRK15426 167 SSSLVERAMYVSRAGFYVSTYPTLFPSDVPTRYYQYVTQPWFIGQSQRRNPGRGVRWFTSQpDDASNTEPQVTASVPVDA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565651138 240 NGRWFGVLAMDFPVSAMRDFLKNALnDDDSGGEILLFDSQLSPIATTASGNDAALHFTAQDKAMLARQMELDNEGDARID 319
Cdd:PRK15426 247 GNYWYGVLAMDIPVRSLQQFLRNAI-DKDLDGEYQLYDSHLRLLTSSAPGVRTGNIFDPRELALLARAMEHDTRGGIRMG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565651138 320 TRFITWAKLDYFDGVLVKVTTVSQSAEGRFGKVAMVLGLLWLLFTAMLFLSWRVIVGMVRNMLTMQRSLKWRAWYDTLTR 399
Cdd:PRK15426 326 SRYVSWERLDHFDGVLVRVHTLREGVRGDFGSISIALTLLWALFTAMLLISWYVIRRMVSNMFVLQSSLQWQAWHDPLTR 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565651138 400 LYNRGAFFERARMAAKTCFAQSEPFSVIQLDLDHFKSINDRYGHQAGDKVLTWAAGMLSRSLRVQDVAGRVGGEEFCVIL 479
Cdd:PRK15426 406 LYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRVGGEEFCVVL 485
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 565651138 480 PGTPAEGARQVAERIRQRINSQEILVRPDTTIRISVSVGVSEARRDGDYDFEHLQSIADHRLYLAKQRGRNQVCDEG 556
Cdd:PRK15426 486 PGASLAEAAQVAERIRLRINEKEILVAKSTTIRISASLGVSSAEEDGDYDFEQLQSLADRRLYLAKQAGRNRVCASD 562
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
391-552 |
4.14e-65 |
|
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: 209.50 E-value: 4.14e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565651138 391 RAWYDTLTRLYNRGAFFERARMAAKTCFAQSEPFSVIQLDLDHFKSINDRYGHQAGDKVLTWAAGMLSRSLRVQDVAGRV 470
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565651138 471 GGEEFCVILPGTPAEGARQVAERIRQRINSQEILVRPDTTIRISVSVGVSEARRDGdYDFEHLQSIADHRLYLAKQRGRN 550
Cdd:TIGR00254 81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSETLTVTVSIGVACYPGHG-LTLEELLKRADEALYQAKKAGRN 159
|
..
gi 565651138 551 QV 552
Cdd:TIGR00254 160 RV 161
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
358-553 |
1.75e-60 |
|
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: 201.36 E-value: 1.75e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565651138 358 LLWLLFTAMLFLSWRVIVGMVRNMLTMQRSLKWRAWYDTLTRLYNRGAFFERARMAAKTCFAQSEPFSVIQLDLDHFKSI 437
Cdd:COG2199 80 VLELLLLLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRI 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565651138 438 NDRYGHQAGDKVLTWAAGMLSRSLRVQDVAGRVGGEEFCVILPGTPAEGARQVAERIRQRINSQEILVrPDTTIRISVSV 517
Cdd:COG2199 160 NDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFEL-EGKELRVTVSI 238
|
170 180 190
....*....|....*....|....*....|....*.
gi 565651138 518 GVSEARRDGDyDFEHLQSIADHRLYLAKQRGRNQVC 553
Cdd:COG2199 239 GVALYPEDGD-SAEELLRRADLALYRAKRAGRNRVV 273
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
394-553 |
3.81e-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: 196.24 E-value: 3.81e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565651138 394 YDTLTRLYNRGAFFERARMAAKTCFAQSEPFSVIQLDLDHFKSINDRYGHQAGDKVLTWAAGMLSRSLRVQDVAGRVGGE 473
Cdd:cd01949 2 TDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565651138 474 EFCVILPGTPAEGARQVAERIRQRINSQEILVrpDTTIRISVSVGVSEARRDGDyDFEHLQSIADHRLYLAKQRGRNQVC 553
Cdd:cd01949 82 EFAILLPGTDLEEAEALAERLREAIEEPFFID--GQEIRVTASIGIATYPEDGE-DAEELLRRADEALYRAKRSGRNRVV 158
|
|
| CHASE7 |
pfam17151 |
Periplasmic sensor domain; CHASE7 is a conserved periplasmic sensor domain found in histidine ... |
34-217 |
1.23e-55 |
|
Periplasmic sensor domain; CHASE7 is a conserved periplasmic sensor domain found in histidine kinases and diguanylate cyclases/phosphodiesterases, including the diguanylate cyclase DgcQ (YedQ) that regulates biofilm formation and motility in Escherichia coli.
Pssm-ID: 407283 Cd Length: 187 Bit Score: 185.40 E-value: 1.23e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565651138 34 TWREGVILQDAFISAQRNQLDSTATAMDRNLQYSVDKLLFYRAGMRYAMHNLLEGPQTDALIDGFKAERDKPEWTLPTGR 113
Cdd:pfam17151 1 IWREVVVLEDAYVASQRNHLENVANALDRLLQFNVDRLLFLRNGMHEALQAPLDFDALRDAIQQFAEHRNDHAWQLRLDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565651138 114 ELAPEIQGVSDAFIGQSTLLERNDALLYSELNATLALGHMLSIADARSERPEvRTFYVSRAGFYLTNLPFFDHGSIPELY 193
Cdd:pfam17151 81 RRTLPVFGVSDAFVTRTPLLSRDDPKLANELTAALELGYLLRLAHNSPDLAE-RIMYVSRSGFYVSTLPTISESDVNTRY 159
|
170 180
....*....|....*....|....
gi 565651138 194 YQQVSSRWFIDQSQRRNPGRGVRW 217
Cdd:pfam17151 160 YQYVTAPWFIGQSQRANPARGVRW 183
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
390-553 |
1.40e-51 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 173.97 E-value: 1.40e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565651138 390 WRAWYDTLTRLYNRGAFFERARMAAKTCFAQSEPFSVIQLDLDHFKSINDRYGHQAGDKVLTWAAGMLSRSLRVQDVAGR 469
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565651138 470 VGGEEFCVILPGTPAEGARQVAERIRQRINSQEILvrPDTTIRISVSVGVSEARRDGDyDFEHLQSIADHRLYLAKQRGR 549
Cdd:smart00267 81 LGGDEFALLLPETSLEEAIALAERILQQLREPIII--HGIPLYLTISIGVAAYPNPGE-DAEDLLKRADTALYQAKKAGR 157
|
....
gi 565651138 550 NQVC 553
Cdd:smart00267 158 NQVA 161
|
|
| diguan_SiaD |
NF038266 |
biofilm regulation diguanylate cyclase SiaD; |
379-552 |
7.53e-43 |
|
biofilm regulation diguanylate cyclase SiaD;
Pssm-ID: 468439 [Multi-domain] Cd Length: 252 Bit Score: 153.60 E-value: 7.53e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565651138 379 RNMLTMQRSLKWRAWYDTLTRLYNRGAFFERARMAAKTCFAQSEPFSVIQLDLDHFKSINDRYGHQAGDKVLTWAAGMLS 458
Cdd:NF038266 81 RMMRDLNEALREASTRDPLTGLPNRRLLMERLREEVERARRSGRPFTLAMLDVDHFKRINDRYGHEVGDRVLVEIARTLR 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565651138 459 RSLRVQDVAGRVGGEEFCVILPGTPAEGARQVAERIRQRINSQEILVRPDtTIRISVSVGVSEARRDGDyDFEHLQSIAD 538
Cdd:NF038266 161 AELREYDLCGRWGGEEFLLLLPETGLEEAQVVLERLREAVRALAVRVGDD-VLSVTASAGLAEHRPPEE-GLSATLSRAD 238
|
170
....*....|....
gi 565651138 539 HRLYLAKQRGRNQV 552
Cdd:NF038266 239 QALYQAKRAGRDRV 252
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
1-556 |
0e+00 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 889.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565651138 1 MPDKLLISRWRTKNPIRVVNFCFCAVFIFSTLLTWREGVILQDAFISAQRNQLDSTATAMDRNLQYSVDKLLFYRAGMRY 80
Cdd:PRK15426 8 ENQSWLKKLARRLGPGHVVNLCFIVVLLFSTLLTWREVVVLEDAYISSQRNHLENVANALDAQLQYNVDKLIFLRNGMRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565651138 81 AMHNLLEGPQTDALIDGFKAERDKPEWTLPTGRELAPEIQGVSDAFIGQSTLLERNDALLYSELNATLALGHMLSIAdAR 160
Cdd:PRK15426 88 ALVAPLDFPALDAAVTQFEQHRDEHVWQLELPRRRTLPVNGVSDAFVSGLTLLSRDDEDLANELTAALELGYLLRLA-HN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565651138 161 SERPEVRTFYVSRAGFYLTNLPFFDHGSIPELYYQQVSSRWFIDQSQRRNPGRGVRWLHGR-DLSMPSGQRVTASIPVDD 239
Cdd:PRK15426 167 SSSLVERAMYVSRAGFYVSTYPTLFPSDVPTRYYQYVTQPWFIGQSQRRNPGRGVRWFTSQpDDASNTEPQVTASVPVDA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565651138 240 NGRWFGVLAMDFPVSAMRDFLKNALnDDDSGGEILLFDSQLSPIATTASGNDAALHFTAQDKAMLARQMELDNEGDARID 319
Cdd:PRK15426 247 GNYWYGVLAMDIPVRSLQQFLRNAI-DKDLDGEYQLYDSHLRLLTSSAPGVRTGNIFDPRELALLARAMEHDTRGGIRMG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565651138 320 TRFITWAKLDYFDGVLVKVTTVSQSAEGRFGKVAMVLGLLWLLFTAMLFLSWRVIVGMVRNMLTMQRSLKWRAWYDTLTR 399
Cdd:PRK15426 326 SRYVSWERLDHFDGVLVRVHTLREGVRGDFGSISIALTLLWALFTAMLLISWYVIRRMVSNMFVLQSSLQWQAWHDPLTR 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565651138 400 LYNRGAFFERARMAAKTCFAQSEPFSVIQLDLDHFKSINDRYGHQAGDKVLTWAAGMLSRSLRVQDVAGRVGGEEFCVIL 479
Cdd:PRK15426 406 LYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRVGGEEFCVVL 485
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 565651138 480 PGTPAEGARQVAERIRQRINSQEILVRPDTTIRISVSVGVSEARRDGDYDFEHLQSIADHRLYLAKQRGRNQVCDEG 556
Cdd:PRK15426 486 PGASLAEAAQVAERIRLRINEKEILVAKSTTIRISASLGVSSAEEDGDYDFEQLQSLADRRLYLAKQAGRNRVCASD 562
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
391-552 |
4.14e-65 |
|
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: 209.50 E-value: 4.14e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565651138 391 RAWYDTLTRLYNRGAFFERARMAAKTCFAQSEPFSVIQLDLDHFKSINDRYGHQAGDKVLTWAAGMLSRSLRVQDVAGRV 470
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565651138 471 GGEEFCVILPGTPAEGARQVAERIRQRINSQEILVRPDTTIRISVSVGVSEARRDGdYDFEHLQSIADHRLYLAKQRGRN 550
Cdd:TIGR00254 81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSETLTVTVSIGVACYPGHG-LTLEELLKRADEALYQAKKAGRN 159
|
..
gi 565651138 551 QV 552
Cdd:TIGR00254 160 RV 161
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
358-553 |
1.75e-60 |
|
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: 201.36 E-value: 1.75e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565651138 358 LLWLLFTAMLFLSWRVIVGMVRNMLTMQRSLKWRAWYDTLTRLYNRGAFFERARMAAKTCFAQSEPFSVIQLDLDHFKSI 437
Cdd:COG2199 80 VLELLLLLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRI 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565651138 438 NDRYGHQAGDKVLTWAAGMLSRSLRVQDVAGRVGGEEFCVILPGTPAEGARQVAERIRQRINSQEILVrPDTTIRISVSV 517
Cdd:COG2199 160 NDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFEL-EGKELRVTVSI 238
|
170 180 190
....*....|....*....|....*....|....*.
gi 565651138 518 GVSEARRDGDyDFEHLQSIADHRLYLAKQRGRNQVC 553
Cdd:COG2199 239 GVALYPEDGD-SAEELLRRADLALYRAKRAGRNRVV 273
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
394-553 |
3.81e-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: 196.24 E-value: 3.81e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565651138 394 YDTLTRLYNRGAFFERARMAAKTCFAQSEPFSVIQLDLDHFKSINDRYGHQAGDKVLTWAAGMLSRSLRVQDVAGRVGGE 473
Cdd:cd01949 2 TDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565651138 474 EFCVILPGTPAEGARQVAERIRQRINSQEILVrpDTTIRISVSVGVSEARRDGDyDFEHLQSIADHRLYLAKQRGRNQVC 553
Cdd:cd01949 82 EFAILLPGTDLEEAEALAERLREAIEEPFFID--GQEIRVTASIGIATYPEDGE-DAEELLRRADEALYRAKRSGRNRVV 158
|
|
| CHASE7 |
pfam17151 |
Periplasmic sensor domain; CHASE7 is a conserved periplasmic sensor domain found in histidine ... |
34-217 |
1.23e-55 |
|
Periplasmic sensor domain; CHASE7 is a conserved periplasmic sensor domain found in histidine kinases and diguanylate cyclases/phosphodiesterases, including the diguanylate cyclase DgcQ (YedQ) that regulates biofilm formation and motility in Escherichia coli.
Pssm-ID: 407283 Cd Length: 187 Bit Score: 185.40 E-value: 1.23e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565651138 34 TWREGVILQDAFISAQRNQLDSTATAMDRNLQYSVDKLLFYRAGMRYAMHNLLEGPQTDALIDGFKAERDKPEWTLPTGR 113
Cdd:pfam17151 1 IWREVVVLEDAYVASQRNHLENVANALDRLLQFNVDRLLFLRNGMHEALQAPLDFDALRDAIQQFAEHRNDHAWQLRLDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565651138 114 ELAPEIQGVSDAFIGQSTLLERNDALLYSELNATLALGHMLSIADARSERPEvRTFYVSRAGFYLTNLPFFDHGSIPELY 193
Cdd:pfam17151 81 RRTLPVFGVSDAFVTRTPLLSRDDPKLANELTAALELGYLLRLAHNSPDLAE-RIMYVSRSGFYVSTLPTISESDVNTRY 159
|
170 180
....*....|....*....|....
gi 565651138 194 YQQVSSRWFIDQSQRRNPGRGVRW 217
Cdd:pfam17151 160 YQYVTAPWFIGQSQRANPARGVRW 183
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
392-551 |
9.43e-55 |
|
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: 182.07 E-value: 9.43e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565651138 392 AWYDTLTRLYNRGAFFERARMAAKTCFAQSEPFSVIQLDLDHFKSINDRYGHQAGDKVLTWAAGMLSRSLRVQDVAGRVG 471
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565651138 472 GEEFCVILPGTPAEGARQVAERIRQRINSQEILVRPDTTIR-ISVSVGVSEARRDGDyDFEHLQSIADHRLYLAKQRGRN 550
Cdd:pfam00990 81 GDEFAILLPETSLEGAQELAERIRRLLAKLKIPHTVSGLPLyVTISIGIAAYPNDGE-DPEDLLKRADTALYQAKQAGRN 159
|
.
gi 565651138 551 Q 551
Cdd:pfam00990 160 R 160
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
390-553 |
1.40e-51 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 173.97 E-value: 1.40e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565651138 390 WRAWYDTLTRLYNRGAFFERARMAAKTCFAQSEPFSVIQLDLDHFKSINDRYGHQAGDKVLTWAAGMLSRSLRVQDVAGR 469
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565651138 470 VGGEEFCVILPGTPAEGARQVAERIRQRINSQEILvrPDTTIRISVSVGVSEARRDGDyDFEHLQSIADHRLYLAKQRGR 549
Cdd:smart00267 81 LGGDEFALLLPETSLEEAIALAERILQQLREPIII--HGIPLYLTISIGVAAYPNPGE-DAEDLLKRADTALYQAKKAGR 157
|
....
gi 565651138 550 NQVC 553
Cdd:smart00267 158 NQVA 161
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
144-553 |
5.93e-43 |
|
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: 163.02 E-value: 5.93e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565651138 144 LNATLALGHMLSIADARSERPEVRTFYVSRAGFYLTNLPFFDHGSIPELYYQQVSSRWFIDQSQRRNPGRGVRWLHGRDL 223
Cdd:COG5001 3 ALAALLLLLLALLLALLLLALLLLALLLAALLALALLLLLLLLLLALLLAALLLLALLALLALLLLAAALLALALAALLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565651138 224 SMPSGQRVTASIPVDDNGRWFGVLAMDFPVSAMRDFLKNALNDDDSGGEILLFDSQLSPIATTASGNDAALHFTAQDKAM 303
Cdd:COG5001 83 AALLAALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARALL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565651138 304 LARQMELDNEGDARIDTRFITWAKLDYFDGVLVKVTTVSQSAEGRFGKVAMVLGLLWLLFTAMLFLSWRVIVGMVRNMLT 383
Cdd:COG5001 163 ALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565651138 384 MQRSLKWRAWYDTLTRLYNRGAFFERARMAAKTCFAQSEPFSVIQLDLDHFKSINDRYGHQAGDKVLTWAAGMLSRSLRV 463
Cdd:COG5001 243 AEERLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLRE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565651138 464 QDVAGRVGGEEFCVILPGTP-AEGARQVAERIRQRInSQEILVRpDTTIRISVSVGVSEARRDGDyDFEHLQSIADHRLY 542
Cdd:COG5001 323 GDTVARLGGDEFAVLLPDLDdPEDAEAVAERILAAL-AEPFELD-GHELYVSASIGIALYPDDGA-DAEELLRNADLAMY 399
|
410
....*....|.
gi 565651138 543 LAKQRGRNQVC 553
Cdd:COG5001 400 RAKAAGRNRYR 410
|
|
| diguan_SiaD |
NF038266 |
biofilm regulation diguanylate cyclase SiaD; |
379-552 |
7.53e-43 |
|
biofilm regulation diguanylate cyclase SiaD;
Pssm-ID: 468439 [Multi-domain] Cd Length: 252 Bit Score: 153.60 E-value: 7.53e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565651138 379 RNMLTMQRSLKWRAWYDTLTRLYNRGAFFERARMAAKTCFAQSEPFSVIQLDLDHFKSINDRYGHQAGDKVLTWAAGMLS 458
Cdd:NF038266 81 RMMRDLNEALREASTRDPLTGLPNRRLLMERLREEVERARRSGRPFTLAMLDVDHFKRINDRYGHEVGDRVLVEIARTLR 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565651138 459 RSLRVQDVAGRVGGEEFCVILPGTPAEGARQVAERIRQRINSQEILVRPDtTIRISVSVGVSEARRDGDyDFEHLQSIAD 538
Cdd:NF038266 161 AELREYDLCGRWGGEEFLLLLPETGLEEAQVVLERLREAVRALAVRVGDD-VLSVTASAGLAEHRPPEE-GLSATLSRAD 238
|
170
....*....|....
gi 565651138 539 HRLYLAKQRGRNQV 552
Cdd:NF038266 239 QALYQAKRAGRDRV 252
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
395-553 |
9.81e-39 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 147.74 E-value: 9.81e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565651138 395 DTLTRLYNRGAF-------FERARmaaktcfAQSEPFSVIQLDLDHFKSINDRYGHQAGDKVLTWAAGMLSRSLRVQDVA 467
Cdd:PRK09581 295 DGLTGLHNRRYFdmhlknlIERAN-------ERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLI 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565651138 468 GRVGGEEFCVILPGTPAEGARQVAERIRQRINSQE-ILVRPDTTIRISVSVGVSEARRDGDyDFEHLQSIADHRLYLAKQ 546
Cdd:PRK09581 368 ARYGGEEFVVVMPDTDIEDAIAVAERIRRKIAEEPfIISDGKERLNVTVSIGVAELRPSGD-TIEALIKRADKALYEAKN 446
|
....*..
gi 565651138 547 RGRNQVC 553
Cdd:PRK09581 447 TGRNRVV 453
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
391-552 |
1.32e-34 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 132.50 E-value: 1.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565651138 391 RAWYDTLTRLYNR---GAFFERARMAAktcfaQSEPFSVIQLDLDHFKSINDRYGHQAGDKVLTWAAGMLSRSLRVQDVA 467
Cdd:PRK09894 128 RSNMDVLTGLPGRrvlDESFDHQLRNR-----EPQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETV 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565651138 468 GRVGGEEFCVILPGTPAEGARQVAERIRQRINSQEIlVRPDTTIRISVSVGVSEARRDgdydfEHLQ---SIADHRLYLA 544
Cdd:PRK09894 203 YRYGGEEFIICLKAATDEEACRAGERIRQLIANHAI-THSDGRINITATFGVSRAFPE-----ETLDvviGRADRAMYEG 276
|
....*...
gi 565651138 545 KQRGRNQV 552
Cdd:PRK09894 277 KQTGRNRV 284
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
385-551 |
5.94e-24 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 103.37 E-value: 5.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565651138 385 QRSLKWRAWYDTLTRLYNRGAFFERARMAAKTCFAQSEPFSVIQLDLDHFKSINDRYGHQAGDKVLTWAAGMLSRSLRVQ 464
Cdd:PRK10245 198 KRRLQVMSTRDGMTGVYNRRHWETLLRNEFDNCRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGS 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565651138 465 DVAGRVGGEEFCVILPGTPAEGARQVAERIRQRINSQEILVRPDTTIRIsvSVGVSEARRDGDYDFEHLQSiADHRLYLA 544
Cdd:PRK10245 278 DVIGRFGGDEFAVIMSGTPAESAITAMSRVHEGLNTLRLPNAPQVTLRI--SVGVAPLNPQMSHYREWLKS-ADLALYKA 354
|
....*..
gi 565651138 545 KQRGRNQ 551
Cdd:PRK10245 355 KNAGRNR 361
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
384-552 |
2.63e-20 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 95.12 E-value: 2.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565651138 384 MQRSLKWRAWYDTLTRLYNRGAFFERARMAAKTCFAQSEPFSVIQLDLDHFKSINDRYGHQAGDKVLTWAAGMLSRSLRV 463
Cdd:PRK09776 657 MLRQLSYSASHDALTHLANRASFEKQLRRLLQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRS 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565651138 464 QDVAGRVGGEEFCVILPGTPAEGARQVAERIRQRINSQEiLVRPDTTIRISVSVGVSeARRDGDYDFEHLQSIADHRLYL 543
Cdd:PRK09776 737 SDVLARLGGDEFGLLLPDCNVESARFIATRIISAINDYH-FPWEGRVYRVGASAGIT-LIDANNHQASEVMSQADIACYA 814
|
....*....
gi 565651138 544 AKQRGRNQV 552
Cdd:PRK09776 815 AKNAGRGRV 823
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
385-553 |
5.50e-18 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 87.43 E-value: 5.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565651138 385 QRSLKWRAWYDTLTRLYNRGAFFERARMAAKTcfAQSEPFSVIQLDLDHFKSINDRYGHQAGDKVLTWAAGMLSRSLRVQ 464
Cdd:PRK10060 230 QERLRILANTDSITGLPNRNAIQELIDHAINA--ADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEED 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565651138 465 DVAGRVGGEEFCVILPGTPAEGARQVAERirqrinsqeILVRPDTTIRI-------SVSVGVSEARRDGDyDFEHLQSIA 537
Cdd:PRK10060 308 QTLARLGGDEFLVLASHTSQAALEAMASR---------ILTRLRLPFRIglievytGCSIGIALAPEHGD-DSESLIRSA 377
|
170
....*....|....*.
gi 565651138 538 DHRLYLAKQRGRNQVC 553
Cdd:PRK10060 378 DTAMYTAKEGGRGQFC 393
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
423-545 |
1.98e-14 |
|
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: 70.08 E-value: 1.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565651138 423 PFSVIQLDLDHFKSINDRYGHQAGDKVLTWAAGMLSRSL-RVQDVAGRVGGEEFCVILPGTPAEGARQVAERIRQRINSQ 501
Cdd:cd07556 1 PVTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIrRSGDLKIKTIGDEFMVVSGLDHPAAAVAFAEDMREAVSAL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 565651138 502 EILVRPDTTIRISVSVGVSEARRDG---DYD-FEHLQSIADHRLYLAK 545
Cdd:cd07556 81 NQSEGNPVRVRIGIHTGPVVVGVIGsrpQYDvWGALVNLASRMESQAK 128
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
465-545 |
1.09e-13 |
|
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: 69.55 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565651138 465 DVAGRVGGEEFCVILPGTPAEGARQVAERIRQRINSQEilvrpdtTIRISVSVGVSEarrdgdydfEHLQSIADhRLYLA 544
Cdd:COG3706 116 DLVARYGGEEFAILLPGTDLEGALAVAERIREAVAELP-------SLRVTVSIGVAG---------DSLLKRAD-ALYQA 178
|
.
gi 565651138 545 K 545
Cdd:COG3706 179 R 179
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
392-547 |
4.04e-12 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 68.11 E-value: 4.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565651138 392 AWYDTLTRLYNRGAFFERARMAAKTCFAQSEPfSVIQLDLDHFKSINDRYGHQAGDKVLTWAAGMLSRSLRVQDVAGRVG 471
Cdd:PRK09966 248 ALHDPLTGLANRAAFRSGINTLMNNSDARKTS-ALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHKAYRLG 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565651138 472 GEEFCVILPGTPAE-GARQVAERIRQRINsqeilvRP---DTTIRISVSVGVSEARRDGDYDFEHLQSIADHRLYLAKQR 547
Cdd:PRK09966 327 GDEFAMVLYDVQSEsEVQQICSALTQIFN------LPfdlHNGHQTTMTLSIGYAMTIEHASAEKLQELADHNMYQAKHQ 400
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
394-540 |
3.44e-11 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 65.95 E-value: 3.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565651138 394 YDTLTRLYNRGAFFeraRMAAKTCFAQSEPfSVIQLDLDHFKSINDRYGHQAGDKVLTWAAGMLSRSLRVQDVAGRVGGE 473
Cdd:PRK11359 378 FDPLTGLPNRNNLH---NYLDDLVDKAVSP-VVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGT 453
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 565651138 474 EFCVILPGTPAEGARQVAERIrQRINSQEILVrPDTTIRISVSVGVS-EARRDGDYDFEHLQSIADHR 540
Cdd:PRK11359 454 QFVLVSLENDVSNITQIADEL-RNVVSKPIMI-DDKPFPLTLSIGISyDVGKNRDYLLSTAHNAMDYI 519
|
|
| dCache_1 |
pfam02743 |
Cache domain; Double cache domain 1 covers the last three strands from the membrane distal ... |
118-336 |
9.28e-05 |
|
Cache domain; Double cache domain 1 covers the last three strands from the membrane distal PAS-like domain, the first two strands of the membrane proximal domain, and the connecting elements between the two domains. This domain when present in chemoreceptors recognize several signals such as proteinogenic amino acids, GABA, Histamine and polyamines, decanoic acid, Autoinducer-2, purine derivatives, quaternary amines, citrate and taurine, among others. When associated with histidine kinases, it recognizes C3/C4-dicarboxylic acids, Spermine, guanosine and Autoinducer-2 (Mantilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1 https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 460673 [Multi-domain] Cd Length: 237 Bit Score: 44.25 E-value: 9.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565651138 118 EIQGVSDAFIGQSTLLERNDALLySELNATLALGHMLSIADARSERPEVRTFYVSRAGFYLTNLpffdHGSIPELYYQQV 197
Cdd:pfam02743 21 NIESYLDSLEEILELLASNPDLQ-DLLSAPAEEELAKLESLLRSNPGISSIYLVDADGRVLASS----DESPSYPGLDVS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565651138 198 SSRWFIDQSQRRNPGRGVrWLHGRDLSMPSGQRVTASIPV-DDNGRWFGVLAMDFPVSAMRDFLKNALNDDdsGGEILLF 276
Cdd:pfam02743 96 ERPWYKEALKGGGGIIWV-FSSPYPSSESGEPVLTIARPIyDDDGEVIGVLVADLDLDTLQELLSQIKLGE--GGYVFIV 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 565651138 277 DSQLSPIATTASGN--DAALHFTAQDKAMLARQMELDNEGDARIDTRFIT-WAKLDYFDGVLV 336
Cdd:pfam02743 173 DSDGRILAHPLGKNlrSLLAPFLGKSLADALPGSGITEIAVDLDGEDYLVaYAPIPGTGWTLV 235
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
466-552 |
1.59e-03 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 41.24 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565651138 466 VAGRVGGEEFCVILPG--TPAEG---ARQVAERIRQRINSQEILVRPdttiriSVSVGVseARRDGDYDFEHLQSIADHR 540
Cdd:PRK13561 301 VLAQISGYDFAIIANGvkEPWHAitlGQQVLTIINERLPIQRIQLRP------SCSIGI--AMFYGDLTAEQLYSRAISA 372
|
90
....*....|..
gi 565651138 541 LYLAKQRGRNQV 552
Cdd:PRK13561 373 AFTARRKGKNQI 384
|
|
| |
