|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
1-564 |
0e+00 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 1031.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530604700 1 MQHETKMENQSWLKKLARRLGPGHVVNLCFIVVLLFSTLLTWREVVVLEDAYISSQRNHLENVANALDKHLQYNVDKLIF 80
Cdd:PRK15426 1 MPHETRLENQSWLKKLARRLGPGHVVNLCFIVVLLFSTLLTWREVVVLEDAYISSQRNHLENVANALDAQLQYNVDKLIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530604700 81 LRNGMREALVAPLDFTSLRDAVTEFEQHRDEHAWKIELNRRRTLPVNGVSDALVSEGNLLSRENESLDNEITAALEVGYL 160
Cdd:PRK15426 81 LRNGMREALVAPLDFPALDAAVTQFEQHRDEHVWQLELPRRRTLPVNGVSDAFVSGLTLLSRDDEDLANELTAALELGYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530604700 161 LRLAHNSSSMVEQAMYVSRAGFYVSTQPTLFTRNVPTRYYGYVTQPWFIGHSQRENRHRAVRWFTSQPEHASNTEPQVTV 240
Cdd:PRK15426 161 LRLAHNSSSLVERAMYVSRAGFYVSTYPTLFPSDVPTRYYQYVTQPWFIGQSQRRNPGRGVRWFTSQPDDASNTEPQVTA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530604700 241 SVPVDSNNYWYGVLGMSIPVRTMQQFLRNAIDKNLDGEYQLYDSKLRFLTSSNPDHPTGNIFDPRELALLAQAMEHDTRG 320
Cdd:PRK15426 241 SVPVDAGNYWYGVLAMDIPVRSLQQFLRNAIDKDLDGEYQLYDSHLRLLTSSAPGVRTGNIFDPRELALLARAMEHDTRG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530604700 321 GIRMYSRYVSWERLDHFDGVLVRVHTLSEGVRGDFGSISIALTLLWALFTTMLLISWYVIRRMVSNMYVLQSSLQWQAWH 400
Cdd:PRK15426 321 GIRMGSRYVSWERLDHFDGVLVRVHTLREGVRGDFGSISIALTLLWALFTAMLLISWYVIRRMVSNMFVLQSSLQWQAWH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530604700 401 DTLTRLYNRGALFEKARPLAKMCQTHQHPFSVIQVDLDHFKAINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRVGGEE 480
Cdd:PRK15426 401 DPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRVGGEE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530604700 481 FCVILPGASLTEAAEVAERIRLKLNEKEMLIAKSTTIRISASLGVSSSEETGDYDFEQLQSLADRRLYLAKQAGRNRVCA 560
Cdd:PRK15426 481 FCVVLPGASLAEAAQVAERIRLRINEKEILVAKSTTIRISASLGVSSAEEDGDYDFEQLQSLADRRLYLAKQAGRNRVCA 560
|
....
gi 2530604700 561 SDNA 564
Cdd:PRK15426 561 SDNA 564
|
|
| CHASE7 |
pfam17151 |
Periplasmic sensor domain; CHASE7 is a conserved periplasmic sensor domain found in histidine ... |
41-227 |
4.05e-109 |
|
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: 324.07 E-value: 4.05e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530604700 41 TWREVVVLEDAYISSQRNHLENVANALDKHLQYNVDKLIFLRNGMREALVAPLDFTSLRDAVTEFEQHRDEHAWKIELNR 120
Cdd:pfam17151 1 IWREVVVLEDAYVASQRNHLENVANALDRLLQFNVDRLLFLRNGMHEALQAPLDFDALRDAIQQFAEHRNDHAWQLRLDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530604700 121 RRTLPVNGVSDALVSEGNLLSRENESLDNEITAALEVGYLLRLAHNSSSMVEQAMYVSRAGFYVSTQPTLFTRNVPTRYY 200
Cdd:pfam17151 81 RRTLPVFGVSDAFVTRTPLLSRDDPKLANELTAALELGYLLRLAHNSPDLAERIMYVSRSGFYVSTLPTISESDVNTRYY 160
|
170 180
....*....|....*....|....*..
gi 2530604700 201 GYVTQPWFIGHSQRENRHRAVRWFTSQ 227
Cdd:pfam17151 161 QYVTAPWFIGQSQRANPARGVRWFTSP 187
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
397-562 |
2.31e-80 |
|
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: 249.18 E-value: 2.31e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530604700 397 QAWHDTLTRLYNRGALFEKARPLAKMCQTHQHPFSVIQVDLDHFKAINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRV 476
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530604700 477 GGEEFCVILPGASLTEAAEVAERIRLKLNEKEMLIAKSTTIRISASLGVSSSEEtGDYDFEQLQSLADRRLYLAKQAGRN 556
Cdd:TIGR00254 81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSETLTVTVSIGVACYPG-HGLTLEELLKRADEALYQAKKAGRN 159
|
....*.
gi 2530604700 557 RVCASD 562
Cdd:TIGR00254 160 RVVVAD 165
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
307-559 |
3.89e-62 |
|
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: 205.98 E-value: 3.89e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530604700 307 LALLAQAMEHDTRGGIRMYSRYVSWERLDHFDGVLVRVHTLSEGVRGDFGSISIALTLLWALFTTMLLISWYVIRRMVSN 386
Cdd:COG2199 23 LLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLLLLALEDITE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530604700 387 MYVLQSSLQWQAWHDTLTRLYNRGALFEKARPLAKMCQTHQHPFSVIQVDLDHFKAINDRFGHQAGDRVLSHAAGLISSS 466
Cdd:COG2199 103 LRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRAS 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530604700 467 LRAQDVAGRVGGEEFCVILPGASLTEAAEVAERIRLKLNEKEMLIaKSTTIRISASLGVSSSEETGDyDFEQLQSLADRR 546
Cdd:COG2199 183 LRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFEL-EGKELRVTVSIGVALYPEDGD-SAEELLRRADLA 260
|
250
....*....|...
gi 2530604700 547 LYLAKQAGRNRVC 559
Cdd:COG2199 261 LYRAKRAGRNRVV 273
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
400-559 |
3.37e-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: 196.62 E-value: 3.37e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530604700 400 HDTLTRLYNRGALFEKARPLAKMCQTHQHPFSVIQVDLDHFKAINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRVGGE 479
Cdd:cd01949 2 TDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530604700 480 EFCVILPGASLTEAAEVAERIRLKLNEKEMLIAKSttIRISASLGVSSSEETGDyDFEQLQSLADRRLYLAKQAGRNRVC 559
Cdd:cd01949 82 EFAILLPGTDLEEAEALAERLREAIEEPFFIDGQE--IRVTASIGIATYPEDGE-DAEELLRRADEALYRAKRSGRNRVV 158
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
396-559 |
8.36e-55 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 182.45 E-value: 8.36e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530604700 396 WQAWHDTLTRLYNRGALFEKARPLAKMCQTHQHPFSVIQVDLDHFKAINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGR 475
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530604700 476 VGGEEFCVILPGASLTEAAEVAERIRLKLNEKEmlIAKSTTIRISASLGVSSSEEtGDYDFEQLQSLADRRLYLAKQAGR 555
Cdd:smart00267 81 LGGDEFALLLPETSLEEAIALAERILQQLREPI--IIHGIPLYLTISIGVAAYPN-PGEDAEDLLKRADTALYQAKKAGR 157
|
....
gi 2530604700 556 NRVC 559
Cdd:smart00267 158 NQVA 161
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
1-564 |
0e+00 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 1031.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530604700 1 MQHETKMENQSWLKKLARRLGPGHVVNLCFIVVLLFSTLLTWREVVVLEDAYISSQRNHLENVANALDKHLQYNVDKLIF 80
Cdd:PRK15426 1 MPHETRLENQSWLKKLARRLGPGHVVNLCFIVVLLFSTLLTWREVVVLEDAYISSQRNHLENVANALDAQLQYNVDKLIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530604700 81 LRNGMREALVAPLDFTSLRDAVTEFEQHRDEHAWKIELNRRRTLPVNGVSDALVSEGNLLSRENESLDNEITAALEVGYL 160
Cdd:PRK15426 81 LRNGMREALVAPLDFPALDAAVTQFEQHRDEHVWQLELPRRRTLPVNGVSDAFVSGLTLLSRDDEDLANELTAALELGYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530604700 161 LRLAHNSSSMVEQAMYVSRAGFYVSTQPTLFTRNVPTRYYGYVTQPWFIGHSQRENRHRAVRWFTSQPEHASNTEPQVTV 240
Cdd:PRK15426 161 LRLAHNSSSLVERAMYVSRAGFYVSTYPTLFPSDVPTRYYQYVTQPWFIGQSQRRNPGRGVRWFTSQPDDASNTEPQVTA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530604700 241 SVPVDSNNYWYGVLGMSIPVRTMQQFLRNAIDKNLDGEYQLYDSKLRFLTSSNPDHPTGNIFDPRELALLAQAMEHDTRG 320
Cdd:PRK15426 241 SVPVDAGNYWYGVLAMDIPVRSLQQFLRNAIDKDLDGEYQLYDSHLRLLTSSAPGVRTGNIFDPRELALLARAMEHDTRG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530604700 321 GIRMYSRYVSWERLDHFDGVLVRVHTLSEGVRGDFGSISIALTLLWALFTTMLLISWYVIRRMVSNMYVLQSSLQWQAWH 400
Cdd:PRK15426 321 GIRMGSRYVSWERLDHFDGVLVRVHTLREGVRGDFGSISIALTLLWALFTAMLLISWYVIRRMVSNMFVLQSSLQWQAWH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530604700 401 DTLTRLYNRGALFEKARPLAKMCQTHQHPFSVIQVDLDHFKAINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRVGGEE 480
Cdd:PRK15426 401 DPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRVGGEE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530604700 481 FCVILPGASLTEAAEVAERIRLKLNEKEMLIAKSTTIRISASLGVSSSEETGDYDFEQLQSLADRRLYLAKQAGRNRVCA 560
Cdd:PRK15426 481 FCVVLPGASLAEAAQVAERIRLRINEKEILVAKSTTIRISASLGVSSAEEDGDYDFEQLQSLADRRLYLAKQAGRNRVCA 560
|
....
gi 2530604700 561 SDNA 564
Cdd:PRK15426 561 SDNA 564
|
|
| CHASE7 |
pfam17151 |
Periplasmic sensor domain; CHASE7 is a conserved periplasmic sensor domain found in histidine ... |
41-227 |
4.05e-109 |
|
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: 324.07 E-value: 4.05e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530604700 41 TWREVVVLEDAYISSQRNHLENVANALDKHLQYNVDKLIFLRNGMREALVAPLDFTSLRDAVTEFEQHRDEHAWKIELNR 120
Cdd:pfam17151 1 IWREVVVLEDAYVASQRNHLENVANALDRLLQFNVDRLLFLRNGMHEALQAPLDFDALRDAIQQFAEHRNDHAWQLRLDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530604700 121 RRTLPVNGVSDALVSEGNLLSRENESLDNEITAALEVGYLLRLAHNSSSMVEQAMYVSRAGFYVSTQPTLFTRNVPTRYY 200
Cdd:pfam17151 81 RRTLPVFGVSDAFVTRTPLLSRDDPKLANELTAALELGYLLRLAHNSPDLAERIMYVSRSGFYVSTLPTISESDVNTRYY 160
|
170 180
....*....|....*....|....*..
gi 2530604700 201 GYVTQPWFIGHSQRENRHRAVRWFTSQ 227
Cdd:pfam17151 161 QYVTAPWFIGQSQRANPARGVRWFTSP 187
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
397-562 |
2.31e-80 |
|
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: 249.18 E-value: 2.31e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530604700 397 QAWHDTLTRLYNRGALFEKARPLAKMCQTHQHPFSVIQVDLDHFKAINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRV 476
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530604700 477 GGEEFCVILPGASLTEAAEVAERIRLKLNEKEMLIAKSTTIRISASLGVSSSEEtGDYDFEQLQSLADRRLYLAKQAGRN 556
Cdd:TIGR00254 81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSETLTVTVSIGVACYPG-HGLTLEELLKRADEALYQAKKAGRN 159
|
....*.
gi 2530604700 557 RVCASD 562
Cdd:TIGR00254 160 RVVVAD 165
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
307-559 |
3.89e-62 |
|
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: 205.98 E-value: 3.89e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530604700 307 LALLAQAMEHDTRGGIRMYSRYVSWERLDHFDGVLVRVHTLSEGVRGDFGSISIALTLLWALFTTMLLISWYVIRRMVSN 386
Cdd:COG2199 23 LLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLLLLALEDITE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530604700 387 MYVLQSSLQWQAWHDTLTRLYNRGALFEKARPLAKMCQTHQHPFSVIQVDLDHFKAINDRFGHQAGDRVLSHAAGLISSS 466
Cdd:COG2199 103 LRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRAS 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530604700 467 LRAQDVAGRVGGEEFCVILPGASLTEAAEVAERIRLKLNEKEMLIaKSTTIRISASLGVSSSEETGDyDFEQLQSLADRR 546
Cdd:COG2199 183 LRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFEL-EGKELRVTVSIGVALYPEDGD-SAEELLRRADLA 260
|
250
....*....|...
gi 2530604700 547 LYLAKQAGRNRVC 559
Cdd:COG2199 261 LYRAKRAGRNRVV 273
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
400-559 |
3.37e-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: 196.62 E-value: 3.37e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530604700 400 HDTLTRLYNRGALFEKARPLAKMCQTHQHPFSVIQVDLDHFKAINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRVGGE 479
Cdd:cd01949 2 TDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530604700 480 EFCVILPGASLTEAAEVAERIRLKLNEKEMLIAKSttIRISASLGVSSSEETGDyDFEQLQSLADRRLYLAKQAGRNRVC 559
Cdd:cd01949 82 EFAILLPGTDLEEAEALAERLREAIEEPFFIDGQE--IRVTASIGIATYPEDGE-DAEELLRRADEALYRAKRSGRNRVV 158
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
398-557 |
5.88e-59 |
|
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: 193.24 E-value: 5.88e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530604700 398 AWHDTLTRLYNRGALFEKARPLAKMCQTHQHPFSVIQVDLDHFKAINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRVG 477
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530604700 478 GEEFCVILPGASLTEAAEVAERIRLKLNEKEMLIAKSTTIR-ISASLGVSSSEETGDyDFEQLQSLADRRLYLAKQAGRN 556
Cdd:pfam00990 81 GDEFAILLPETSLEGAQELAERIRRLLAKLKIPHTVSGLPLyVTISIGIAAYPNDGE-DPEDLLKRADTALYQAKQAGRN 159
|
.
gi 2530604700 557 R 557
Cdd:pfam00990 160 R 160
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
396-559 |
8.36e-55 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 182.45 E-value: 8.36e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530604700 396 WQAWHDTLTRLYNRGALFEKARPLAKMCQTHQHPFSVIQVDLDHFKAINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGR 475
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530604700 476 VGGEEFCVILPGASLTEAAEVAERIRLKLNEKEmlIAKSTTIRISASLGVSSSEEtGDYDFEQLQSLADRRLYLAKQAGR 555
Cdd:smart00267 81 LGGDEFALLLPETSLEEAIALAERILQQLREPI--IIHGIPLYLTISIGVAAYPN-PGEDAEDLLKRADTALYQAKKAGR 157
|
....
gi 2530604700 556 NRVC 559
Cdd:smart00267 158 NQVA 161
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
305-559 |
3.96e-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: 163.79 E-value: 3.96e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530604700 305 RELALLAQAMEHDTRGGIRMYSRYVSWERLDHFDGVLVRVHTLSEGVRGDFGSISIALTLLWALFTTMLLISWYVIRRMV 384
Cdd:COG5001 158 ARALLALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLI 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530604700 385 SNMYVLQSSLQWQAWHDTLTRLYNRGALFEKARPLAKMCQTHQHPFSVIQVDLDHFKAINDRFGHQAGDRVLSHAAGLIS 464
Cdd:COG5001 238 TERKRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLR 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530604700 465 SSLRAQDVAGRVGGEEFCVILPG-ASLTEAAEVAERIRLKLNEKeMLIAkSTTIRISASLGVSSSEETGDyDFEQLQSLA 543
Cdd:COG5001 318 ACLREGDTVARLGGDEFAVLLPDlDDPEDAEAVAERILAALAEP-FELD-GHELYVSASIGIALYPDDGA-DAEELLRNA 394
|
250
....*....|....*.
gi 2530604700 544 DRRLYLAKQAGRNRVC 559
Cdd:COG5001 395 DLAMYRAKAAGRNRYR 410
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
390-562 |
9.67e-39 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 147.74 E-value: 9.67e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530604700 390 LQSSLQwQAWHDTLTRLYNR-------GALFEKARPLAKmcqthqhPFSVIQVDLDHFKAINDRFGHQAGDRVLSHAAGL 462
Cdd:PRK09581 285 LEQSIE-MAVTDGLTGLHNRryfdmhlKNLIERANERGK-------PLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKR 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530604700 463 ISSSLRAQDVAGRVGGEEFCVILPGASLTEAAEVAERIRLKLNEKEMLIAKS-TTIRISASLGVSSSEETGDyDFEQLQS 541
Cdd:PRK09581 357 LRNNIRGTDLIARYGGEEFVVVMPDTDIEDAIAVAERIRRKIAEEPFIISDGkERLNVTVSIGVAELRPSGD-TIEALIK 435
|
170 180
....*....|....*....|.
gi 2530604700 542 LADRRLYLAKQAGRNRVCASD 562
Cdd:PRK09581 436 RADKALYEAKNTGRNRVVALA 456
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
401-558 |
5.73e-33 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 127.88 E-value: 5.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530604700 401 DTLTRLYNRGAL---FEKARplakmCQTHQHPFSVIQVDLDHFKAINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRVG 477
Cdd:PRK09894 132 DVLTGLPGRRVLdesFDHQL-----RNREPQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYG 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530604700 478 GEEFCVILPGASLTEAAEVAERIRLKLNEKEMLIAKStTIRISASLGVssSEETGDYDFEQLQSLADRRLYLAKQAGRNR 557
Cdd:PRK09894 207 GEEFIICLKAATDEEACRAGERIRQLIANHAITHSDG-RINITATFGV--SRAFPEETLDVVIGRADRAMYEGKQTGRNR 283
|
.
gi 2530604700 558 V 558
Cdd:PRK09894 284 V 284
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
390-558 |
1.01e-24 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 109.38 E-value: 1.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530604700 390 LQSSLQWQAWHDTLTRLYNRgALFEKArpLAKMCQT-----HQHPFSVIqvDLDHFKAINDRFGHQAGDRVLSHAAGLIS 464
Cdd:PRK09776 657 MLRQLSYSASHDALTHLANR-ASFEKQ--LRRLLQTvnsthQRHALVFI--DLDRFKAVNDSAGHAAGDALLRELASLML 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530604700 465 SSLRAQDVAGRVGGEEFCVILPGASLTEAAEVAERIRLKLNEKEmLIAKSTTIRISASLGVSSSEETgDYDFEQLQSLAD 544
Cdd:PRK09776 732 SMLRSSDVLARLGGDEFGLLLPDCNVESARFIATRIISAINDYH-FPWEGRVYRVGASAGITLIDAN-NHQASEVMSQAD 809
|
170
....*....|....
gi 2530604700 545 RRLYLAKQAGRNRV 558
Cdd:PRK09776 810 IACYAAKNAGRGRV 823
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
394-557 |
3.52e-20 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 92.20 E-value: 3.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530604700 394 LQWQAWHDTLTRLYNRGALFEKARPLAKMCQTHQHPFSVIQVDLDHFKAINDRFGHQAGDRVLSHAAGLISSSLRAQDVA 473
Cdd:PRK10245 201 LQVMSTRDGMTGVYNRRHWETLLRNEFDNCRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSDVI 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530604700 474 GRVGGEEFCVILPGASLTEAAEVAERIRLKLNEKEMLIAKSTTIRIsaSLGVSS-SEETGDYDfEQLQSlADRRLYLAKQ 552
Cdd:PRK10245 281 GRFGGDEFAVIMSGTPAESAITAMSRVHEGLNTLRLPNAPQVTLRI--SVGVAPlNPQMSHYR-EWLKS-ADLALYKAKN 356
|
....*
gi 2530604700 553 AGRNR 557
Cdd:PRK10245 357 AGRNR 361
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
391-559 |
1.81e-18 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 88.97 E-value: 1.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530604700 391 QSSLQWQAWHDTLTRLYNRGALFEKARplAKMCQTHQHPFSVIQVDLDHFKAINDRFGHQAGDRVLSHAAGLISSSLRAQ 470
Cdd:PRK10060 230 QERLRILANTDSITGLPNRNAIQELID--HAINAADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEED 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530604700 471 DVAGRVGGEEFCVILPGASLTEAAEVAERI--RLKLNEKEMLIAKSTtiriSASLGVSSSEETGDyDFEQLQSLADRRLY 548
Cdd:PRK10060 308 QTLARLGGDEFLVLASHTSQAALEAMASRIltRLRLPFRIGLIEVYT----GCSIGIALAPEHGD-DSESLIRSADTAMY 382
|
170
....*....|.
gi 2530604700 549 LAKQAGRNRVC 559
Cdd:PRK10060 383 TAKEGGRGQFC 393
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
429-551 |
6.83e-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: 68.54 E-value: 6.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530604700 429 PFSVIQVDLDHFKAINDRFGHQAGDRVLSHAAGLISSSL-RAQDVAGRVGGEEFCVILPGASLTEAAEVAERIRLKLNEk 507
Cdd:cd07556 1 PVTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIrRSGDLKIKTIGDEFMVVSGLDHPAAAVAFAEDMREAVSA- 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2530604700 508 emlIAKSTTIRISASLGVSSSEETGDYD--------FEQLQSLADRRLYLAK 551
Cdd:cd07556 80 ---LNQSEGNPVRVRIGIHTGPVVVGVIgsrpqydvWGALVNLASRMESQAK 128
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
316-552 |
1.24e-12 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 69.65 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530604700 316 HDTRGGiRMYSRYVSWERLDHFdgvlvrvHTLSEgvrgDFGSisialtllwaLFTTMlliSWYVIRRMVSNMYVLQSSLq 395
Cdd:PRK09966 196 HDVRSN-RNFSRRVSEERIAEF-------HRFAL----DFNS----------LLDEM---EEWQLRLQAKNAQLLRTAL- 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530604700 396 wqawHDTLTRLYNRGALFEKARPLAKMCQTHQHPfSVIQVDLDHFKAINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGR 475
Cdd:PRK09966 250 ----HDPLTGLANRAAFRSGINTLMNNSDARKTS-ALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHKAYR 324
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2530604700 476 VGGEEFCVILPGA-SLTEAAEVAERIRLKLNEK-EMLIAKSTTIRISASLGVSSSEETGdydfEQLQSLADRRLYLAKQ 552
Cdd:PRK09966 325 LGGDEFAMVLYDVqSESEVQQICSALTQIFNLPfDLHNGHQTTMTLSIGYAMTIEHASA----EKLQELADHNMYQAKH 399
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
471-551 |
1.06e-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: 63.77 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530604700 471 DVAGRVGGEEFCVILPGASLTEAAEVAERIRLKlnekemlIAKSTTIRISASLGVSsseetgdydFEQLQSLADrRLYLA 550
Cdd:COG3706 116 DLVARYGGEEFAILLPGTDLEGALAVAERIREA-------VAELPSLRVTVSIGVA---------GDSLLKRAD-ALYQA 178
|
.
gi 2530604700 551 K 551
Cdd:COG3706 179 R 179
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
401-554 |
1.16e-11 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 67.49 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530604700 401 DTLTRLYNRGALFekaRPLAKMCQThQHPFSVIQVDLDHFKAINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRVGGEE 480
Cdd:PRK11359 379 DPLTGLPNRNNLH---NYLDDLVDK-AVSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGTQ 454
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2530604700 481 FCVILPGASLTEAAEVAERIRlKLNEKEMLIAkSTTIRISASLGVSSSeetGDYDFEQLQSLADRRL-YLAKQAG 554
Cdd:PRK11359 455 FVLVSLENDVSNITQIADELR-NVVSKPIMID-DKPFPLTLSIGISYD---VGKNRDYLLSTAHNAMdYIRKNGG 524
|
|
| dCache_1 |
pfam02743 |
Cache domain; Double cache domain 1 covers the last three strands from the membrane distal ... |
126-342 |
2.84e-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: 45.79 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530604700 126 VNGVSDALVSEGNLLSRENESLDNEITAALEVGYLLRLAHNSSSMVEQAMYVSRAGFYVSTQPTLFTRNvptrYYGYVTQ 205
Cdd:pfam02743 22 IESYLDSLEEILELLASNPDLQDLLSAPAEEELAKLESLLRSNPGISSIYLVDADGRVLASSDESPSYP----GLDVSER 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530604700 206 PWFIghSQRENRHRAVRWFTSQPEHASNTEPQVTVSVPV-DSNNYWYGVLGMSIPVRTMQQFLRNaIDKNLDGEYQLYDS 284
Cdd:pfam02743 98 PWYK--EALKGGGGIIWVFSSPYPSSESGEPVLTIARPIyDDDGEVIGVLVADLDLDTLQELLSQ-IKLGEGGYVFIVDS 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2530604700 285 KLRFLTSSNPDHPTGNIFDPRELALLAQAMEHDTRGGIRMY---SRYVSWERLDHFDGVLV 342
Cdd:pfam02743 175 DGRILAHPLGKNLRSLLAPFLGKSLADALPGSGITEIAVDLdgeDYLVAYAPIPGTGWTLV 235
|
|
| |
