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Conserved domains on  [gi|15831948|ref|NP_310721|]
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membrane-anchored diguanylate cyclase [Escherichia coli O157:H7 str. Sakai]

Protein Classification

cellulose biosynthesis regulator YedQ( domain architecture ID 11487790)

cellulose biosynthesis regulator YedQ is involved in the regulation of cellulose production and may function as a diguanylate cyclase

Graphical summary

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List of domain hits

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: 1026.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831948    1 MQHETKMENQSWLKKLARRLGPGHIVNLCFIVVLLFSTLLTWREVVVLEDAYISSQRNHLENVANALDKHLQYNVDKLIF 80
Cdd:PRK15426   1 MPHETRLENQSWLKKLARRLGPGHVVNLCFIVVLLFSTLLTWREVVVLEDAYISSQRNHLENVANALDAQLQYNVDKLIF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831948   81 LRNGMREALVAPLDFTSLRDAVTEFEQHRDEHAWQIELNRRRTLSVNGVSDALVSEGNLLSRENESLDNEITAALEVGYL 160
Cdd:PRK15426  81 LRNGMREALVAPLDFPALDAAVTQFEQHRDEHVWQLELPRRRTLPVNGVSDAFVSGLTLLSRDDEDLANELTAALELGYL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831948  161 LRLAHNSSSMVEQAMYVSRAGFYVSTQPTLFTRNVPTRYYGYVTQPWFIGHSQRENRHRAVRWFTSQPEHASNTEPQVTV 240
Cdd:PRK15426 161 LRLAHNSSSLVERAMYVSRAGFYVSTYPTLFPSDVPTRYYQYVTQPWFIGQSQRRNPGRGVRWFTSQPDDASNTEPQVTA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831948  241 SVPVDSNNYWYGVLGMSIPVRTMQQFLRNAIDKNLDGEYQLYDSKLRFLTSSNPDHPTGNIFDPRELALLAQAMEHDTRG 320
Cdd:PRK15426 241 SVPVDAGNYWYGVLAMDIPVRSLQQFLRNAIDKDLDGEYQLYDSHLRLLTSSAPGVRTGNIFDPRELALLARAMEHDTRG 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831948  321 GIRMDSRYVSWERLDHFDGVLVRVHTLSEGVRGDFGSISIALTLLWALFTTMLLISWYVIRRMVSNMYVLQSSLQWQAWH 400
Cdd:PRK15426 321 GIRMGSRYVSWERLDHFDGVLVRVHTLREGVRGDFGSISIALTLLWALFTAMLLISWYVIRRMVSNMFVLQSSLQWQAWH 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831948  401 DTLTRLYNRGALFEKARPLAKLCQTHQHPFSVIQVDLDHFKAINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRVGGEE 480
Cdd:PRK15426 401 DPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRVGGEE 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831948  481 FCVILPGASLTEAAEVAERIRLKLNEKEMLIAKSTTIRISASLGVSSSEETGDYDFEQLQSLADRRLYLAKQAGRNRVFA 560
Cdd:PRK15426 481 FCVVLPGASLAEAAQVAERIRLRINEKEILVAKSTTIRISASLGVSSAEEDGDYDFEQLQSLADRRLYLAKQAGRNRVCA 560

                 ....
gi 15831948  561 SDNA 564
Cdd:PRK15426 561 SDNA 564
 
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: 1026.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831948    1 MQHETKMENQSWLKKLARRLGPGHIVNLCFIVVLLFSTLLTWREVVVLEDAYISSQRNHLENVANALDKHLQYNVDKLIF 80
Cdd:PRK15426   1 MPHETRLENQSWLKKLARRLGPGHVVNLCFIVVLLFSTLLTWREVVVLEDAYISSQRNHLENVANALDAQLQYNVDKLIF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831948   81 LRNGMREALVAPLDFTSLRDAVTEFEQHRDEHAWQIELNRRRTLSVNGVSDALVSEGNLLSRENESLDNEITAALEVGYL 160
Cdd:PRK15426  81 LRNGMREALVAPLDFPALDAAVTQFEQHRDEHVWQLELPRRRTLPVNGVSDAFVSGLTLLSRDDEDLANELTAALELGYL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831948  161 LRLAHNSSSMVEQAMYVSRAGFYVSTQPTLFTRNVPTRYYGYVTQPWFIGHSQRENRHRAVRWFTSQPEHASNTEPQVTV 240
Cdd:PRK15426 161 LRLAHNSSSLVERAMYVSRAGFYVSTYPTLFPSDVPTRYYQYVTQPWFIGQSQRRNPGRGVRWFTSQPDDASNTEPQVTA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831948  241 SVPVDSNNYWYGVLGMSIPVRTMQQFLRNAIDKNLDGEYQLYDSKLRFLTSSNPDHPTGNIFDPRELALLAQAMEHDTRG 320
Cdd:PRK15426 241 SVPVDAGNYWYGVLAMDIPVRSLQQFLRNAIDKDLDGEYQLYDSHLRLLTSSAPGVRTGNIFDPRELALLARAMEHDTRG 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831948  321 GIRMDSRYVSWERLDHFDGVLVRVHTLSEGVRGDFGSISIALTLLWALFTTMLLISWYVIRRMVSNMYVLQSSLQWQAWH 400
Cdd:PRK15426 321 GIRMGSRYVSWERLDHFDGVLVRVHTLREGVRGDFGSISIALTLLWALFTAMLLISWYVIRRMVSNMFVLQSSLQWQAWH 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831948  401 DTLTRLYNRGALFEKARPLAKLCQTHQHPFSVIQVDLDHFKAINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRVGGEE 480
Cdd:PRK15426 401 DPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRVGGEE 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831948  481 FCVILPGASLTEAAEVAERIRLKLNEKEMLIAKSTTIRISASLGVSSSEETGDYDFEQLQSLADRRLYLAKQAGRNRVFA 560
Cdd:PRK15426 481 FCVVLPGASLAEAAQVAERIRLRINEKEILVAKSTTIRISASLGVSSAEEDGDYDFEQLQSLADRRLYLAKQAGRNRVCA 560

                 ....
gi 15831948  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 1.97e-107

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: 319.83  E-value: 1.97e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831948    41 TWREVVVLEDAYISSQRNHLENVANALDKHLQYNVDKLIFLRNGMREALVAPLDFTSLRDAVTEFEQHRDEHAWQIELNR 120
Cdd:pfam17151   1 IWREVVVLEDAYVASQRNHLENVANALDRLLQFNVDRLLFLRNGMHEALQAPLDFDALRDAIQQFAEHRNDHAWQLRLDR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831948   121 RRTLSVNGVSDALVSEGNLLSRENESLDNEITAALEVGYLLRLAHNSSSMVEQAMYVSRAGFYVSTQPTLFTRNVPTRYY 200
Cdd:pfam17151  81 RRTLPVFGVSDAFVTRTPLLSRDDPKLANELTAALELGYLLRLAHNSPDLAERIMYVSRSGFYVSTLPTISESDVNTRYY 160
                         170       180
                  ....*....|....*....|....*..
gi 15831948   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 1.28e-81

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: 252.64  E-value: 1.28e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831948   397 QAWHDTLTRLYNRGALFEKARPLAKLCQTHQHPFSVIQVDLDHFKAINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRV 476
Cdd:TIGR00254   1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831948   477 GGEEFCVILPGASLTEAAEVAERIRLKLNEKEMLIAKSTTIRISASLGVSSSEEtGDYDFEQLQSLADRRLYLAKQAGRN 556
Cdd:TIGR00254  81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSETLTVTVSIGVACYPG-HGLTLEELLKRADEALYQAKKAGRN 159

                  ....*.
gi 15831948   557 RVFASD 562
Cdd:TIGR00254 160 RVVVAD 165
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
307-558 2.46e-61

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: 203.67  E-value: 2.46e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831948 307 LALLAQAMEHDTRGGIRMDSRYVSWERLDHFDGVLVRVHTLSEGVRGDFGSISIALTLLWALFTTMLLISWYVIRRMVSN 386
Cdd:COG2199  23 LLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLLLLALEDITE 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831948 387 MYVLQSSLQWQAWHDTLTRLYNRGALFEKARPLAKLCQTHQHPFSVIQVDLDHFKAINDRFGHQAGDRVLSHAAGLISSS 466
Cdd:COG2199 103 LRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRAS 182
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831948 467 LRAQDVAGRVGGEEFCVILPGASLTEAAEVAERIRLKLNEKEMLIaKSTTIRISASLGVSSSEETGDyDFEQLQSLADRR 546
Cdd:COG2199 183 LRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFEL-EGKELRVTVSIGVALYPEDGD-SAEELLRRADLA 260
                       250
                ....*....|..
gi 15831948 547 LYLAKQAGRNRV 558
Cdd:COG2199 261 LYRAKRAGRNRV 272
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
400-558 1.04e-59

Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as a domain of unknown function 1 (DUF1). This domain is widely present in bacteria, linked to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain shows homology to the adenylyl cyclase catalytic domain. This correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesion in bacteria.


Pssm-ID: 143635 [Multi-domain]  Cd Length: 158  Bit Score: 195.08  E-value: 1.04e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831948 400 HDTLTRLYNRGALFEKARPLAKLCQTHQHPFSVIQVDLDHFKAINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRVGGE 479
Cdd:cd01949   2 TDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGD 81
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15831948 480 EFCVILPGASLTEAAEVAERIRLKLNEKEMLIAKSttIRISASLGVSSSEETGDyDFEQLQSLADRRLYLAKQAGRNRV 558
Cdd:cd01949  82 EFAILLPGTDLEEAEALAERLREAIEEPFFIDGQE--IRVTASIGIATYPEDGE-DAEELLRRADEALYRAKRSGRNRV 157
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
396-559 3.79e-54

diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 180.91  E-value: 3.79e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831948    396 WQAWHDTLTRLYNRGALFEKARPLAKLCQTHQHPFSVIQVDLDHFKAINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGR 475
Cdd:smart00267   1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831948    476 VGGEEFCVILPGASLTEAAEVAERIRLKLNEKEmlIAKSTTIRISASLGVSSSEEtGDYDFEQLQSLADRRLYLAKQAGR 555
Cdd:smart00267  81 LGGDEFALLLPETSLEEAIALAERILQQLREPI--IIHGIPLYLTISIGVAAYPN-PGEDAEDLLKRADTALYQAKKAGR 157

                   ....
gi 15831948    556 NRVF 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: 1026.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831948    1 MQHETKMENQSWLKKLARRLGPGHIVNLCFIVVLLFSTLLTWREVVVLEDAYISSQRNHLENVANALDKHLQYNVDKLIF 80
Cdd:PRK15426   1 MPHETRLENQSWLKKLARRLGPGHVVNLCFIVVLLFSTLLTWREVVVLEDAYISSQRNHLENVANALDAQLQYNVDKLIF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831948   81 LRNGMREALVAPLDFTSLRDAVTEFEQHRDEHAWQIELNRRRTLSVNGVSDALVSEGNLLSRENESLDNEITAALEVGYL 160
Cdd:PRK15426  81 LRNGMREALVAPLDFPALDAAVTQFEQHRDEHVWQLELPRRRTLPVNGVSDAFVSGLTLLSRDDEDLANELTAALELGYL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831948  161 LRLAHNSSSMVEQAMYVSRAGFYVSTQPTLFTRNVPTRYYGYVTQPWFIGHSQRENRHRAVRWFTSQPEHASNTEPQVTV 240
Cdd:PRK15426 161 LRLAHNSSSLVERAMYVSRAGFYVSTYPTLFPSDVPTRYYQYVTQPWFIGQSQRRNPGRGVRWFTSQPDDASNTEPQVTA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831948  241 SVPVDSNNYWYGVLGMSIPVRTMQQFLRNAIDKNLDGEYQLYDSKLRFLTSSNPDHPTGNIFDPRELALLAQAMEHDTRG 320
Cdd:PRK15426 241 SVPVDAGNYWYGVLAMDIPVRSLQQFLRNAIDKDLDGEYQLYDSHLRLLTSSAPGVRTGNIFDPRELALLARAMEHDTRG 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831948  321 GIRMDSRYVSWERLDHFDGVLVRVHTLSEGVRGDFGSISIALTLLWALFTTMLLISWYVIRRMVSNMYVLQSSLQWQAWH 400
Cdd:PRK15426 321 GIRMGSRYVSWERLDHFDGVLVRVHTLREGVRGDFGSISIALTLLWALFTAMLLISWYVIRRMVSNMFVLQSSLQWQAWH 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831948  401 DTLTRLYNRGALFEKARPLAKLCQTHQHPFSVIQVDLDHFKAINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRVGGEE 480
Cdd:PRK15426 401 DPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRVGGEE 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831948  481 FCVILPGASLTEAAEVAERIRLKLNEKEMLIAKSTTIRISASLGVSSSEETGDYDFEQLQSLADRRLYLAKQAGRNRVFA 560
Cdd:PRK15426 481 FCVVLPGASLAEAAQVAERIRLRINEKEILVAKSTTIRISASLGVSSAEEDGDYDFEQLQSLADRRLYLAKQAGRNRVCA 560

                 ....
gi 15831948  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 1.97e-107

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: 319.83  E-value: 1.97e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831948    41 TWREVVVLEDAYISSQRNHLENVANALDKHLQYNVDKLIFLRNGMREALVAPLDFTSLRDAVTEFEQHRDEHAWQIELNR 120
Cdd:pfam17151   1 IWREVVVLEDAYVASQRNHLENVANALDRLLQFNVDRLLFLRNGMHEALQAPLDFDALRDAIQQFAEHRNDHAWQLRLDR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831948   121 RRTLSVNGVSDALVSEGNLLSRENESLDNEITAALEVGYLLRLAHNSSSMVEQAMYVSRAGFYVSTQPTLFTRNVPTRYY 200
Cdd:pfam17151  81 RRTLPVFGVSDAFVTRTPLLSRDDPKLANELTAALELGYLLRLAHNSPDLAERIMYVSRSGFYVSTLPTISESDVNTRYY 160
                         170       180
                  ....*....|....*....|....*..
gi 15831948   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 1.28e-81

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: 252.64  E-value: 1.28e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831948   397 QAWHDTLTRLYNRGALFEKARPLAKLCQTHQHPFSVIQVDLDHFKAINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRV 476
Cdd:TIGR00254   1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831948   477 GGEEFCVILPGASLTEAAEVAERIRLKLNEKEMLIAKSTTIRISASLGVSSSEEtGDYDFEQLQSLADRRLYLAKQAGRN 556
Cdd:TIGR00254  81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSETLTVTVSIGVACYPG-HGLTLEELLKRADEALYQAKKAGRN 159

                  ....*.
gi 15831948   557 RVFASD 562
Cdd:TIGR00254 160 RVVVAD 165
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
307-558 2.46e-61

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: 203.67  E-value: 2.46e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831948 307 LALLAQAMEHDTRGGIRMDSRYVSWERLDHFDGVLVRVHTLSEGVRGDFGSISIALTLLWALFTTMLLISWYVIRRMVSN 386
Cdd:COG2199  23 LLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLLLLALEDITE 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831948 387 MYVLQSSLQWQAWHDTLTRLYNRGALFEKARPLAKLCQTHQHPFSVIQVDLDHFKAINDRFGHQAGDRVLSHAAGLISSS 466
Cdd:COG2199 103 LRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRAS 182
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831948 467 LRAQDVAGRVGGEEFCVILPGASLTEAAEVAERIRLKLNEKEMLIaKSTTIRISASLGVSSSEETGDyDFEQLQSLADRR 546
Cdd:COG2199 183 LRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFEL-EGKELRVTVSIGVALYPEDGD-SAEELLRRADLA 260
                       250
                ....*....|..
gi 15831948 547 LYLAKQAGRNRV 558
Cdd:COG2199 261 LYRAKRAGRNRV 272
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
400-558 1.04e-59

Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as a domain of unknown function 1 (DUF1). This domain is widely present in bacteria, linked to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain shows homology to the adenylyl cyclase catalytic domain. This correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesion in bacteria.


Pssm-ID: 143635 [Multi-domain]  Cd Length: 158  Bit Score: 195.08  E-value: 1.04e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831948 400 HDTLTRLYNRGALFEKARPLAKLCQTHQHPFSVIQVDLDHFKAINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRVGGE 479
Cdd:cd01949   2 TDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGD 81
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15831948 480 EFCVILPGASLTEAAEVAERIRLKLNEKEMLIAKSttIRISASLGVSSSEETGDyDFEQLQSLADRRLYLAKQAGRNRV 558
Cdd:cd01949  82 EFAILLPGTDLEEAEALAERLREAIEEPFFIDGQE--IRVTASIGIATYPEDGE-DAEELLRRADEALYRAKRSGRNRV 157
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
398-557 3.19e-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: 194.01  E-value: 3.19e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831948   398 AWHDTLTRLYNRGALFEKARPLAKLCQTHQHPFSVIQVDLDHFKAINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRVG 477
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831948   478 GEEFCVILPGASLTEAAEVAERIRLKLNEKEMLIAKSTTIR-ISASLGVSSSEETGDyDFEQLQSLADRRLYLAKQAGRN 556
Cdd:pfam00990  81 GDEFAILLPETSLEGAQELAERIRRLLAKLKIPHTVSGLPLyVTISIGIAAYPNDGE-DPEDLLKRADTALYQAKQAGRN 159

                  .
gi 15831948   557 R 557
Cdd:pfam00990 160 R 160
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
396-559 3.79e-54

diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 180.91  E-value: 3.79e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831948    396 WQAWHDTLTRLYNRGALFEKARPLAKLCQTHQHPFSVIQVDLDHFKAINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGR 475
Cdd:smart00267   1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831948    476 VGGEEFCVILPGASLTEAAEVAERIRLKLNEKEmlIAKSTTIRISASLGVSSSEEtGDYDFEQLQSLADRRLYLAKQAGR 555
Cdd:smart00267  81 LGGDEFALLLPETSLEEAIALAERILQQLREPI--IIHGIPLYLTISIGVAAYPN-PGEDAEDLLKRADTALYQAKKAGR 157

                   ....
gi 15831948    556 NRVF 559
Cdd:smart00267 158 NQVA 161
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
305-558 1.07e-42

Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain [Signal transduction mechanisms];


Pssm-ID: 444025 [Multi-domain]  Cd Length: 678  Bit Score: 162.64  E-value: 1.07e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831948 305 RELALLAQAMEHDTRGGIRMDSRYVSWERLDHFDGVLVRVHTLSEGVRGDFGSISIALTLLWALFTTMLLISWYVIRRMV 384
Cdd:COG5001 158 ARALLALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLI 237
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831948 385 SNMYVLQSSLQWQAWHDTLTRLYNRGALFEKARPLAKLCQTHQHPFSVIQVDLDHFKAINDRFGHQAGDRVLSHAAGLIS 464
Cdd:COG5001 238 TERKRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLR 317
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831948 465 SSLRAQDVAGRVGGEEFCVILPG-ASLTEAAEVAERIRLKLNEKeMLIAkSTTIRISASLGVSSSEETGDyDFEQLQSLA 543
Cdd:COG5001 318 ACLREGDTVARLGGDEFAVLLPDlDDPEDAEAVAERILAALAEP-FELD-GHELYVSASIGIALYPDDGA-DAEELLRNA 394
                       250
                ....*....|....*
gi 15831948 544 DRRLYLAKQAGRNRV 558
Cdd:COG5001 395 DLAMYRAKAAGRNRY 409
pleD PRK09581
response regulator PleD; Reviewed
390-562 6.74e-38

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 145.43  E-value: 6.74e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831948  390 LQSSLQwQAWHDTLTRLYNR-------GALFEKARPLAKlcqthqhPFSVIQVDLDHFKAINDRFGHQAGDRVLSHAAGL 462
Cdd:PRK09581 285 LEQSIE-MAVTDGLTGLHNRryfdmhlKNLIERANERGK-------PLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKR 356
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831948  463 ISSSLRAQDVAGRVGGEEFCVILPGASLTEAAEVAERIRLKLNEKEMLIAKS-TTIRISASLGVSSSEETGDyDFEQLQS 541
Cdd:PRK09581 357 LRNNIRGTDLIARYGGEEFVVVMPDTDIEDAIAVAERIRRKIAEEPFIISDGkERLNVTVSIGVAELRPSGD-TIEALIK 435
                        170       180
                 ....*....|....*....|.
gi 15831948  542 LADRRLYLAKQAGRNRVFASD 562
Cdd:PRK09581 436 RADKALYEAKNTGRNRVVALA 456
PRK09894 PRK09894
diguanylate cyclase; Provisional
401-558 4.75e-33

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 128.26  E-value: 4.75e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831948  401 DTLTRLYNRGALFEKARplAKLCQTHQHPFSVIQVDLDHFKAINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRVGGEE 480
Cdd:PRK09894 132 DVLTGLPGRRVLDESFD--HQLRNREPQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGGEE 209
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15831948  481 FCVILPGASLTEAAEVAERIRLKLNEKEMLIAKStTIRISASLGVssSEETGDYDFEQLQSLADRRLYLAKQAGRNRV 558
Cdd:PRK09894 210 FIICLKAATDEEACRAGERIRQLIANHAITHSDG-RINITATFGV--SRAFPEETLDVVIGRADRAMYEGKQTGRNRV 284
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
390-558 4.39e-25

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 110.53  E-value: 4.39e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831948   390 LQSSLQWQAWHDTLTRLYNRgALFEKArpLAKLCQT-----HQHPFSVIqvDLDHFKAINDRFGHQAGDRVLSHAAGLIS 464
Cdd:PRK09776  657 MLRQLSYSASHDALTHLANR-ASFEKQ--LRRLLQTvnsthQRHALVFI--DLDRFKAVNDSAGHAAGDALLRELASLML 731
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831948   465 SSLRAQDVAGRVGGEEFCVILPGASLTEAAEVAERIRLKLNEKEmLIAKSTTIRISASLGVSSSEETgDYDFEQLQSLAD 544
Cdd:PRK09776  732 SMLRSSDVLARLGGDEFGLLLPDCNVESARFIATRIISAINDYH-FPWEGRVYRVGASAGITLIDAN-NHQASEVMSQAD 809
                         170
                  ....*....|....
gi 15831948   545 RRLYLAKQAGRNRV 558
Cdd:PRK09776  810 IACYAAKNAGRGRV 823
adrA PRK10245
diguanylate cyclase AdrA; Provisional
394-557 2.32e-20

diguanylate cyclase AdrA; Provisional


Pssm-ID: 182329 [Multi-domain]  Cd Length: 366  Bit Score: 92.97  E-value: 2.32e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831948  394 LQWQAWHDTLTRLYNRGALFEKARPLAKLCQTHQHPFSVIQVDLDHFKAINDRFGHQAGDRVLSHAAGLISSSLRAQDVA 473
Cdd:PRK10245 201 LQVMSTRDGMTGVYNRRHWETLLRNEFDNCRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSDVI 280
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831948  474 GRVGGEEFCVILPGASLTEAAEVAERIRLKLNEKEMLIAKSTTIRIsaSLGVSS-SEETGDYDfEQLQSlADRRLYLAKQ 552
Cdd:PRK10245 281 GRFGGDEFAVIMSGTPAESAITAMSRVHEGLNTLRLPNAPQVTLRI--SVGVAPlNPQMSHYR-EWLKS-ADLALYKAKN 356

                 ....*
gi 15831948  553 AGRNR 557
Cdd:PRK10245 357 AGRNR 361
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
391-560 9.50e-19

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 90.13  E-value: 9.50e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831948  391 QSSLQWQAWHDTLTRLYNRGALFEKARplAKLCQTHQHPFSVIQVDLDHFKAINDRFGHQAGDRVLSHAAGLISSSLRAQ 470
Cdd:PRK10060 230 QERLRILANTDSITGLPNRNAIQELID--HAINAADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEED 307
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831948  471 DVAGRVGGEEFCVILPGASLTEAAEVAERI--RLKLNEKEMLIAKSTtiriSASLGVSSSEETGDyDFEQLQSLADRRLY 548
Cdd:PRK10060 308 QTLARLGGDEFLVLASHTSQAALEAMASRIltRLRLPFRIGLIEVYT----GCSIGIALAPEHGD-DSESLIRSADTAMY 382
                        170
                 ....*....|....
gi 15831948  549 LAKQAGRN--RVFA 560
Cdd:PRK10060 383 TAKEGGRGqfCVFS 396
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
429-551 7.75e-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: 7.75e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831948 429 PFSVIQVDLDHFKAINDRFGHQAGDRVLSHAAGLISSSL-RAQDVAGRVGGEEFCVILPGASLTEAAEVAERIRLKLNEk 507
Cdd:cd07556   1 PVTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIrRSGDLKIKTIGDEFMVVSGLDHPAAAVAFAEDMREAVSA- 79
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 15831948 508 emlIAKSTTIRISASLGVSSSEETGDYD--------FEQLQSLADRRLYLAK 551
Cdd:cd07556  80 ---LNQSEGNPVRVRIGIHTGPVVVGVIgsrpqydvWGALVNLASRMESQAK 128
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
401-561 4.80e-12

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 69.03  E-value: 4.80e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831948  401 DTLTRLYNRGALFekaRPLAKLCQThQHPFSVIQVDLDHFKAINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRVGGEE 480
Cdd:PRK11359 379 DPLTGLPNRNNLH---NYLDDLVDK-AVSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGTQ 454
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831948  481 FCVILPGASLTEAAEVAERIRlKLNEKEMLIAkSTTIRISASLGVSSSeetGDYDFEQLQSLADRRL-YLAKQAGRNRVF 559
Cdd:PRK11359 455 FVLVSLENDVSNITQIADELR-NVVSKPIMID-DKPFPLTLSIGISYD---VGKNRDYLLSTAHNAMdYIRKNGGNGWQF 529

                 ..
gi 15831948  560 AS 561
Cdd:PRK11359 530 FS 531
PRK09966 PRK09966
diguanylate cyclase DgcN;
316-552 1.29e-11

diguanylate cyclase DgcN;


Pssm-ID: 182171 [Multi-domain]  Cd Length: 407  Bit Score: 66.57  E-value: 1.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831948  316 HDTRGGiRMDSRYVSWERLDHFdgvlvrvHTLSEgvrgDFGSisialtllwaLFTTMlliSWYVIRRMVSNMYVLQSSLq 395
Cdd:PRK09966 196 HDVRSN-RNFSRRVSEERIAEF-------HRFAL----DFNS----------LLDEM---EEWQLRLQAKNAQLLRTAL- 249
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831948  396 wqawHDTLTRLYNRGALFEKARPLAKlCQTHQHPFSVIQVDLDHFKAINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGR 475
Cdd:PRK09966 250 ----HDPLTGLANRAAFRSGINTLMN-NSDARKTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHKAYR 324
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15831948  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 1.32e-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: 63.39  E-value: 1.32e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831948 471 DVAGRVGGEEFCVILPGASLTEAAEVAERIRLKlnekemlIAKSTTIRISASLGVSsseetgdydFEQLQSLADrRLYLA 550
Cdd:COG3706 116 DLVARYGGEEFAILLPGTDLEGALAVAERIREA-------VAELPSLRVTVSIGVA---------GDSLLKRAD-ALYQA 178

                .
gi 15831948 551 K 551
Cdd:COG3706 179 R 179
dCache_1 pfam02743
Cache domain; Double cache domain 1 covers the last three strands from the membrane distal ...
125-295 5.48e-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: 45.02  E-value: 5.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831948   125 SVNGVSDALVSEGNLLSRENESLDNEITaalevgyLLRLAHNSSSMVEQAMYVSRAGFYVSTQPTLFTRNvptrYYGYVT 204
Cdd:pfam02743  28 SLEEILELLASNPDLQDLLSAPAEEELA-------KLESLLRSNPGISSIYLVDADGRVLASSDESPSYP----GLDVSE 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831948   205 QPWFIghSQRENRHRAVRWFTSQPEHASNTEPQVTVSVPV-DSNNYWYGVLGMSIPVRTMQQFLRNaIDKNLDGEYQLYD 283
Cdd:pfam02743  97 RPWYK--EALKGGGGIIWVFSSPYPSSESGEPVLTIARPIyDDDGEVIGVLVADLDLDTLQELLSQ-IKLGEGGYVFIVD 173
                         170
                  ....*....|..
gi 15831948   284 SKLRFLTSSNPD 295
Cdd:pfam02743 174 SDGRILAHPLGK 185
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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