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Conserved domains on  [gi|1657513|gb|AAB18041|]
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hypothetical protein [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

DNA-binding response regulator; diguanylate phosphodiesterase( domain architecture ID 10864347)

two-component system response regulator binds DNA upon phosphorylation and functions as transcriptional regulator; diguanylate phosphodiesterase is a BLUF and EAL domain-containing protein, which may function as a bifunctional blue light photoreceptor/diguanylate phosphodiesterase, similar to Klebsiella pneumoniae BlrP1 that is a light-regulated cyclic nucleotide phosphodiesterase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
 112-352 1.81e-104

Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.


:

Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 307.22  E-value: 1.81e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1657513     112 PEAISLALENHEFKPWIQPVFCAQTGVLTGCEVLVRWEHPQTGIIPPDQFIPLAESSGLIVIMTRQLMKQTADILMPVKH 191
Cdd:smart00052   1 ERELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1657513     192 LLPDNFHIGINVSAGCFLAAGFEKECLNLVNKLGNDKIKLVLELTERNPIPVTPEARAIFDSLHQHNITFALDDFGTGYA 271
Cdd:smart00052  81 QGPPPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1657513     272 TYRYLQAFPVDFIKIDKSFVQMASVDEISGHIVDNIVELARKPGLSIVAEGVETQEQADLMIGKGVHFLQGYLYSPPVPG 351
Cdd:smart00052 161 SLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPL 240


                   .
gi 1657513     352 N 352
Cdd:smart00052 241 D 241
LuxR_C_like cd06170
C-terminal DNA-binding domain of LuxR-like proteins. This domain contains a helix-turn-helix ...
 28-82 8.21e-10

C-terminal DNA-binding domain of LuxR-like proteins. This domain contains a helix-turn-helix motif and binds DNA. Proteins belonging to this group are response regulators; some act as transcriptional activators, others as transcriptional repressors. Many are active as homodimers. Many are two domain proteins in which the DNA binding property of the C-terminal DNA binding domain is modulated by modifications of the N-terminal domain. For example in the case of Lux R which participates in the regulation of gene expression in response to fluctuations in cell-population density (quorum-sensing), a signaling molecule, the pheromone Acyl HSL (N-acyl derivatives of homoserine lactone), binds to the N-terminal domain and leads to LuxR dimerization. For others phophorylation of the N-terminal domain leads to multimerization, for example Escherichia coli NarL and Sinorhizobium melilot FixJ. NarL controls gene expression of many respiratory-related operons when environmental nitrate or nitrite is present under anerobic conditions. FixJ is involved in the transcriptional activation of nitrogen fixation genes. The group also includes small proteins which lack an N-terminal signaling domain, such as Bacillus subtilis GerE. GerE is dimeric and acts in conjunction with sigmaK as an activator or a repressor modulating the expression of various genes in particular those encoding the spore-coat. These LuxR family regulators may share a similar organization of their target binding sites. For example the LuxR dimer binds the lux box, a 20bp inverted repeat, GerE dimers bind two 12bp consensus sequences in inverted orientation having the central four bases overlap, and the NarL dimer binds two 7bp inverted repeats separated by 2 bp.


:

Pssm-ID: 99777 [Multi-domain]  Cd Length: 57  Bit Score: 54.08  E-value: 8.21e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 1657513   28 SEKERLLLKLLMQGMSVTEISQYRNRSAKTISHQKKQLFEKLGIQSDITFWRDIF 82
Cdd:cd06170   2 TPREREVLRLLAEGKTNKEIADILGISEKTVKTHLRNIMRKLGVKSRTQLVAYAI 56
 
Name Accession Description Interval E-value
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
 112-352 1.81e-104

Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 307.22  E-value: 1.81e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1657513     112 PEAISLALENHEFKPWIQPVFCAQTGVLTGCEVLVRWEHPQTGIIPPDQFIPLAESSGLIVIMTRQLMKQTADILMPVKH 191
Cdd:smart00052   1 ERELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1657513     192 LLPDNFHIGINVSAGCFLAAGFEKECLNLVNKLGNDKIKLVLELTERNPIPVTPEARAIFDSLHQHNITFALDDFGTGYA 271
Cdd:smart00052  81 QGPPPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1657513     272 TYRYLQAFPVDFIKIDKSFVQMASVDEISGHIVDNIVELARKPGLSIVAEGVETQEQADLMIGKGVHFLQGYLYSPPVPG 351
Cdd:smart00052 161 SLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPL 240


                   .
gi 1657513     352 N 352
Cdd:smart00052 241 D 241
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 113-350 5.57e-89

EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues and is also known as domain of unknown function 2 (DUF2). The EAL domain has been shown to stimulate degradation of a second messenger, cyclic di-GMP, and is a good candidate for a diguanylate phosphodiesterase function. Together with the GGDEF domain, EAL might be involved in regulating cell surface adhesiveness in bacteria.


Pssm-ID: 238923 [Multi-domain]  Cd Length: 240  Bit Score: 267.49  E-value: 5.57e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1657513  113 EAISLALENHEFKPWIQPVFCAQTGVLTGCEVLVRWEHPQTGIIPPDQFIPLAESSGLIVIMTRQLMKQTADILMPVKHL 192
Cdd:cd01948   1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1657513  193 LPDnFHIGINVSAGCFLAAGFEKECLNLVNKLGNDKIKLVLELTERNPIPVTPEARAIFDSLHQHNITFALDDFGTGYAT 272
Cdd:cd01948  81 GPD-LRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSS 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1657513  273 YRYLQAFPVDFIKIDKSFVQMASVDEISGHIVDNIVELARKPGLSIVAEGVETQEQADLMIGKGVHFLQGYLYSPPVP 350
Cdd:cd01948 160 LSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLP 237
YjcC COG4943
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ...
 115-359 5.83e-88

Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal transduction mechanisms];


Pssm-ID: 443970 [Multi-domain]  Cd Length: 528  Bit Score: 274.49  E-value: 5.83e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1657513  115 ISLALENHEFKPWIQPVFCAQTGVLTGCEVLVRWEHPQTGIIPPDQFIPLAESSGLIVIMTRQLMKQTADILMPVKHLLP 194
Cdd:COG4943 276 LRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRDPDGSVISPDIFIPLAEQSGLISPLTRQVIEQVFRDLGDLLAADP 355

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1657513  195 DnFHIGINVSAGCFLAAGFEKECLNLVNKLGNDKIKLVLELTERNPIPVtPEARAIFDSLHQHNITFALDDFGTGYATYR 274
Cdd:COG4943 356 D-FHISINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITERGFIDP-AKARAVIAALREAGHRIAIDDFGTGYSSLS 433

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1657513  275 YLQAFPVDFIKIDKSFVQMASVDEISGHIVDNIVELARKPGLSIVAEGVETQEQADLMIGKGVHFLQGYLYSPPVPGNKF 354
Cdd:COG4943 434 YLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQGWLFAKPLPAEEF 513


                ....*
gi 1657513  355 IsEWV 359
Cdd:COG4943 514 I-AWL 517
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 113-348 7.33e-72

EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues. The EAL domain is a good candidate for a diguanylate phosphodiesterase function. The domain contains many conserved acidic residues that could participate in metal binding and might form the phosphodiesterase active site.


Pssm-ID: 425752 [Multi-domain]  Cd Length: 235  Bit Score: 223.73  E-value: 7.33e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1657513    113 EAISLALENHEFKPWIQPVFCAQTGVLTGCEVLVRWEHPQTGIIPPDQFIPLAESSGLIVIMTRQLMKQTADILMpvKHL 192
Cdd:pfam00563   2 RALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLA--QLQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1657513    193 LPDNFHIGINVSAGCFLAAGFEKECLNLVNKLGNDKIKLVLELTERNPIPVTPEARAIFDSLHQHNITFALDDFGTGYAT 272
Cdd:pfam00563  80 LGPDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSS 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1657513    273 YRYLQAFPVDFIKIDKSFVQMASVDEISGHIVDNIVELARKPGLSIVAEGVETQEQADLMIGKGVHFLQGYLYSPP 348
Cdd:pfam00563 160 LSYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
PRK10551 PRK10551
cyclic di-GMP phosphodiesterase;
115-355 1.32e-62

cyclic di-GMP phosphodiesterase;


Pssm-ID: 182541 [Multi-domain]  Cd Length: 518  Bit Score: 208.31  E-value: 1.32e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1657513   115 ISLALENHEFKPWIQPVFCAQTGVLTGCEVLVRWEHPQTGIIPPDQFIPLAESSGLIVIMTRQLMKQTADILMPVKHLLP 194
Cdd:PRK10551 268 ILTGIKRGQFYVEYQPVVDTQTLRVTGLEALLRWRHPTAGEIPPDAFINYAEAQKLIVPLTQHLFELIARDAAELQKVLP 347

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1657513   195 DNFHIGINVSAGCFLAAGFEKECLNLVNKLGNDKIKLVLELTERNPIPvTPEARAIFDSLHQHNITFALDDFGTGYATYR 274
Cdd:PRK10551 348 VGAKLGINISPAHLHSDSFKADVQRLLASLPADHFQIVLEITERDMVQ-EEEATKLFAWLHSQGIEIAIDDFGTGHSALI 426

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1657513   275 YLQAFPVDFIKIDKSFVQMASVDEISGHIVDNIVELARKPGLSIVAEGVETQEQADLMIGKGVHFLQGYLYSPPVPGNKF 354
Cdd:PRK10551 427 YLERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNFLQGYWISRPLPLEDF 506


                 .
gi 1657513   355 I 355
Cdd:PRK10551 507 V 507
LuxR_C_like cd06170
C-terminal DNA-binding domain of LuxR-like proteins. This domain contains a helix-turn-helix ...
 28-82 8.21e-10

C-terminal DNA-binding domain of LuxR-like proteins. This domain contains a helix-turn-helix motif and binds DNA. Proteins belonging to this group are response regulators; some act as transcriptional activators, others as transcriptional repressors. Many are active as homodimers. Many are two domain proteins in which the DNA binding property of the C-terminal DNA binding domain is modulated by modifications of the N-terminal domain. For example in the case of Lux R which participates in the regulation of gene expression in response to fluctuations in cell-population density (quorum-sensing), a signaling molecule, the pheromone Acyl HSL (N-acyl derivatives of homoserine lactone), binds to the N-terminal domain and leads to LuxR dimerization. For others phophorylation of the N-terminal domain leads to multimerization, for example Escherichia coli NarL and Sinorhizobium melilot FixJ. NarL controls gene expression of many respiratory-related operons when environmental nitrate or nitrite is present under anerobic conditions. FixJ is involved in the transcriptional activation of nitrogen fixation genes. The group also includes small proteins which lack an N-terminal signaling domain, such as Bacillus subtilis GerE. GerE is dimeric and acts in conjunction with sigmaK as an activator or a repressor modulating the expression of various genes in particular those encoding the spore-coat. These LuxR family regulators may share a similar organization of their target binding sites. For example the LuxR dimer binds the lux box, a 20bp inverted repeat, GerE dimers bind two 12bp consensus sequences in inverted orientation having the central four bases overlap, and the NarL dimer binds two 7bp inverted repeats separated by 2 bp.


Pssm-ID: 99777 [Multi-domain]  Cd Length: 57  Bit Score: 54.08  E-value: 8.21e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 1657513   28 SEKERLLLKLLMQGMSVTEISQYRNRSAKTISHQKKQLFEKLGIQSDITFWRDIF 82
Cdd:cd06170   2 TPREREVLRLLAEGKTNKEIADILGISEKTVKTHLRNIMRKLGVKSRTQLVAYAI 56
HTH_LUXR smart00421
helix_turn_helix, Lux Regulon; lux regulon (activates the bioluminescence operon
 24-79 1.46e-07

helix_turn_helix, Lux Regulon; lux regulon (activates the bioluminescence operon


Pssm-ID: 197715 [Multi-domain]  Cd Length: 58  Bit Score: 47.91  E-value: 1.46e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1657513      24 PGSVSEKERLLLKLLMQGMSVTEISQYRNRSAKTISHQKKQLFEKLGIQSDITFWR 79
Cdd:smart00421   1 LASLTPREREVLRLLAEGLTNKEIAERLGISEKTVKTHLSNIMRKLGVRSRTQAVR 56
PRK10840 PRK10840
transcriptional regulator RcsB; Provisional
 26-75 7.62e-07

transcriptional regulator RcsB; Provisional


Pssm-ID: 182771 [Multi-domain]  Cd Length: 216  Bit Score: 49.45  E-value: 7.62e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 1657513    26 SVSEKERLLLKLLMQGMSVTEISQYRNRSAKTISHQKKQLFEKLGIQSDI 75
Cdd:PRK10840 150 RLSPKESEVLRLFAEGFLVTEIAKKLNRSIKTISSQKKSAMMKLGVENDI 199
CsgD COG2771
DNA-binding transcriptional regulator, CsgD family [Transcription];
28-73 3.05e-04

DNA-binding transcriptional regulator, CsgD family [Transcription];


Pssm-ID: 442052 [Multi-domain]  Cd Length: 188  Bit Score: 41.28  E-value: 3.05e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 1657513   28 SEKERLLLKLLMQGMSVTEISQYRNRSAKTISHQKKQLFEKLGIQS 73
Cdd:COG2771 129 TPREREVLRLLAEGLTLKEIARILGISERTVRTHLKRIYRKLGVSS 174
GerE pfam00196
Bacterial regulatory proteins, luxR family;
26-74 9.30e-03

Bacterial regulatory proteins, luxR family;


Pssm-ID: 425517 [Multi-domain]  Cd Length: 57  Bit Score: 34.10  E-value: 9.30e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1657513     26 SVSEKERLLLKLLMQGMSVTEISQYRNRSAKTISHQKKQLFEKLGIQSD 74
Cdd:pfam00196   2 SLSPREREVLRWLAAGKSNKEIADELGISEKTVKVHRSNIMRKLNVHSR 50
 
Name Accession Description Interval E-value
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
 112-352 1.81e-104

Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 307.22  E-value: 1.81e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1657513     112 PEAISLALENHEFKPWIQPVFCAQTGVLTGCEVLVRWEHPQTGIIPPDQFIPLAESSGLIVIMTRQLMKQTADILMPVKH 191
Cdd:smart00052   1 ERELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1657513     192 LLPDNFHIGINVSAGCFLAAGFEKECLNLVNKLGNDKIKLVLELTERNPIPVTPEARAIFDSLHQHNITFALDDFGTGYA 271
Cdd:smart00052  81 QGPPPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1657513     272 TYRYLQAFPVDFIKIDKSFVQMASVDEISGHIVDNIVELARKPGLSIVAEGVETQEQADLMIGKGVHFLQGYLYSPPVPG 351
Cdd:smart00052 161 SLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPL 240


                   .
gi 1657513     352 N 352
Cdd:smart00052 241 D 241
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 113-350 5.57e-89

EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues and is also known as domain of unknown function 2 (DUF2). The EAL domain has been shown to stimulate degradation of a second messenger, cyclic di-GMP, and is a good candidate for a diguanylate phosphodiesterase function. Together with the GGDEF domain, EAL might be involved in regulating cell surface adhesiveness in bacteria.


Pssm-ID: 238923 [Multi-domain]  Cd Length: 240  Bit Score: 267.49  E-value: 5.57e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1657513  113 EAISLALENHEFKPWIQPVFCAQTGVLTGCEVLVRWEHPQTGIIPPDQFIPLAESSGLIVIMTRQLMKQTADILMPVKHL 192
Cdd:cd01948   1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1657513  193 LPDnFHIGINVSAGCFLAAGFEKECLNLVNKLGNDKIKLVLELTERNPIPVTPEARAIFDSLHQHNITFALDDFGTGYAT 272
Cdd:cd01948  81 GPD-LRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSS 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1657513  273 YRYLQAFPVDFIKIDKSFVQMASVDEISGHIVDNIVELARKPGLSIVAEGVETQEQADLMIGKGVHFLQGYLYSPPVP 350
Cdd:cd01948 160 LSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLP 237
YjcC COG4943
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ...
 115-359 5.83e-88

Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal transduction mechanisms];


Pssm-ID: 443970 [Multi-domain]  Cd Length: 528  Bit Score: 274.49  E-value: 5.83e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1657513  115 ISLALENHEFKPWIQPVFCAQTGVLTGCEVLVRWEHPQTGIIPPDQFIPLAESSGLIVIMTRQLMKQTADILMPVKHLLP 194
Cdd:COG4943 276 LRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRDPDGSVISPDIFIPLAEQSGLISPLTRQVIEQVFRDLGDLLAADP 355

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1657513  195 DnFHIGINVSAGCFLAAGFEKECLNLVNKLGNDKIKLVLELTERNPIPVtPEARAIFDSLHQHNITFALDDFGTGYATYR 274
Cdd:COG4943 356 D-FHISINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITERGFIDP-AKARAVIAALREAGHRIAIDDFGTGYSSLS 433

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1657513  275 YLQAFPVDFIKIDKSFVQMASVDEISGHIVDNIVELARKPGLSIVAEGVETQEQADLMIGKGVHFLQGYLYSPPVPGNKF 354
Cdd:COG4943 434 YLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQGWLFAKPLPAEEF 513


                ....*
gi 1657513  355 IsEWV 359
Cdd:COG4943 514 I-AWL 517
EAL COG2200
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
 113-356 5.71e-81

EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) [Signal transduction mechanisms];


Pssm-ID: 441802 [Multi-domain]  Cd Length: 576  Bit Score: 257.79  E-value: 5.71e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1657513  113 EAISLALENHEFKPWIQPVFCAQTGVLTGCEVLVRWEHPQTGIIPPDQFIPLAESSGLIVIMTRQLMKQTADILMpVKHL 192
Cdd:COG2200 331 SELREALEEGELRLYYQPIVDLRTGRVVGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELDRWVLERALRQLA-RWPE 409

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1657513  193 LPDNFHIGINVSAGCFLAAGFEKECLNLVNKLGNDKIKLVLELTERNPIPVTPEARAIFDSLHQHNITFALDDFGTGYAT 272
Cdd:COG2200 410 RGLDLRLSVNLSARSLLDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRIALDDFGTGYSS 489

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1657513  273 YRYLQAFPVDFIKIDKSFVQMASVDEISGHIVDNIVELARKPGLSIVAEGVETQEQADLMIGKGVHFLQGYLYSPPVPGN 352
Cdd:COG2200 490 LSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRPLPLE 569


                ....
gi 1657513  353 KFIS 356
Cdd:COG2200 570 ELEA 573
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 118-355 2.94e-76

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: 248.15  E-value: 2.94e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1657513  118 ALENHEFKPWIQPVFCAQTGVLTGCEVLVRWEHPQTGIIPPDQFIPLAESSGLIVIMTRQLMKQTADILMPVKHLLPDNF 197
Cdd:COG5001 433 ALERGELELHYQPQVDLATGRIVGAEALLRWQHPERGLVSPAEFIPLAEETGLIVPLGEWVLREACRQLAAWQDAGLPDL 512

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1657513  198 HIGINVSAGCFLAAGFEKECLNLVNKLGNDKIKLVLELTERNPIPVTPEARAIFDSLHQHNITFALDDFGTGYATYRYLQ 277
Cdd:COG5001 513 RVAVNLSARQLRDPDLVDRVRRALAETGLPPSRLELEITESALLEDPEEALETLRALRALGVRIALDDFGTGYSSLSYLK 592

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1657513  278 AFPVDFIKIDKSFVQMASVDEISGHIVDNIVELARKPGLSIVAEGVETQEQADLMIGKGVHFLQGYLYSPPVPGNKFI 355
Cdd:COG5001 593 RLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGCDYAQGYLFSRPLPAEELE 670
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 113-348 7.33e-72

EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues. The EAL domain is a good candidate for a diguanylate phosphodiesterase function. The domain contains many conserved acidic residues that could participate in metal binding and might form the phosphodiesterase active site.


Pssm-ID: 425752 [Multi-domain]  Cd Length: 235  Bit Score: 223.73  E-value: 7.33e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1657513    113 EAISLALENHEFKPWIQPVFCAQTGVLTGCEVLVRWEHPQTGIIPPDQFIPLAESSGLIVIMTRQLMKQTADILMpvKHL 192
Cdd:pfam00563   2 RALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLA--QLQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1657513    193 LPDNFHIGINVSAGCFLAAGFEKECLNLVNKLGNDKIKLVLELTERNPIPVTPEARAIFDSLHQHNITFALDDFGTGYAT 272
Cdd:pfam00563  80 LGPDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSS 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1657513    273 YRYLQAFPVDFIKIDKSFVQMASVDEISGHIVDNIVELARKPGLSIVAEGVETQEQADLMIGKGVHFLQGYLYSPP 348
Cdd:pfam00563 160 LSYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
PRK10551 PRK10551
cyclic di-GMP phosphodiesterase;
115-355 1.32e-62

cyclic di-GMP phosphodiesterase;


Pssm-ID: 182541 [Multi-domain]  Cd Length: 518  Bit Score: 208.31  E-value: 1.32e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1657513   115 ISLALENHEFKPWIQPVFCAQTGVLTGCEVLVRWEHPQTGIIPPDQFIPLAESSGLIVIMTRQLMKQTADILMPVKHLLP 194
Cdd:PRK10551 268 ILTGIKRGQFYVEYQPVVDTQTLRVTGLEALLRWRHPTAGEIPPDAFINYAEAQKLIVPLTQHLFELIARDAAELQKVLP 347

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1657513   195 DNFHIGINVSAGCFLAAGFEKECLNLVNKLGNDKIKLVLELTERNPIPvTPEARAIFDSLHQHNITFALDDFGTGYATYR 274
Cdd:PRK10551 348 VGAKLGINISPAHLHSDSFKADVQRLLASLPADHFQIVLEITERDMVQ-EEEATKLFAWLHSQGIEIAIDDFGTGHSALI 426

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1657513   275 YLQAFPVDFIKIDKSFVQMASVDEISGHIVDNIVELARKPGLSIVAEGVETQEQADLMIGKGVHFLQGYLYSPPVPGNKF 354
Cdd:PRK10551 427 YLERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNFLQGYWISRPLPLEDF 506


                 .
gi 1657513   355 I 355
Cdd:PRK10551 507 V 507
PRK13561 PRK13561
putative diguanylate cyclase; Provisional
 114-359 4.71e-48

putative diguanylate cyclase; Provisional


Pssm-ID: 184143 [Multi-domain]  Cd Length: 651  Bit Score: 171.82  E-value: 4.71e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1657513   114 AISLALENHEFKPWIQPVFCAQTGVLTGCEVLVRWEHPQTGIIPPDQFIPLAESSGLIVIMTRQLMKQTADILMPVKH-- 191
Cdd:PRK13561 404 DILNALENHQFAIWLQPQVEMRSGKLVSAEALLRMQQPDGSWDLPEGLIDRIESCGLMVTVGHWVLEESCRLLAAWQErg 483

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1657513   192 -LLPdnfhIGINVSAGCFLAAGFEKECLNLVNKLGNDKIKLVLELTERNPIPVTPEARAIFDSLHQHNITFALDDFGTGY 270
Cdd:PRK13561 484 iMLP----LSVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTESRRIDDPHAAVAILRPLRNAGVRVALDDFGMGY 559

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1657513   271 ATYRYLQAF---PVDFIKIDKSFVQMASVDEisgHIVDNIVELARKPGLSIVAEGVETQEQADLMIGKGVHFLQGYLYSP 347
Cdd:PRK13561 560 AGLRQLQHMkslPIDVLKIDKMFVDGLPEDD---SMVAAIIMLAQSLNLQVIAEGVETEAQRDWLLKAGVGIAQGFLFAR 636

                        250
                 ....*....|..
gi 1657513   348 PVPGNKFISEWV 359
Cdd:PRK13561 637 ALPIEIFEERYL 648
PRK11829 PRK11829
biofilm formation regulator HmsP; Provisional
 118-362 5.66e-45

biofilm formation regulator HmsP; Provisional


Pssm-ID: 183329 [Multi-domain]  Cd Length: 660  Bit Score: 163.57  E-value: 5.66e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1657513   118 ALENHEFKPWIQPVFCAQTGVLTGCEVLVRWEHPQTGIIPPDQFIPLAESSGLIVIMTRQLMKQTADILMPVKH---LLP 194
Cdd:PRK11829 413 AIENHDFTLFLQPQWDMKRQQVIGAEALLRWCQPDGSYVLPSGFVHFAEEEGMMVPLGNWVLEEACRILADWKArgvSLP 492

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1657513   195 dnfhIGINVSAGCFLAAGFEKECLNLVNKLGNDKIKLVLELTERNPIPVTPEARAIFDSLHQHNITFALDDFGTGYATYR 274
Cdd:PRK11829 493 ----LSVNISGLQVQNKQFLPHLKTLISHYHIDPQQLLLEITETAQIQDLDEALRLLRELQGLGLLIALDDFGIGYSSLR 568

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1657513   275 YL---QAFPVDFIKIDKSFVQMASVDEISGHIVDNIVELARkpgLSIVAEGVETQEQADLMIGKGVHFLQGYLYSPPVPG 351
Cdd:PRK11829 569 YLnhlKSLPIHMIKLDKSFVKNLPEDDAIARIISCVSDVLK---VRVMAEGVETEEQRQWLLEHGIQCGQGFLFSPPLPR 645

                        250
                 ....*....|.
gi 1657513   352 NKFISEWVMKA 362
Cdd:PRK11829 646 AEFEAQYFSSA 656
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
118-354 8.57e-39

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 146.37  E-value: 8.57e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1657513   118 ALENHEFKPWIQPVFCAqTGVLTGCEVLVRWEHPQTGIIPPDQFIPLAESSGLIVIMTRQLM----KQTADilMPVKHLl 193
Cdd:PRK10060 416 ALENDQLVIHYQPKITW-RGEVRSLEALVRWQSPERGLIPPLEFISYAEESGLIVPLGRWVMldvvRQVAK--WRDKGI- 491

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1657513   194 pdNFHIGINVSAGCFLAAGFEKECLNLVNKLGNDKIKLVLELTERNPIPVTPEARAIFDSLHQHNITFALDDFGTGYATY 273
Cdd:PRK10060 492 --NLRVAVNVSARQLADQTIFTALKQALQELNFEYCPIDVELTESCLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSL 569

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1657513   274 RYLQAFPVDFIKIDKSFVQMASVDEISGHIVDNIVELARKPGLSIVAEGVETQEQADLMIGKGVHFLQGYLYSPPVPGNK 353
Cdd:PRK10060 570 SQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKPMPAVA 649


                 .
gi 1657513   354 F 354
Cdd:PRK10060 650 F 650
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 114-359 7.38e-33

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 129.89  E-value: 7.38e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1657513   114 AISLALENHEFKPWIQPVFCAQTGVLTGCEVLVRWEHPQTGIIPPDQFIPLAESSGLIVIMT--------RQLMK-QTAD 184
Cdd:PRK11359 547 ALKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLAEEIGEIENIGrwviaeacRQLAEwRSQN 626

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1657513   185 ILMPVkhllpdnfhIGINVSAGCFLAAGFEKECLNLVNKLGNDKIKLVLELTERNPIPVTPEARAIFDSLHQHNITFALD 264
Cdd:PRK11359 627 IHIPA---------LSVNLSALHFRSNQLPNQVSDAMQAWGIDGHQLTVEITESMMMEHDTEIFKRIQILRDMGVGLSVD 697

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1657513   265 DFGTGYATYRYLQAFPVDFIKIDKSFVQMASVDEISGHIVDNIVELARKPGLSIVAEGVETQEQADLMIGKGVHFLQGYL 344
Cdd:PRK11359 698 DFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRVIQGYF 777

                        250
                 ....*....|....*
gi 1657513   345 YSPPVPGNKfISEWV 359
Cdd:PRK11359 778 FSRPLPAEE-IPGWM 791
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 105-350 3.87e-20

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 92.04  E-value: 3.87e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1657513    105 HYHHIVTPEAISLALENHEFK---PWIQPVFCAQTGVLtgcEVLVRWEHPQTGIIPPDQFIPLAESSGLI------VImt 175
Cdd:PRK09776  836 EHRALSLAEQWRMIKENQLMMlahGVASPRIPEARNHW---LISLRLWDPEGEIIDEGAFRPAAEDPALMhaldrrVI-- 910

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1657513    176 RQLMKQTAdilmpvKHLLPDNFHIGINVSAGCFLAAGFEKECLNLVNKLGNDKIKLVLELTERNPIPVTPEARAIFDSLH 255
Cdd:PRK09776  911 HEFFRQAA------KAVASKGLSIALPLSVAGLSSPTLLPFLLEQLENSPLPPRLLHLEITETALLNHAESASRLVQKLR 984

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1657513    256 QHNITFALDDFGTGYATYRYLQAFPVDFIKIDKSFVQMAS---VDEIsghIVDNIVELARKPGLSIVAEGVETQEQADLM 332
Cdd:PRK09776  985 LAGCRVVLSDFGRGLSSFNYLKAFMADYLKLDGELVANLHgnlMDEM---LISIIQGHAQRLGMKTIAGPVELPLVLDTL 1061

                         250
                  ....*....|....*...
gi 1657513    333 IGKGVHFLQGYLYSPPVP 350
Cdd:PRK09776 1062 SGIGVDLAYGYAIARPQP 1079
YuxH COG3434
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ...
 227-350 4.87e-17

c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction mechanisms];


Pssm-ID: 442660 [Multi-domain]  Cd Length: 407  Bit Score: 81.77  E-value: 4.87e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1657513  227 DKIKLVLELTERnpIPVTPEARAIFDSLHQHNITFALDDFGtgyATYRYLQAFP-VDFIKIDksfVQMASVDEIsghivD 305
Cdd:COG3434  82 PPERVVLEILED--VEPDEELLEALKELKEKGYRIALDDFV---LDPEWDPLLPlADIIKID---VLALDLEEL-----A 148

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 1657513  306 NIVELARKPGLSIVAEGVETQEQADLMIGKGVHFLQGYLYSPPVP 350
Cdd:COG3434 149 ELVARLKRYGIKLLAEKVETREEFELCKELGFDLFQGYFFSKPEI 193
LuxR_C_like cd06170
C-terminal DNA-binding domain of LuxR-like proteins. This domain contains a helix-turn-helix ...
 28-82 8.21e-10

C-terminal DNA-binding domain of LuxR-like proteins. This domain contains a helix-turn-helix motif and binds DNA. Proteins belonging to this group are response regulators; some act as transcriptional activators, others as transcriptional repressors. Many are active as homodimers. Many are two domain proteins in which the DNA binding property of the C-terminal DNA binding domain is modulated by modifications of the N-terminal domain. For example in the case of Lux R which participates in the regulation of gene expression in response to fluctuations in cell-population density (quorum-sensing), a signaling molecule, the pheromone Acyl HSL (N-acyl derivatives of homoserine lactone), binds to the N-terminal domain and leads to LuxR dimerization. For others phophorylation of the N-terminal domain leads to multimerization, for example Escherichia coli NarL and Sinorhizobium melilot FixJ. NarL controls gene expression of many respiratory-related operons when environmental nitrate or nitrite is present under anerobic conditions. FixJ is involved in the transcriptional activation of nitrogen fixation genes. The group also includes small proteins which lack an N-terminal signaling domain, such as Bacillus subtilis GerE. GerE is dimeric and acts in conjunction with sigmaK as an activator or a repressor modulating the expression of various genes in particular those encoding the spore-coat. These LuxR family regulators may share a similar organization of their target binding sites. For example the LuxR dimer binds the lux box, a 20bp inverted repeat, GerE dimers bind two 12bp consensus sequences in inverted orientation having the central four bases overlap, and the NarL dimer binds two 7bp inverted repeats separated by 2 bp.


Pssm-ID: 99777 [Multi-domain]  Cd Length: 57  Bit Score: 54.08  E-value: 8.21e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 1657513   28 SEKERLLLKLLMQGMSVTEISQYRNRSAKTISHQKKQLFEKLGIQSDITFWRDIF 82
Cdd:cd06170   2 TPREREVLRLLAEGKTNKEIADILGISEKTVKTHLRNIMRKLGVKSRTQLVAYAI 56
HTH_LUXR smart00421
helix_turn_helix, Lux Regulon; lux regulon (activates the bioluminescence operon
 24-79 1.46e-07

helix_turn_helix, Lux Regulon; lux regulon (activates the bioluminescence operon


Pssm-ID: 197715 [Multi-domain]  Cd Length: 58  Bit Score: 47.91  E-value: 1.46e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1657513      24 PGSVSEKERLLLKLLMQGMSVTEISQYRNRSAKTISHQKKQLFEKLGIQSDITFWR 79
Cdd:smart00421   1 LASLTPREREVLRLLAEGLTNKEIAERLGISEKTVKTHLSNIMRKLGVRSRTQAVR 56
PRK10840 PRK10840
transcriptional regulator RcsB; Provisional
 26-75 7.62e-07

transcriptional regulator RcsB; Provisional


Pssm-ID: 182771 [Multi-domain]  Cd Length: 216  Bit Score: 49.45  E-value: 7.62e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 1657513    26 SVSEKERLLLKLLMQGMSVTEISQYRNRSAKTISHQKKQLFEKLGIQSDI 75
Cdd:PRK10840 150 RLSPKESEVLRLFAEGFLVTEIAKKLNRSIKTISSQKKSAMMKLGVENDI 199
PRK11059 PRK11059
regulatory protein CsrD; Provisional
 118-350 5.75e-05

regulatory protein CsrD; Provisional


Pssm-ID: 236833 [Multi-domain]  Cd Length: 640  Bit Score: 44.85  E-value: 5.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1657513   118 ALENHEFKPWIQPVFCAQtGVLTGCEVLVRWEHPQTGIIPPDQFIPLAESSGLIVIMTRQLMKQTADILMPvkhlLPDNf 197
Cdd:PRK11059 411 TLVRGGPRLYQQPAVTRD-GKVHHRELFCRIRDGQGELLSAELFMPMVQQLGLSEQYDRQVIERVLPLLRY----WPEE- 484

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1657513   198 HIGINVSAGCFLAAGFEK-------ECLNLVNKlgndkiKLVLELTERNPIPVTPEARAIFDSLHQHNITFALDDFG-TG 269
Cdd:PRK11059 485 NLSINLSVDSLLSRAFQRwlrdtllQCPRSQRK------RLIFELAEADVCQHISRLRPVLRMLRGLGCRLAVDQAGlTV 558

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1657513   270 YATYrYLQAFPVDFIKIDKSFV---------QMAsvdeisghiVDNIVELARKPGLSIVAEGVETQEQADLMIGKGVHFL 340
Cdd:PRK11059 559 VSTS-YIKELNVELIKLHPSLVrnihkrtenQLF---------VRSLVGACAGTETQVFATGVESREEWQTLQELGVSGG 628

                        250
                 ....*....|
gi 1657513   341 QGYLYSPPVP 350
Cdd:PRK11059 629 QGDFFAESQP 638
PRK11596 PRK11596
cyclic-di-GMP phosphodiesterase; Provisional
 263-350 6.41e-05

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183222 [Multi-domain]  Cd Length: 255  Bit Score: 43.84  E-value: 6.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1657513   263 LDDFGTGYATYRYLQAFPVDFIKIDKSFVQMASVDEISGHIVDNIVELARKPGLSIVAEGVETQEQADLMIGKGVHFLQG 342
Cdd:PRK11596 157 LDDFGTGMANFSALSEVRYDYIKVARELFIMLRQSEEGRNLFSQLLHLMNRYCRGVIVEGVETPEEWRDVQRSPAFAAQG 236


                 ....*...
gi 1657513   343 YLYSPPVP 350
Cdd:PRK11596 237 YFLSRPAP 244
CsgD COG2771
DNA-binding transcriptional regulator, CsgD family [Transcription];
28-73 3.05e-04

DNA-binding transcriptional regulator, CsgD family [Transcription];


Pssm-ID: 442052 [Multi-domain]  Cd Length: 188  Bit Score: 41.28  E-value: 3.05e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 1657513   28 SEKERLLLKLLMQGMSVTEISQYRNRSAKTISHQKKQLFEKLGIQS 73
Cdd:COG2771 129 TPREREVLRLLAEGLTLKEIARILGISERTVRTHLKRIYRKLGVSS 174
PRK09483 PRK09483
response regulator; Provisional
 26-75 3.70e-04

response regulator; Provisional


Pssm-ID: 236538 [Multi-domain]  Cd Length: 217  Bit Score: 41.24  E-value: 3.70e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 1657513    26 SVSEKERLLLKLLMQGMSVTEISQYRNRSAKTISHQKKQLFEKLGIQSDI 75
Cdd:PRK09483 148 SLSERELQIMLMITKGQKVNEISEQLNLSPKTVNSYRYRMFSKLNISGDV 197
PRK10360 PRK10360
transcriptional regulator UhpA;
27-82 1.50e-03

transcriptional regulator UhpA;


Pssm-ID: 182408 [Multi-domain]  Cd Length: 196  Bit Score: 39.19  E-value: 1.50e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 1657513    27 VSEKERLLLKLLMQGMSVTEISQYRNRSAKTISHQKKQLFEKLGIQSDITFWRDIF 82
Cdd:PRK10360 138 LTKRERQVAEKLAQGMAVKEIAAELGLSPKTVHVHRANLMEKLGVSNDVELARRMF 193
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
 40-73 2.39e-03

DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 441799 [Multi-domain]  Cd Length: 131  Bit Score: 37.56  E-value: 2.39e-03
                        10        20        30
                ....*....|....*....|....*....|....
gi 1657513   40 QGMSVTEISQYRNRSAKTISHQKKQLFEKLGIQS 73
Cdd:COG2197  83 EGLSNKEIAERLGISERTVKTHVSNILRKLGVRN 116
GerE pfam00196
Bacterial regulatory proteins, luxR family;
26-74 9.30e-03

Bacterial regulatory proteins, luxR family;


Pssm-ID: 425517 [Multi-domain]  Cd Length: 57  Bit Score: 34.10  E-value: 9.30e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1657513     26 SVSEKERLLLKLLMQGMSVTEISQYRNRSAKTISHQKKQLFEKLGIQSD 74
Cdd:pfam00196   2 SLSPREREVLRWLAAGKSNKEIADELGISEKTVKVHRSNIMRKLNVHSR 50
 
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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