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Conserved domains on  [gi|16129126|ref|NP_415681|]
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blue light- and temperature-regulated antirepressor BluF [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

diguanylate phosphodiesterase( domain architecture ID 11279125)

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 ...
 150-389 1.29e-67

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


:

Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 214.39  E-value: 1.29e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129126    150 WLFIADGSDKELDSCALSPTINDHFAFHPIVDPLSRRIIAFEAIVQKNEDSPSAIAVGQRKDGEIYTADLKSKALAFTMA 229
Cdd:smart00052   1 ERELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129126    230 HALElgDKMISINLLPMTLVNePDAVSFLLNEIKANALVPEQIIVEFTESEVISRFDEFAEAIKSLKAAGISVAIDHFGA 309
Cdd:smart00052  81 QGPP--PLLISINLSARQLIS-PDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGT 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129126    310 GFAGLLLLSRFQPDRIKISQELITNVHKSGPRQAIIQAIIKCCTSLEIQVSAMGVATPEEWMWLESAGIEMFQGDLFAKA 389
Cdd:smart00052 158 GYSSLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRP 237
BLUF smart01034
Sensors of blue-light using FAD; The BLUF domain has been shown to bind FAD in the AppA ...
 2-93 5.04e-36

Sensors of blue-light using FAD; The BLUF domain has been shown to bind FAD in the AppA protein. AppA is involved in the repression of photosynthesis genes in response to blue-light.


:

Pssm-ID: 198102  Cd Length: 92  Bit Score: 126.92  E-value: 5.04e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129126      2 LTTLIYRSHIRDDEPVKKIEEMVSIANRRNMQSDVTGILLFNGSHFFQLLEGPEEQVKMIYRAICQDPRHYNIVELLCDY 81
Cdd:smart01034   1 LHRLVYVSRARPDLSPEDLEDILAQARRNNARLGITGVLLYNGGHFLQVLEGPEEAVEALYERIQRDPRHRDVQVLLYEP 80

                           90
                   ....*....|..
gi 16129126     82 APARRFGKAGME 93
Cdd:smart01034  81 IPERRFPDWSMG 92
 
Name Accession Description Interval E-value
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
 150-389 1.29e-67

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


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 214.39  E-value: 1.29e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129126    150 WLFIADGSDKELDSCALSPTINDHFAFHPIVDPLSRRIIAFEAIVQKNEDSPSAIAVGQRKDGEIYTADLKSKALAFTMA 229
Cdd:smart00052   1 ERELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129126    230 HALElgDKMISINLLPMTLVNePDAVSFLLNEIKANALVPEQIIVEFTESEVISRFDEFAEAIKSLKAAGISVAIDHFGA 309
Cdd:smart00052  81 QGPP--PLLISINLSARQLIS-PDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGT 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129126    310 GFAGLLLLSRFQPDRIKISQELITNVHKSGPRQAIIQAIIKCCTSLEIQVSAMGVATPEEWMWLESAGIEMFQGDLFAKA 389
Cdd:smart00052 158 GYSSLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRP 237
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 173-389 7.96e-55

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: 180.98  E-value: 7.96e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129126   173 HFAFHPIVDPLSRRIIAFEAIVQKNED-----SPSAIAVGQRKDGEIYTADLK--SKALAFtMAHALELGDKMISINLLP 245
Cdd:pfam00563  14 VLYYQPIVDLRTGRVVGYEALLRWQHPdggliSPARFLPLAEELGLIAELDRWvlEQALAD-LAQLQLGPDIKLSINLSP 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129126   246 MTLVnEPDAVSFLLNEIKANALVPEQIIVEFTESEVISRFDEFAEAIKSLKAAGISVAIDHFGAGFAGLLLLSRFQPDRI 325
Cdd:pfam00563  93 ASLA-DPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSLSYLLRLPPDFV 171

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129126   326 KISQELITNVHKSGPRQAIIQAIIKCCTSLEIQVSAMGVATPEEWMWLESAGIEMFQGDLFAKA 389
Cdd:pfam00563 172 KIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 173-389 1.04e-49

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: 167.72  E-value: 1.04e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129126 173 HFAFHPIVDPLSRRIIAFEAIV-----QKNEDSPS---AIAvgqRKDGEIYTADLK--SKALAFTMAHALELGDKMISIN 242
Cdd:cd01948  13 ELYYQPIVDLRTGRIVGYEALLrwrhpEGGLISPAefiPLA---EETGLIVELGRWvlEEACRQLARWQAGGPDLRLSVN 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129126 243 LLPMTLVNePDAVSFLLNEIKANALVPEQIIVEFTESEVISRFDEFAEAIKSLKAAGISVAIDHFGAGFAGLLLLSRFQP 322
Cdd:cd01948  90 LSARQLRD-PDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSLSYLKRLPV 168

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129126 323 DRIKISQELITNVHKSGPRQAIIQAIIKCCTSLEIQVSAMGVATPEEWMWLESAGIEMFQGDLFAKA 389
Cdd:cd01948 169 DYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRP 235
EAL COG2200
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
 173-389 6.08e-41

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: 152.63  E-value: 6.08e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129126 173 HFAFHPIVDPLSRRIIAFEAIVQKNEDSPSAIAVGQ-----RKDGEIYTADLK--SKALAFTMAHALELGDKMISINLLP 245
Cdd:COG2200 343 RLYYQPIVDLRTGRVVGYEALLRWRHPDGGLISPAEfipaaERSGLIVELDRWvlERALRQLARWPERGLDLRLSVNLSA 422

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129126 246 MTLVNePDAVSFLLNEIKANALVPEQIIVEFTESEVISRFDEFAEAIKSLKAAGISVAIDHFGAGFAGLLLLSRFQPDRI 325
Cdd:COG2200 423 RSLLD-PDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRIALDDFGTGYSSLSYLKRLPPDYL 501

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129126 326 KISQELITNVHKSGPRQAIIQAIIKCCTSLEIQVSAMGVATPEEWMWLESAGIEMFQGDLFAKA 389
Cdd:COG2200 502 KIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRP 565
BLUF smart01034
Sensors of blue-light using FAD; The BLUF domain has been shown to bind FAD in the AppA ...
 2-93 5.04e-36

Sensors of blue-light using FAD; The BLUF domain has been shown to bind FAD in the AppA protein. AppA is involved in the repression of photosynthesis genes in response to blue-light.


Pssm-ID: 198102  Cd Length: 92  Bit Score: 126.92  E-value: 5.04e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129126      2 LTTLIYRSHIRDDEPVKKIEEMVSIANRRNMQSDVTGILLFNGSHFFQLLEGPEEQVKMIYRAICQDPRHYNIVELLCDY 81
Cdd:smart01034   1 LHRLVYVSRARPDLSPEDLEDILAQARRNNARLGITGVLLYNGGHFLQVLEGPEEAVEALYERIQRDPRHRDVQVLLYEP 80

                           90
                   ....*....|..
gi 16129126     82 APARRFGKAGME 93
Cdd:smart01034  81 IPERRFPDWSMG 92
BLUF pfam04940
Sensors of blue-light using FAD; The BLUF domain has been shown to bind FAD in the AppA ...
 5-92 4.18e-31

Sensors of blue-light using FAD; The BLUF domain has been shown to bind FAD in the AppA protein. AppA is involved in the repression of photosynthesis genes in response to blue-light.


Pssm-ID: 461495  Cd Length: 89  Bit Score: 113.76  E-value: 4.18e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129126     5 LIYRSHIRDDEPVKKIEEMVSIANRRNMQSDVTGILLFNGSHFFQLLEGPEEQVKMIYRAICQDPRHYNIVELLCDYAPA 84
Cdd:pfam04940   1 LIYVSRAAADLSEEDLADILEQSRRNNARLGITGVLLYDGGRFLQVLEGPEEAVDALYERIKRDPRHTDVTVLEEGPIEE 80


                  ....*...
gi 16129126    85 RRFGKAGM 92
Cdd:pfam04940  81 RRFPDWSM 88
PRK13561 PRK13561
putative diguanylate cyclase; Provisional
 239-389 7.38e-19

putative diguanylate cyclase; Provisional


Pssm-ID: 184143 [Multi-domain]  Cd Length: 651  Bit Score: 88.62  E-value: 7.38e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129126  239 ISINLLPMTLVnEPDAVSFLLNEIKANALVPEQIIVEFTESeviSRFDEFAEAI---KSLKAAGISVAIDHFGAGFAGLL 315
Cdd:PRK13561 488 LSVNLSALQLM-HPNMVADMLELLTRYRIQPGTLILEVTES---RRIDDPHAAVailRPLRNAGVRVALDDFGMGYAGLR 563

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129126  316 LLSRFQP---DRIKISQELITNVHKSgprQAIIQAIIKCCTSLEIQVSAMGVATPEEWMWLESAGIEMFQGDLFAKA 389
Cdd:PRK13561 564 QLQHMKSlpiDVLKIDKMFVDGLPED---DSMVAAIIMLAQSLNLQVIAEGVETEAQRDWLLKAGVGIAQGFLFARA 637
 
Name Accession Description Interval E-value
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
 150-389 1.29e-67

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


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 214.39  E-value: 1.29e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129126    150 WLFIADGSDKELDSCALSPTINDHFAFHPIVDPLSRRIIAFEAIVQKNEDSPSAIAVGQRKDGEIYTADLKSKALAFTMA 229
Cdd:smart00052   1 ERELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129126    230 HALElgDKMISINLLPMTLVNePDAVSFLLNEIKANALVPEQIIVEFTESEVISRFDEFAEAIKSLKAAGISVAIDHFGA 309
Cdd:smart00052  81 QGPP--PLLISINLSARQLIS-PDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGT 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129126    310 GFAGLLLLSRFQPDRIKISQELITNVHKSGPRQAIIQAIIKCCTSLEIQVSAMGVATPEEWMWLESAGIEMFQGDLFAKA 389
Cdd:smart00052 158 GYSSLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRP 237
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 173-389 7.96e-55

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: 180.98  E-value: 7.96e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129126   173 HFAFHPIVDPLSRRIIAFEAIVQKNED-----SPSAIAVGQRKDGEIYTADLK--SKALAFtMAHALELGDKMISINLLP 245
Cdd:pfam00563  14 VLYYQPIVDLRTGRVVGYEALLRWQHPdggliSPARFLPLAEELGLIAELDRWvlEQALAD-LAQLQLGPDIKLSINLSP 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129126   246 MTLVnEPDAVSFLLNEIKANALVPEQIIVEFTESEVISRFDEFAEAIKSLKAAGISVAIDHFGAGFAGLLLLSRFQPDRI 325
Cdd:pfam00563  93 ASLA-DPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSLSYLLRLPPDFV 171

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129126   326 KISQELITNVHKSGPRQAIIQAIIKCCTSLEIQVSAMGVATPEEWMWLESAGIEMFQGDLFAKA 389
Cdd:pfam00563 172 KIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 173-389 1.04e-49

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: 167.72  E-value: 1.04e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129126 173 HFAFHPIVDPLSRRIIAFEAIV-----QKNEDSPS---AIAvgqRKDGEIYTADLK--SKALAFTMAHALELGDKMISIN 242
Cdd:cd01948  13 ELYYQPIVDLRTGRIVGYEALLrwrhpEGGLISPAefiPLA---EETGLIVELGRWvlEEACRQLARWQAGGPDLRLSVN 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129126 243 LLPMTLVNePDAVSFLLNEIKANALVPEQIIVEFTESEVISRFDEFAEAIKSLKAAGISVAIDHFGAGFAGLLLLSRFQP 322
Cdd:cd01948  90 LSARQLRD-PDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSLSYLKRLPV 168

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129126 323 DRIKISQELITNVHKSGPRQAIIQAIIKCCTSLEIQVSAMGVATPEEWMWLESAGIEMFQGDLFAKA 389
Cdd:cd01948 169 DYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRP 235
EAL COG2200
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
 173-389 6.08e-41

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: 152.63  E-value: 6.08e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129126 173 HFAFHPIVDPLSRRIIAFEAIVQKNEDSPSAIAVGQ-----RKDGEIYTADLK--SKALAFTMAHALELGDKMISINLLP 245
Cdd:COG2200 343 RLYYQPIVDLRTGRVVGYEALLRWRHPDGGLISPAEfipaaERSGLIVELDRWvlERALRQLARWPERGLDLRLSVNLSA 422

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129126 246 MTLVNePDAVSFLLNEIKANALVPEQIIVEFTESEVISRFDEFAEAIKSLKAAGISVAIDHFGAGFAGLLLLSRFQPDRI 325
Cdd:COG2200 423 RSLLD-PDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRIALDDFGTGYSSLSYLKRLPPDYL 501

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129126 326 KISQELITNVHKSGPRQAIIQAIIKCCTSLEIQVSAMGVATPEEWMWLESAGIEMFQGDLFAKA 389
Cdd:COG2200 502 KIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRP 565
BLUF smart01034
Sensors of blue-light using FAD; The BLUF domain has been shown to bind FAD in the AppA ...
 2-93 5.04e-36

Sensors of blue-light using FAD; The BLUF domain has been shown to bind FAD in the AppA protein. AppA is involved in the repression of photosynthesis genes in response to blue-light.


Pssm-ID: 198102  Cd Length: 92  Bit Score: 126.92  E-value: 5.04e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129126      2 LTTLIYRSHIRDDEPVKKIEEMVSIANRRNMQSDVTGILLFNGSHFFQLLEGPEEQVKMIYRAICQDPRHYNIVELLCDY 81
Cdd:smart01034   1 LHRLVYVSRARPDLSPEDLEDILAQARRNNARLGITGVLLYNGGHFLQVLEGPEEAVEALYERIQRDPRHRDVQVLLYEP 80

                           90
                   ....*....|..
gi 16129126     82 APARRFGKAGME 93
Cdd:smart01034  81 IPERRFPDWSMG 92
BLUF pfam04940
Sensors of blue-light using FAD; The BLUF domain has been shown to bind FAD in the AppA ...
 5-92 4.18e-31

Sensors of blue-light using FAD; The BLUF domain has been shown to bind FAD in the AppA protein. AppA is involved in the repression of photosynthesis genes in response to blue-light.


Pssm-ID: 461495  Cd Length: 89  Bit Score: 113.76  E-value: 4.18e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129126     5 LIYRSHIRDDEPVKKIEEMVSIANRRNMQSDVTGILLFNGSHFFQLLEGPEEQVKMIYRAICQDPRHYNIVELLCDYAPA 84
Cdd:pfam04940   1 LIYVSRAAADLSEEDLADILEQSRRNNARLGITGVLLYDGGRFLQVLEGPEEAVDALYERIKRDPRHTDVTVLEEGPIEE 80


                  ....*...
gi 16129126    85 RRFGKAGM 92
Cdd:pfam04940  81 RRFPDWSM 88
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 171-389 1.39e-29

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: 121.03  E-value: 1.39e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129126 171 NDHFAFH--PIVDPLSRRIIAFEAIV-----QKN-----------EDSPSAIAVGQ---RKdgeiytadlkskALAFTMA 229
Cdd:COG5001 436 RGELELHyqPQVDLATGRIVGAEALLrwqhpERGlvspaefiplaEETGLIVPLGEwvlRE------------ACRQLAA 503

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129126 230 -HALELGDKMISINLLPMTLvNEPDAVSFLLNEIKANALVPEQIIVEFTESEVISRFDEFAEAIKSLKAAGISVAIDHFG 308
Cdd:COG5001 504 wQDAGLPDLRVAVNLSARQL-RDPDLVDRVRRALAETGLPPSRLELEITESALLEDPEEALETLRALRALGVRIALDDFG 582

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129126 309 AGFAGLLLLSRFQPDRIKISQELITNVHKSGPRQAIIQAIIKCCTSLEIQVSAMGVATPEEWMWLESAGIEMFQGDLFAK 388
Cdd:COG5001 583 TGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGCDYAQGYLFSR 662


                .
gi 16129126 389 A 389
Cdd:COG5001 663 P 663
YjcC COG4943
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ...
 239-389 9.52e-20

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: 91.13  E-value: 9.52e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129126 239 ISINLLPMTLVNePDAVSFLLNEIKANALVPEQIIVEFTESEVISrFDEFAEAIKSLKAAGISVAIDHFGAGFAGLLLLS 318
Cdd:COG4943 359 ISINLSASDLLS-PRFLDDLERLLARTGVAPQQIVLEITERGFID-PAKARAVIAALREAGHRIAIDDFGTGYSSLSYLQ 436

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129126 319 RFQPDRIKISQELITNVHKSGPRQAIIQAIIKCCTSLEIQVSAMGVATPEEWMWLESAGIEMFQGDLFAKA 389
Cdd:COG4943 437 TLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQGWLFAKP 507
PRK13561 PRK13561
putative diguanylate cyclase; Provisional
 239-389 7.38e-19

putative diguanylate cyclase; Provisional


Pssm-ID: 184143 [Multi-domain]  Cd Length: 651  Bit Score: 88.62  E-value: 7.38e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129126  239 ISINLLPMTLVnEPDAVSFLLNEIKANALVPEQIIVEFTESeviSRFDEFAEAI---KSLKAAGISVAIDHFGAGFAGLL 315
Cdd:PRK13561 488 LSVNLSALQLM-HPNMVADMLELLTRYRIQPGTLILEVTES---RRIDDPHAAVailRPLRNAGVRVALDDFGMGYAGLR 563

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129126  316 LLSRFQP---DRIKISQELITNVHKSgprQAIIQAIIKCCTSLEIQVSAMGVATPEEWMWLESAGIEMFQGDLFAKA 389
Cdd:PRK13561 564 QLQHMKSlpiDVLKIDKMFVDGLPED---DSMVAAIIMLAQSLNLQVIAEGVETEAQRDWLLKAGVGIAQGFLFARA 637
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
255-388 1.24e-16

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 81.65  E-value: 1.24e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129126  255 VSFLLNEIKANALVPEQIIVEFTESEVISRFDEFAEAIKSLKAAGISVAIDHFGAGFAGLLLLSRFQPDRIKISQELITN 334
Cdd:PRK10060 510 FTALKQALQELNFEYCPIDVELTESCLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRD 589

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 16129126  335 VHKSGPRQAIIQAIIKCCTSLEIQVSAMGVATPEEWMWLESAGIEMFQGDLFAK 388
Cdd:PRK10060 590 IHKQPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAK 643
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 239-399 1.64e-14

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 75.58  E-value: 1.64e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129126  239 ISINLLPMTLVNE--PDAVSFLLNEIkanALVPEQIIVEFTESEVISRFDEFAEAIKSLKAAGISVAIDHFGAGFAGLLL 316
Cdd:PRK11359 632 LSVNLSALHFRSNqlPNQVSDAMQAW---GIDGHQLTVEITESMMMEHDTEIFKRIQILRDMGVGLSVDDFGTGFSGLSR 708

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129126  317 LSRFQPDRIKISQELITNVHKSGPRQAIIQAIIKCCTSLEIQVSAMGVATPEEWMWLESAGIEMFQGDLFAKA-KLNGIP 395
Cdd:PRK11359 709 LVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRPlPAEEIP 788


                 ....
gi 16129126  396 siAW 399
Cdd:PRK11359 789 --GW 790
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 239-389 5.51e-14

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 73.94  E-value: 5.51e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129126   239 ISINLLPMTLvNEPDAVSFLLNEIKANALVPEQIIVEFTESEVISRFDEFAEAIKSLKAAGISVAIDHFGAGFAGLLLLS 318
Cdd:PRK09776  928 IALPLSVAGL-SSPTLLPFLLEQLENSPLPPRLLHLEITETALLNHAESASRLVQKLRLAGCRVVLSDFGRGLSSFNYLK 1006

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129126   319 RFQPDRIKISQELITNVHKSGPRQAIIQAIIKCCTSLEIQVSAMGVATPEEWMWLESAGIEMFQGDLFAKA 389
Cdd:PRK09776 1007 AFMADYLKLDGELVANLHGNLMDEMLISIIQGHAQRLGMKTIAGPVELPLVLDTLSGIGVDLAYGYAIARP 1077
PRK11829 PRK11829
biofilm formation regulator HmsP; Provisional
 262-389 1.80e-13

biofilm formation regulator HmsP; Provisional


Pssm-ID: 183329 [Multi-domain]  Cd Length: 660  Bit Score: 71.90  E-value: 1.80e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129126  262 IKANALVPEQIIVEFTESEVISRFDEFAEAIKSLKAAGISVAIDHFGAGFAGLLLLSRFQP---DRIKISQELITNVhks 338
Cdd:PRK11829 515 ISHYHIDPQQLLLEITETAQIQDLDEALRLLRELQGLGLLIALDDFGIGYSSLRYLNHLKSlpiHMIKLDKSFVKNL--- 591

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 16129126  339 gPRQAIIQAIIKCCTS-LEIQVSAMGVATPEEWMWLESAGIEMFQGDLFAKA 389
Cdd:PRK11829 592 -PEDDAIARIISCVSDvLKVRVMAEGVETEEQRQWLLEHGIQCGQGFLFSPP 642
PRK11059 PRK11059
regulatory protein CsrD; Provisional
 270-387 7.88e-10

regulatory protein CsrD; Provisional


Pssm-ID: 236833 [Multi-domain]  Cd Length: 640  Bit Score: 60.65  E-value: 7.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129126  270 EQIIVEFTESEVISRFDEFAEAIKSLKAAGISVAIDHfgagfAGLLLLS-----RFQPDRIKISQELITNVHKSGPRQAI 344
Cdd:PRK11059 517 KRLIFELAEADVCQHISRLRPVLRMLRGLGCRLAVDQ-----AGLTVVStsyikELNVELIKLHPSLVRNIHKRTENQLF 591

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 16129126  345 IQAIIKCCTSLEIQVSAMGVATPEEWMWLESAGIEMFQGDLFA 387
Cdd:PRK11059 592 VRSLVGACAGTETQVFATGVESREEWQTLQELGVSGGQGDFFA 634
PRK10551 PRK10551
cyclic di-GMP phosphodiesterase;
225-388 9.01e-10

cyclic di-GMP phosphodiesterase;


Pssm-ID: 182541 [Multi-domain]  Cd Length: 518  Bit Score: 60.39  E-value: 9.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129126  225 AFTMAHALELGDKmISINLLPMTLVNEP--DAVSFLLNEIKANALvpeQIIVEFTESEVISRfdefAEAIKS---LKAAG 299
Cdd:PRK10551 339 AAELQKVLPVGAK-LGINISPAHLHSDSfkADVQRLLASLPADHF---QIVLEITERDMVQE----EEATKLfawLHSQG 410

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129126  300 ISVAIDHFGAGFAGLLLLSRFQPDRIKISQELITNVHKSGPRQAIIQAIIKCCTSLEIQVSAMGVATPEEWMWLESAGIE 379
Cdd:PRK10551 411 IEIAIDDFGTGHSALIYLERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERGVN 490


                 ....*....
gi 16129126  380 MFQGDLFAK 388
Cdd:PRK10551 491 FLQGYWISR 499
YuxH COG3434
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ...
 256-388 4.88e-06

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


Pssm-ID: 442660 [Multi-domain]  Cd Length: 407  Bit Score: 48.26  E-value: 4.88e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129126 256 SFLLNEIkANALVPEQIIVEFTESEVISrfDEFAEAIKSLKAAGISVAIDHFGAGFAGLLLLSRFqpDRIKIsqelitNV 335
Cdd:COG3434  71 ELLLSDL-PELLPPERVVLEILEDVEPD--EELLEALKELKEKGYRIALDDFVLDPEWDPLLPLA--DIIKI------DV 139

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 16129126 336 HKSGPRQaiIQAIIKCCTSLEIQVSAMGVATPEEWMWLESAGIEMFQGDLFAK 388
Cdd:COG3434 140 LALDLEE--LAELVARLKRYGIKLLAEKVETREEFELCKELGFDLFQGYFFSK 190
 
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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