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Conserved domains on  [gi|695731284|ref|WP_032657802|]
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MULTISPECIES: diguanylate phosphodiesterase [Enterobacter]

Protein Classification

diguanylate phosphodiesterase( domain architecture ID 11279124)

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 pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 173-389 2.90e-50

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: 169.42  E-value: 2.90e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731284  173 SFAFQPIVDPFMQQVVSWEALLR--TPDGGA-PGDYFANLPRDEVYASDLHS---KQVALSMASALGLQDQTLSLNLRPM 246
Cdd:pfam00563  14 VLYYQPIVDLRTGRVVGYEALLRwqHPDGGLiSPARFLPLAEELGLIAELDRwvlEQALADLAQLQLGPDIKLSINLSPA 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731284  247 TLVNiPNAVDFLLTAIEANGFVPEQIVVEFTESEAISRFDEFTDSVRQLKSAGISVTIDHFGAGFAGLQLLAQFQPDRIK 326
Cdd:pfam00563  94 SLAD-PGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSLSYLLRLPPDFVK 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695731284  327 INRDLVANVHKSGPRQAIIQAIIKCCSSLEIQFCAVGVEKAEEWMWLESAGISQFQGHLFASP 389
Cdd:pfam00563 173 IDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
BLUF smart01034
Sensors of blue-light using FAD; The BLUF domain has been shown to bind FAD in the AppA ...
 2-93 1.80e-34

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: 123.07  E-value: 1.80e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731284     2 LTTIIYRSHICEDVPVKALEAMVAAANSKNRQSNVTGILLFNGTHFFQLLEGPVEHVSAIYEQICNDPRHHNVVELMRDH 81
Cdd:smart01034   1 LHRLVYVSRARPDLSPEDLEDILAQARRNNARLGITGVLLYNGGHFLQVLEGPEEAVEALYERIQRDPRHRDVQVLLYEP 80

                           90
                   ....*....|..
gi 695731284    82 GPVRRFGNVGME 93
Cdd:smart01034  81 IPERRFPDWSMG 92
 
Name Accession Description Interval E-value
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 173-389 2.90e-50

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: 169.42  E-value: 2.90e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731284  173 SFAFQPIVDPFMQQVVSWEALLR--TPDGGA-PGDYFANLPRDEVYASDLHS---KQVALSMASALGLQDQTLSLNLRPM 246
Cdd:pfam00563  14 VLYYQPIVDLRTGRVVGYEALLRwqHPDGGLiSPARFLPLAEELGLIAELDRwvlEQALADLAQLQLGPDIKLSINLSPA 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731284  247 TLVNiPNAVDFLLTAIEANGFVPEQIVVEFTESEAISRFDEFTDSVRQLKSAGISVTIDHFGAGFAGLQLLAQFQPDRIK 326
Cdd:pfam00563  94 SLAD-PGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSLSYLLRLPPDFVK 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695731284  327 INRDLVANVHKSGPRQAIIQAIIKCCSSLEIQFCAVGVEKAEEWMWLESAGISQFQGHLFASP 389
Cdd:pfam00563 173 IDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
 176-389 5.44e-48

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


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 163.54  E-value: 5.44e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731284   176 FQPIVDPFMQQVVSWEALLR--TPDGG--APGDYfanLPRDEvyASDL---------HSKQVALSMASALGLQDQTLSLN 242
Cdd:smart00052  17 YQPIVSLRTGRLVGVEALIRwqHPEGGiiSPDEF---IPLAE--ETGLivplgrwvlEQACQQLAEWQAQGPPPLLISIN 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731284   243 LRPMTLVNiPNAVDFLLTAIEANGFVPEQIVVEFTESeAISRFDEFTDSV-RQLKSAGISVTIDHFGAGFAGLQLLAQFQ 321
Cdd:smart00052  92 LSARQLIS-PDLVPRVLELLEETGLPPQRLELEITES-VLLDDDESAVATlQRLRELGVRIALDDFGTGYSSLSYLKRLP 169

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695731284   322 PDRIKINRDLVANVHKSGPRQAIIQAIIKCCSSLEIQFCAVGVEKAEEWMWLESAGISQFQGHLFASP 389
Cdd:smart00052 170 VDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRP 237
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 175-389 1.17e-47

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: 162.71  E-value: 1.17e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731284 175 AFQPIVDPFMQQVVSWEALLR--TPDGGA-PGDYFanLPRDEvyASDLHSK---QV---ALSMASAL--GLQDQTLSLNL 243
Cdd:cd01948   15 YYQPIVDLRTGRIVGYEALLRwrHPEGGLiSPAEF--IPLAE--ETGLIVElgrWVleeACRQLARWqaGGPDLRLSVNL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731284 244 RPMTLVNiPNAVDFLLTAIEANGFVPEQIVVEFTESEAISRFDEFTDSVRQLKSAGISVTIDHFGAGFAGLQLLAQFQPD 323
Cdd:cd01948   91 SARQLRD-PDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSLSYLKRLPVD 169

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695731284 324 RIKINRDLVANVHKSGPRQAIIQAIIKCCSSLEIQFCAVGVEKAEEWMWLESAGISQFQGHLFASP 389
Cdd:cd01948  170 YLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRP 235
EAL COG2200
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
 173-390 2.85e-45

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: 164.57  E-value: 2.85e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731284 173 SFAFQPIVDPFMQQVVSWEALLR--TPDGG--APGDYFANLPRDEVYAS-DLHSKQVALSMASALGLQ--DQTLSLNLRP 245
Cdd:COG2200  343 RLYYQPIVDLRTGRVVGYEALLRwrHPDGGliSPAEFIPAAERSGLIVElDRWVLERALRQLARWPERglDLRLSVNLSA 422

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731284 246 MTLVNiPNAVDFLLTAIEANGFVPEQIVVEFTESEAISRFDEFTDSVRQLKSAGISVTIDHFGAGFAGLQLLAQFQPDRI 325
Cdd:COG2200  423 RSLLD-PDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRIALDDFGTGYSSLSYLKRLPPDYL 501

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695731284 326 KINRDLVANVHKSGPRQAIIQAIIKCCSSLEIQFCAVGVEKAEEWMWLESAGISQFQGHLFASPR 390
Cdd:COG2200  502 KIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRPL 566
BLUF smart01034
Sensors of blue-light using FAD; The BLUF domain has been shown to bind FAD in the AppA ...
 2-93 1.80e-34

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: 123.07  E-value: 1.80e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731284     2 LTTIIYRSHICEDVPVKALEAMVAAANSKNRQSNVTGILLFNGTHFFQLLEGPVEHVSAIYEQICNDPRHHNVVELMRDH 81
Cdd:smart01034   1 LHRLVYVSRARPDLSPEDLEDILAQARRNNARLGITGVLLYNGGHFLQVLEGPEEAVEALYERIQRDPRHRDVQVLLYEP 80

                           90
                   ....*....|..
gi 695731284    82 GPVRRFGNVGME 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 1.09e-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: 115.68  E-value: 1.09e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731284    5 IIYRSHICEDVPVKALEAMVAAANSKNRQSNVTGILLFNGTHFFQLLEGPVEHVSAIYEQICNDPRHHNVVELMRDHGPV 84
Cdd:pfam04940   1 LIYVSRAAADLSEEDLADILEQSRRNNARLGITGVLLYDGGRFLQVLEGPEEAVDALYERIKRDPRHTDVTVLEEGPIEE 80


                  ....*...
gi 695731284   85 RRFGNVGM 92
Cdd:pfam04940  81 RRFPDWSM 88
PRK13561 PRK13561
putative diguanylate cyclase; Provisional
 154-389 1.14e-21

putative diguanylate cyclase; Provisional


Pssm-ID: 184143 [Multi-domain]  Cd Length: 651  Bit Score: 97.09  E-value: 1.14e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731284 154 REETRLSAQPEVVAKGADCSFA--FQPIVDPFMQQVVSWEALLR--TPDG--GAPGDYFANLPRDEVYAS------DLHS 221
Cdd:PRK13561 394 AAQKRLTEESDILNALENHQFAiwLQPQVEMRSGKLVSAEALLRmqQPDGswDLPEGLIDRIESCGLMVTvghwvlEESC 473

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731284 222 KQVALSMASALGLqdqTLSLNLRPMTLVNiPNAVDFLLTAIEANGFVPEQIVVEFTESEAISRFDEFTDSVRQLKSAGIS 301
Cdd:PRK13561 474 RLLAAWQERGIML---PLSVNLSALQLMH-PNMVADMLELLTRYRIQPGTLILEVTESRRIDDPHAAVAILRPLRNAGVR 549

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731284 302 VTIDHFGAGFAGLQLLAQFQP---DRIKINRDLVANVHKSgprQAIIQAIIKCCSSLEIQFCAVGVEKAEEWMWLESAGI 378
Cdd:PRK13561 550 VALDDFGMGYAGLRQLQHMKSlpiDVLKIDKMFVDGLPED---DSMVAAIIMLAQSLNLQVIAEGVETEAQRDWLLKAGV 626

                        250
                 ....*....|.
gi 695731284 379 SQFQGHLFASP 389
Cdd:PRK13561 627 GIAQGFLFARA 637
 
Name Accession Description Interval E-value
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 173-389 2.90e-50

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: 169.42  E-value: 2.90e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731284  173 SFAFQPIVDPFMQQVVSWEALLR--TPDGGA-PGDYFANLPRDEVYASDLHS---KQVALSMASALGLQDQTLSLNLRPM 246
Cdd:pfam00563  14 VLYYQPIVDLRTGRVVGYEALLRwqHPDGGLiSPARFLPLAEELGLIAELDRwvlEQALADLAQLQLGPDIKLSINLSPA 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731284  247 TLVNiPNAVDFLLTAIEANGFVPEQIVVEFTESEAISRFDEFTDSVRQLKSAGISVTIDHFGAGFAGLQLLAQFQPDRIK 326
Cdd:pfam00563  94 SLAD-PGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSLSYLLRLPPDFVK 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695731284  327 INRDLVANVHKSGPRQAIIQAIIKCCSSLEIQFCAVGVEKAEEWMWLESAGISQFQGHLFASP 389
Cdd:pfam00563 173 IDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
 176-389 5.44e-48

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


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 163.54  E-value: 5.44e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731284   176 FQPIVDPFMQQVVSWEALLR--TPDGG--APGDYfanLPRDEvyASDL---------HSKQVALSMASALGLQDQTLSLN 242
Cdd:smart00052  17 YQPIVSLRTGRLVGVEALIRwqHPEGGiiSPDEF---IPLAE--ETGLivplgrwvlEQACQQLAEWQAQGPPPLLISIN 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731284   243 LRPMTLVNiPNAVDFLLTAIEANGFVPEQIVVEFTESeAISRFDEFTDSV-RQLKSAGISVTIDHFGAGFAGLQLLAQFQ 321
Cdd:smart00052  92 LSARQLIS-PDLVPRVLELLEETGLPPQRLELEITES-VLLDDDESAVATlQRLRELGVRIALDDFGTGYSSLSYLKRLP 169

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695731284   322 PDRIKINRDLVANVHKSGPRQAIIQAIIKCCSSLEIQFCAVGVEKAEEWMWLESAGISQFQGHLFASP 389
Cdd:smart00052 170 VDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRP 237
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 175-389 1.17e-47

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: 162.71  E-value: 1.17e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731284 175 AFQPIVDPFMQQVVSWEALLR--TPDGGA-PGDYFanLPRDEvyASDLHSK---QV---ALSMASAL--GLQDQTLSLNL 243
Cdd:cd01948   15 YYQPIVDLRTGRIVGYEALLRwrHPEGGLiSPAEF--IPLAE--ETGLIVElgrWVleeACRQLARWqaGGPDLRLSVNL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731284 244 RPMTLVNiPNAVDFLLTAIEANGFVPEQIVVEFTESEAISRFDEFTDSVRQLKSAGISVTIDHFGAGFAGLQLLAQFQPD 323
Cdd:cd01948   91 SARQLRD-PDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSLSYLKRLPVD 169

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695731284 324 RIKINRDLVANVHKSGPRQAIIQAIIKCCSSLEIQFCAVGVEKAEEWMWLESAGISQFQGHLFASP 389
Cdd:cd01948  170 YLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRP 235
EAL COG2200
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
 173-390 2.85e-45

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: 164.57  E-value: 2.85e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731284 173 SFAFQPIVDPFMQQVVSWEALLR--TPDGG--APGDYFANLPRDEVYAS-DLHSKQVALSMASALGLQ--DQTLSLNLRP 245
Cdd:COG2200  343 RLYYQPIVDLRTGRVVGYEALLRwrHPDGGliSPAEFIPAAERSGLIVElDRWVLERALRQLARWPERglDLRLSVNLSA 422

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731284 246 MTLVNiPNAVDFLLTAIEANGFVPEQIVVEFTESEAISRFDEFTDSVRQLKSAGISVTIDHFGAGFAGLQLLAQFQPDRI 325
Cdd:COG2200  423 RSLLD-PDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRIALDDFGTGYSSLSYLKRLPPDYL 501

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695731284 326 KINRDLVANVHKSGPRQAIIQAIIKCCSSLEIQFCAVGVEKAEEWMWLESAGISQFQGHLFASPR 390
Cdd:COG2200  502 KIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRPL 566
BLUF smart01034
Sensors of blue-light using FAD; The BLUF domain has been shown to bind FAD in the AppA ...
 2-93 1.80e-34

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: 123.07  E-value: 1.80e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731284     2 LTTIIYRSHICEDVPVKALEAMVAAANSKNRQSNVTGILLFNGTHFFQLLEGPVEHVSAIYEQICNDPRHHNVVELMRDH 81
Cdd:smart01034   1 LHRLVYVSRARPDLSPEDLEDILAQARRNNARLGITGVLLYNGGHFLQVLEGPEEAVEALYERIQRDPRHRDVQVLLYEP 80

                           90
                   ....*....|..
gi 695731284    82 GPVRRFGNVGME 93
Cdd:smart01034  81 IPERRFPDWSMG 92
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 176-389 2.41e-32

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: 129.12  E-value: 2.41e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731284 176 FQPIVDPFMQQVVSWEALLR--TPDGG--APGDyFanLPrdevYASDLH-----SKQV---ALSMASAL---GLQDQTLS 240
Cdd:COG5001  443 YQPQVDLATGRIVGAEALLRwqHPERGlvSPAE-F--IP----LAEETGlivplGEWVlreACRQLAAWqdaGLPDLRVA 515

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731284 241 LNLRPMTLVNiPNAVDFLLTAIEANGFVPEQIVVEFTESEAISRFDEFTDSVRQLKSAGISVTIDHFGAGFAGLQLLAQF 320
Cdd:COG5001  516 VNLSARQLRD-PDLVDRVRRALAETGLPPSRLELEITESALLEDPEEALETLRALRALGVRIALDDFGTGYSSLSYLKRL 594

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695731284 321 QPDRIKINRDLVANVHKSGPRQAIIQAIIKCCSSLEIQFCAVGVEKAEEWMWLESAGISQFQGHLFASP 389
Cdd:COG5001  595 PVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGCDYAQGYLFSRP 663
BLUF pfam04940
Sensors of blue-light using FAD; The BLUF domain has been shown to bind FAD in the AppA ...
 5-92 1.09e-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: 115.68  E-value: 1.09e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731284    5 IIYRSHICEDVPVKALEAMVAAANSKNRQSNVTGILLFNGTHFFQLLEGPVEHVSAIYEQICNDPRHHNVVELMRDHGPV 84
Cdd:pfam04940   1 LIYVSRAAADLSEEDLADILEQSRRNNARLGITGVLLYDGGRFLQVLEGPEEAVDALYERIKRDPRHTDVTVLEEGPIEE 80


                  ....*...
gi 695731284   85 RRFGNVGM 92
Cdd:pfam04940  81 RRFPDWSM 88
YjcC COG4943
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ...
 176-389 4.42e-22

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: 98.06  E-value: 4.42e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731284 176 FQPIVDPFMQQVVSWEALLR--TPDGGA-PGDYFANLPRDEVYASDLhSKQV---ALS-MASALGLQ-DQTLSLNLRPMT 247
Cdd:COG4943  289 YQPIVDLKTGRCVGAEALVRwrDPDGSViSPDIFIPLAEQSGLISPL-TRQVieqVFRdLGDLLAADpDFHISINLSASD 367

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731284 248 LVNiPNAVDFLLTAIEANGFVPEQIVVEFTESEAISrFDEFTDSVRQLKSAGISVTIDHFGAGFAGLQLLAQFQPDRIKI 327
Cdd:COG4943  368 LLS-PRFLDDLERLLARTGVAPQQIVLEITERGFID-PAKARAVIAALREAGHRIAIDDFGTGYSSLSYLQTLPVDILKI 445

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695731284 328 NRDLVANVHKSGPRQAIIQAIIKCCSSLEIQFCAVGVEKAEEWMWLESAGISQFQGHLFASP 389
Cdd:COG4943  446 DKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQGWLFAKP 507
PRK13561 PRK13561
putative diguanylate cyclase; Provisional
 154-389 1.14e-21

putative diguanylate cyclase; Provisional


Pssm-ID: 184143 [Multi-domain]  Cd Length: 651  Bit Score: 97.09  E-value: 1.14e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731284 154 REETRLSAQPEVVAKGADCSFA--FQPIVDPFMQQVVSWEALLR--TPDG--GAPGDYFANLPRDEVYAS------DLHS 221
Cdd:PRK13561 394 AAQKRLTEESDILNALENHQFAiwLQPQVEMRSGKLVSAEALLRmqQPDGswDLPEGLIDRIESCGLMVTvghwvlEESC 473

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731284 222 KQVALSMASALGLqdqTLSLNLRPMTLVNiPNAVDFLLTAIEANGFVPEQIVVEFTESEAISRFDEFTDSVRQLKSAGIS 301
Cdd:PRK13561 474 RLLAAWQERGIML---PLSVNLSALQLMH-PNMVADMLELLTRYRIQPGTLILEVTESRRIDDPHAAVAILRPLRNAGVR 549

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731284 302 VTIDHFGAGFAGLQLLAQFQP---DRIKINRDLVANVHKSgprQAIIQAIIKCCSSLEIQFCAVGVEKAEEWMWLESAGI 378
Cdd:PRK13561 550 VALDDFGMGYAGLRQLQHMKSlpiDVLKIDKMFVDGLPED---DSMVAAIIMLAQSLNLQVIAEGVETEAQRDWLLKAGV 626

                        250
                 ....*....|.
gi 695731284 379 SQFQGHLFASP 389
Cdd:PRK13561 627 GIAQGFLFARA 637
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
176-398 2.01e-19

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 90.51  E-value: 2.01e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731284 176 FQPIVDpFMQQVVSWEALLR--TPDGG--APGDY--FAN-----------LPRDEV-YASDLHSKQVALSMA---SALGL 234
Cdd:PRK10060 426 YQPKIT-WRGEVRSLEALVRwqSPERGliPPLEFisYAEesglivplgrwVMLDVVrQVAKWRDKGINLRVAvnvSARQL 504

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731284 235 QDQTLslnlrpmtlvnipnaVDFLLTAIEANGFVPEQIVVEFTESEAISRFDEFTDSVRQLKSAGISVTIDHFGAGFAGL 314
Cdd:PRK10060 505 ADQTI---------------FTALKQALQELNFEYCPIDVELTESCLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSL 569

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731284 315 QLLAQFQPDRIKINRDLVANVHKSGPRQAIIQAIIKCCSSLEIQFCAVGVEKAEEWMWLESAGISQFQGHLFASPrhggI 394
Cdd:PRK10060 570 SQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKP----M 645


                 ....
gi 695731284 395 PAIA 398
Cdd:PRK10060 646 PAVA 649
PRK11829 PRK11829
biofilm formation regulator HmsP; Provisional
 154-389 7.20e-18

biofilm formation regulator HmsP; Provisional


Pssm-ID: 183329 [Multi-domain]  Cd Length: 660  Bit Score: 85.76  E-value: 7.20e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731284 154 REETRLSAQPEVVA--KGADCSFAFQPIVDPFMQQVVSWEALLR--TPDGGApgdyfaNLPRDEVYASDLHSKQVALS-- 227
Cdd:PRK11829 399 KTHKRLTQENDLLQaiENHDFTLFLQPQWDMKRQQVIGAEALLRwcQPDGSY------VLPSGFVHFAEEEGMMVPLGnw 472

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731284 228 ------------MASALGLqdqTLSLNLRPMTLVNiPNAVDFLLTAIEANGFVPEQIVVEFTESEAISRFDEFTDSVRQL 295
Cdd:PRK11829 473 vleeacriladwKARGVSL---PLSVNISGLQVQN-KQFLPHLKTLISHYHIDPQQLLLEITETAQIQDLDEALRLLREL 548

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731284 296 KSAGISVTIDHFGAGFAGLQLLAQFQP---DRIKINRDLVANVhksgPRQAIIQAIIKCCSS-LEIQFCAVGVEKAEEWM 371
Cdd:PRK11829 549 QGLGLLIALDDFGIGYSSLRYLNHLKSlpiHMIKLDKSFVKNL----PEDDAIARIISCVSDvLKVRVMAEGVETEEQRQ 624

                        250
                 ....*....|....*...
gi 695731284 372 WLESAGISQFQGHLFASP 389
Cdd:PRK11829 625 WLLEHGIQCGQGFLFSPP 642
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 176-389 1.08e-16

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 82.12  E-value: 1.08e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731284 176 FQPIVDPFMQQVVSWEALLRTPD---GGAPGDYFANLPRD--EVYASDLHSKQVA---LSMASALGLQDQTLSLNLRPMT 247
Cdd:PRK11359 561 YQPQIFAETGELYGIEALARWHDplhGHVPPSRFIPLAEEigEIENIGRWVIAEAcrqLAEWRSQNIHIPALSVNLSALH 640

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731284 248 LVNiPNAVDFLLTAIEANGFVPEQIVVEFTESEAISRFDEFTDSVRQLKSAGISVTIDHFGAGFAGLQLLAQFQPDRIKI 327
Cdd:PRK11359 641 FRS-NQLPNQVSDAMQAWGIDGHQLTVEITESMMMEHDTEIFKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKI 719

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695731284 328 NRDLVANVHKSGPRQAIIQAIIKCCSSLEIQFCAVGVEKAEEWMWLESAGISQFQGHLFASP 389
Cdd:PRK11359 720 DKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRP 781
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 190-389 3.44e-13

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 71.63  E-value: 3.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731284  190 WEALLR--TPDGG--APGDYFANLPRDEVyasdLHS------KQVALSMASALGLQDQTLSLNLRPMTLVNiPNAVDFLL 259
Cdd:PRK09776  873 WLISLRlwDPEGEiiDEGAFRPAAEDPAL----MHAldrrviHEFFRQAAKAVASKGLSIALPLSVAGLSS-PTLLPFLL 947

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731284  260 TAIEANGFVPEQIVVEFTESEAISRFDEFTDSVRQLKSAGISVTIDHFGAGFAGLQLLAQFQPDRIKINRDLVANVHKSG 339
Cdd:PRK09776  948 EQLENSPLPPRLLHLEITETALLNHAESASRLVQKLRLAGCRVVLSDFGRGLSSFNYLKAFMADYLKLDGELVANLHGNL 1027

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 695731284  340 PRQAIIQAIIKCCSSLEIQFCAVGVEKAEEWMWLESAGISQFQGHLFASP 389
Cdd:PRK09776 1028 MDEMLISIIQGHAQRLGMKTIAGPVELPLVLDTLSGIGVDLAYGYAIARP 1077
PRK10551 PRK10551
cyclic di-GMP phosphodiesterase;
176-390 7.73e-13

cyclic di-GMP phosphodiesterase;


Pssm-ID: 182541 [Multi-domain]  Cd Length: 518  Bit Score: 70.02  E-value: 7.73e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731284 176 FQPIVDPFMQQVVSWEALLR--TPDGGA-PGDYFAN----------LPRD--EVYASDLHSKQVALSMASALGLqdqtls 240
Cdd:PRK10551 281 YQPVVDTQTLRVTGLEALLRwrHPTAGEiPPDAFINyaeaqklivpLTQHlfELIARDAAELQKVLPVGAKLGI------ 354

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731284 241 lNLRPMTLVN--IPNAVDFLLTAIEANGFvpeQIVVEFTE------SEAISRFDeftdsvrQLKSAGISVTIDHFGAGFA 312
Cdd:PRK10551 355 -NISPAHLHSdsFKADVQRLLASLPADHF---QIVLEITErdmvqeEEATKLFA-------WLHSQGIEIAIDDFGTGHS 423

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695731284 313 GLQLLAQFQPDRIKINRDLVANVHKSGPRQAIIQAIIKCCSSLEIQFCAVGVEKAEEWMWLESAGISQFQGHLFASPR 390
Cdd:PRK10551 424 ALIYLERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNFLQGYWISRPL 501
PRK11059 PRK11059
regulatory protein CsrD; Provisional
 270-389 2.53e-10

regulatory protein CsrD; Provisional


Pssm-ID: 236833 [Multi-domain]  Cd Length: 640  Bit Score: 62.19  E-value: 2.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731284 270 EQIVVEFTESEAISRFDEFTDSVRQLKSAGISVTIDHfgagfAGLQL-----LAQFQPDRIKINRDLVANVHKSGPRQAI 344
Cdd:PRK11059 517 KRLIFELAEADVCQHISRLRPVLRMLRGLGCRLAVDQ-----AGLTVvstsyIKELNVELIKLHPSLVRNIHKRTENQLF 591

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 695731284 345 IQAIIKCCSSLEIQFCAVGVEKAEEWMWLESAGISQFQGHLFASP 389
Cdd:PRK11059 592 VRSLVGACAGTETQVFATGVESREEWQTLQELGVSGGQGDFFAES 636
 
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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