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Conserved domains on  [gi|490987284|ref|WP_004849017|]
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MULTISPECIES: diguanylate phosphodiesterase [Klebsiella]

Protein Classification

diguanylate phosphodiesterase( domain architecture ID 13930490)

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 super family cl29561
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 174-387 1.75e-54

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.


The actual alignment was detected with superfamily member smart00052:

Pssm-ID: 453023 [Multi-domain]  Cd Length: 242  Bit Score: 180.49  E-value: 1.75e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490987284   174 FQPVIDPFAKEVVSYEALLRTTSGD----SPAVYFD-----GLSREEIYWTDLH-SKRIAFAMAGllHLRGRTLSINLLP 243
Cdd:smart00052  17 YQPIVSLRTGRLVGVEALIRWQHPEggiiSPDEFIPlaeetGLIVPLGRWVLEQaCQQLAEWQAQ--GPPPLLISINLSA 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490987284   244 MTLVNvPNAVEFLLAEIEASGLIPEQIIVEFTESEAISRLDEFTDSVRKLKSAGIRVAIDHFGAGFAGLLLLAQFQPDRI 323
Cdd:smart00052  95 RQLIS-PDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYSSLSYLKRLPVDLL 173

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490987284   324 KINRQLVKDIHKHGPKQAIVQAIIKCCHSLEIAISAVGIEQAEEWMWLESAGITHFQGNLFASP 387
Cdd:smart00052 174 KIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRP 237
BLUF smart01034
Sensors of blue-light using FAD; The BLUF domain has been shown to bind FAD in the AppA ...
 2-93 6.31e-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: 121.53  E-value: 6.31e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490987284     2 LTTIIYRSHICDNVSIKSLESMVAEANVKNSQEDVSGILLFNGTHFFQLLEGPEEKVEEIYRHICADPRHHNLVELLRDH 81
Cdd:smart01034   1 LHRLVYVSRARPDLSPEDLEDILAQARRNNARLGITGVLLYNGGHFLQVLEGPEEAVEALYERIQRDPRHRDVQVLLYEP 80

                           90
                   ....*....|..
gi 490987284    82 GPTRRFGKIGME 93
Cdd:smart01034  81 IPERRFPDWSMG 92
 
Name Accession Description Interval E-value
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
 174-387 1.75e-54

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


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 180.49  E-value: 1.75e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490987284   174 FQPVIDPFAKEVVSYEALLRTTSGD----SPAVYFD-----GLSREEIYWTDLH-SKRIAFAMAGllHLRGRTLSINLLP 243
Cdd:smart00052  17 YQPIVSLRTGRLVGVEALIRWQHPEggiiSPDEFIPlaeetGLIVPLGRWVLEQaCQQLAEWQAQ--GPPPLLISINLSA 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490987284   244 MTLVNvPNAVEFLLAEIEASGLIPEQIIVEFTESEAISRLDEFTDSVRKLKSAGIRVAIDHFGAGFAGLLLLAQFQPDRI 323
Cdd:smart00052  95 RQLIS-PDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYSSLSYLKRLPVDLL 173

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490987284   324 KINRQLVKDIHKHGPKQAIVQAIIKCCHSLEIAISAVGIEQAEEWMWLESAGITHFQGNLFASP 387
Cdd:smart00052 174 KIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRP 237
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 171-387 4.72e-54

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: 179.05  E-value: 4.72e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490987284  171 SFAFQPVIDPFAKEVVSYEALLRTTSGD----SPAVYFDGLsREEIYWTDLHSKRIAFA---MAGLLHLRGRTLSINLLP 243
Cdd:pfam00563  14 VLYYQPIVDLRTGRVVGYEALLRWQHPDggliSPARFLPLA-EELGLIAELDRWVLEQAladLAQLQLGPDIKLSINLSP 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490987284  244 MTLVNvPNAVEFLLAEIEASGLIPEQIIVEFTESEAISRLDEFTDSVRKLKSAGIRVAIDHFGAGFAGLLLLAQFQPDRI 323
Cdd:pfam00563  93 ASLAD-PGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSLSYLLRLPPDFV 171

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490987284  324 KINRQLVKDIHKHGPKQAIVQAIIKCCHSLEIAISAVGIEQAEEWMWLESAGITHFQGNLFASP 387
Cdd:pfam00563 172 KIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 165-387 2.90e-53

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: 177.35  E-value: 2.90e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490987284 165 LQEAECSFAFQPVIDPFAKEVVSYEALLRTTSGD----SPAVyFDGLSREeiywTDLHSK------RIAFAMAGLLHLRG 234
Cdd:cd01948    7 LERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEggliSPAE-FIPLAEE----TGLIVElgrwvlEEACRQLARWQAGG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490987284 235 R--TLSINLLPMTLVNvPNAVEFLLAEIEASGLIPEQIIVEFTESEAISRLDEFTDSVRKLKSAGIRVAIDHFGAGFAGL 312
Cdd:cd01948   82 PdlRLSVNLSARQLRD-PDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSL 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490987284 313 LLLAQFQPDRIKINRQLVKDIHKHGPKQAIVQAIIKCCHSLEIAISAVGIEQAEEWMWLESAGITHFQGNLFASP 387
Cdd:cd01948  161 SYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRP 235
EAL COG2200
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
 165-387 7.02e-49

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: 174.59  E-value: 7.02e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490987284 165 LQEAECSFAFQPVIDPFAKEVVSYEALLRTTSGD----SPAVYFDGLSREEIYWT-DLHSKRIAFAMAGLLHLRGR--TL 237
Cdd:COG2200  337 LEEGELRLYYQPIVDLRTGRVVGYEALLRWRHPDggliSPAEFIPAAERSGLIVElDRWVLERALRQLARWPERGLdlRL 416

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490987284 238 SINLLPMTLVNvPNAVEFLLAEIEASGLIPEQIIVEFTESEAISRLDEFTDSVRKLKSAGIRVAIDHFGAGFAGLLLLAQ 317
Cdd:COG2200  417 SVNLSARSLLD-PDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRIALDDFGTGYSSLSYLKR 495

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490987284 318 FQPDRIKINRQLVKDIHKHGPKQAIVQAIIKCCHSLEIAISAVGIEQAEEWMWLESAGITHFQGNLFASP 387
Cdd:COG2200  496 LPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRP 565
BLUF smart01034
Sensors of blue-light using FAD; The BLUF domain has been shown to bind FAD in the AppA ...
 2-93 6.31e-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: 121.53  E-value: 6.31e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490987284     2 LTTIIYRSHICDNVSIKSLESMVAEANVKNSQEDVSGILLFNGTHFFQLLEGPEEKVEEIYRHICADPRHHNLVELLRDH 81
Cdd:smart01034   1 LHRLVYVSRARPDLSPEDLEDILAQARRNNARLGITGVLLYNGGHFLQVLEGPEEAVEALYERIQRDPRHRDVQVLLYEP 80

                           90
                   ....*....|..
gi 490987284    82 GPTRRFGKIGME 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 2.94e-30

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: 111.83  E-value: 2.94e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490987284    5 IIYRSHICDNVSIKSLESMVAEANVKNSQEDVSGILLFNGTHFFQLLEGPEEKVEEIYRHICADPRHHNLVELLRDHGPT 84
Cdd:pfam04940   1 LIYVSRAAADLSEEDLADILEQSRRNNARLGITGVLLYDGGRFLQVLEGPEEAVDALYERIKRDPRHTDVTVLEEGPIEE 80


                  ....*...
gi 490987284   85 RRFGKIGM 92
Cdd:pfam04940  81 RRFPDWSM 88
PRK13561 PRK13561
putative diguanylate cyclase; Provisional
 175-387 8.10e-23

putative diguanylate cyclase; Provisional


Pssm-ID: 184143 [Multi-domain]  Cd Length: 651  Bit Score: 100.56  E-value: 8.10e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490987284 175 QPVIDPFAKEVVSYEALLRTTSGDSPAVYFDGL--SREEI-------YWTDLHSKRIafamagLLHLRGR----TLSINL 241
Cdd:PRK13561 419 QPQVEMRSGKLVSAEALLRMQQPDGSWDLPEGLidRIESCglmvtvgHWVLEESCRL------LAAWQERgimlPLSVNL 492

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490987284 242 LPMTLVNvPNAVEFLLAEIEASGLIPEQIIVEFTESEAISRLDEFTDSVRKLKSAGIRVAIDHFGAGFAGLLLLAQFQP- 320
Cdd:PRK13561 493 SALQLMH-PNMVADMLELLTRYRIQPGTLILEVTESRRIDDPHAAVAILRPLRNAGVRVALDDFGMGYAGLRQLQHMKSl 571

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490987284 321 --DRIKINRQLVKDIhkhgPKQ-AIVQAIIKCCHSLEIAISAVGIEQAEEWMWLESAGITHFQGNLFASP 387
Cdd:PRK13561 572 piDVLKIDKMFVDGL----PEDdSMVAAIIMLAQSLNLQVIAEGVETEAQRDWLLKAGVGIAQGFLFARA 637
 
Name Accession Description Interval E-value
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
 174-387 1.75e-54

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


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 180.49  E-value: 1.75e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490987284   174 FQPVIDPFAKEVVSYEALLRTTSGD----SPAVYFD-----GLSREEIYWTDLH-SKRIAFAMAGllHLRGRTLSINLLP 243
Cdd:smart00052  17 YQPIVSLRTGRLVGVEALIRWQHPEggiiSPDEFIPlaeetGLIVPLGRWVLEQaCQQLAEWQAQ--GPPPLLISINLSA 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490987284   244 MTLVNvPNAVEFLLAEIEASGLIPEQIIVEFTESEAISRLDEFTDSVRKLKSAGIRVAIDHFGAGFAGLLLLAQFQPDRI 323
Cdd:smart00052  95 RQLIS-PDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYSSLSYLKRLPVDLL 173

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490987284   324 KINRQLVKDIHKHGPKQAIVQAIIKCCHSLEIAISAVGIEQAEEWMWLESAGITHFQGNLFASP 387
Cdd:smart00052 174 KIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRP 237
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 171-387 4.72e-54

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: 179.05  E-value: 4.72e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490987284  171 SFAFQPVIDPFAKEVVSYEALLRTTSGD----SPAVYFDGLsREEIYWTDLHSKRIAFA---MAGLLHLRGRTLSINLLP 243
Cdd:pfam00563  14 VLYYQPIVDLRTGRVVGYEALLRWQHPDggliSPARFLPLA-EELGLIAELDRWVLEQAladLAQLQLGPDIKLSINLSP 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490987284  244 MTLVNvPNAVEFLLAEIEASGLIPEQIIVEFTESEAISRLDEFTDSVRKLKSAGIRVAIDHFGAGFAGLLLLAQFQPDRI 323
Cdd:pfam00563  93 ASLAD-PGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSLSYLLRLPPDFV 171

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490987284  324 KINRQLVKDIHKHGPKQAIVQAIIKCCHSLEIAISAVGIEQAEEWMWLESAGITHFQGNLFASP 387
Cdd:pfam00563 172 KIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 165-387 2.90e-53

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: 177.35  E-value: 2.90e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490987284 165 LQEAECSFAFQPVIDPFAKEVVSYEALLRTTSGD----SPAVyFDGLSREeiywTDLHSK------RIAFAMAGLLHLRG 234
Cdd:cd01948    7 LERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEggliSPAE-FIPLAEE----TGLIVElgrwvlEEACRQLARWQAGG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490987284 235 R--TLSINLLPMTLVNvPNAVEFLLAEIEASGLIPEQIIVEFTESEAISRLDEFTDSVRKLKSAGIRVAIDHFGAGFAGL 312
Cdd:cd01948   82 PdlRLSVNLSARQLRD-PDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSL 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490987284 313 LLLAQFQPDRIKINRQLVKDIHKHGPKQAIVQAIIKCCHSLEIAISAVGIEQAEEWMWLESAGITHFQGNLFASP 387
Cdd:cd01948  161 SYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRP 235
EAL COG2200
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
 165-387 7.02e-49

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: 174.59  E-value: 7.02e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490987284 165 LQEAECSFAFQPVIDPFAKEVVSYEALLRTTSGD----SPAVYFDGLSREEIYWT-DLHSKRIAFAMAGLLHLRGR--TL 237
Cdd:COG2200  337 LEEGELRLYYQPIVDLRTGRVVGYEALLRWRHPDggliSPAEFIPAAERSGLIVElDRWVLERALRQLARWPERGLdlRL 416

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490987284 238 SINLLPMTLVNvPNAVEFLLAEIEASGLIPEQIIVEFTESEAISRLDEFTDSVRKLKSAGIRVAIDHFGAGFAGLLLLAQ 317
Cdd:COG2200  417 SVNLSARSLLD-PDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRIALDDFGTGYSSLSYLKR 495

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490987284 318 FQPDRIKINRQLVKDIHKHGPKQAIVQAIIKCCHSLEIAISAVGIEQAEEWMWLESAGITHFQGNLFASP 387
Cdd:COG2200  496 LPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRP 565
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 174-387 8.08e-35

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: 136.06  E-value: 8.08e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490987284 174 FQPVIDPFAKEVVSYEALLRTTSGD----SPAVYFD-----GLSREEIYWTdLhskRIAFAMAGLLHLRGR---TLSINL 241
Cdd:COG5001  443 YQPQVDLATGRIVGAEALLRWQHPErglvSPAEFIPlaeetGLIVPLGEWV-L---REACRQLAAWQDAGLpdlRVAVNL 518

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490987284 242 LPMTLVNvPNAVEFLLAEIEASGLIPEQIIVEFTESEAISRLDEFTDSVRKLKSAGIRVAIDHFGAGFAGLLLLAQFQPD 321
Cdd:COG5001  519 SARQLRD-PDLVDRVRRALAETGLPPSRLELEITESALLEDPEEALETLRALRALGVRIALDDFGTGYSSLSYLKRLPVD 597

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490987284 322 RIKINRQLVKDIHKHGPKQAIVQAIIKCCHSLEIAISAVGIEQAEEWMWLESAGITHFQGNLFASP 387
Cdd:COG5001  598 TLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGCDYAQGYLFSRP 663
BLUF smart01034
Sensors of blue-light using FAD; The BLUF domain has been shown to bind FAD in the AppA ...
 2-93 6.31e-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: 121.53  E-value: 6.31e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490987284     2 LTTIIYRSHICDNVSIKSLESMVAEANVKNSQEDVSGILLFNGTHFFQLLEGPEEKVEEIYRHICADPRHHNLVELLRDH 81
Cdd:smart01034   1 LHRLVYVSRARPDLSPEDLEDILAQARRNNARLGITGVLLYNGGHFLQVLEGPEEAVEALYERIQRDPRHRDVQVLLYEP 80

                           90
                   ....*....|..
gi 490987284    82 GPTRRFGKIGME 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 2.94e-30

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: 111.83  E-value: 2.94e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490987284    5 IIYRSHICDNVSIKSLESMVAEANVKNSQEDVSGILLFNGTHFFQLLEGPEEKVEEIYRHICADPRHHNLVELLRDHGPT 84
Cdd:pfam04940   1 LIYVSRAAADLSEEDLADILEQSRRNNARLGITGVLLYDGGRFLQVLEGPEEAVDALYERIKRDPRHTDVTVLEEGPIEE 80


                  ....*...
gi 490987284   85 RRFGKIGM 92
Cdd:pfam04940  81 RRFPDWSM 88
YjcC COG4943
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ...
 149-387 3.63e-24

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: 104.23  E-value: 3.63e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490987284 149 SWEFVIEDAacypetpLQEAECSFAFQPVIDPFAKEVVSYEALLR--TTSGD--SPAVyFDGLSREE-IYW--TDLHSKR 221
Cdd:COG4943  271 SPRRRLRRA-------IKRREFYVHYQPIVDLKTGRCVGAEALVRwrDPDGSviSPDI-FIPLAEQSgLISplTRQVIEQ 342

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490987284 222 IAFAMAGLLHL-RGRTLSINLLPMTLVNvPNAVEFLLAEIEASGLIPEQIIVEFTESEAISrLDEFTDSVRKLKSAGIRV 300
Cdd:COG4943  343 VFRDLGDLLAAdPDFHISINLSASDLLS-PRFLDDLERLLARTGVAPQQIVLEITERGFID-PAKARAVIAALREAGHRI 420

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490987284 301 AIDHFGAGFAGLLLLAQFQPDRIKINRQLVKDIHKHGPKQAIVQAIIKCCHSLEIAISAVGIEQAEEWMWLESAGITHFQ 380
Cdd:COG4943  421 AIDDFGTGYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQ 500


                 ....*..
gi 490987284 381 GNLFASP 387
Cdd:COG4943  501 GWLFAKP 507
PRK13561 PRK13561
putative diguanylate cyclase; Provisional
 175-387 8.10e-23

putative diguanylate cyclase; Provisional


Pssm-ID: 184143 [Multi-domain]  Cd Length: 651  Bit Score: 100.56  E-value: 8.10e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490987284 175 QPVIDPFAKEVVSYEALLRTTSGDSPAVYFDGL--SREEI-------YWTDLHSKRIafamagLLHLRGR----TLSINL 241
Cdd:PRK13561 419 QPQVEMRSGKLVSAEALLRMQQPDGSWDLPEGLidRIESCglmvtvgHWVLEESCRL------LAAWQERgimlPLSVNL 492

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490987284 242 LPMTLVNvPNAVEFLLAEIEASGLIPEQIIVEFTESEAISRLDEFTDSVRKLKSAGIRVAIDHFGAGFAGLLLLAQFQP- 320
Cdd:PRK13561 493 SALQLMH-PNMVADMLELLTRYRIQPGTLILEVTESRRIDDPHAAVAILRPLRNAGVRVALDDFGMGYAGLRQLQHMKSl 571

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490987284 321 --DRIKINRQLVKDIhkhgPKQ-AIVQAIIKCCHSLEIAISAVGIEQAEEWMWLESAGITHFQGNLFASP 387
Cdd:PRK13561 572 piDVLKIDKMFVDGL----PEDdSMVAAIIMLAQSLNLQVIAEGVETEAQRDWLLKAGVGIAQGFLFARA 637
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 174-387 1.45e-17

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 84.82  E-value: 1.45e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490987284 174 FQPVIDPFAKEVVSYEALLR---TTSGDSPAVYFDGLSRE--EI----YWTDLHSKRiAFAMAGLLHLRGRTLSINLLPM 244
Cdd:PRK11359 561 YQPQIFAETGELYGIEALARwhdPLHGHVPPSRFIPLAEEigEIenigRWVIAEACR-QLAEWRSQNIHIPALSVNLSAL 639

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490987284 245 TL--VNVPNAVEFLLAEIEASGlipEQIIVEFTESEAISRLDEFTDSVRKLKSAGIRVAIDHFGAGFAGLLLLAQFQPDR 322
Cdd:PRK11359 640 HFrsNQLPNQVSDAMQAWGIDG---HQLTVEITESMMMEHDTEIFKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTE 716

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490987284 323 IKINRQLVKDIHKHGPKQAIVQAIIKCCHSLEIAISAVGIEQAEEWMWLESAGITHFQGNLFASP 387
Cdd:PRK11359 717 IKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRP 781
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
174-387 1.55e-17

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 84.73  E-value: 1.55e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490987284 174 FQPVIDpFAKEVVSYEALLRTTS---GDSPAVYF------DGLSREEIYWTDLHS-KRIAFAMAGLLHLRgrtLSINLLP 243
Cdd:PRK10060 426 YQPKIT-WRGEVRSLEALVRWQSperGLIPPLEFisyaeeSGLIVPLGRWVMLDVvRQVAKWRDKGINLR---VAVNVSA 501

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490987284 244 MTLVNVpNAVEFLLAEIEASGLIPEQIIVEFTESEAISRLDEFTDSVRKLKSAGIRVAIDHFGAGFAGLLLLAQFQPDRI 323
Cdd:PRK10060 502 RQLADQ-TIFTALKQALQELNFEYCPIDVELTESCLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAI 580

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490987284 324 KINRQLVKDIHKHGPKQAIVQAIIKCCHSLEIAISAVGIEQAEEWMWLESAGITHFQGNLFASP 387
Cdd:PRK10060 581 KLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKP 644
PRK11829 PRK11829
biofilm formation regulator HmsP; Provisional
 165-387 4.51e-17

biofilm formation regulator HmsP; Provisional


Pssm-ID: 183329 [Multi-domain]  Cd Length: 660  Bit Score: 83.07  E-value: 4.51e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490987284 165 LQEAECSFAFQPVIDPFAKEVVSYEALLRTTSGDSPAVY---FDGLSREEIYWTDLHSKRIAFAMAGLLHLRGRTLSINL 241
Cdd:PRK11829 414 IENHDFTLFLQPQWDMKRQQVIGAEALLRWCQPDGSYVLpsgFVHFAEEEGMMVPLGNWVLEEACRILADWKARGVSLPL 493

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490987284 242 -LPMTLVNVPNA--VEFLLAEIEASGLIPEQIIVEFTESEAISRLDEFTDSVRKLKSAGIRVAIDHFGAGFAGLLLLAQF 318
Cdd:PRK11829 494 sVNISGLQVQNKqfLPHLKTLISHYHIDPQQLLLEITETAQIQDLDEALRLLRELQGLGLLIALDDFGIGYSSLRYLNHL 573

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490987284 319 QP---DRIKINRQLVKDIHKHGpkqAIVQAIIKCCHSLEIAISAVGIEQAEEWMWLESAGITHFQGNLFASP 387
Cdd:PRK11829 574 KSlpiHMIKLDKSFVKNLPEDD---AIARIISCVSDVLKVRVMAEGVETEEQRQWLLEHGIQCGQGFLFSPP 642
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 230-387 1.59e-15

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 78.56  E-value: 1.59e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490987284  230 LHLRGRTLSINLLPMTLVNvPNAVEFLLAEIEASGLIPEQIIVEFTESEAISRLDEFTDSVRKLKSAGIRVAIDHFGAGF 309
Cdd:PRK09776  921 VASKGLSIALPLSVAGLSS-PTLLPFLLEQLENSPLPPRLLHLEITETALLNHAESASRLVQKLRLAGCRVVLSDFGRGL 999

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490987284  310 AGLLLLAQFQPDRIKINRQLVKDIHKHGPKQAIVQAIIKCCHSLEIAISAVGIEQAEEWMWLESAGITHFQGNLFASP 387
Cdd:PRK09776 1000 SSFNYLKAFMADYLKLDGELVANLHGNLMDEMLISIIQGHAQRLGMKTIAGPVELPLVLDTLSGIGVDLAYGYAIARP 1077
PRK11059 PRK11059
regulatory protein CsrD; Provisional
 268-387 5.13e-11

regulatory protein CsrD; Provisional


Pssm-ID: 236833 [Multi-domain]  Cd Length: 640  Bit Score: 64.50  E-value: 5.13e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490987284 268 EQIIVEFTESEAISRLDEFTDSVRKLKSAGIRVAIDHfgagfAGLLL-----LAQFQPDRIKINRQLVKDIHKHGPKQAI 342
Cdd:PRK11059 517 KRLIFELAEADVCQHISRLRPVLRMLRGLGCRLAVDQ-----AGLTVvstsyIKELNVELIKLHPSLVRNIHKRTENQLF 591

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 490987284 343 VQAIIKCCHSLEIAISAVGIEQAEEWMWLESAGITHFQGNLFASP 387
Cdd:PRK11059 592 VRSLVGACAGTETQVFATGVESREEWQTLQELGVSGGQGDFFAES 636
PRK10551 PRK10551
cyclic di-GMP phosphodiesterase;
174-387 1.21e-10

cyclic di-GMP phosphodiesterase;


Pssm-ID: 182541 [Multi-domain]  Cd Length: 518  Bit Score: 63.09  E-value: 1.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490987284 174 FQPVIDPFAKEVVSYEALLR---TTSGDSPAVYFdglsreeiywtdlhskrIAFAMAGLL------HL------------ 232
Cdd:PRK10551 281 YQPVVDTQTLRVTGLEALLRwrhPTAGEIPPDAF-----------------INYAEAQKLivpltqHLfeliardaaelq 343

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490987284 233 ----RGRTLSINLLPMTLVN--VPNAVEFLLAEIEASGLipeQIIVEFTESEAISRlDEFTDSVRKLKSAGIRVAIDHFG 306
Cdd:PRK10551 344 kvlpVGAKLGINISPAHLHSdsFKADVQRLLASLPADHF---QIVLEITERDMVQE-EEATKLFAWLHSQGIEIAIDDFG 419

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490987284 307 AGFAGLLLLAQFQPDRIKINRQLVKDIHKHGPKQAIVQAIIKCCHSLEIAISAVGIEQAEEWMWLESAGITHFQGNLFAS 386
Cdd:PRK10551 420 TGHSALIYLERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNFLQGYWISR 499


                 .
gi 490987284 387 P 387
Cdd:PRK10551 500 P 500
 
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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