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Conserved domains on  [gi|490245417|ref|WP_004143607|]
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MULTISPECIES: diguanylate phosphodiesterase [Klebsiella]

Protein Classification

diguanylate phosphodiesterase( domain architecture ID 10660065)

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 cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 170-386 9.20e-61

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: 196.61  E-value: 9.20e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245417 170 QFALQAIVEPAKKRVSSFEALIR--SPTGG--SPVEmFAAIAAEDRYRFDLESKAY--AFALAGQLPLGKHQ--LAINLL 241
Cdd:cd01948   13 ELYYQPIVDLRTGRIVGYEALLRwrHPEGGliSPAE-FIPLAEETGLIVELGRWVLeeACRQLARWQAGGPDlrLSVNLS 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245417 242 PGSLYHhPDAVGWLMDSLLAAGLRPDQVLIEVTETEVITCFDQFRKVLKALRVAGMKLAIDDFGAGYSGLSLLTRFQPDK 321
Cdd:cd01948   92 ARQLRD-PDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSLSYLKRLPVDY 170

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490245417 322 IKVDAELVRDIHISGTKQAIVASVVRCCEDLGITVVAEGVETLEEWCWLQSVGIRLFQGFLFSRP 386
Cdd:cd01948  171 LKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRP 235
BLUF smart01034
Sensors of blue-light using FAD; The BLUF domain has been shown to bind FAD in the AppA ...
 2-93 6.91e-35

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: 124.22  E-value: 6.91e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245417     2 LTTLIYRSQVHPDRPPVDLDALVHRASSKNLPLGITGILLFNGLQFFQVLEGTEEALESLFSEIQSDPRHRDVVELMRDY 81
Cdd:smart01034   1 LHRLVYVSRARPDLSPEDLEDILAQARRNNARLGITGVLLYNGGHFLQVLEGPEEAVEALYERIQRDPRHRDVQVLLYEP 80

                           90
                   ....*....|..
gi 490245417    82 SAYRRFHGTGMR 93
Cdd:smart01034  81 IPERRFPDWSMG 92
 
Name Accession Description Interval E-value
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 170-386 9.20e-61

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: 196.61  E-value: 9.20e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245417 170 QFALQAIVEPAKKRVSSFEALIR--SPTGG--SPVEmFAAIAAEDRYRFDLESKAY--AFALAGQLPLGKHQ--LAINLL 241
Cdd:cd01948   13 ELYYQPIVDLRTGRIVGYEALLRwrHPEGGliSPAE-FIPLAEETGLIVELGRWVLeeACRQLARWQAGGPDlrLSVNLS 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245417 242 PGSLYHhPDAVGWLMDSLLAAGLRPDQVLIEVTETEVITCFDQFRKVLKALRVAGMKLAIDDFGAGYSGLSLLTRFQPDK 321
Cdd:cd01948   92 ARQLRD-PDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSLSYLKRLPVDY 170

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490245417 322 IKVDAELVRDIHISGTKQAIVASVVRCCEDLGITVVAEGVETLEEWCWLQSVGIRLFQGFLFSRP 386
Cdd:cd01948  171 LKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRP 235
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
 169-386 7.15e-55

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


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 181.65  E-value: 7.15e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245417   169 CQFAL--QAIVEPAKKRVSSFEALIR--SPTGG--SPVEmFAAIAAE-------DRYRFDLESKAYAFALAgQLPLGKHq 235
Cdd:smart00052  11 GQFLLyyQPIVSLRTGRLVGVEALIRwqHPEGGiiSPDE-FIPLAEEtglivplGRWVLEQACQQLAEWQA-QGPPPLL- 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245417   236 LAINLLPGSLyHHPDAVGWLMDSLLAAGLRPDQVLIEVTETEVITCFDQFRKVLKALRVAGMKLAIDDFGAGYSGLSLLT 315
Cdd:smart00052  88 ISINLSARQL-ISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYSSLSYLK 166

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490245417   316 RFQPDKIKVDAELVRDIHISGTKQAIVASVVRCCEDLGITVVAEGVETLEEWCWLQSVGIRLFQGFLFSRP 386
Cdd:smart00052 167 RLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRP 237
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 171-386 2.47e-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: 179.82  E-value: 2.47e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245417  171 FALQAIVEPAKKRVSSFEALIR--SPTGGS-PVEMFAAIAAEDRYRFDLES----KAYAFaLAGQLPLGKHQLAINLLPG 243
Cdd:pfam00563  15 LYYQPIVDLRTGRVVGYEALLRwqHPDGGLiSPARFLPLAEELGLIAELDRwvleQALAD-LAQLQLGPDIKLSINLSPA 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245417  244 SLyHHPDAVGWLMDSLLAAGLRPDQVLIEVTETEVITCFDQFRKVLKALRVAGMKLAIDDFGAGYSGLSLLTRFQPDKIK 323
Cdd:pfam00563  94 SL-ADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSLSYLLRLPPDFVK 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490245417  324 VDAELVRDIHISGTKQAIVASVVRCCEDLGITVVAEGVETLEEWCWLQSVGIRLFQGFLFSRP 386
Cdd:pfam00563 173 IDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
EAL COG2200
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
 170-386 2.33e-52

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: 183.83  E-value: 2.33e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245417 170 QFALQAIVEPAKKRVSSFEALIR--SPTGG--SPVEmFAAIAAEDRYRFDLE----SKAYAFALAGQLPLGKHQLAINLL 241
Cdd:COG2200  343 RLYYQPIVDLRTGRVVGYEALLRwrHPDGGliSPAE-FIPAAERSGLIVELDrwvlERALRQLARWPERGLDLRLSVNLS 421

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245417 242 PGSLyHHPDAVGWLMDSLLAAGLRPDQVLIEVTETEVITCFDQFRKVLKALRVAGMKLAIDDFGAGYSGLSLLTRFQPDK 321
Cdd:COG2200  422 ARSL-LDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRIALDDFGTGYSSLSYLKRLPPDY 500

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490245417 322 IKVDAELVRDIHISGTKQAIVASVVRCCEDLGITVVAEGVETLEEWCWLQSVGIRLFQGFLFSRP 386
Cdd:COG2200  501 LKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRP 565
BLUF smart01034
Sensors of blue-light using FAD; The BLUF domain has been shown to bind FAD in the AppA ...
 2-93 6.91e-35

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: 124.22  E-value: 6.91e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245417     2 LTTLIYRSQVHPDRPPVDLDALVHRASSKNLPLGITGILLFNGLQFFQVLEGTEEALESLFSEIQSDPRHRDVVELMRDY 81
Cdd:smart01034   1 LHRLVYVSRARPDLSPEDLEDILAQARRNNARLGITGVLLYNGGHFLQVLEGPEEAVEALYERIQRDPRHRDVQVLLYEP 80

                           90
                   ....*....|..
gi 490245417    82 SAYRRFHGTGMR 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 ...
 5-93 3.40e-29

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: 108.75  E-value: 3.40e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245417    5 LIYRSQVHPDRPPVDLDALVHRASSKNLPLGITGILLFNGLQFFQVLEGTEEALESLFSEIQSDPRHRDVVELMRDYSAY 84
Cdd:pfam04940   1 LIYVSRAAADLSEEDLADILEQSRRNNARLGITGVLLYDGGRFLQVLEGPEEAVDALYERIKRDPRHTDVTVLEEGPIEE 80


                  ....*....
gi 490245417   85 RRFHGTGMR 93
Cdd:pfam04940  81 RRFPDWSMG 89
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
183-386 3.61e-25

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 107.85  E-value: 3.61e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245417 183 RVSSFEALIR--SPTGG--SPVEMFaaiaaedryRFDLESkayafALAGqlPLGKH-------------------QLAIN 239
Cdd:PRK10060 435 EVRSLEALVRwqSPERGliPPLEFI---------SYAEES-----GLIV--PLGRWvmldvvrqvakwrdkginlRVAVN 498

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245417 240 -----LLPGSLYHHpdavgwLMDSLLAAGLRPDQVLIEVTETEVITCFDQFRKVLKALRVAGMKLAIDDFGAGYSGLSLL 314
Cdd:PRK10060 499 vsarqLADQTIFTA------LKQALQELNFEYCPIDVELTESCLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQL 572

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490245417 315 TRFQPDKIKVDAELVRDIHISGTKQAIVASVVRCCEDLGITVVAEGVETLEEWCWLQSVGIRLFQGFLFSRP 386
Cdd:PRK10060 573 ARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKP 644
 
Name Accession Description Interval E-value
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 170-386 9.20e-61

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: 196.61  E-value: 9.20e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245417 170 QFALQAIVEPAKKRVSSFEALIR--SPTGG--SPVEmFAAIAAEDRYRFDLESKAY--AFALAGQLPLGKHQ--LAINLL 241
Cdd:cd01948   13 ELYYQPIVDLRTGRIVGYEALLRwrHPEGGliSPAE-FIPLAEETGLIVELGRWVLeeACRQLARWQAGGPDlrLSVNLS 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245417 242 PGSLYHhPDAVGWLMDSLLAAGLRPDQVLIEVTETEVITCFDQFRKVLKALRVAGMKLAIDDFGAGYSGLSLLTRFQPDK 321
Cdd:cd01948   92 ARQLRD-PDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSLSYLKRLPVDY 170

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490245417 322 IKVDAELVRDIHISGTKQAIVASVVRCCEDLGITVVAEGVETLEEWCWLQSVGIRLFQGFLFSRP 386
Cdd:cd01948  171 LKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRP 235
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
 169-386 7.15e-55

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


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 181.65  E-value: 7.15e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245417   169 CQFAL--QAIVEPAKKRVSSFEALIR--SPTGG--SPVEmFAAIAAE-------DRYRFDLESKAYAFALAgQLPLGKHq 235
Cdd:smart00052  11 GQFLLyyQPIVSLRTGRLVGVEALIRwqHPEGGiiSPDE-FIPLAEEtglivplGRWVLEQACQQLAEWQA-QGPPPLL- 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245417   236 LAINLLPGSLyHHPDAVGWLMDSLLAAGLRPDQVLIEVTETEVITCFDQFRKVLKALRVAGMKLAIDDFGAGYSGLSLLT 315
Cdd:smart00052  88 ISINLSARQL-ISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYSSLSYLK 166

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490245417   316 RFQPDKIKVDAELVRDIHISGTKQAIVASVVRCCEDLGITVVAEGVETLEEWCWLQSVGIRLFQGFLFSRP 386
Cdd:smart00052 167 RLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRP 237
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 171-386 2.47e-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: 179.82  E-value: 2.47e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245417  171 FALQAIVEPAKKRVSSFEALIR--SPTGGS-PVEMFAAIAAEDRYRFDLES----KAYAFaLAGQLPLGKHQLAINLLPG 243
Cdd:pfam00563  15 LYYQPIVDLRTGRVVGYEALLRwqHPDGGLiSPARFLPLAEELGLIAELDRwvleQALAD-LAQLQLGPDIKLSINLSPA 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245417  244 SLyHHPDAVGWLMDSLLAAGLRPDQVLIEVTETEVITCFDQFRKVLKALRVAGMKLAIDDFGAGYSGLSLLTRFQPDKIK 323
Cdd:pfam00563  94 SL-ADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSLSYLLRLPPDFVK 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490245417  324 VDAELVRDIHISGTKQAIVASVVRCCEDLGITVVAEGVETLEEWCWLQSVGIRLFQGFLFSRP 386
Cdd:pfam00563 173 IDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
EAL COG2200
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
 170-386 2.33e-52

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: 183.83  E-value: 2.33e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245417 170 QFALQAIVEPAKKRVSSFEALIR--SPTGG--SPVEmFAAIAAEDRYRFDLE----SKAYAFALAGQLPLGKHQLAINLL 241
Cdd:COG2200  343 RLYYQPIVDLRTGRVVGYEALLRwrHPDGGliSPAE-FIPAAERSGLIVELDrwvlERALRQLARWPERGLDLRLSVNLS 421

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245417 242 PGSLyHHPDAVGWLMDSLLAAGLRPDQVLIEVTETEVITCFDQFRKVLKALRVAGMKLAIDDFGAGYSGLSLLTRFQPDK 321
Cdd:COG2200  422 ARSL-LDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRIALDDFGTGYSSLSYLKRLPPDY 500

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490245417 322 IKVDAELVRDIHISGTKQAIVASVVRCCEDLGITVVAEGVETLEEWCWLQSVGIRLFQGFLFSRP 386
Cdd:COG2200  501 LKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRP 565
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 170-386 4.89e-45

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: 165.33  E-value: 4.89e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245417 170 QFAL--QAIVEPAKKRVSSFEALIR--SPTGG--SPVEmFAAIAAE-------DRYRFDlesKAYAFALA----GQLPLg 232
Cdd:COG5001  438 ELELhyQPQVDLATGRIVGAEALLRwqHPERGlvSPAE-FIPLAEEtglivplGEWVLR---EACRQLAAwqdaGLPDL- 512

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245417 233 khQLAINLLPGSLyHHPDAVGWLMDSLLAAGLRPDQVLIEVTETEVITCFDQFRKVLKALRVAGMKLAIDDFGAGYSGLS 312
Cdd:COG5001  513 --RVAVNLSARQL-RDPDLVDRVRRALAETGLPPSRLELEITESALLEDPEEALETLRALRALGVRIALDDFGTGYSSLS 589

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490245417 313 LLTRFQPDKIKVDAELVRDIHISGTKQAIVASVVRCCEDLGITVVAEGVETLEEWCWLQSVGIRLFQGFLFSRP 386
Cdd:COG5001  590 YLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGCDYAQGYLFSRP 663
BLUF smart01034
Sensors of blue-light using FAD; The BLUF domain has been shown to bind FAD in the AppA ...
 2-93 6.91e-35

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: 124.22  E-value: 6.91e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245417     2 LTTLIYRSQVHPDRPPVDLDALVHRASSKNLPLGITGILLFNGLQFFQVLEGTEEALESLFSEIQSDPRHRDVVELMRDY 81
Cdd:smart01034   1 LHRLVYVSRARPDLSPEDLEDILAQARRNNARLGITGVLLYNGGHFLQVLEGPEEAVEALYERIQRDPRHRDVQVLLYEP 80

                           90
                   ....*....|..
gi 490245417    82 SAYRRFHGTGMR 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 ...
 5-93 3.40e-29

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: 108.75  E-value: 3.40e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245417    5 LIYRSQVHPDRPPVDLDALVHRASSKNLPLGITGILLFNGLQFFQVLEGTEEALESLFSEIQSDPRHRDVVELMRDYSAY 84
Cdd:pfam04940   1 LIYVSRAAADLSEEDLADILEQSRRNNARLGITGVLLYDGGRFLQVLEGPEEAVDALYERIKRDPRHTDVTVLEEGPIEE 80


                  ....*....
gi 490245417   85 RRFHGTGMR 93
Cdd:pfam04940  81 RRFPDWSMG 89
YjcC COG4943
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ...
 236-386 9.02e-29

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: 117.71  E-value: 9.02e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245417 236 LAINLLPGSLyHHPDAVGWLMDSLLAAGLRPDQVLIEVTETEVITcFDQFRKVLKALRVAGMKLAIDDFGAGYSGLSLLT 315
Cdd:COG4943  359 ISINLSASDL-LSPRFLDDLERLLARTGVAPQQIVLEITERGFID-PAKARAVIAALREAGHRIAIDDFGTGYSSLSYLQ 436

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490245417 316 RFQPDKIKVDAELVRDIHISGTKQAIVASVVRCCEDLGITVVAEGVETLEEWCWLQSVGIRLFQGFLFSRP 386
Cdd:COG4943  437 TLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQGWLFAKP 507
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
183-386 3.61e-25

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 107.85  E-value: 3.61e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245417 183 RVSSFEALIR--SPTGG--SPVEMFaaiaaedryRFDLESkayafALAGqlPLGKH-------------------QLAIN 239
Cdd:PRK10060 435 EVRSLEALVRwqSPERGliPPLEFI---------SYAEES-----GLIV--PLGRWvmldvvrqvakwrdkginlRVAVN 498

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245417 240 -----LLPGSLYHHpdavgwLMDSLLAAGLRPDQVLIEVTETEVITCFDQFRKVLKALRVAGMKLAIDDFGAGYSGLSLL 314
Cdd:PRK10060 499 vsarqLADQTIFTA------LKQALQELNFEYCPIDVELTESCLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQL 572

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490245417 315 TRFQPDKIKVDAELVRDIHISGTKQAIVASVVRCCEDLGITVVAEGVETLEEWCWLQSVGIRLFQGFLFSRP 386
Cdd:PRK10060 573 ARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKP 644
PRK13561 PRK13561
putative diguanylate cyclase; Provisional
 236-386 4.90e-22

putative diguanylate cyclase; Provisional


Pssm-ID: 184143 [Multi-domain]  Cd Length: 651  Bit Score: 98.25  E-value: 4.90e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245417 236 LAINLLPGSLyHHPDAVGWLMDSLLAAGLRPDQVLIEVTETEVITCFDQFRKVLKALRVAGMKLAIDDFGAGYSGLSLLT 315
Cdd:PRK13561 488 LSVNLSALQL-MHPNMVADMLELLTRYRIQPGTLILEVTESRRIDDPHAAVAILRPLRNAGVRVALDDFGMGYAGLRQLQ 566

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490245417 316 RFQP---DKIKVDAELVRDIHISGTKQAIVASVVRcceDLGITVVAEGVETLEEWCWLQSVGIRLFQGFLFSRP 386
Cdd:PRK13561 567 HMKSlpiDVLKIDKMFVDGLPEDDSMVAAIIMLAQ---SLNLQVIAEGVETEAQRDWLLKAGVGIAQGFLFARA 637
PRK10551 PRK10551
cyclic di-GMP phosphodiesterase;
174-386 6.37e-21

cyclic di-GMP phosphodiesterase;


Pssm-ID: 182541 [Multi-domain]  Cd Length: 518  Bit Score: 94.67  E-value: 6.37e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245417 174 QAIVEPAKKRVSSFEALIR--SPTGGS-PVEMFAAIAAED-------RYRFDLESKAyAFALAGQLPLGKhQLAINLLPG 243
Cdd:PRK10551 282 QPVVDTQTLRVTGLEALLRwrHPTAGEiPPDAFINYAEAQklivpltQHLFELIARD-AAELQKVLPVGA-KLGINISPA 359

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245417 244 slyhHPDAVGWLMD-SLLAAGLRPD--QVLIEVTETEVItcfdQFRKVLKA---LRVAGMKLAIDDFGAGYSGLSLLTRF 317
Cdd:PRK10551 360 ----HLHSDSFKADvQRLLASLPADhfQIVLEITERDMV----QEEEATKLfawLHSQGIEIAIDDFGTGHSALIYLERF 431

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490245417 318 QPDKIKVDAELVRDIHISGTKQAIVASVVRCCEDLGITVVAEGVETLEEWCWLQSVGIRLFQGFLFSRP 386
Cdd:PRK10551 432 TLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNFLQGYWISRP 500
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 236-386 1.17e-19

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 91.27  E-value: 1.17e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245417  236 LAINLLPGSLYHhPDAVGWLMDSLLAAGLRPDQVLIEVTETEVITCFDQFRKVLKALRVAGMKLAIDDFGAGYSGLSLLT 315
Cdd:PRK09776  928 IALPLSVAGLSS-PTLLPFLLEQLENSPLPPRLLHLEITETALLNHAESASRLVQKLRLAGCRVVLSDFGRGLSSFNYLK 1006

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490245417  316 RFQPDKIKVDAELVRDIHISGTKQAIVASVVRCCEDLGITVVAEGVETLEEWCWLQSVGIRLFQGFLFSRP 386
Cdd:PRK09776 1007 AFMADYLKLDGELVANLHGNLMDEMLISIIQGHAQRLGMKTIAGPVELPLVLDTLSGIGVDLAYGYAIARP 1077
PRK11829 PRK11829
biofilm formation regulator HmsP; Provisional
 259-386 5.33e-19

biofilm formation regulator HmsP; Provisional


Pssm-ID: 183329 [Multi-domain]  Cd Length: 660  Bit Score: 89.23  E-value: 5.33e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245417 259 LLAAGLRPDQVLIEVTETEVITCFDQFRKVLKALRVAGMKLAIDDFGAGYSGLSLLTRFQP---DKIKVDAELVRDIHIS 335
Cdd:PRK11829 515 ISHYHIDPQQLLLEITETAQIQDLDEALRLLRELQGLGLLIALDDFGIGYSSLRYLNHLKSlpiHMIKLDKSFVKNLPED 594

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 490245417 336 GTKQAIVASVvrcCEDLGITVVAEGVETLEEWCWLQSVGIRLFQGFLFSRP 386
Cdd:PRK11829 595 DAIARIISCV---SDVLKVRVMAEGVETEEQRQWLLEHGIQCGQGFLFSPP 642
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 236-386 5.76e-19

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 89.06  E-value: 5.76e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245417 236 LAINLLPGSlYHHPDAVGWLMDSLLAAGLRPDQVLIEVTETEVITCFDQFRKVLKALRVAGMKLAIDDFGAGYSGLSLLT 315
Cdd:PRK11359 632 LSVNLSALH-FRSNQLPNQVSDAMQAWGIDGHQLTVEITESMMMEHDTEIFKRIQILRDMGVGLSVDDFGTGFSGLSRLV 710

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490245417 316 RFQPDKIKVDAELVRDIHISGTKQAIVASVVRCCEDLGITVVAEGVETLEEWCWLQSVGIRLFQGFLFSRP 386
Cdd:PRK11359 711 SLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRP 781
YuxH COG3434
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ...
 255-386 4.53e-13

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


Pssm-ID: 442660 [Multi-domain]  Cd Length: 407  Bit Score: 70.22  E-value: 4.53e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245417 255 LMDSLLAAGLRPDQVLIEVTETEVITcfDQFRKVLKALRVAGMKLAIDDFGAGYSGLSLLTRFqpDKIKVDaelvrdihI 334
Cdd:COG3434   72 LLLSDLPELLPPERVVLEILEDVEPD--EELLEALKELKEKGYRIALDDFVLDPEWDPLLPLA--DIIKID--------V 139

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 490245417 335 SGTKQAIVASVVRCCEDLGITVVAEGVETLEEWCWLQSVGIRLFQGFLFSRP 386
Cdd:COG3434  140 LALDLEELAELVARLKRYGIKLLAEKVETREEFELCKELGFDLFQGYFFSKP 191
PRK11059 PRK11059
regulatory protein CsrD; Provisional
 236-386 7.74e-13

regulatory protein CsrD; Provisional


Pssm-ID: 236833 [Multi-domain]  Cd Length: 640  Bit Score: 69.89  E-value: 7.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245417 236 LAINLLPGSLYHhPDAVGWLMDSLL--AAGLRPdQVLIEVTETEVITCFDQFRKVLKALRVAGMKLAIDDFGAGYSGLSL 313
Cdd:PRK11059 486 LSINLSVDSLLS-RAFQRWLRDTLLqcPRSQRK-RLIFELAEADVCQHISRLRPVLRMLRGLGCRLAVDQAGLTVVSTSY 563

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490245417 314 LTRFQPDKIKVDAELVRDIHISGTKQAIVASVVRCCEDLGITVVAEGVETLEEWCWLQSVGIRLFQGFLFSRP 386
Cdd:PRK11059 564 IKELNVELIKLHPSLVRNIHKRTENQLFVRSLVGACAGTETQVFATGVESREEWQTLQELGVSGGQGDFFAES 636
PRK11596 PRK11596
cyclic-di-GMP phosphodiesterase; Provisional
 288-386 5.49e-08

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183222 [Multi-domain]  Cd Length: 255  Bit Score: 53.47  E-value: 5.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245417 288 VLKALRVAGM----KLAIDDFGAGYSGLSLLTRFQPDKIKVDAELVrdIHISGTKQ------AIVASVVRCCEDlgitVV 357
Cdd:PRK11596 140 LPKDSPFASMcefgPLWLDDFGTGMANFSALSEVRYDYIKVARELF--IMLRQSEEgrnlfsQLLHLMNRYCRG----VI 213

                         90       100
                 ....*....|....*....|....*....
gi 490245417 358 AEGVETLEEWCWLQSVGIRLFQGFLFSRP 386
Cdd:PRK11596 214 VEGVETPEEWRDVQRSPAFAAQGYFLSRP 242
 
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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