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Conserved domains on  [gi|764952584|ref|WP_044522842|]
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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 5.44e-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: 197.38  E-value: 5.44e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952584 170 QFALQAIVEPATKRVSSFEALIR--SPTGG--SPVEmFaaIPAEDRYRFDLESKAY----AFSLAGQLPLGKHQ--LAIN 239
Cdd:cd01948   13 ELYYQPIVDLRTGRIVGYEALLRwrHPEGGliSPAE-F--IPLAEETGLIVELGRWvleeACRQLARWQAGGPDlrLSVN 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952584 240 LLPGSLYnHPDAVGWLMNSLLAAGLRPDQVLIEVTETEVITCFDQFRKVLKALRVAGMKLAIDDFGAGYSGLSLLTRFQP 319
Cdd:cd01948   90 LSARQLR-DPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSLSYLKRLPV 168

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 764952584 320 DKIKVDAELVRNIHISGAKQAIVASVVRCCEDLGITVVAEGVETLEEWCWLQSVGIRLFQGFLFSRP 386
Cdd:cd01948  169 DYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRP 235
BLUF smart01034
Sensors of blue-light using FAD; The BLUF domain has been shown to bind FAD in the AppA ...
 2-93 6.63e-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: 6.63e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952584     2 LTTLIYRSQVNPARPPTDLDALIHRASGKNMPLGITGILLFNGLQFFQVLEGSEEDLESLFHEIQSDPRHRDVVELMRDY 81
Cdd:smart01034   1 LHRLVYVSRARPDLSPEDLEDILAQARRNNARLGITGVLLYNGGHFLQVLEGPEEAVEALYERIQRDPRHRDVQVLLYEP 80

                           90
                   ....*....|..
gi 764952584    82 SAYRRFHDTGMR 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 5.44e-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: 197.38  E-value: 5.44e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952584 170 QFALQAIVEPATKRVSSFEALIR--SPTGG--SPVEmFaaIPAEDRYRFDLESKAY----AFSLAGQLPLGKHQ--LAIN 239
Cdd:cd01948   13 ELYYQPIVDLRTGRIVGYEALLRwrHPEGGliSPAE-F--IPLAEETGLIVELGRWvleeACRQLARWQAGGPDlrLSVN 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952584 240 LLPGSLYnHPDAVGWLMNSLLAAGLRPDQVLIEVTETEVITCFDQFRKVLKALRVAGMKLAIDDFGAGYSGLSLLTRFQP 319
Cdd:cd01948   90 LSARQLR-DPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSLSYLKRLPV 168

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 764952584 320 DKIKVDAELVRNIHISGAKQAIVASVVRCCEDLGITVVAEGVETLEEWCWLQSVGIRLFQGFLFSRP 386
Cdd:cd01948  169 DYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRP 235
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
 169-386 2.24e-54

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


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 180.11  E-value: 2.24e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952584   169 CQFAL--QAIVEPATKRVSSFEALIR--SPTGG--SP------VEMFAAIPAEDRYRFDLESKAYAFsLAGQLPLGKHqL 236
Cdd:smart00052  11 GQFLLyyQPIVSLRTGRLVGVEALIRwqHPEGGiiSPdefiplAEETGLIVPLGRWVLEQACQQLAE-WQAQGPPPLL-I 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952584   237 AINLLPGSLYnHPDAVGWLMNSLLAAGLRPDQVLIEVTETEVITCFDQFRKVLKALRVAGMKLAIDDFGAGYSGLSLLTR 316
Cdd:smart00052  89 SINLSARQLI-SPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYSSLSYLKR 167

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952584   317 FQPDKIKVDAELVRNIHISGAKQAIVASVVRCCEDLGITVVAEGVETLEEWCWLQSVGIRLFQGFLFSRP 386
Cdd:smart00052 168 LPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRP 237
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 171-386 1.96e-53

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: 177.51  E-value: 1.96e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952584  171 FALQAIVEPATKRVSSFEALIR--SPTGGS-PVEMFAAIPAEDRYRFDLES----KAYAFsLAGQLPLGKHQLAINLLPG 243
Cdd:pfam00563  15 LYYQPIVDLRTGRVVGYEALLRwqHPDGGLiSPARFLPLAEELGLIAELDRwvleQALAD-LAQLQLGPDIKLSINLSPA 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952584  244 SLYnHPDAVGWLMNSLLAAGLRPDQVLIEVTETEVITCFDQFRKVLKALRVAGMKLAIDDFGAGYSGLSLLTRFQPDKIK 323
Cdd:pfam00563  94 SLA-DPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSLSYLLRLPPDFVK 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 764952584  324 VDAELVRNIHISGAKQAIVASVVRCCEDLGITVVAEGVETLEEWCWLQSVGIRLFQGFLFSRP 386
Cdd:pfam00563 173 IDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
EAL COG2200
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
 170-386 8.50e-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: 182.29  E-value: 8.50e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952584 170 QFALQAIVEPATKRVSSFEALIR--SPTGG--SPVEMFAAIPAEDRY-RFDLESKAYAFSLAGQLPLGKHQ--LAINLLP 242
Cdd:COG2200  343 RLYYQPIVDLRTGRVVGYEALLRwrHPDGGliSPAEFIPAAERSGLIvELDRWVLERALRQLARWPERGLDlrLSVNLSA 422

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952584 243 GSLyNHPDAVGWLMNSLLAAGLRPDQVLIEVTETEVITCFDQFRKVLKALRVAGMKLAIDDFGAGYSGLSLLTRFQPDKI 322
Cdd:COG2200  423 RSL-LDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRIALDDFGTGYSSLSYLKRLPPDYL 501

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 764952584 323 KVDAELVRNIHISGAKQAIVASVVRCCEDLGITVVAEGVETLEEWCWLQSVGIRLFQGFLFSRP 386
Cdd:COG2200  502 KIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRP 565
BLUF smart01034
Sensors of blue-light using FAD; The BLUF domain has been shown to bind FAD in the AppA ...
 2-93 6.63e-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: 6.63e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952584     2 LTTLIYRSQVNPARPPTDLDALIHRASGKNMPLGITGILLFNGLQFFQVLEGSEEDLESLFHEIQSDPRHRDVVELMRDY 81
Cdd:smart01034   1 LHRLVYVSRARPDLSPEDLEDILAQARRNNARLGITGVLLYNGGHFLQVLEGPEEAVEALYERIQRDPRHRDVQVLLYEP 80

                           90
                   ....*....|..
gi 764952584    82 SAYRRFHDTGMR 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 7.53e-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: 107.98  E-value: 7.53e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952584    5 LIYRSQVNPARPPTDLDALIHRASGKNMPLGITGILLFNGLQFFQVLEGSEEDLESLFHEIQSDPRHRDVVELMRDYSAY 84
Cdd:pfam04940   1 LIYVSRAAADLSEEDLADILEQSRRNNARLGITGVLLYDGGRFLQVLEGPEEAVDALYERIKRDPRHTDVTVLEEGPIEE 80


                  ....*....
gi 764952584   85 RRFHDTGMR 93
Cdd:pfam04940  81 RRFPDWSMG 89
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
255-386 7.86e-25

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 106.69  E-value: 7.86e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952584 255 LMNSLLAAGLRPDQVLIEVTETEVITCFDQFRKVLKALRVAGMKLAIDDFGAGYSGLSLLTRFQPDKIKVDAELVRNIHI 334
Cdd:PRK10060 513 LKQALQELNFEYCPIDVELTESCLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHK 592

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 764952584 335 SGAKQAIVASVVRCCEDLGITVVAEGVETLEEWCWLQSVGIRLFQGFLFSRP 386
Cdd:PRK10060 593 QPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKP 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 5.44e-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: 197.38  E-value: 5.44e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952584 170 QFALQAIVEPATKRVSSFEALIR--SPTGG--SPVEmFaaIPAEDRYRFDLESKAY----AFSLAGQLPLGKHQ--LAIN 239
Cdd:cd01948   13 ELYYQPIVDLRTGRIVGYEALLRwrHPEGGliSPAE-F--IPLAEETGLIVELGRWvleeACRQLARWQAGGPDlrLSVN 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952584 240 LLPGSLYnHPDAVGWLMNSLLAAGLRPDQVLIEVTETEVITCFDQFRKVLKALRVAGMKLAIDDFGAGYSGLSLLTRFQP 319
Cdd:cd01948   90 LSARQLR-DPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSLSYLKRLPV 168

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 764952584 320 DKIKVDAELVRNIHISGAKQAIVASVVRCCEDLGITVVAEGVETLEEWCWLQSVGIRLFQGFLFSRP 386
Cdd:cd01948  169 DYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRP 235
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
 169-386 2.24e-54

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


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 180.11  E-value: 2.24e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952584   169 CQFAL--QAIVEPATKRVSSFEALIR--SPTGG--SP------VEMFAAIPAEDRYRFDLESKAYAFsLAGQLPLGKHqL 236
Cdd:smart00052  11 GQFLLyyQPIVSLRTGRLVGVEALIRwqHPEGGiiSPdefiplAEETGLIVPLGRWVLEQACQQLAE-WQAQGPPPLL-I 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952584   237 AINLLPGSLYnHPDAVGWLMNSLLAAGLRPDQVLIEVTETEVITCFDQFRKVLKALRVAGMKLAIDDFGAGYSGLSLLTR 316
Cdd:smart00052  89 SINLSARQLI-SPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYSSLSYLKR 167

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952584   317 FQPDKIKVDAELVRNIHISGAKQAIVASVVRCCEDLGITVVAEGVETLEEWCWLQSVGIRLFQGFLFSRP 386
Cdd:smart00052 168 LPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRP 237
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 171-386 1.96e-53

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: 177.51  E-value: 1.96e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952584  171 FALQAIVEPATKRVSSFEALIR--SPTGGS-PVEMFAAIPAEDRYRFDLES----KAYAFsLAGQLPLGKHQLAINLLPG 243
Cdd:pfam00563  15 LYYQPIVDLRTGRVVGYEALLRwqHPDGGLiSPARFLPLAEELGLIAELDRwvleQALAD-LAQLQLGPDIKLSINLSPA 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952584  244 SLYnHPDAVGWLMNSLLAAGLRPDQVLIEVTETEVITCFDQFRKVLKALRVAGMKLAIDDFGAGYSGLSLLTRFQPDKIK 323
Cdd:pfam00563  94 SLA-DPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSLSYLLRLPPDFVK 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 764952584  324 VDAELVRNIHISGAKQAIVASVVRCCEDLGITVVAEGVETLEEWCWLQSVGIRLFQGFLFSRP 386
Cdd:pfam00563 173 IDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
EAL COG2200
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
 170-386 8.50e-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: 182.29  E-value: 8.50e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952584 170 QFALQAIVEPATKRVSSFEALIR--SPTGG--SPVEMFAAIPAEDRY-RFDLESKAYAFSLAGQLPLGKHQ--LAINLLP 242
Cdd:COG2200  343 RLYYQPIVDLRTGRVVGYEALLRwrHPDGGliSPAEFIPAAERSGLIvELDRWVLERALRQLARWPERGLDlrLSVNLSA 422

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952584 243 GSLyNHPDAVGWLMNSLLAAGLRPDQVLIEVTETEVITCFDQFRKVLKALRVAGMKLAIDDFGAGYSGLSLLTRFQPDKI 322
Cdd:COG2200  423 RSL-LDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRIALDDFGTGYSSLSYLKRLPPDYL 501

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 764952584 323 KVDAELVRNIHISGAKQAIVASVVRCCEDLGITVVAEGVETLEEWCWLQSVGIRLFQGFLFSRP 386
Cdd:COG2200  502 KIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRP 565
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 170-386 6.14e-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: 164.95  E-value: 6.14e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952584 170 QFAL--QAIVEPATKRVSSFEALIR--SPTGG--SPVEmFaaIP-AEDryrfdleskayafslAGQ-LPLGKH------- 234
Cdd:COG5001  438 ELELhyQPQVDLATGRIVGAEALLRwqHPERGlvSPAE-F--IPlAEE---------------TGLiVPLGEWvlreacr 499

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952584 235 -------------QLAINLLPGSLyNHPDAVGWLMNSLLAAGLRPDQVLIEVTETEVITCFDQFRKVLKALRVAGMKLAI 301
Cdd:COG5001  500 qlaawqdaglpdlRVAVNLSARQL-RDPDLVDRVRRALAETGLPPSRLELEITESALLEDPEEALETLRALRALGVRIAL 578

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952584 302 DDFGAGYSGLSLLTRFQPDKIKVDAELVRNIHISGAKQAIVASVVRCCEDLGITVVAEGVETLEEWCWLQSVGIRLFQGF 381
Cdd:COG5001  579 DDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGCDYAQGY 658


                 ....*
gi 764952584 382 LFSRP 386
Cdd:COG5001  659 LFSRP 663
BLUF smart01034
Sensors of blue-light using FAD; The BLUF domain has been shown to bind FAD in the AppA ...
 2-93 6.63e-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: 6.63e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952584     2 LTTLIYRSQVNPARPPTDLDALIHRASGKNMPLGITGILLFNGLQFFQVLEGSEEDLESLFHEIQSDPRHRDVVELMRDY 81
Cdd:smart01034   1 LHRLVYVSRARPDLSPEDLEDILAQARRNNARLGITGVLLYNGGHFLQVLEGPEEAVEALYERIQRDPRHRDVQVLLYEP 80

                           90
                   ....*....|..
gi 764952584    82 SAYRRFHDTGMR 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 7.53e-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: 107.98  E-value: 7.53e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952584    5 LIYRSQVNPARPPTDLDALIHRASGKNMPLGITGILLFNGLQFFQVLEGSEEDLESLFHEIQSDPRHRDVVELMRDYSAY 84
Cdd:pfam04940   1 LIYVSRAAADLSEEDLADILEQSRRNNARLGITGVLLYDGGRFLQVLEGPEEAVDALYERIKRDPRHTDVTVLEEGPIEE 80


                  ....*....
gi 764952584   85 RRFHDTGMR 93
Cdd:pfam04940  81 RRFPDWSMG 89
YjcC COG4943
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ...
 174-386 8.60e-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: 8.60e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952584 174 QAIVEPATKRVSSFEALIR--SPTGG--SPvEMFaaIP-AED--------RYRFDLeskayAFSLAGQLPLGKHQL--AI 238
Cdd:COG4943  290 QPIVDLKTGRCVGAEALVRwrDPDGSviSP-DIF--IPlAEQsglispltRQVIEQ-----VFRDLGDLLAADPDFhiSI 361

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952584 239 NLLPGSLyNHPDAVGWLMNSLLAAGLRPDQVLIEVTETEVITcFDQFRKVLKALRVAGMKLAIDDFGAGYSGLSLLTRFQ 318
Cdd:COG4943  362 NLSASDL-LSPRFLDDLERLLARTGVAPQQIVLEITERGFID-PAKARAVIAALREAGHRIAIDDFGTGYSSLSYLQTLP 439

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 764952584 319 PDKIKVDAELVRNIHISGAKQAIVASVVRCCEDLGITVVAEGVETLEEWCWLQSVGIRLFQGFLFSRP 386
Cdd:COG4943  440 VDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQGWLFAKP 507
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
255-386 7.86e-25

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 106.69  E-value: 7.86e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952584 255 LMNSLLAAGLRPDQVLIEVTETEVITCFDQFRKVLKALRVAGMKLAIDDFGAGYSGLSLLTRFQPDKIKVDAELVRNIHI 334
Cdd:PRK10060 513 LKQALQELNFEYCPIDVELTESCLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHK 592

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 764952584 335 SGAKQAIVASVVRCCEDLGITVVAEGVETLEEWCWLQSVGIRLFQGFLFSRP 386
Cdd:PRK10060 593 QPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKP 644
PRK13561 PRK13561
putative diguanylate cyclase; Provisional
 236-386 8.74e-22

putative diguanylate cyclase; Provisional


Pssm-ID: 184143 [Multi-domain]  Cd Length: 651  Bit Score: 97.48  E-value: 8.74e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952584 236 LAINLLPGSLYnHPDAVGWLMNSLLAAGLRPDQVLIEVTETEVITCFDQFRKVLKALRVAGMKLAIDDFGAGYSGLSLLT 315
Cdd:PRK13561 488 LSVNLSALQLM-HPNMVADMLELLTRYRIQPGTLILEVTESRRIDDPHAAVAILRPLRNAGVRVALDDFGMGYAGLRQLQ 566

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 764952584 316 RFQP---DKIKVDAELVRNIHISGAKQAIVASVVRcceDLGITVVAEGVETLEEWCWLQSVGIRLFQGFLFSRP 386
Cdd:PRK13561 567 HMKSlpiDVLKIDKMFVDGLPEDDSMVAAIIMLAQ---SLNLQVIAEGVETEAQRDWLLKAGVGIAQGFLFARA 637
PRK10551 PRK10551
cyclic di-GMP phosphodiesterase;
174-386 1.11e-21

cyclic di-GMP phosphodiesterase;


Pssm-ID: 182541 [Multi-domain]  Cd Length: 518  Bit Score: 96.98  E-value: 1.11e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952584 174 QAIVEPATKRVSSFEALIR--SPTGGS-PVEMFaaIP-AE--------DRYRFDLESKAyAFSLAGQLPLGKhQLAINLL 241
Cdd:PRK10551 282 QPVVDTQTLRVTGLEALLRwrHPTAGEiPPDAF--INyAEaqklivplTQHLFELIARD-AAELQKVLPVGA-KLGINIS 357

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952584 242 PGSLynHPDAVGWLMNSLLAAgLRPD--QVLIEVTETEVItcfdQFRKVLKA---LRVAGMKLAIDDFGAGYSGLSLLTR 316
Cdd:PRK10551 358 PAHL--HSDSFKADVQRLLAS-LPADhfQIVLEITERDMV----QEEEATKLfawLHSQGIEIAIDDFGTGHSALIYLER 430

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952584 317 FQPDKIKVDAELVRNIHISGAKQAIVASVVRCCEDLGITVVAEGVETLEEWCWLQSVGIRLFQGFLFSRP 386
Cdd:PRK10551 431 FTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNFLQGYWISRP 500
PRK11829 PRK11829
biofilm formation regulator HmsP; Provisional
 259-386 3.00e-20

biofilm formation regulator HmsP; Provisional


Pssm-ID: 183329 [Multi-domain]  Cd Length: 660  Bit Score: 93.08  E-value: 3.00e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952584 259 LLAAGLRPDQVLIEVTETEVITCFDQFRKVLKALRVAGMKLAIDDFGAGYSGLSLLTRFQP---DKIKVDAELVRNIHIS 335
Cdd:PRK11829 515 ISHYHIDPQQLLLEITETAQIQDLDEALRLLRELQGLGLLIALDDFGIGYSSLRYLNHLKSlpiHMIKLDKSFVKNLPED 594

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 764952584 336 GAKQAIVASVvrcCEDLGITVVAEGVETLEEWCWLQSVGIRLFQGFLFSRP 386
Cdd:PRK11829 595 DAIARIISCV---SDVLKVRVMAEGVETEEQRQWLLEHGIQCGQGFLFSPP 642
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 236-386 5.27e-20

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 92.43  E-value: 5.27e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952584  236 LAINLLPGSLYNhPDAVGWLMNSLLAAGLRPDQVLIEVTETEVITCFDQFRKVLKALRVAGMKLAIDDFGAGYSGLSLLT 315
Cdd:PRK09776  928 IALPLSVAGLSS-PTLLPFLLEQLENSPLPPRLLHLEITETALLNHAESASRLVQKLRLAGCRVVLSDFGRGLSSFNYLK 1006

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 764952584  316 RFQPDKIKVDAELVRNIHISGAKQAIVASVVRCCEDLGITVVAEGVETLEEWCWLQSVGIRLFQGFLFSRP 386
Cdd:PRK09776 1007 AFMADYLKLDGELVANLHGNLMDEMLISIIQGHAQRLGMKTIAGPVELPLVLDTLSGIGVDLAYGYAIARP 1077
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 249-386 6.54e-19

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 89.06  E-value: 6.54e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952584 249 PDAVGWLMNSLlaaGLRPDQVLIEVTETEVITCFDQFRKVLKALRVAGMKLAIDDFGAGYSGLSLLTRFQPDKIKVDAEL 328
Cdd:PRK11359 647 PNQVSDAMQAW---GIDGHQLTVEITESMMMEHDTEIFKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSF 723

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 764952584 329 VRNIHISGAKQAIVASVVRCCEDLGITVVAEGVETLEEWCWLQSVGIRLFQGFLFSRP 386
Cdd:PRK11359 724 VDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRP 781
PRK11059 PRK11059
regulatory protein CsrD; Provisional
 236-386 5.72e-13

regulatory protein CsrD; Provisional


Pssm-ID: 236833 [Multi-domain]  Cd Length: 640  Bit Score: 70.28  E-value: 5.72e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952584 236 LAINLLPGSLyNHPDAVGWLMNSLL--AAGLRPdQVLIEVTETEVITCFDQFRKVLKALRVAGMKLAIDDFGAGYSGLSL 313
Cdd:PRK11059 486 LSINLSVDSL-LSRAFQRWLRDTLLqcPRSQRK-RLIFELAEADVCQHISRLRPVLRMLRGLGCRLAVDQAGLTVVSTSY 563

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 764952584 314 LTRFQPDKIKVDAELVRNIHISGAKQAIVASVVRCCEDLGITVVAEGVETLEEWCWLQSVGIRLFQGFLFSRP 386
Cdd:PRK11059 564 IKELNVELIKLHPSLVRNIHKRTENQLFVRSLVGACAGTETQVFATGVESREEWQTLQELGVSGGQGDFFAES 636
YuxH COG3434
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ...
 255-386 8.99e-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: 69.06  E-value: 8.99e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952584 255 LMNSLLAAgLRPDQVLIEVTETEVITcfDQFRKVLKALRVAGMKLAIDDFGAGYSGLSLLTRFqpDKIKVDaelVRNIHI 334
Cdd:COG3434   73 LLSDLPEL-LPPERVVLEILEDVEPD--EELLEALKELKEKGYRIALDDFVLDPEWDPLLPLA--DIIKID---VLALDL 144

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 764952584 335 SGAKQaivasVVRCCEDLGITVVAEGVETLEEWCWLQSVGIRLFQGFLFSRP 386
Cdd:COG3434  145 EELAE-----LVARLKRYGIKLLAEKVETREEFELCKELGFDLFQGYFFSKP 191
PRK11596 PRK11596
cyclic-di-GMP phosphodiesterase; Provisional
 288-386 5.69e-08

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183222 [Multi-domain]  Cd Length: 255  Bit Score: 53.47  E-value: 5.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764952584 288 VLKALRVAGM----KLAIDDFGAGYSGLSLLTRFQPDKIKVDAELV---------RNIHIsgakqAIVASVVRCCEDlgi 354
Cdd:PRK11596 140 LPKDSPFASMcefgPLWLDDFGTGMANFSALSEVRYDYIKVARELFimlrqseegRNLFS-----QLLHLMNRYCRG--- 211

                         90       100       110
                 ....*....|....*....|....*....|..
gi 764952584 355 tVVAEGVETLEEWCWLQSVGIRLFQGFLFSRP 386
Cdd:PRK11596 212 -VIVEGVETPEEWRDVQRSPAFAAQGYFLSRP 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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