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Conserved domains on  [gi|1375608435|gb|AVW71087|]
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EAL domain-containing protein [Listeria monocytogenes]

Protein Classification

EAL domain-containing protein( domain architecture ID 10112612)

EAL domain-containing protein may act as a cyclic diguanylate phosphodiesterase

PubMed:  28186120|20691189|25447517

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 ...
 6-235 2.83e-26

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: 101.85  E-value: 2.83e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375608435   6 FQLFIQPKLDVLQGNIVEYEILLR-DDSAVPRFPLSELEAVLADEELYLAFSEW-FSEAFLDV---LKKYPNDRFAINIA 80
Cdd:cd01948    12 FELYYQPIVDLRTGRIVGYEALLRwRHPEGGLISPAEFIPLAEETGLIVELGRWvLEEACRQLarwQAGGPDLRLSVNLS 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375608435  81 PQQLFYIETLHWLDKLKSES----HRITVEMTEDIFDvpghkrhlnanDKNAFILNKIKVIHGLGYHIAIDDVSCGLNSL 156
Cdd:cd01948    92 ARQLRDPDFLDRLLELLAETglppRRLVLEITESALI-----------DDLEEALATLRRLRALGVRIALDDFGTGYSSL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375608435 157 ERVMSYLPYIIEIKFSLIHfkNIPL-EDLLLFIKAWANFAQKNKLDFVVEGIETKETMTLLESHGVSIFQGYLVNKPFPV 235
Cdd:cd01948   161 SYLKRLPVDYLKIDRSFVR--DIETdPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPA 238
 
Name Accession Description Interval E-value
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 6-235 2.83e-26

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: 101.85  E-value: 2.83e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375608435   6 FQLFIQPKLDVLQGNIVEYEILLR-DDSAVPRFPLSELEAVLADEELYLAFSEW-FSEAFLDV---LKKYPNDRFAINIA 80
Cdd:cd01948    12 FELYYQPIVDLRTGRIVGYEALLRwRHPEGGLISPAEFIPLAEETGLIVELGRWvLEEACRQLarwQAGGPDLRLSVNLS 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375608435  81 PQQLFYIETLHWLDKLKSES----HRITVEMTEDIFDvpghkrhlnanDKNAFILNKIKVIHGLGYHIAIDDVSCGLNSL 156
Cdd:cd01948    92 ARQLRDPDFLDRLLELLAETglppRRLVLEITESALI-----------DDLEEALATLRRLRALGVRIALDDFGTGYSSL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375608435 157 ERVMSYLPYIIEIKFSLIHfkNIPL-EDLLLFIKAWANFAQKNKLDFVVEGIETKETMTLLESHGVSIFQGYLVNKPFPV 235
Cdd:cd01948   161 SYLKRLPVDYLKIDRSFVR--DIETdPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPA 238
EAL COG2200
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
 6-235 5.36e-25

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: 102.56  E-value: 5.36e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375608435   6 FQLFIQPKLDVLQGNIVEYEILLRDDSAVPRF-PLSELEAVLADEELYLAFSEWFSEAFLDVLKKYPND----RFAINIA 80
Cdd:COG2200   342 LRLYYQPIVDLRTGRVVGYEALLRWRHPDGGLiSPAEFIPAAERSGLIVELDRWVLERALRQLARWPERgldlRLSVNLS 421

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375608435  81 PQQL----FYIETLHWLDKLKSESHRITVEMTEdifdvpghkRHLNANDKNAfiLNKIKVIHGLGYHIAIDDVSCGLNSL 156
Cdd:COG2200   422 ARSLldpdFLERLLELLAEYGLPPERLVLEITE---------SALLEDLEAA--IELLARLRALGVRIALDDFGTGYSSL 490

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375608435 157 ERVMSYLPYIIEIKFSLIHfkNIPL-EDLLLFIKAWANFAQKNKLDFVVEGIETKETMTLLESHGVSIFQGYLVNKPFPV 235
Cdd:COG2200   491 SYLKRLPPDYLKIDRSFVR--DIARdPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRPLPL 568
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 6-232 6.41e-23

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: 92.77  E-value: 6.41e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375608435   6 FQLFIQPKLDVLQGNIVEYEILLR-DDSAVPRFPLSELEAVLADEELYLAFSEWFSEAFLDVLKKYPND---RFAINIAP 81
Cdd:pfam00563  13 FVLYYQPIVDLRTGRVVGYEALLRwQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQLGpdiKLSINLSP 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375608435  82 QQLFYIETLHWLDKLKSESH----RITVEMTEDifDVPGHKRHLNANdknafilnkIKVIHGLGYHIAIDDVSCGLNSLE 157
Cdd:pfam00563  93 ASLADPGFLELLRALLKQAGpppsRLVLEITES--DLLARLEALREV---------LKRLRALGIRIALDDFGTGYSSLS 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1375608435 158 RVmSYLPyIIEIKF--SLIHfkNIPLEDLL-LFIKAWANFAQKNKLDFVVEGIETKETMTLLESHGVSIFQGYLVNKP 232
Cdd:pfam00563 162 YL-LRLP-PDFVKIdrSLIA--DIDKDGEArAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
 6-235 5.79e-21

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


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 87.66  E-value: 5.79e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375608435    6 FQLFIQPKLDVLQGNIVEYEILLR----DDSAVP--RF-PLSEleavlaDEELYLAFSEW-FSEAFLDVL----KKYPND 73
Cdd:smart00052  13 FLLYYQPIVSLRTGRLVGVEALIRwqhpEGGIISpdEFiPLAE------ETGLIVPLGRWvLEQACQQLAewqaQGPPPL 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375608435   74 RFAINIAPQQL----FYIETLHWLDKLKSESHRITVEMTEDIF-DVPGHKRHLnandknafilnkIKVIHGLGYHIAIDD 148
Cdd:smart00052  87 LISINLSARQLispdLVPRVLELLEETGLPPQRLELEITESVLlDDDESAVAT------------LQRLRELGVRIALDD 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375608435  149 VSCGLNSLERVMSYLPYIIEIKFSLIhfKNIP--LEDLLLfIKAWANFAQKNKLDFVVEGIETKETMTLLESHGVSIFQG 226
Cdd:smart00052 155 FGTGYSSLSYLKRLPVDLLKIDKSFV--RDLQtdPEDEAI-VQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQG 231


                   ....*....
gi 1375608435  227 YLVNKPFPV 235
Cdd:smart00052 232 YLFSRPLPL 240
PRK11829 PRK11829
biofilm formation regulator HmsP; Provisional
 6-234 8.05e-13

biofilm formation regulator HmsP; Provisional


Pssm-ID: 183329 [Multi-domain]  Cd Length: 660  Bit Score: 67.27  E-value: 8.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375608435   6 FQLFIQPKLDVLQGNIVEYEILLR----DDSAV-PR--FPLSEleavlaDEELYLAFSEWFSEAFLDVLKKYPNDRFAI- 77
Cdd:PRK11829  419 FTLFLQPQWDMKRQQVIGAEALLRwcqpDGSYVlPSgfVHFAE------EEGMMVPLGNWVLEEACRILADWKARGVSLp 492

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375608435  78 ---NIAPQQLFYIETLHWLDKLKSESH----RITVEMTED--IFDVpghkrhlnanDKNAFILNKIKvihGLGYHIAIDD 148
Cdd:PRK11829  493 lsvNISGLQVQNKQFLPHLKTLISHYHidpqQLLLEITETaqIQDL----------DEALRLLRELQ---GLGLLIALDD 559

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375608435 149 VSCGLNSLE--RVMSYLP-YIIEIKFSLIhfKNIPLEDLLLFIKAwaNFAQKNKLDFVVEGIETKETMTLLESHGVSIFQ 225
Cdd:PRK11829  560 FGIGYSSLRylNHLKSLPiHMIKLDKSFV--KNLPEDDAIARIIS--CVSDVLKVRVMAEGVETEEQRQWLLEHGIQCGQ 635


                  ....*....
gi 1375608435 226 GYLVNKPFP 234
Cdd:PRK11829  636 GFLFSPPLP 644
 
Name Accession Description Interval E-value
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 6-235 2.83e-26

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: 101.85  E-value: 2.83e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375608435   6 FQLFIQPKLDVLQGNIVEYEILLR-DDSAVPRFPLSELEAVLADEELYLAFSEW-FSEAFLDV---LKKYPNDRFAINIA 80
Cdd:cd01948    12 FELYYQPIVDLRTGRIVGYEALLRwRHPEGGLISPAEFIPLAEETGLIVELGRWvLEEACRQLarwQAGGPDLRLSVNLS 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375608435  81 PQQLFYIETLHWLDKLKSES----HRITVEMTEDIFDvpghkrhlnanDKNAFILNKIKVIHGLGYHIAIDDVSCGLNSL 156
Cdd:cd01948    92 ARQLRDPDFLDRLLELLAETglppRRLVLEITESALI-----------DDLEEALATLRRLRALGVRIALDDFGTGYSSL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375608435 157 ERVMSYLPYIIEIKFSLIHfkNIPL-EDLLLFIKAWANFAQKNKLDFVVEGIETKETMTLLESHGVSIFQGYLVNKPFPV 235
Cdd:cd01948   161 SYLKRLPVDYLKIDRSFVR--DIETdPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPA 238
EAL COG2200
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
 6-235 5.36e-25

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: 102.56  E-value: 5.36e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375608435   6 FQLFIQPKLDVLQGNIVEYEILLRDDSAVPRF-PLSELEAVLADEELYLAFSEWFSEAFLDVLKKYPND----RFAINIA 80
Cdd:COG2200   342 LRLYYQPIVDLRTGRVVGYEALLRWRHPDGGLiSPAEFIPAAERSGLIVELDRWVLERALRQLARWPERgldlRLSVNLS 421

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375608435  81 PQQL----FYIETLHWLDKLKSESHRITVEMTEdifdvpghkRHLNANDKNAfiLNKIKVIHGLGYHIAIDDVSCGLNSL 156
Cdd:COG2200   422 ARSLldpdFLERLLELLAEYGLPPERLVLEITE---------SALLEDLEAA--IELLARLRALGVRIALDDFGTGYSSL 490

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375608435 157 ERVMSYLPYIIEIKFSLIHfkNIPL-EDLLLFIKAWANFAQKNKLDFVVEGIETKETMTLLESHGVSIFQGYLVNKPFPV 235
Cdd:COG2200   491 SYLKRLPPDYLKIDRSFVR--DIARdPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRPLPL 568
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 6-232 6.41e-23

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: 92.77  E-value: 6.41e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375608435   6 FQLFIQPKLDVLQGNIVEYEILLR-DDSAVPRFPLSELEAVLADEELYLAFSEWFSEAFLDVLKKYPND---RFAINIAP 81
Cdd:pfam00563  13 FVLYYQPIVDLRTGRVVGYEALLRwQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQLGpdiKLSINLSP 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375608435  82 QQLFYIETLHWLDKLKSESH----RITVEMTEDifDVPGHKRHLNANdknafilnkIKVIHGLGYHIAIDDVSCGLNSLE 157
Cdd:pfam00563  93 ASLADPGFLELLRALLKQAGpppsRLVLEITES--DLLARLEALREV---------LKRLRALGIRIALDDFGTGYSSLS 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1375608435 158 RVmSYLPyIIEIKF--SLIHfkNIPLEDLL-LFIKAWANFAQKNKLDFVVEGIETKETMTLLESHGVSIFQGYLVNKP 232
Cdd:pfam00563 162 YL-LRLP-PDFVKIdrSLIA--DIDKDGEArAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
 6-235 5.79e-21

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


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 87.66  E-value: 5.79e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375608435    6 FQLFIQPKLDVLQGNIVEYEILLR----DDSAVP--RF-PLSEleavlaDEELYLAFSEW-FSEAFLDVL----KKYPND 73
Cdd:smart00052  13 FLLYYQPIVSLRTGRLVGVEALIRwqhpEGGIISpdEFiPLAE------ETGLIVPLGRWvLEQACQQLAewqaQGPPPL 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375608435   74 RFAINIAPQQL----FYIETLHWLDKLKSESHRITVEMTEDIF-DVPGHKRHLnandknafilnkIKVIHGLGYHIAIDD 148
Cdd:smart00052  87 LISINLSARQLispdLVPRVLELLEETGLPPQRLELEITESVLlDDDESAVAT------------LQRLRELGVRIALDD 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375608435  149 VSCGLNSLERVMSYLPYIIEIKFSLIhfKNIP--LEDLLLfIKAWANFAQKNKLDFVVEGIETKETMTLLESHGVSIFQG 226
Cdd:smart00052 155 FGTGYSSLSYLKRLPVDLLKIDKSFV--RDLQtdPEDEAI-VQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQG 231


                   ....*....
gi 1375608435  227 YLVNKPFPV 235
Cdd:smart00052 232 YLFSRPLPL 240
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 6-235 3.68e-14

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: 70.96  E-value: 3.68e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375608435   6 FQLFIQPKLDVLQGNIVEYEILLR----DDSAVP--RF-PLSE------------LEAVLADeelylaFSEWFSEAFLDV 66
Cdd:COG5001   439 LELHYQPQVDLATGRIVGAEALLRwqhpERGLVSpaEFiPLAEetglivplgewvLREACRQ------LAAWQDAGLPDL 512

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375608435  67 lkkypndRFAINIAPQQLfyiETLHWLDKLKS-------ESHRITVEMTEDIF--DVPGHKRHLNAndknafilnkikvI 137
Cdd:COG5001   513 -------RVAVNLSARQL---RDPDLVDRVRRalaetglPPSRLELEITESALleDPEEALETLRA-------------L 569

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375608435 138 HGLGYHIAIDDVSCGLNSLervmSYL---PyIIEIKF--SLIHfkNIP--LEDLLLfIKAWANFAQKNKLDFVVEGIETK 210
Cdd:COG5001   570 RALGVRIALDDFGTGYSSL----SYLkrlP-VDTLKIdrSFVR--DLAedPDDAAI-VRAIIALAHSLGLEVVAEGVETE 641

                         250       260
                  ....*....|....*....|....*
gi 1375608435 211 ETMTLLESHGVSIFQGYLVNKPFPV 235
Cdd:COG5001   642 EQLEFLRELGCDYAQGYLFSRPLPA 666
PRK11829 PRK11829
biofilm formation regulator HmsP; Provisional
 6-234 8.05e-13

biofilm formation regulator HmsP; Provisional


Pssm-ID: 183329 [Multi-domain]  Cd Length: 660  Bit Score: 67.27  E-value: 8.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375608435   6 FQLFIQPKLDVLQGNIVEYEILLR----DDSAV-PR--FPLSEleavlaDEELYLAFSEWFSEAFLDVLKKYPNDRFAI- 77
Cdd:PRK11829  419 FTLFLQPQWDMKRQQVIGAEALLRwcqpDGSYVlPSgfVHFAE------EEGMMVPLGNWVLEEACRILADWKARGVSLp 492

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375608435  78 ---NIAPQQLFYIETLHWLDKLKSESH----RITVEMTED--IFDVpghkrhlnanDKNAFILNKIKvihGLGYHIAIDD 148
Cdd:PRK11829  493 lsvNISGLQVQNKQFLPHLKTLISHYHidpqQLLLEITETaqIQDL----------DEALRLLRELQ---GLGLLIALDD 559

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375608435 149 VSCGLNSLE--RVMSYLP-YIIEIKFSLIhfKNIPLEDLLLFIKAwaNFAQKNKLDFVVEGIETKETMTLLESHGVSIFQ 225
Cdd:PRK11829  560 FGIGYSSLRylNHLKSLPiHMIKLDKSFV--KNLPEDDAIARIIS--CVSDVLKVRVMAEGVETEEQRQWLLEHGIQCGQ 635


                  ....*....
gi 1375608435 226 GYLVNKPFP 234
Cdd:PRK11829  636 GFLFSPPLP 644
YuxH COG3434
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ...
 11-232 3.40e-11

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


Pssm-ID: 442660 [Multi-domain]  Cd Length: 407  Bit Score: 62.13  E-value: 3.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375608435  11 QPKLDVlQGNIVEYEILLRDdSAVPRFPLSELEAvladeelylAFSEWFSEAFLDV-LKKYPNDRFA-INIAPQQLF--Y 86
Cdd:COG3434     9 QPILDR-DQRVVGYELLFRS-GLENSAPDVDGDQ---------ATARVLLNAFLEIgLDRLLGGKLAfINFTEELLLsdL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375608435  87 IETLHwldklkseSHRITVEMTEDIfdvpghkrhlnanDKNAFILNKIKVIHGLGYHIAIDDVSCglnsLERVMSYLPYI 166
Cdd:COG3434    78 PELLP--------PERVVLEILEDV-------------EPDEELLEALKELKEKGYRIALDDFVL----DPEWDPLLPLA 132

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1375608435 167 IEIKFSlihFKNIPLEDLLLFIKAwanfAQKNKLDFVVEGIETKETMTLLESHGVSIFQGYLVNKP 232
Cdd:COG3434   133 DIIKID---VLALDLEELAELVAR----LKRYGIKLLAEKVETREEFELCKELGFDLFQGYFFSKP 191
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 101-234 3.97e-11

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 62.09  E-value: 3.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375608435 101 HRITVEMTEDIfdvpghkrhlnANDKNAFILNKIKVIHGLGYHIAIDDVSCGLNSLERvMSYLPyIIEIKF--SLIHfKN 178
Cdd:PRK11359  662 HQLTVEITESM-----------MMEHDTEIFKRIQILRDMGVGLSVDDFGTGFSGLSR-LVSLP-VTEIKIdkSFVD-RC 727

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1375608435 179 IPLEDLLLFIKAWANFAQKNKLDFVVEGIETKETMTLLESHGVSIFQGYLVNKPFP 234
Cdd:PRK11359  728 LTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRPLP 783
PRK13561 PRK13561
putative diguanylate cyclase; Provisional
 5-234 1.66e-10

putative diguanylate cyclase; Provisional


Pssm-ID: 184143 [Multi-domain]  Cd Length: 651  Bit Score: 60.11  E-value: 1.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375608435   5 KFQLFIQPKLDVLQGNIVEYEILLRDDSAVPRFPLSELEAVLADE-ELYLAFSEWFSEAFLDVLKKYP----NDRFAINI 79
Cdd:PRK13561  413 QFAIWLQPQVEMRSGKLVSAEALLRMQQPDGSWDLPEGLIDRIEScGLMVTVGHWVLEESCRLLAAWQergiMLPLSVNL 492

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375608435  80 APQQLFYIETL-HWLDKLksESHRI-----TVEMTEdifdvpghKRHLNANDKNAFILnkiKVIHGLGYHIAIDDVSCG- 152
Cdd:PRK13561  493 SALQLMHPNMVaDMLELL--TRYRIqpgtlILEVTE--------SRRIDDPHAAVAIL---RPLRNAGVRVALDDFGMGy 559

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375608435 153 --LNSLERvMSYLPY-IIEIKFSLIhfKNIPLEDLLlfIKAWANFAQKNKLDFVVEGIETKETMTLLESHGVSIFQGYLV 229
Cdd:PRK13561  560 agLRQLQH-MKSLPIdVLKIDKMFV--DGLPEDDSM--VAAIIMLAQSLNLQVIAEGVETEAQRDWLLKAGVGIAQGFLF 634


                  ....*
gi 1375608435 230 NKPFP 234
Cdd:PRK13561  635 ARALP 639
PRK10551 PRK10551
cyclic di-GMP phosphodiesterase;
74-235 1.20e-09

cyclic di-GMP phosphodiesterase;


Pssm-ID: 182541 [Multi-domain]  Cd Length: 518  Bit Score: 57.69  E-value: 1.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375608435  74 RFAINIAPQQL----FYIETLHWLDKLKSESHRITVEMTEDifdvpGHKRHLNANDKNAFIlnkikviHGLGYHIAIDDV 149
Cdd:PRK10551  351 KLGINISPAHLhsdsFKADVQRLLASLPADHFQIVLEITER-----DMVQEEEATKLFAWL-------HSQGIEIAIDDF 418

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375608435 150 SCG---LNSLERV-MSYLPyiIEIKF-SLIHFKNI--PLEDLLLFIkawanfAQKNKLDFVVEGIETKETMTLLESHGVS 222
Cdd:PRK10551  419 GTGhsaLIYLERFtLDYLK--IDRGFiQAIGTETVtsPVLDAVLTL------AKRLNMLTVAEGVETPEQARWLRERGVN 490

                         170
                  ....*....|...
gi 1375608435 223 IFQGYLVNKPFPV 235
Cdd:PRK10551  491 FLQGYWISRPLPL 503
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
5-234 2.00e-07

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 51.22  E-value: 2.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375608435   5 KFQLFIQPKLDvLQGNIVEYEILLRDDSavP-RFPLSELEAVLADEE--LYLAFSEWfseAFLDVLK-------KYPNDR 74
Cdd:PRK10060  421 QLVIHYQPKIT-WRGEVRSLEALVRWQS--PeRGLIPPLEFISYAEEsgLIVPLGRW---VMLDVVRqvakwrdKGINLR 494

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375608435  75 FAINIAPQQL----FYIETLHWLDKLKSESHRITVEMTEdifdvpghkRHLNANDKNAfiLNKIKVIHGLGYHIAIDDVS 150
Cdd:PRK10060  495 VAVNVSARQLadqtIFTALKQALQELNFEYCPIDVELTE---------SCLIENEELA--LSVIQQFSQLGAQVHLDDFG 563

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375608435 151 CGLNSLERvMSYLPyIIEIKFSLIHFKNI---PLEDLLlfIKAWANFAQKNKLDFVVEGIETKETMTLLESHGVSIFQGY 227
Cdd:PRK10060  564 TGYSSLSQ-LARFP-IDAIKLDQSFVRDIhkqPVSQSL--VRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNERQGF 639


                  ....*..
gi 1375608435 228 LVNKPFP 234
Cdd:PRK10060  640 LFAKPMP 646
 
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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