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Conserved domains on  [gi|446467900|ref|WP_000545754|]
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MULTISPECIES: EAL domain-containing protein [Salmonella]

Protein Classification

EAL domain-containing protein( domain architecture ID 10112612)

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

CATH:  3.20.20.450
EC:  3.1.4.52
Gene Ontology:  GO:0071111
PubMed:  15306016|26055114|19756011
SCOP:  4002400

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 ...
 7-163 4.15e-38

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: 130.74  E-value: 4.15e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467900   7 RLQQAIRNREFTPFYQPIVCATGGEVVGCEMLARWLHPQKGLLSAGNFIPAIEATGLGGALLRGLADEVCGDGQDLaRSA 86
Cdd:cd01948    2 DLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARW-QAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467900  87 GRRLMMTLNLSLSLVMTPLFRPHLLALsirLEQAGMTP---VFEITEREDIRAFPQA-AVFRQLAAGGLRFAVDDFGTGH 162
Cdd:cd01948   81 GPDLRLSVNLSARQLRDPDFLDRLLEL---LAETGLPPrrlVLEITESALIDDLEEAlATLRRLRALGVRIALDDFGTGY 157


                 .
gi 446467900 163 A 163
Cdd:cd01948  158 S 158
 
Name Accession Description Interval E-value
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 7-163 4.15e-38

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: 130.74  E-value: 4.15e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467900   7 RLQQAIRNREFTPFYQPIVCATGGEVVGCEMLARWLHPQKGLLSAGNFIPAIEATGLGGALLRGLADEVCGDGQDLaRSA 86
Cdd:cd01948    2 DLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARW-QAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467900  87 GRRLMMTLNLSLSLVMTPLFRPHLLALsirLEQAGMTP---VFEITEREDIRAFPQA-AVFRQLAAGGLRFAVDDFGTGH 162
Cdd:cd01948   81 GPDLRLSVNLSARQLRDPDFLDRLLEL---LAETGLPPrrlVLEITESALIDDLEEAlATLRRLRALGVRIALDDFGTGY 157


                 .
gi 446467900 163 A 163
Cdd:cd01948  158 S 158
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
 7-164 1.25e-34

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


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 121.94  E-value: 1.25e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467900     7 RLQQAIRNREFTPFYQPIVCATGGEVVGCEMLARWLHPQKGLLSAGNFIPAIEATGLGGALLRGLADEVCGDGQDLARSA 86
Cdd:smart00052   3 ELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQG 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467900    87 GRRLMMTLNLSLSLVMTPLFRPHLLALsirLEQAGMTP---VFEITEREDIRAFPQA-AVFRQLAAGGLRFAVDDFGTGH 162
Cdd:smart00052  83 PPPLLISINLSARQLISPDLVPRVLEL---LEETGLPPqrlELEITESVLLDDDESAvATLQRLRELGVRIALDDFGTGY 159


                   ..
gi 446467900   163 AG 164
Cdd:smart00052 160 SS 161
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 7-166 4.23e-32

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: 115.11  E-value: 4.23e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467900    7 RLQQAIRNREFTPFYQPIVCATGGEVVGCEMLARWLHPQKGLLSAGNFIPAIEATGLGGALLRGLADEVCGDGQDLARSA 86
Cdd:pfam00563   3 ALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQLGP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467900   87 GRRLMmtLNLSLSLVMTPLFRPHLLALSIRLEQAGMTPVFEITEREDIRAFPQA-AVFRQLAAGGLRFAVDDFGTGHAGP 165
Cdd:pfam00563  83 DIKLS--INLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALrEVLKRLRALGIRIALDDFGTGYSSL 160


                  .
gi 446467900  166 A 166
Cdd:pfam00563 161 S 161
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 7-163 5.06e-31

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: 117.95  E-value: 5.06e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467900   7 RLQQAIRNREFTPFYQPIVCATGGEVVGCEMLARWLHPQKGLLSAGNFIPAIEATGLGGALLRGLADEVCGDGQDLARSA 86
Cdd:COG5001  429 DLRRALERGELELHYQPQVDLATGRIVGAEALLRWQHPERGLVSPAEFIPLAEETGLIVPLGEWVLREACRQLAAWQDAG 508

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467900  87 GRRLMMTLNLSLSLVMTPLFRPHLLALsirLEQAGMTP---VFEITEREDIRAFPQA-AVFRQLAAGGLRFAVDDFGTGH 162
Cdd:COG5001  509 LPDLRVAVNLSARQLRDPDLVDRVRRA---LAETGLPPsrlELEITESALLEDPEEAlETLRALRALGVRIALDDFGTGY 585


                 .
gi 446467900 163 A 163
Cdd:COG5001  586 S 586
PRK10551 PRK10551
cyclic di-GMP phosphodiesterase;
10-162 1.79e-18

cyclic di-GMP phosphodiesterase;


Pssm-ID: 182541 [Multi-domain]  Cd Length: 518  Bit Score: 81.96  E-value: 1.79e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467900  10 QAIRNREFTPFYQPIVCATGGEVVGCEMLARWLHPQKGLLSAGNFIPAIEATGLGGALLRGLADEVCGDGQDLARS--AG 87
Cdd:PRK10551 270 TGIKRGQFYVEYQPVVDTQTLRVTGLEALLRWRHPTAGEIPPDAFINYAEAQKLIVPLTQHLFELIARDAAELQKVlpVG 349

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446467900  88 RRLmmTLNLSLSLVMTPLFRPHLLALSIRLEQAGMTPVFEITEREDIRAFPQAAVFRQLAAGGLRFAVDDFGTGH 162
Cdd:PRK10551 350 AKL--GINISPAHLHSDSFKADVQRLLASLPADHFQIVLEITERDMVQEEEATKLFAWLHSQGIEIAIDDFGTGH 422
 
Name Accession Description Interval E-value
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 7-163 4.15e-38

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: 130.74  E-value: 4.15e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467900   7 RLQQAIRNREFTPFYQPIVCATGGEVVGCEMLARWLHPQKGLLSAGNFIPAIEATGLGGALLRGLADEVCGDGQDLaRSA 86
Cdd:cd01948    2 DLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARW-QAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467900  87 GRRLMMTLNLSLSLVMTPLFRPHLLALsirLEQAGMTP---VFEITEREDIRAFPQA-AVFRQLAAGGLRFAVDDFGTGH 162
Cdd:cd01948   81 GPDLRLSVNLSARQLRDPDFLDRLLEL---LAETGLPPrrlVLEITESALIDDLEEAlATLRRLRALGVRIALDDFGTGY 157


                 .
gi 446467900 163 A 163
Cdd:cd01948  158 S 158
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
 7-164 1.25e-34

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


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 121.94  E-value: 1.25e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467900     7 RLQQAIRNREFTPFYQPIVCATGGEVVGCEMLARWLHPQKGLLSAGNFIPAIEATGLGGALLRGLADEVCGDGQDLARSA 86
Cdd:smart00052   3 ELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQG 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467900    87 GRRLMMTLNLSLSLVMTPLFRPHLLALsirLEQAGMTP---VFEITEREDIRAFPQA-AVFRQLAAGGLRFAVDDFGTGH 162
Cdd:smart00052  83 PPPLLISINLSARQLISPDLVPRVLEL---LEETGLPPqrlELEITESVLLDDDESAvATLQRLRELGVRIALDDFGTGY 159


                   ..
gi 446467900   163 AG 164
Cdd:smart00052 160 SS 161
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 7-166 4.23e-32

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: 115.11  E-value: 4.23e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467900    7 RLQQAIRNREFTPFYQPIVCATGGEVVGCEMLARWLHPQKGLLSAGNFIPAIEATGLGGALLRGLADEVCGDGQDLARSA 86
Cdd:pfam00563   3 ALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQLGP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467900   87 GRRLMmtLNLSLSLVMTPLFRPHLLALSIRLEQAGMTPVFEITEREDIRAFPQA-AVFRQLAAGGLRFAVDDFGTGHAGP 165
Cdd:pfam00563  83 DIKLS--INLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALrEVLKRLRALGIRIALDDFGTGYSSL 160


                  .
gi 446467900  166 A 166
Cdd:pfam00563 161 S 161
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 7-163 5.06e-31

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: 117.95  E-value: 5.06e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467900   7 RLQQAIRNREFTPFYQPIVCATGGEVVGCEMLARWLHPQKGLLSAGNFIPAIEATGLGGALLRGLADEVCGDGQDLARSA 86
Cdd:COG5001  429 DLRRALERGELELHYQPQVDLATGRIVGAEALLRWQHPERGLVSPAEFIPLAEETGLIVPLGEWVLREACRQLAAWQDAG 508

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467900  87 GRRLMMTLNLSLSLVMTPLFRPHLLALsirLEQAGMTP---VFEITEREDIRAFPQA-AVFRQLAAGGLRFAVDDFGTGH 162
Cdd:COG5001  509 LPDLRVAVNLSARQLRDPDLVDRVRRA---LAETGLPPsrlELEITESALLEDPEEAlETLRALRALGVRIALDDFGTGY 585


                 .
gi 446467900 163 A 163
Cdd:COG5001  586 S 586
EAL COG2200
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
 7-163 3.32e-29

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: 112.57  E-value: 3.32e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467900   7 RLQQAIRNREFTPFYQPIVCATGGEVVGCEMLARWLHPQKGLLSAGNFIPAIEATGLGGALLRGLADEVCGDGQDLaRSA 86
Cdd:COG2200  332 ELREALEEGELRLYYQPIVDLRTGRVVGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELDRWVLERALRQLARW-PER 410

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467900  87 GRRLMMTLNLSLSLVMTPLFRPHLLALsirLEQAGMTP---VFEITEREDIRAFPQA-AVFRQLAAGGLRFAVDDFGTGH 162
Cdd:COG2200  411 GLDLRLSVNLSARSLLDPDFLERLLEL---LAEYGLPPerlVLEITESALLEDLEAAiELLARLRALGVRIALDDFGTGY 487


                 .
gi 446467900 163 A 163
Cdd:COG2200  488 S 488
YjcC COG4943
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ...
 5-162 1.72e-26

Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal transduction mechanisms];


Pssm-ID: 443970 [Multi-domain]  Cd Length: 528  Bit Score: 104.61  E-value: 1.72e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467900   5 AFRLQQAIRNREFTPFYQPIVCATGGEVVGCEMLARWLHPQKGLLSAGNFIPAIEATGLGGALLRGLADEVCGD-GQDLA 83
Cdd:COG4943  273 RRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRDPDGSVISPDIFIPLAEQSGLISPLTRQVIEQVFRDlGDLLA 352

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467900  84 RSAGRRLmmTLNLSLSLVMTPLFRPHLLALsirLEQAGMTP---VFEITEREDIRAFPQAAVFRQLAAGGLRFAVDDFGT 160
Cdd:COG4943  353 ADPDFHI--SINLSASDLLSPRFLDDLERL---LARTGVAPqqiVLEITERGFIDPAKARAVIAALREAGHRIAIDDFGT 427


                 ..
gi 446467900 161 GH 162
Cdd:COG4943  428 GY 429
PRK10551 PRK10551
cyclic di-GMP phosphodiesterase;
10-162 1.79e-18

cyclic di-GMP phosphodiesterase;


Pssm-ID: 182541 [Multi-domain]  Cd Length: 518  Bit Score: 81.96  E-value: 1.79e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467900  10 QAIRNREFTPFYQPIVCATGGEVVGCEMLARWLHPQKGLLSAGNFIPAIEATGLGGALLRGLADEVCGDGQDLARS--AG 87
Cdd:PRK10551 270 TGIKRGQFYVEYQPVVDTQTLRVTGLEALLRWRHPTAGEIPPDAFINYAEAQKLIVPLTQHLFELIARDAAELQKVlpVG 349

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446467900  88 RRLmmTLNLSLSLVMTPLFRPHLLALSIRLEQAGMTPVFEITEREDIRAFPQAAVFRQLAAGGLRFAVDDFGTGH 162
Cdd:PRK10551 350 AKL--GINISPAHLHSDSFKADVQRLLASLPADHFQIVLEITERDMVQEEEATKLFAWLHSQGIEIAIDDFGTGH 422
PRK13561 PRK13561
putative diguanylate cyclase; Provisional
 8-164 8.62e-17

putative diguanylate cyclase; Provisional


Pssm-ID: 184143 [Multi-domain]  Cd Length: 651  Bit Score: 77.06  E-value: 8.62e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467900   8 LQQAIRNREFTPFYQPIVCATGGEVVGCEMLARWLHPQKGLLSAGNFIPAIEATGLGGALLRGLADEVCgdgQDLARSAG 87
Cdd:PRK13561 405 ILNALENHQFAIWLQPQVEMRSGKLVSAEALLRMQQPDGSWDLPEGLIDRIESCGLMVTVGHWVLEESC---RLLAAWQE 481

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467900  88 RRLMMTLNLSLSLV--MTPLFRPHLLALSIRLEQAGMTPVFEITEREDIRAFPQA-AVFRQLAAGGLRFAVDDFGTGHAG 164
Cdd:PRK13561 482 RGIMLPLSVNLSALqlMHPNMVADMLELLTRYRIQPGTLILEVTESRRIDDPHAAvAILRPLRNAGVRVALDDFGMGYAG 561
PRK11829 PRK11829
biofilm formation regulator HmsP; Provisional
 8-164 9.65e-13

biofilm formation regulator HmsP; Provisional


Pssm-ID: 183329 [Multi-domain]  Cd Length: 660  Bit Score: 65.35  E-value: 9.65e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467900   8 LQQAIRNREFTPFYQPIVCATGGEVVGCEMLARWLHPQKGLLSAGNFIPAIEATGLGGALLRGLADEVCGDGQDLARSaG 87
Cdd:PRK11829 410 LLQAIENHDFTLFLQPQWDMKRQQVIGAEALLRWCQPDGSYVLPSGFVHFAEEEGMMVPLGNWVLEEACRILADWKAR-G 488

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446467900  88 RRLMMTLNLSLSLVMTPLFRPHLLALSIRLEQAGMTPVFEITEREDIRAFPQAA-VFRQLAAGGLRFAVDDFGTGHAG 164
Cdd:PRK11829 489 VSLPLSVNISGLQVQNKQFLPHLKTLISHYHIDPQQLLLEITETAQIQDLDEALrLLRELQGLGLLIALDDFGIGYSS 566
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 8-169 2.17e-11

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 61.71  E-value: 2.17e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467900   8 LQQAIRNREFTPFYQPIVCATGGEVVGCEMLARWLHPQKGLLSAGNFIPAIEATGLGGALLRGLADEVCgdgQDLA--RS 85
Cdd:PRK11359 548 LKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLAEEIGEIENIGRWVIAEAC---RQLAewRS 624

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467900  86 AGRRL-MMTLNLSlslvmtPL-FRPHLLA--LSIRLEQAGMTP---VFEITEREDIRAFPQA-AVFRQLAAGGLRFAVDD 157
Cdd:PRK11359 625 QNIHIpALSVNLS------ALhFRSNQLPnqVSDAMQAWGIDGhqlTVEITESMMMEHDTEIfKRIQILRDMGVGLSVDD 698

                        170
                 ....*....|..
gi 446467900 158 FGTGHAGPASTV 169
Cdd:PRK11359 699 FGTGFSGLSRLV 710
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
8-163 9.39e-09

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 53.92  E-value: 9.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467900   8 LQQAIRNREFTPFYQPIVCATGgEVVGCEMLARWLHPQKGLLSAGNFIP-AIEATGLGGALLRGLADEVcgdgQDLA--R 84
Cdd:PRK10060 413 LRKALENDQLVIHYQPKITWRG-EVRSLEALVRWQSPERGLIPPLEFISyAEESGLIVPLGRWVMLDVV----RQVAkwR 487

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467900  85 SAGRRLMMTLNLSL-SLVMTPLFRphllALSIRLEQAGMTPV---FEITER----EDIRAFPQAAVFRQLAAgglRFAVD 156
Cdd:PRK10060 488 DKGINLRVAVNVSArQLADQTIFT----ALKQALQELNFEYCpidVELTESclieNEELALSVIQQFSQLGA---QVHLD 560


                 ....*..
gi 446467900 157 DFGTGHA 163
Cdd:PRK10060 561 DFGTGYS 567
 
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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