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Conserved domains on  [gi|505806740|ref|WP_015704499|]
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MULTISPECIES: EAL domain-containing protein [Klebsiella]

Protein Classification

EAL domain-containing protein( domain architecture ID 1000813)

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 super family cl29561
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 12-228 4.96e-35

EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues and is also known as domain of unknown function 2 (DUF2). The EAL domain has been shown to stimulate degradation of a second messenger, cyclic di-GMP, and is a good candidate for a diguanylate phosphodiesterase function. Together with the GGDEF domain, EAL might be involved in regulating cell surface adhesiveness in bacteria.


The actual alignment was detected with superfamily member PRK11596:

Pssm-ID: 453023 [Multi-domain]  Cd Length: 255  Bit Score: 125.11  E-value: 4.96e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505806740  12 RYVFQPMFNREGKMIAVECLTRFAHhePASPQDI---ERFFSEASESLRARILLEQIELVRQHQQWFRQNDVMVTLNVDE 88
Cdd:PRK11596  31 AYTFQPIYRTSGRLMAIELLTAVTH--PSNPSQRlspERYFAEITVSHRLDVVKEQLDLLAQWADFFVRHGLLASVNIDG 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505806740  89 STLHMLHDDfiAECVKTIGC---LHFEVNEfsNTLVKRTPTIDALTDKYSFWLDDFGAGYAGFAALTAQPFRFIKTDKNL 165
Cdd:PRK11596 109 PTLIALRQQ--PAILRLIERlpwLRFELVE--HIRLPKDSPFASMCEFGPLWLDDFGTGMANFSALSEVRYDYIKVAREL 184

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505806740 166 LWSLLEKKNGQQLMDSLLHYFqaNQY--QVIVEGIETEAHLQWLENMPWFALQG-LLWREQTIEAL 228
Cdd:PRK11596 185 FIMLRQSEEGRNLFSQLLHLM--NRYcrGVIVEGVETPEEWRDVQRSPAFAAQGyFLSRPAPFETL 248
 
Name Accession Description Interval E-value
PRK11596 PRK11596
cyclic-di-GMP phosphodiesterase; Provisional
 12-228 4.96e-35

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183222 [Multi-domain]  Cd Length: 255  Bit Score: 125.11  E-value: 4.96e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505806740  12 RYVFQPMFNREGKMIAVECLTRFAHhePASPQDI---ERFFSEASESLRARILLEQIELVRQHQQWFRQNDVMVTLNVDE 88
Cdd:PRK11596  31 AYTFQPIYRTSGRLMAIELLTAVTH--PSNPSQRlspERYFAEITVSHRLDVVKEQLDLLAQWADFFVRHGLLASVNIDG 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505806740  89 STLHMLHDDfiAECVKTIGC---LHFEVNEfsNTLVKRTPTIDALTDKYSFWLDDFGAGYAGFAALTAQPFRFIKTDKNL 165
Cdd:PRK11596 109 PTLIALRQQ--PAILRLIERlpwLRFELVE--HIRLPKDSPFASMCEFGPLWLDDFGTGMANFSALSEVRYDYIKVAREL 184

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505806740 166 LWSLLEKKNGQQLMDSLLHYFqaNQY--QVIVEGIETEAHLQWLENMPWFALQG-LLWREQTIEAL 228
Cdd:PRK11596 185 FIMLRQSEEGRNLFSQLLHLM--NRYcrGVIVEGVETPEEWRDVQRSPAFAAQGyFLSRPAPFETL 248
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 11-220 1.98e-33

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: 120.50  E-value: 1.98e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505806740   11 LRYVFQPMFN-REGKMIAVECLTRFAH--HEPASPqdiERFFSEAsESLRARILLEQIEL---VRQHQQWFRQNDVMVTL 84
Cdd:pfam00563  13 FVLYYQPIVDlRTGRVVGYEALLRWQHpdGGLISP---ARFLPLA-EELGLIAELDRWVLeqaLADLAQLQLGPDIKLSI 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505806740   85 NVDESTLHM--LHDDFIAECVKTI---GCLHFEVNEfsNTLVKRTPTIDALTDK-----YSFWLDDFGAGYAGFAALTAQ 154
Cdd:pfam00563  89 NLSPASLADpgFLELLRALLKQAGpppSRLVLEITE--SDLLARLEALREVLKRlralgIRIALDDFGTGYSSLSYLLRL 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505806740  155 PFRFIKTDKNLLWSLLEKKNGQQLMDSLLHYFQANQYQVIVEGIETEAHLQWLENMPWFALQGLLW 220
Cdd:pfam00563 167 PPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYF 232
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 11-219 5.28e-28

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: 106.48  E-value: 5.28e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505806740  11 LRYVFQPMFN-REGKMIAVECLTRFAH--HEPASPQDierFFSEASES-----LRARILLEQIELVRQHQQwfRQNDVMV 82
Cdd:cd01948   12 FELYYQPIVDlRTGRIVGYEALLRWRHpeGGLISPAE---FIPLAEETgliveLGRWVLEEACRQLARWQA--GGPDLRL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505806740  83 TLNVdeSTLHMLHDDFIAECVKTI-------GCLHFEVNEfsNTLVKRTPTIDALTDKY-----SFWLDDFGAGYAGFAA 150
Cdd:cd01948   87 SVNL--SARQLRDPDFLDRLLELLaetglppRRLVLEITE--SALIDDLEEALATLRRLralgvRIALDDFGTGYSSLSY 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505806740 151 LTAQPFRFIKTDKNLLWSLLEKKNGQQLMDSLLHYFQANQYQVIVEGIETEAHLQWLENMPWFALQGLL 219
Cdd:cd01948  163 LKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYL 231
EAL COG2200
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
 11-233 9.06e-28

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: 110.64  E-value: 9.06e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505806740  11 LRYVFQPMFN-REGKMIAVECLTRFAHHEPA--SPqdiERFFSEASES-LRARILLEQIELV-RQHQQWFRQN-DVMVTL 84
Cdd:COG2200  342 LRLYYQPIVDlRTGRVVGYEALLRWRHPDGGliSP---AEFIPAAERSgLIVELDRWVLERAlRQLARWPERGlDLRLSV 418

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505806740  85 NVdeSTLHMLHDDFIAECVKTI-------GCLHFEVNEfsNTLVKRTPTIDALTDKY-----SFWLDDFGAGYAGFAALT 152
Cdd:COG2200  419 NL--SARSLLDPDFLERLLELLaeyglppERLVLEITE--SALLEDLEAAIELLARLralgvRIALDDFGTGYSSLSYLK 494

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505806740 153 AQPFRFIKTDKNLLWSLLEKKNGQQLMDSLLHYFQANQYQVIVEGIETEAHLQWLENMPWFALQG-LLWREQTIEALVAS 231
Cdd:COG2200  495 RLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGyLFGRPLPLEELEAL 574


                 ..
gi 505806740 232 VE 233
Cdd:COG2200  575 LR 576
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
 10-220 1.69e-25

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


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 99.98  E-value: 1.69e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505806740    10 GLRYVFQPMFN-REGKMIAVECLTRFAH--HEPASPQdieRFFSEASES-LRARILLEQIELV-RQHQQWFRQN--DVMV 82
Cdd:smart00052  12 QFLLYYQPIVSlRTGRLVGVEALIRWQHpeGGIISPD---EFIPLAEETgLIVPLGRWVLEQAcQQLAEWQAQGppPLLI 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505806740    83 TLNVDESTLHmlHDDFIAECVKTI-------GCLHFEVNE--FSNTLVKRTPTIDALTDK-YSFWLDDFGAGYAGFAALT 152
Cdd:smart00052  89 SINLSARQLI--SPDLVPRVLELLeetglppQRLELEITEsvLLDDDESAVATLQRLRELgVRIALDDFGTGYSSLSYLK 166

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505806740   153 AQPFRFIKTDKNLLWSLLEKKNGQQLMDSLLHYFQANQYQVIVEGIETEAHLQWLENMPWFALQGLLW 220
Cdd:smart00052 167 RLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLF 234
 
Name Accession Description Interval E-value
PRK11596 PRK11596
cyclic-di-GMP phosphodiesterase; Provisional
 12-228 4.96e-35

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183222 [Multi-domain]  Cd Length: 255  Bit Score: 125.11  E-value: 4.96e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505806740  12 RYVFQPMFNREGKMIAVECLTRFAHhePASPQDI---ERFFSEASESLRARILLEQIELVRQHQQWFRQNDVMVTLNVDE 88
Cdd:PRK11596  31 AYTFQPIYRTSGRLMAIELLTAVTH--PSNPSQRlspERYFAEITVSHRLDVVKEQLDLLAQWADFFVRHGLLASVNIDG 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505806740  89 STLHMLHDDfiAECVKTIGC---LHFEVNEfsNTLVKRTPTIDALTDKYSFWLDDFGAGYAGFAALTAQPFRFIKTDKNL 165
Cdd:PRK11596 109 PTLIALRQQ--PAILRLIERlpwLRFELVE--HIRLPKDSPFASMCEFGPLWLDDFGTGMANFSALSEVRYDYIKVAREL 184

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505806740 166 LWSLLEKKNGQQLMDSLLHYFqaNQY--QVIVEGIETEAHLQWLENMPWFALQG-LLWREQTIEAL 228
Cdd:PRK11596 185 FIMLRQSEEGRNLFSQLLHLM--NRYcrGVIVEGVETPEEWRDVQRSPAFAAQGyFLSRPAPFETL 248
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 11-220 1.98e-33

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: 120.50  E-value: 1.98e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505806740   11 LRYVFQPMFN-REGKMIAVECLTRFAH--HEPASPqdiERFFSEAsESLRARILLEQIEL---VRQHQQWFRQNDVMVTL 84
Cdd:pfam00563  13 FVLYYQPIVDlRTGRVVGYEALLRWQHpdGGLISP---ARFLPLA-EELGLIAELDRWVLeqaLADLAQLQLGPDIKLSI 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505806740   85 NVDESTLHM--LHDDFIAECVKTI---GCLHFEVNEfsNTLVKRTPTIDALTDK-----YSFWLDDFGAGYAGFAALTAQ 154
Cdd:pfam00563  89 NLSPASLADpgFLELLRALLKQAGpppSRLVLEITE--SDLLARLEALREVLKRlralgIRIALDDFGTGYSSLSYLLRL 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505806740  155 PFRFIKTDKNLLWSLLEKKNGQQLMDSLLHYFQANQYQVIVEGIETEAHLQWLENMPWFALQGLLW 220
Cdd:pfam00563 167 PPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYF 232
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 11-219 5.28e-28

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: 106.48  E-value: 5.28e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505806740  11 LRYVFQPMFN-REGKMIAVECLTRFAH--HEPASPQDierFFSEASES-----LRARILLEQIELVRQHQQwfRQNDVMV 82
Cdd:cd01948   12 FELYYQPIVDlRTGRIVGYEALLRWRHpeGGLISPAE---FIPLAEETgliveLGRWVLEEACRQLARWQA--GGPDLRL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505806740  83 TLNVdeSTLHMLHDDFIAECVKTI-------GCLHFEVNEfsNTLVKRTPTIDALTDKY-----SFWLDDFGAGYAGFAA 150
Cdd:cd01948   87 SVNL--SARQLRDPDFLDRLLELLaetglppRRLVLEITE--SALIDDLEEALATLRRLralgvRIALDDFGTGYSSLSY 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505806740 151 LTAQPFRFIKTDKNLLWSLLEKKNGQQLMDSLLHYFQANQYQVIVEGIETEAHLQWLENMPWFALQGLL 219
Cdd:cd01948  163 LKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYL 231
EAL COG2200
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
 11-233 9.06e-28

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: 110.64  E-value: 9.06e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505806740  11 LRYVFQPMFN-REGKMIAVECLTRFAHHEPA--SPqdiERFFSEASES-LRARILLEQIELV-RQHQQWFRQN-DVMVTL 84
Cdd:COG2200  342 LRLYYQPIVDlRTGRVVGYEALLRWRHPDGGliSP---AEFIPAAERSgLIVELDRWVLERAlRQLARWPERGlDLRLSV 418

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505806740  85 NVdeSTLHMLHDDFIAECVKTI-------GCLHFEVNEfsNTLVKRTPTIDALTDKY-----SFWLDDFGAGYAGFAALT 152
Cdd:COG2200  419 NL--SARSLLDPDFLERLLELLaeyglppERLVLEITE--SALLEDLEAAIELLARLralgvRIALDDFGTGYSSLSYLK 494

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505806740 153 AQPFRFIKTDKNLLWSLLEKKNGQQLMDSLLHYFQANQYQVIVEGIETEAHLQWLENMPWFALQG-LLWREQTIEALVAS 231
Cdd:COG2200  495 RLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGyLFGRPLPLEELEAL 574


                 ..
gi 505806740 232 VE 233
Cdd:COG2200  575 LR 576
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
 10-220 1.69e-25

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


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 99.98  E-value: 1.69e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505806740    10 GLRYVFQPMFN-REGKMIAVECLTRFAH--HEPASPQdieRFFSEASES-LRARILLEQIELV-RQHQQWFRQN--DVMV 82
Cdd:smart00052  12 QFLLYYQPIVSlRTGRLVGVEALIRWQHpeGGIISPD---EFIPLAEETgLIVPLGRWVLEQAcQQLAEWQAQGppPLLI 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505806740    83 TLNVDESTLHmlHDDFIAECVKTI-------GCLHFEVNE--FSNTLVKRTPTIDALTDK-YSFWLDDFGAGYAGFAALT 152
Cdd:smart00052  89 SINLSARQLI--SPDLVPRVLELLeetglppQRLELEITEsvLLDDDESAVATLQRLRELgVRIALDDFGTGYSSLSYLK 166

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505806740   153 AQPFRFIKTDKNLLWSLLEKKNGQQLMDSLLHYFQANQYQVIVEGIETEAHLQWLENMPWFALQGLLW 220
Cdd:smart00052 167 RLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLF 234
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 11-210 2.27e-15

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: 74.81  E-value: 2.27e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505806740  11 LRYVFQPMFN-REGKMIAVECLTRFAH--HEPASPqdiERFFSEASES-LRARI---LLEQIelVRQHQQWFRQN--DVM 81
Cdd:COG5001  439 LELHYQPQVDlATGRIVGAEALLRWQHpeRGLVSP---AEFIPLAEETgLIVPLgewVLREA--CRQLAAWQDAGlpDLR 513

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505806740  82 VTLNVdeSTLHMLHDDFIAEcVKTI--------GCLHFEVNEfsNTLVKRTP----TIDALTDK-YSFWLDDFGAGYAGF 148
Cdd:COG5001  514 VAVNL--SARQLRDPDLVDR-VRRAlaetglppSRLELEITE--SALLEDPEealeTLRALRALgVRIALDDFGTGYSSL 588

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505806740 149 AALTAQPFRFIKTDKNLLWSLLEKKNGQQLMDSLLHYFQANQYQVIVEGIETEAHLQWLENM 210
Cdd:COG5001  589 SYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLREL 650
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 11-220 1.00e-09

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 57.86  E-value: 1.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505806740  11 LRYVFQP-MFNREGKMIAVECLTRF--AHHEPASPQdieRFFSEASESLRarilLEQI------ELVRQHQQWFRQNDVM 81
Cdd:PRK11359 557 LKLVYQPqIFAETGELYGIEALARWhdPLHGHVPPS---RFIPLAEEIGE----IENIgrwviaEACRQLAEWRSQNIHI 629

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505806740  82 VTLNVDESTLHMLHDD---FIAECVKTIG----CLHFEVNE-----FSNTLVKRTPTIDALTDKYSfwLDDFGAGYAGFA 149
Cdd:PRK11359 630 PALSVNLSALHFRSNQlpnQVSDAMQAWGidghQLTVEITEsmmmeHDTEIFKRIQILRDMGVGLS--VDDFGTGFSGLS 707

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505806740 150 ALTAQPFRFIKTDKNLLWSLLEKKNGQQLMDSLLHYFQANQYQVIVEGIETEAHLQWLENMPWFALQGLLW 220
Cdd:PRK11359 708 RLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRVIQGYFF 778
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
15-202 3.63e-07

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 50.45  E-value: 3.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505806740  15 FQPMFNREGKMIAVECLTRFAHHEPA--SPQDierFFSEASESLRARILLEQIEL--VRQHQQWFRQN-DVMVTLNV--- 86
Cdd:PRK10060 426 YQPKITWRGEVRSLEALVRWQSPERGliPPLE---FISYAEESGLIVPLGRWVMLdvVRQVAKWRDKGiNLRVAVNVsar 502

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505806740  87 ---DESTLH----MLHDDFIAECV----KTIGCLhFEVNEFSNTLVKRTPTIDAltdkySFWLDDFGAGYAGFAALTAQP 155
Cdd:PRK10060 503 qlaDQTIFTalkqALQELNFEYCPidveLTESCL-IENEELALSVIQQFSQLGA-----QVHLDDFGTGYSSLSQLARFP 576

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 505806740 156 FRFIKTDKNLLWSLLEKKNGQQLMDSLLHYFQANQYQVIVEGIETEA 202
Cdd:PRK10060 577 IDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAEGVETAK 623
PRK13561 PRK13561
putative diguanylate cyclase; Provisional
 16-222 1.65e-06

putative diguanylate cyclase; Provisional


Pssm-ID: 184143 [Multi-domain]  Cd Length: 651  Bit Score: 48.17  E-value: 1.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505806740  16 QPMFN-REGKMIAVECLTRFAHHEP--ASPQD-IERFFSEASESLRARILLEqiELVRQHQQWfRQNDVMVTLNVDESTL 91
Cdd:PRK13561 419 QPQVEmRSGKLVSAEALLRMQQPDGswDLPEGlIDRIESCGLMVTVGHWVLE--ESCRLLAAW-QERGIMLPLSVNLSAL 495

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505806740  92 HMLHDDFIAECVKTI-------GCLHFEVNEfsntlvkrTPTIDALTDKYSFW-----------LDDFGAGYAGFAALT- 152
Cdd:PRK13561 496 QLMHPNMVADMLELLtryriqpGTLILEVTE--------SRRIDDPHAAVAILrplrnagvrvaLDDFGMGYAGLRQLQh 567

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505806740 153 --AQPFRFIKTDKNLLWSLLEKKNGQQLMDSLLhyfQANQYQVIVEGIETEAHLQWLENMPWFALQGLLWRE 222
Cdd:PRK13561 568 mkSLPIDVLKIDKMFVDGLPEDDSMVAAIIMLA---QSLNLQVIAEGVETEAQRDWLLKAGVGIAQGFLFAR 636
PRK11829 PRK11829
biofilm formation regulator HmsP; Provisional
 15-207 2.34e-04

biofilm formation regulator HmsP; Provisional


Pssm-ID: 183329 [Multi-domain]  Cd Length: 660  Bit Score: 41.85  E-value: 2.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505806740  15 FQPMFN-REGKMIAVECLTRFaHHEPASPQDIERFFSEASESLRARILLEQI--ELVRQHQQWFRQNdVMVTLNVDESTL 91
Cdd:PRK11829 423 LQPQWDmKRQQVIGAEALLRW-CQPDGSYVLPSGFVHFAEEEGMMVPLGNWVleEACRILADWKARG-VSLPLSVNISGL 500

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505806740  92 HMLHDDFIAEcVKTI--------GCLHFEVNE--FSNTLVKRTPTIDALTDK-YSFWLDDFGAGYAGFAAL---TAQPFR 157
Cdd:PRK11829 501 QVQNKQFLPH-LKTLishyhidpQQLLLEITEtaQIQDLDEALRLLRELQGLgLLIALDDFGIGYSSLRYLnhlKSLPIH 579

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 505806740 158 FIKTDKNLLWSLLEKKNGQQLMDSLLHYFQAnqyQVIVEGIETEAHLQWL 207
Cdd:PRK11829 580 MIKLDKSFVKNLPEDDAIARIISCVSDVLKV---RVMAEGVETEEQRQWL 626
PRK10551 PRK10551
cyclic di-GMP phosphodiesterase;
14-230 4.38e-03

cyclic di-GMP phosphodiesterase;


Pssm-ID: 182541 [Multi-domain]  Cd Length: 518  Bit Score: 37.66  E-value: 4.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505806740  14 VFQPMFN-REGKMIAVECLTRFAH-HEPASPQDIerFFSEAsESLRARILLEQ--IELVRQHQQWFRQN-DVMVTLNVDE 88
Cdd:PRK10551 280 EYQPVVDtQTLRVTGLEALLRWRHpTAGEIPPDA--FINYA-EAQKLIVPLTQhlFELIARDAAELQKVlPVGAKLGINI 356

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505806740  89 STLHMLHDDFIAECVKTIGCL---HFE-VNEfsntLVKRTPTIDALTDKYSFWL---------DDFGAGYAGFAALTAQP 155
Cdd:PRK10551 357 SPAHLHSDSFKADVQRLLASLpadHFQiVLE----ITERDMVQEEEATKLFAWLhsqgieiaiDDFGTGHSALIYLERFT 432

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505806740 156 FRFIKTDKNLLWSLLEKKNGQQLMDSLLHYFQANQYQVIVEGIETEAHLQWLENMPWFALQG-LLWREQTIEALVA 230
Cdd:PRK10551 433 LDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNFLQGyWISRPLPLEDFVR 508
 
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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