NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|499407585|ref|WP_011095052|]
View 

EAL domain-containing protein [Pectobacterium atrosepticum]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 14-239 3.02e-52

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: 169.26  E-value: 3.02e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499407585  14 RLTAEFQPIIHLPKNKIFRYEALARFYNSEGALTPTQQTIDKIEKCQAIDKVTDFMFDVVCQVIK----NKNSMTISFNL 89
Cdd:cd01948   11 EFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLArwqaGGPDLRLSVNL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499407585  90 SHLLFNNTLYLESLYQKCLSNNVSPQNIEIEISEKTTRQQLIDGIPFLNQAKKYGFMISLDDFGAGNLQIDSLSLFNFDT 169
Cdd:cd01948   91 SARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSLSYLKRLPVDY 170

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499407585 170 IKIDRSIIDGIGKEETKSQKLKVLLNKLIPLGVNIICEGVEKATDLNRLNKYHPIGIQGYIFYRPLTFSQ 239
Cdd:cd01948  171 LKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAEE 240
 
Name Accession Description Interval E-value
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 14-239 3.02e-52

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: 169.26  E-value: 3.02e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499407585  14 RLTAEFQPIIHLPKNKIFRYEALARFYNSEGALTPTQQTIDKIEKCQAIDKVTDFMFDVVCQVIK----NKNSMTISFNL 89
Cdd:cd01948   11 EFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLArwqaGGPDLRLSVNL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499407585  90 SHLLFNNTLYLESLYQKCLSNNVSPQNIEIEISEKTTRQQLIDGIPFLNQAKKYGFMISLDDFGAGNLQIDSLSLFNFDT 169
Cdd:cd01948   91 SARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSLSYLKRLPVDY 170

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499407585 170 IKIDRSIIDGIGKEETKSQKLKVLLNKLIPLGVNIICEGVEKATDLNRLNKYHPIGIQGYIFYRPLTFSQ 239
Cdd:cd01948  171 LKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAEE 240
EAL COG2200
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
 14-241 1.08e-46

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: 163.03  E-value: 1.08e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499407585  14 RLTAEFQPIIHLPKNKIFRYEALARFYNSEGALTPTQQTIDKIEKCQAIDKVTDFMFDVVCQVIKNKN----SMTISFNL 89
Cdd:COG2200  341 ELRLYYQPIVDLRTGRVVGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELDRWVLERALRQLARWPerglDLRLSVNL 420

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499407585  90 SHLLFNNTLYLESLYQKCLSNNVSPQNIEIEISEKTTRQQLIDGIPFLNQAKKYGFMISLDDFGAGNLQIDSLSLFNFDT 169
Cdd:COG2200  421 SARSLLDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRIALDDFGTGYSSLSYLKRLPPDY 500

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499407585 170 IKIDRSIIDGIGKEETKSQKLKVLLNKLIPLGVNIICEGVEKATDLNRLNKYHPIGIQGYIFYRPLTFSQLR 241
Cdd:COG2200  501 LKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRPLPLEELE 572
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 14-234 7.89e-42

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: 142.46  E-value: 7.89e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499407585   14 RLTAEFQPIIHLPKNKIFRYEALARFYNSEGALTPTQQTIDKIEKCQAIDKVTDFMFDVVCQVIKNK---NSMTISFNLS 90
Cdd:pfam00563  12 EFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLqlgPDIKLSINLS 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499407585   91 HLLFNNTLYLESLYQKCLSNNVSPQNIEIEISEKTTRQQLIDGIPFLNQAKKYGFMISLDDFGAGNLQIDSLSLFNFDTI 170
Cdd:pfam00563  92 PASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSLSYLLRLPPDFV 171

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499407585  171 KIDRSIIDGIGKEETKSQKLKVLLNKLIPLGVNIICEGVEKATDLNRLNKYHPIGIQGYIFYRP 234
Cdd:pfam00563 172 KIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
 19-237 9.86e-31

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


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 113.85  E-value: 9.86e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499407585    19 FQPIIHLPKNKIFRYEALARFYNSEGALTPTQQTIDKIEKCQAIDKVTDFMFDVVCQVI-----KNKNSMTISFNLSHLL 93
Cdd:smart00052  17 YQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLaewqaQGPPPLLISINLSARQ 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499407585    94 FNNTLYLESLYQKCLSNNVSPQNIEIEISEKTTRQQLIDGIPFLNQAKKYGFMISLDDFGAGNLQIDSLSLFNFDTIKID 173
Cdd:smart00052  97 LISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYSSLSYLKRLPVDLLKID 176

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499407585   174 RSIIDGIGKEETKSQKLKVLLNKLIPLGVNIICEGVEKATDLNRLNKYHPIGIQGYIFYRPLTF 237
Cdd:smart00052 177 KSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPL 240
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 8-235 1.79e-16

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 78.27  E-value: 1.79e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499407585   8 IDGEILRLtaEFQPIIHLPKNKIFRYEALARFYNSEGALTPTQQTIDKIEKCQAIDKVTDFMFDVVCQVI-----KNKNS 82
Cdd:PRK11359 552 ISNNQLKL--VYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLAEEIGEIENIGRWVIAEACRQLaewrsQNIHI 629

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499407585  83 MTISFNLSHLLFNNTLYLESLYQKCLSNNVSPQNIEIEISEKTTRQQLIDGIPFLNQAKKYGFMISLDDFGAGNLQIDSL 162
Cdd:PRK11359 630 PALSVNLSALHFRSNQLPNQVSDAMQAWGIDGHQLTVEITESMMMEHDTEIFKRIQILRDMGVGLSVDDFGTGFSGLSRL 709

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499407585 163 SLFNFDTIKIDRSIIDGIGKEEtksqKLKVLLNKLIPLGVN----IICEGVEKATDLNRLNKYHPIGIQGYIFYRPL 235
Cdd:PRK11359 710 VSLPVTEIKIDKSFVDRCLTEK----RILALLEAITSIGQSlnltVVAEGVETKEQFEMLRKIHCRVIQGYFFSRPL 782
 
Name Accession Description Interval E-value
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 14-239 3.02e-52

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: 169.26  E-value: 3.02e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499407585  14 RLTAEFQPIIHLPKNKIFRYEALARFYNSEGALTPTQQTIDKIEKCQAIDKVTDFMFDVVCQVIK----NKNSMTISFNL 89
Cdd:cd01948   11 EFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLArwqaGGPDLRLSVNL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499407585  90 SHLLFNNTLYLESLYQKCLSNNVSPQNIEIEISEKTTRQQLIDGIPFLNQAKKYGFMISLDDFGAGNLQIDSLSLFNFDT 169
Cdd:cd01948   91 SARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSLSYLKRLPVDY 170

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499407585 170 IKIDRSIIDGIGKEETKSQKLKVLLNKLIPLGVNIICEGVEKATDLNRLNKYHPIGIQGYIFYRPLTFSQ 239
Cdd:cd01948  171 LKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAEE 240
EAL COG2200
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
 14-241 1.08e-46

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: 163.03  E-value: 1.08e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499407585  14 RLTAEFQPIIHLPKNKIFRYEALARFYNSEGALTPTQQTIDKIEKCQAIDKVTDFMFDVVCQVIKNKN----SMTISFNL 89
Cdd:COG2200  341 ELRLYYQPIVDLRTGRVVGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELDRWVLERALRQLARWPerglDLRLSVNL 420

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499407585  90 SHLLFNNTLYLESLYQKCLSNNVSPQNIEIEISEKTTRQQLIDGIPFLNQAKKYGFMISLDDFGAGNLQIDSLSLFNFDT 169
Cdd:COG2200  421 SARSLLDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRIALDDFGTGYSSLSYLKRLPPDY 500

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499407585 170 IKIDRSIIDGIGKEETKSQKLKVLLNKLIPLGVNIICEGVEKATDLNRLNKYHPIGIQGYIFYRPLTFSQLR 241
Cdd:COG2200  501 LKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRPLPLEELE 572
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 14-234 7.89e-42

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: 142.46  E-value: 7.89e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499407585   14 RLTAEFQPIIHLPKNKIFRYEALARFYNSEGALTPTQQTIDKIEKCQAIDKVTDFMFDVVCQVIKNK---NSMTISFNLS 90
Cdd:pfam00563  12 EFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLqlgPDIKLSINLS 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499407585   91 HLLFNNTLYLESLYQKCLSNNVSPQNIEIEISEKTTRQQLIDGIPFLNQAKKYGFMISLDDFGAGNLQIDSLSLFNFDTI 170
Cdd:pfam00563  92 PASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSLSYLLRLPPDFV 171

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499407585  171 KIDRSIIDGIGKEETKSQKLKVLLNKLIPLGVNIICEGVEKATDLNRLNKYHPIGIQGYIFYRP 234
Cdd:pfam00563 172 KIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
YjcC COG4943
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ...
 14-243 9.47e-34

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: 127.34  E-value: 9.47e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499407585  14 RLTAEFQPIIHLPKNKIFRYEALARFYNSEGALTPTQQTIDKIEKCQAIDKVTDFMFDVV----CQVIKNKNSMTISFNL 89
Cdd:COG4943  284 EFYVHYQPIVDLKTGRCVGAEALVRWRDPDGSVISPDIFIPLAEQSGLISPLTRQVIEQVfrdlGDLLAADPDFHISINL 363

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499407585  90 S--HLLfnNTLYLESLYQKCLSNNVSPQNIEIEISEKTTrqqlIDG---IPFLNQAKKYGFMISLDDFGAG--NLQidSL 162
Cdd:COG4943  364 SasDLL--SPRFLDDLERLLARTGVAPQQIVLEITERGF----IDPakaRAVIAALREAGHRIAIDDFGTGysSLS--YL 435

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499407585 163 SLFNFDTIKIDRSIIDGIGKEETKSqklkvllnKLIP--------LGVNIICEGVEKATDLNRLNKYHPIGIQGYIFYRP 234
Cdd:COG4943  436 QTLPVDILKIDKSFVDAIGTDSANS--------AVVPhiiemaktLNLDVVAEGVETEEQADYLRARGVQYGQGWLFAKP 507


                 ....*....
gi 499407585 235 LTFSQLRLL 243
Cdd:COG4943  508 LPAEEFIAW 516
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
 19-237 9.86e-31

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


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 113.85  E-value: 9.86e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499407585    19 FQPIIHLPKNKIFRYEALARFYNSEGALTPTQQTIDKIEKCQAIDKVTDFMFDVVCQVI-----KNKNSMTISFNLSHLL 93
Cdd:smart00052  17 YQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLaewqaQGPPPLLISINLSARQ 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499407585    94 FNNTLYLESLYQKCLSNNVSPQNIEIEISEKTTRQQLIDGIPFLNQAKKYGFMISLDDFGAGNLQIDSLSLFNFDTIKID 173
Cdd:smart00052  97 LISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYSSLSYLKRLPVDLLKID 176

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499407585   174 RSIIDGIGKEETKSQKLKVLLNKLIPLGVNIICEGVEKATDLNRLNKYHPIGIQGYIFYRPLTF 237
Cdd:smart00052 177 KSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPL 240
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 19-241 3.20e-28

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: 112.56  E-value: 3.20e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499407585  19 FQPIIHLPKNKIFRYEALARFYNSE-GALTPTQqTIDKIEKCQAIDKVTDFMFDVVCQVIK-----NKNSMTISFNLSHL 92
Cdd:COG5001  443 YQPQVDLATGRIVGAEALLRWQHPErGLVSPAE-FIPLAEETGLIVPLGEWVLREACRQLAawqdaGLPDLRVAVNLSAR 521

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499407585  93 LFNNTLYLESLYQKCLSNNVSPQNIEIEISEKTTRQQLIDGIPFLNQAKKYGFMISLDDFGAGNlqiDSLSL---FNFDT 169
Cdd:COG5001  522 QLRDPDLVDRVRRALAETGLPPSRLELEITESALLEDPEEALETLRALRALGVRIALDDFGTGY---SSLSYlkrLPVDT 598

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499407585 170 IKIDRSIIDGIGKEETKsqklKVLLNKLIP----LGVNIICEGVEKATDLNRLNKYHPIGIQGYIFYRPLTFSQLR 241
Cdd:COG5001  599 LKIDRSFVRDLAEDPDD----AAIVRAIIAlahsLGLEVVAEGVETEEQLEFLRELGCDYAQGYLFSRPLPAEELE 670
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 8-235 1.79e-16

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 78.27  E-value: 1.79e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499407585   8 IDGEILRLtaEFQPIIHLPKNKIFRYEALARFYNSEGALTPTQQTIDKIEKCQAIDKVTDFMFDVVCQVI-----KNKNS 82
Cdd:PRK11359 552 ISNNQLKL--VYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLAEEIGEIENIGRWVIAEACRQLaewrsQNIHI 629

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499407585  83 MTISFNLSHLLFNNTLYLESLYQKCLSNNVSPQNIEIEISEKTTRQQLIDGIPFLNQAKKYGFMISLDDFGAGNLQIDSL 162
Cdd:PRK11359 630 PALSVNLSALHFRSNQLPNQVSDAMQAWGIDGHQLTVEITESMMMEHDTEIFKRIQILRDMGVGLSVDDFGTGFSGLSRL 709

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499407585 163 SLFNFDTIKIDRSIIDGIGKEEtksqKLKVLLNKLIPLGVN----IICEGVEKATDLNRLNKYHPIGIQGYIFYRPL 235
Cdd:PRK11359 710 VSLPVTEIKIDKSFVDRCLTEK----RILALLEAITSIGQSlnltVVAEGVETKEQFEMLRKIHCRVIQGYFFSRPL 782
PRK13561 PRK13561
putative diguanylate cyclase; Provisional
 20-239 8.91e-15

putative diguanylate cyclase; Provisional


Pssm-ID: 184143 [Multi-domain]  Cd Length: 651  Bit Score: 73.21  E-value: 8.91e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499407585  20 QPIIHLPKNKIFRYEALARFYNSEGALTPTQQTIDKIEKCQAIDKVTDFMFDVVCQVI----KNKNSMTISFNLSHLLFN 95
Cdd:PRK13561 419 QPQVEMRSGKLVSAEALLRMQQPDGSWDLPEGLIDRIESCGLMVTVGHWVLEESCRLLaawqERGIMLPLSVNLSALQLM 498

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499407585  96 NTLYLESLYQKCLSNNVSPQNIEIEISEktTRQqlID----GIPFLNQAKKYGFMISLDDFGAG--NL-QIDSLSLFNFD 168
Cdd:PRK13561 499 HPNMVADMLELLTRYRIQPGTLILEVTE--SRR--IDdphaAVAILRPLRNAGVRVALDDFGMGyaGLrQLQHMKSLPID 574

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499407585 169 TIKIDRSIIDGIGKEETKSQKLKVLLNKlipLGVNIICEGVEKATDLNRLNKyhpIGI---QGYIFYRPLTFSQ 239
Cdd:PRK13561 575 VLKIDKMFVDGLPEDDSMVAAIIMLAQS---LNLQVIAEGVETEAQRDWLLK---AGVgiaQGFLFARALPIEI 642
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
15-235 1.20e-12

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 67.01  E-value: 1.20e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499407585  15 LTAEFQPIIHLpKNKIFRYEALARFYNSEGALTPTQQTIDKIEKCQAIDKVTDF-MFDVVCQVIKNKN---SMTISFNLS 90
Cdd:PRK10060 422 LVIHYQPKITW-RGEVRSLEALVRWQSPERGLIPPLEFISYAEESGLIVPLGRWvMLDVVRQVAKWRDkgiNLRVAVNVS 500

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499407585  91 HLLFNNTLYLESLYQKCLSNNVSPQNIEIEISEKTtrqqLID----GIPFLNQAKKYGFMISLDDFGAGNLQIDSLSLFN 166
Cdd:PRK10060 501 ARQLADQTIFTALKQALQELNFEYCPIDVELTESC----LIEneelALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFP 576

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499407585 167 FDTIKIDRSIIDGIGKeETKSQKLK---VLLNKLIPLGVniICEGVEKATDLNRLNKyhpIGI---QGYIFYRPL 235
Cdd:PRK10060 577 IDAIKLDQSFVRDIHK-QPVSQSLVraiVAVAQALNLQV--IAEGVETAKEDAFLTK---NGVnerQGFLFAKPM 645
PRK11829 PRK11829
biofilm formation regulator HmsP; Provisional
 19-236 2.06e-12

biofilm formation regulator HmsP; Provisional


Pssm-ID: 183329 [Multi-domain]  Cd Length: 660  Bit Score: 66.12  E-value: 2.06e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499407585  19 FQPIIHLPKNKIFRYEALARFYNSEGALTPTQQTIDKIEKCQAIDKVTDFMFDVVCQVIKNKN----SMTISFNLSHLLF 94
Cdd:PRK11829 423 LQPQWDMKRQQVIGAEALLRWCQPDGSYVLPSGFVHFAEEEGMMVPLGNWVLEEACRILADWKargvSLPLSVNISGLQV 502

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499407585  95 NNTLYLESLYQKCLSNNVSPQNIEIEISEKTTRQQLIDGIPFLNQAKKYGFMISLDDFGAGNLQIDSL---SLFNFDTIK 171
Cdd:PRK11829 503 QNKQFLPHLKTLISHYHIDPQQLLLEITETAQIQDLDEALRLLRELQGLGLLIALDDFGIGYSSLRYLnhlKSLPIHMIK 582

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499407585 172 IDRSIIDGIGKEETKSQKLKVLLNKlipLGVNIICEGVEKATDLNRLNKYHPIGIQGYIFYRPLT 236
Cdd:PRK11829 583 LDKSFVKNLPEDDAIARIISCVSDV---LKVRVMAEGVETEEQRQWLLEHGIQCGQGFLFSPPLP 644
PRK10551 PRK10551
cyclic di-GMP phosphodiesterase;
18-240 9.91e-11

cyclic di-GMP phosphodiesterase;


Pssm-ID: 182541 [Multi-domain]  Cd Length: 518  Bit Score: 61.16  E-value: 9.91e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499407585  18 EFQPIIHLPKNKIFRYEALARF-YNSEGALTPtQQTIDKIEKCQAIDKVTDFMFDVVCQ-VIKNKNSM----TISFNLS- 90
Cdd:PRK10551 280 EYQPVVDTQTLRVTGLEALLRWrHPTAGEIPP-DAFINYAEAQKLIVPLTQHLFELIARdAAELQKVLpvgaKLGINISp 358

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499407585  91 -HLLFNNtlYLESLYQkcLSNNVSPQNIEI--EISEKTTRQQL--IDGIPFLNQAkkyGFMISLDDFGAGNLQIDSLSLF 165
Cdd:PRK10551 359 aHLHSDS--FKADVQR--LLASLPADHFQIvlEITERDMVQEEeaTKLFAWLHSQ---GIEIAIDDFGTGHSALIYLERF 431

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499407585 166 NFDTIKIDRSIIDGIGKEETKSQKLKVLLNKLIPLGVNIICEGVEKATDLNRLNKYHPIGIQGYIFYRPLTFSQL 240
Cdd:PRK10551 432 TLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNFLQGYWISRPLPLEDF 506
PRK11596 PRK11596
cyclic-di-GMP phosphodiesterase; Provisional
 149-243 4.05e-07

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183222 [Multi-domain]  Cd Length: 255  Bit Score: 49.61  E-value: 4.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499407585 149 LDDFGAGNLQIDSLSLFNFDTIKIDRSIIDGIgkeeTKSQKLKVLLNKLIPL------GVniICEGVEKATDLNRLNKYH 222
Cdd:PRK11596 157 LDDFGTGMANFSALSEVRYDYIKVARELFIML----RQSEEGRNLFSQLLHLmnrycrGV--IVEGVETPEEWRDVQRSP 230

                         90       100
                 ....*....|....*....|.
gi 499407585 223 PIGIQGYIFYRPLTFSQLRLL 243
Cdd:PRK11596 231 AFAAQGYFLSRPAPFETLETL 251
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 33-245 1.28e-06

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 48.90  E-value: 1.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499407585   33 YEALARFYNSEGALTPTQQTIDKIEK---CQAIDK--VTDFMFDVVCQVikNKNSMTISFNLSHLLFNNTLYLESLYQKC 107
Cdd:PRK09776  873 WLISLRLWDPEGEIIDEGAFRPAAEDpalMHALDRrvIHEFFRQAAKAV--ASKGLSIALPLSVAGLSSPTLLPFLLEQL 950

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499407585  108 LSNNVSPQNIEIEISEKTTRQQLIDGIPFLNQAKKYGFMISLDDFGAGNLQIDSLSLFNFDTIKIDR------------- 174
Cdd:PRK09776  951 ENSPLPPRLLHLEITETALLNHAESASRLVQKLRLAGCRVVLSDFGRGLSSFNYLKAFMADYLKLDGelvanlhgnlmde 1030

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499407585  175 ---SIIDGIGKEetksqklkvllnklipLGVNIICEGVEKATDLNRLNKYHPIGIQGYIFYRPLTFSqlRLLEG 245
Cdd:PRK09776 1031 mliSIIQGHAQR----------------LGMKTIAGPVELPLVLDTLSGIGVDLAYGYAIARPQPLD--LLLNS 1086
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH