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Conserved domains on  [gi|1101977958|ref|WP_071527918|]
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MULTISPECIES: EAL domain-containing protein [Enterobacterales]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG5001 super family cl34859
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 6-102 3.63e-48

Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain [Signal transduction mechanisms];


The actual alignment was detected with superfamily member COG5001:

Pssm-ID: 444025 [Multi-domain]  Cd Length: 678  Bit Score: 162.25  E-value: 3.63e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101977958   6 FGTGYSSLNYLREFPFDAIKLDRTFISGIAHVARDLSIVRSIVSLGKAFSLGIVAEGVENNEQFELLKNMNCDEFQGYYY 85
Cdd:COG5001   581 FGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGCDYAQGYLF 660

                          90
                  ....*....|....*..
gi 1101977958  86 SKPLSGDQLIDFLRGQK 102
Cdd:COG5001   661 SRPLPAEELEALLRARA 677
 
Name Accession Description Interval E-value
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 6-102 3.63e-48

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: 162.25  E-value: 3.63e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101977958   6 FGTGYSSLNYLREFPFDAIKLDRTFISGIAHVARDLSIVRSIVSLGKAFSLGIVAEGVENNEQFELLKNMNCDEFQGYYY 85
Cdd:COG5001   581 FGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGCDYAQGYLF 660

                          90
                  ....*....|....*..
gi 1101977958  86 SKPLSGDQLIDFLRGQK 102
Cdd:COG5001   661 SRPLPAEELEALLRARA 677
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 5-93 5.69e-44

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: 142.30  E-value: 5.69e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101977958   5 HFGTGYSSLNYLREFPFDAIKLDRTFISGIAHVARDLSIVRSIVSLGKAFSLGIVAEGVENNEQFELLKNMNCDEFQGYY 84
Cdd:cd01948   152 DFGTGYSSLSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYL 231


                  ....*....
gi 1101977958  85 YSKPLSGDQ 93
Cdd:cd01948   232 FSRPLPAEE 240
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
 5-93 5.72e-39

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


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 129.64  E-value: 5.72e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101977958    5 HFGTGYSSLNYLREFPFDAIKLDRTFISGIAHVARDLSIVRSIVSLGKAFSLGIVAEGVENNEQFELLKNMNCDEFQGYY 84
Cdd:smart00052 154 DFGTGYSSLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYL 233


                   ....*....
gi 1101977958   85 YSKPLSGDQ 93
Cdd:smart00052 234 FSRPLPLDD 242
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 4-88 2.76e-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: 115.11  E-value: 2.76e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101977958   4 SHFGTGYSSLNYLREFPFDAIKLDRTFISGIAHVARDLSIVRSIVSLGKAFSLGIVAEGVENNEQFELLKNMNCDEFQGY 83
Cdd:pfam00563 151 DDFGTGYSSLSYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGY 230


                  ....*
gi 1101977958  84 YYSKP 88
Cdd:pfam00563 231 YFSKP 235
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
6-94 8.70e-29

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 108.23  E-value: 8.70e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101977958   6 FGTGYSSLNYLREFPFDAIKLDRTFISGIAHVARDLSIVRSIVSLGKAFSLGIVAEGVENNEQFELLKNMNCDEFQGYYY 85
Cdd:PRK10060  562 FGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNERQGFLF 641


                  ....*....
gi 1101977958  86 SKPLSGDQL 94
Cdd:PRK10060  642 AKPMPAVAF 650
 
Name Accession Description Interval E-value
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 6-102 3.63e-48

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: 162.25  E-value: 3.63e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101977958   6 FGTGYSSLNYLREFPFDAIKLDRTFISGIAHVARDLSIVRSIVSLGKAFSLGIVAEGVENNEQFELLKNMNCDEFQGYYY 85
Cdd:COG5001   581 FGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGCDYAQGYLF 660

                          90
                  ....*....|....*..
gi 1101977958  86 SKPLSGDQLIDFLRGQK 102
Cdd:COG5001   661 SRPLPAEELEALLRARA 677
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 5-93 5.69e-44

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: 142.30  E-value: 5.69e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101977958   5 HFGTGYSSLNYLREFPFDAIKLDRTFISGIAHVARDLSIVRSIVSLGKAFSLGIVAEGVENNEQFELLKNMNCDEFQGYY 84
Cdd:cd01948   152 DFGTGYSSLSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYL 231


                  ....*....
gi 1101977958  85 YSKPLSGDQ 93
Cdd:cd01948   232 FSRPLPAEE 240
EAL COG2200
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
 5-99 3.67e-41

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: 142.23  E-value: 3.67e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101977958   5 HFGTGYSSLNYLREFPFDAIKLDRTFISGIAHVARDLSIVRSIVSLGKAFSLGIVAEGVENNEQFELLKNMNCDEFQGYY 84
Cdd:COG2200   482 DFGTGYSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYL 561

                          90
                  ....*....|....*
gi 1101977958  85 YSKPLSGDQLIDFLR 99
Cdd:COG2200   562 FGRPLPLEELEALLR 576
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
 5-93 5.72e-39

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


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 129.64  E-value: 5.72e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101977958    5 HFGTGYSSLNYLREFPFDAIKLDRTFISGIAHVARDLSIVRSIVSLGKAFSLGIVAEGVENNEQFELLKNMNCDEFQGYY 84
Cdd:smart00052 154 DFGTGYSSLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYL 233


                   ....*....
gi 1101977958   85 YSKPLSGDQ 93
Cdd:smart00052 234 FSRPLPLDD 242
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 4-88 2.76e-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: 115.11  E-value: 2.76e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101977958   4 SHFGTGYSSLNYLREFPFDAIKLDRTFISGIAHVARDLSIVRSIVSLGKAFSLGIVAEGVENNEQFELLKNMNCDEFQGY 83
Cdd:pfam00563 151 DDFGTGYSSLSYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGY 230


                  ....*
gi 1101977958  84 YYSKP 88
Cdd:pfam00563 231 YFSKP 235
YjcC COG4943
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ...
 6-103 3.86e-31

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: 114.24  E-value: 3.86e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101977958   6 FGTGYSSLNYLREFPFDAIKLDRTFISGIAHVARDLSIVRSIVSLGKAFSLGIVAEGVENNEQFELLKNMNCDEFQGYYY 85
Cdd:COG4943   425 FGTGYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQGWLF 504

                          90
                  ....*....|....*...
gi 1101977958  86 SKPLSGDQLIDFLRGQKK 103
Cdd:COG4943   505 AKPLPAEEFIAWLAAQRA 522
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
6-94 8.70e-29

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 108.23  E-value: 8.70e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101977958   6 FGTGYSSLNYLREFPFDAIKLDRTFISGIAHVARDLSIVRSIVSLGKAFSLGIVAEGVENNEQFELLKNMNCDEFQGYYY 85
Cdd:PRK10060  562 FGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNERQGFLF 641


                  ....*....
gi 1101977958  86 SKPLSGDQL 94
Cdd:PRK10060  642 AKPMPAVAF 650
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 6-99 1.18e-23

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 93.68  E-value: 1.18e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101977958   6 FGTGYSSLNYLREFPFDAIKLDRTFISGIAHVARDLSIVRSIVSLGKAFSLGIVAEGVENNEQFELLKNMNCDEFQGYYY 85
Cdd:PRK11359  699 FGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRVIQGYFF 778

                          90
                  ....*....|....
gi 1101977958  86 SKPLSGDQLIDFLR 99
Cdd:PRK11359  779 SRPLPAEEIPGWMS 792
PRK10551 PRK10551
cyclic di-GMP phosphodiesterase;
6-98 1.10e-20

cyclic di-GMP phosphodiesterase;


Pssm-ID: 182541 [Multi-domain]  Cd Length: 518  Bit Score: 85.04  E-value: 1.10e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101977958   6 FGTGYSSLNYLREFPFDAIKLDRTFISGIAHVARDLSIVRSIVSLGKAFSLGIVAEGVENNEQFELLKNMNCDEFQGYYY 85
Cdd:PRK10551  418 FGTGHSALIYLERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNFLQGYWI 497

                          90
                  ....*....|...
gi 1101977958  86 SKPLSGDQLIDFL 98
Cdd:PRK10551  498 SRPLPLEDFVRWL 510
PRK13561 PRK13561
putative diguanylate cyclase; Provisional
 6-93 1.14e-18

putative diguanylate cyclase; Provisional


Pssm-ID: 184143 [Multi-domain]  Cd Length: 651  Bit Score: 79.37  E-value: 1.14e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101977958   6 FGTGYSSLNYLREF---PFDAIKLDRTFISGIAHvarDLSIVRSIVSLGKAFSLGIVAEGVENNEQFELLKNMNCDEFQG 82
Cdd:PRK13561  555 FGMGYAGLRQLQHMkslPIDVLKIDKMFVDGLPE---DDSMVAAIIMLAQSLNLQVIAEGVETEAQRDWLLKAGVGIAQG 631

                          90
                  ....*....|.
gi 1101977958  83 YYYSKPLSGDQ 93
Cdd:PRK13561  632 FLFARALPIEI 642
PRK11829 PRK11829
biofilm formation regulator HmsP; Provisional
 6-90 3.87e-16

biofilm formation regulator HmsP; Provisional


Pssm-ID: 183329 [Multi-domain]  Cd Length: 660  Bit Score: 72.28  E-value: 3.87e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101977958   6 FGTGYSSLNYLR---EFPFDAIKLDRTFISGIahvARDLSIVRSIVSLGKAFSLGIVAEGVENNEQFELLKNMNCDEFQG 82
Cdd:PRK11829  560 FGIGYSSLRYLNhlkSLPIHMIKLDKSFVKNL---PEDDAIARIISCVSDVLKVRVMAEGVETEEQRQWLLEHGIQCGQG 636


                  ....*...
gi 1101977958  83 YYYSKPLS 90
Cdd:PRK11829  637 FLFSPPLP 644
YuxH COG3434
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ...
 22-88 2.21e-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: 58.27  E-value: 2.21e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1101977958  22 DAIKLDrtfisgIAHVARDLsiVRSIVSLGKAFSLGIVAEGVENNEQFELLKNMNCDEFQGYYYSKP 88
Cdd:COG3434   133 DIIKID------VLALDLEE--LAELVARLKRYGIKLLAEKVETREEFELCKELGFDLFQGYFFSKP 191
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 4-88 3.50e-10

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 55.06  E-value: 3.50e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101977958    4 SHFGTGYSSLNYLREFPFDAIKLDRTFISGIAHVARDLSIVRSIVSLGKAFSLGIVAEGVENNEQFELLKNMNCDEFQGY 83
Cdd:PRK09776   993 SDFGRGLSSFNYLKAFMADYLKLDGELVANLHGNLMDEMLISIIQGHAQRLGMKTIAGPVELPLVLDTLSGIGVDLAYGY 1072


                   ....*
gi 1101977958   84 YYSKP 88
Cdd:PRK09776  1073 AIARP 1077
PRK11596 PRK11596
cyclic-di-GMP phosphodiesterase; Provisional
 6-94 5.63e-08

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183222 [Multi-domain]  Cd Length: 255  Bit Score: 48.46  E-value: 5.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101977958   6 FGTG---YSSLNYLRefpFDAIKldrtfisgiahVARDLSIV-----------RSIVSLGKAFSLGIVAEGVENNEQFEL 71
Cdd:PRK11596  160 FGTGmanFSALSEVR---YDYIK-----------VARELFIMlrqseegrnlfSQLLHLMNRYCRGVIVEGVETPEEWRD 225

                          90       100
                  ....*....|....*....|...
gi 1101977958  72 LKNMNCDEFQGYYYSKPLSGDQL 94
Cdd:PRK11596  226 VQRSPAFAAQGYFLSRPAPFETL 248
PRK11059 PRK11059
regulatory protein CsrD; Provisional
 12-88 9.14e-03

regulatory protein CsrD; Provisional


Pssm-ID: 236833 [Multi-domain]  Cd Length: 640  Bit Score: 34.07  E-value: 9.14e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1101977958  12 SLNYLREFPFDAIKLDRTFISGIAHVARDLSIVRSIVSLGKAFSLGIVAEGVENNEQFELLKNMNCDEFQGYYYSKP 88
Cdd:PRK11059  560 STSYIKELNVELIKLHPSLVRNIHKRTENQLFVRSLVGACAGTETQVFATGVESREEWQTLQELGVSGGQGDFFAES 636
 
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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