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Conserved domains on  [gi|1123914561|ref|WP_074428705|]
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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 ...
 2-79 2.90e-32

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: 116.80  E-value: 2.90e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1123914561   2 KLDRTFISGIAHVARDLSIVRSIVSLGKAFSLGIVAEGVENNEQFELLKNMNCDEFQGYYYSKPLSGDQLIDFLRGQK 79
Cdd:COG5001   600 KIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGCDYAQGYLFSRPLPAEELEALLRARA 677
 
Name Accession Description Interval E-value
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 2-79 2.90e-32

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: 116.80  E-value: 2.90e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1123914561   2 KLDRTFISGIAHVARDLSIVRSIVSLGKAFSLGIVAEGVENNEQFELLKNMNCDEFQGYYYSKPLSGDQLIDFLRGQK 79
Cdd:COG5001   600 KIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGCDYAQGYLFSRPLPAEELEALLRARA 677
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 2-70 3.86e-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: 100.70  E-value: 3.86e-28
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1123914561   2 KLDRTFISGIAHVARDLSIVRSIVSLGKAFSLGIVAEGVENNEQFELLKNMNCDEFQGYYYSKPLSGDQ 70
Cdd:cd01948   172 KIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAEE 240
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
 2-70 2.70e-24

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


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 91.12  E-value: 2.70e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1123914561    2 KLDRTFISGIAHVARDLSIVRSIVSLGKAFSLGIVAEGVENNEQFELLKNMNCDEFQGYYYSKPLSGDQ 70
Cdd:smart00052 174 KIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPLDD 242
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 2-65 3.16e-20

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: 80.05  E-value: 3.16e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1123914561   2 KLDRTFISGIAHVARDLSIVRSIVSLGKAFSLGIVAEGVENNEQFELLKNMNCDEFQGYYYSKP 65
Cdd:pfam00563 172 KIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 1-76 1.96e-17

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 74.81  E-value: 1.96e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1123914561   1 MKLDRTFISGIAHVARDLSIVRSIVSLGKAFSLGIVAEGVENNEQFELLKNMNCDEFQGYYYSKPLSGDQLIDFLR 76
Cdd:PRK11359  717 IKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRPLPAEEIPGWMS 792
 
Name Accession Description Interval E-value
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 2-79 2.90e-32

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: 116.80  E-value: 2.90e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1123914561   2 KLDRTFISGIAHVARDLSIVRSIVSLGKAFSLGIVAEGVENNEQFELLKNMNCDEFQGYYYSKPLSGDQLIDFLRGQK 79
Cdd:COG5001   600 KIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGCDYAQGYLFSRPLPAEELEALLRARA 677
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 2-70 3.86e-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: 100.70  E-value: 3.86e-28
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1123914561   2 KLDRTFISGIAHVARDLSIVRSIVSLGKAFSLGIVAEGVENNEQFELLKNMNCDEFQGYYYSKPLSGDQ 70
Cdd:cd01948   172 KIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAEE 240
EAL COG2200
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
 2-76 5.39e-27

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: 101.78  E-value: 5.39e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1123914561   2 KLDRTFISGIAHVARDLSIVRSIVSLGKAFSLGIVAEGVENNEQFELLKNMNCDEFQGYYYSKPLSGDQLIDFLR 76
Cdd:COG2200   502 KIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRPLPLEELEALLR 576
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
 2-70 2.70e-24

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


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 91.12  E-value: 2.70e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1123914561    2 KLDRTFISGIAHVARDLSIVRSIVSLGKAFSLGIVAEGVENNEQFELLKNMNCDEFQGYYYSKPLSGDQ 70
Cdd:smart00052 174 KIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPLDD 242
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 2-65 3.16e-20

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: 80.05  E-value: 3.16e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1123914561   2 KLDRTFISGIAHVARDLSIVRSIVSLGKAFSLGIVAEGVENNEQFELLKNMNCDEFQGYYYSKP 65
Cdd:pfam00563 172 KIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
YjcC COG4943
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ...
 2-80 9.61e-18

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: 75.34  E-value: 9.61e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1123914561   2 KLDRTFISGIAHVARDLSIVRSIVSLGKAFSLGIVAEGVENNEQFELLKNMNCDEFQGYYYSKPLSGDQLIDFLRGQKK 80
Cdd:COG4943   444 KIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQGWLFAKPLPAEEFIAWLAAQRA 522
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 1-76 1.96e-17

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 74.81  E-value: 1.96e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1123914561   1 MKLDRTFISGIAHVARDLSIVRSIVSLGKAFSLGIVAEGVENNEQFELLKNMNCDEFQGYYYSKPLSGDQLIDFLR 76
Cdd:PRK11359  717 IKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRPLPAEEIPGWMS 792
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
1-71 2.11e-17

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 74.72  E-value: 2.11e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1123914561   1 MKLDRTFISGIAHVARDLSIVRSIVSLGKAFSLGIVAEGVENNEQFELLKNMNCDEFQGYYYSKPLSGDQL 71
Cdd:PRK10060  580 IKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKPMPAVAF 650
PRK10551 PRK10551
cyclic di-GMP phosphodiesterase;
1-75 7.40e-12

cyclic di-GMP phosphodiesterase;


Pssm-ID: 182541 [Multi-domain]  Cd Length: 518  Bit Score: 58.85  E-value: 7.40e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1123914561   1 MKLDRTFISGIAHVARDLSIVRSIVSLGKAFSLGIVAEGVENNEQFELLKNMNCDEFQGYYYSKPLSGDQLIDFL 75
Cdd:PRK10551  436 LKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNFLQGYWISRPLPLEDFVRWL 510
PRK13561 PRK13561
putative diguanylate cyclase; Provisional
 1-70 5.20e-11

putative diguanylate cyclase; Provisional


Pssm-ID: 184143 [Multi-domain]  Cd Length: 651  Bit Score: 56.26  E-value: 5.20e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123914561   1 MKLDRTFISGIAHvarDLSIVRSIVSLGKAFSLGIVAEGVENNEQFELLKNMNCDEFQGYYYSKPLSGDQ 70
Cdd:PRK13561  576 LKIDKMFVDGLPE---DDSMVAAIIMLAQSLNLQVIAEGVETEAQRDWLLKAGVGIAQGFLFARALPIEI 642
YuxH COG3434
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ...
 22-65 6.89e-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: 55.96  E-value: 6.89e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1123914561  22 RSIVSLGKAFSLGIVAEGVENNEQFELLKNMNCDEFQGYYYSKP 65
Cdd:COG3434   148 AELVARLKRYGIKLLAEKVETREEFELCKELGFDLFQGYFFSKP 191
PRK11829 PRK11829
biofilm formation regulator HmsP; Provisional
 1-67 4.59e-08

biofilm formation regulator HmsP; Provisional


Pssm-ID: 183329 [Multi-domain]  Cd Length: 660  Bit Score: 48.01  E-value: 4.59e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1123914561   1 MKLDRTFISGIAhvaRDLSIVRSIVSLGKAFSLGIVAEGVENNEQFELLKNMNCDEFQGYYYSKPLS 67
Cdd:PRK11829  581 IKLDKSFVKNLP---EDDAIARIISCVSDVLKVRVMAEGVETEEQRQWLLEHGIQCGQGFLFSPPLP 644
PRK11596 PRK11596
cyclic-di-GMP phosphodiesterase; Provisional
 14-71 9.11e-06

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183222 [Multi-domain]  Cd Length: 255  Bit Score: 41.53  E-value: 9.11e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1123914561  14 VARDLSIV-----------RSIVSLGKAFSLGIVAEGVENNEQFELLKNMNCDEFQGYYYSKPLSGDQL 71
Cdd:PRK11596  180 VARELFIMlrqseegrnlfSQLLHLMNRYCRGVIVEGVETPEEWRDVQRSPAFAAQGYFLSRPAPFETL 248
 
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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