NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2158999856|ref|WP_230836787|]
View 

MULTISPECIES: diguanylate phosphodiesterase [Klebsiella]

Protein Classification

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 super family cl43641
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
 2-61 2.90e-10

EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) [Signal transduction mechanisms];


The actual alignment was detected with superfamily member COG2200:

Pssm-ID: 441802 [Multi-domain]  Cd Length: 576  Bit Score: 53.63  E-value: 2.90e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158999856   2 DDPVKRALLVSVVKGLRGTGKPLVFEGVETPGQFEFACSLGPGYlVQGWYAGKPETISAM 61
Cdd:COG2200   513 RDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDY-AQGYLFGRPLPLEEL 571
 
Name Accession Description Interval E-value
EAL COG2200
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
 2-61 2.90e-10

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: 53.63  E-value: 2.90e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158999856   2 DDPVKRALLVSVVKGLRGTGKPLVFEGVETPGQFEFACSLGPGYlVQGWYAGKPETISAM 61
Cdd:COG2200   513 RDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDY-AQGYLFGRPLPLEEL 571
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 2-55 3.69e-09

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: 50.01  E-value: 3.69e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2158999856   2 DDPVKRALLVSVVKGLRGTGKPLVFEGVETPGQFEFACSLGPgYLVQGWYAGKP 55
Cdd:pfam00563 183 KDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGC-DLVQGYYFSKP 235
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 2-55 4.58e-09

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: 49.85  E-value: 4.58e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2158999856   2 DDPVKRALLVSVVKGLRGTGKPLVFEGVETPGQFEFACSLGPGYlVQGWYAGKP 55
Cdd:cd01948   183 TDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDY-VQGYLFSRP 235
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
 3-55 6.62e-06

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


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 41.05  E-value: 6.62e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2158999856    3 DPVKRALLVSVVKGLRGTGKPLVFEGVETPGQFEFACSLGPGYLvQGWYAGKP 55
Cdd:smart00052 186 DPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYG-QGYLFSRP 237
 
Name Accession Description Interval E-value
EAL COG2200
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
 2-61 2.90e-10

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: 53.63  E-value: 2.90e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158999856   2 DDPVKRALLVSVVKGLRGTGKPLVFEGVETPGQFEFACSLGPGYlVQGWYAGKPETISAM 61
Cdd:COG2200   513 RDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDY-AQGYLFGRPLPLEEL 571
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 2-55 3.69e-09

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: 50.01  E-value: 3.69e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2158999856   2 DDPVKRALLVSVVKGLRGTGKPLVFEGVETPGQFEFACSLGPgYLVQGWYAGKP 55
Cdd:pfam00563 183 KDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGC-DLVQGYYFSKP 235
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 2-55 4.58e-09

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: 49.85  E-value: 4.58e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2158999856   2 DDPVKRALLVSVVKGLRGTGKPLVFEGVETPGQFEFACSLGPGYlVQGWYAGKP 55
Cdd:cd01948   183 TDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDY-VQGYLFSRP 235
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
 3-55 6.62e-06

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


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 41.05  E-value: 6.62e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2158999856    3 DPVKRALLVSVVKGLRGTGKPLVFEGVETPGQFEFACSLGPGYLvQGWYAGKP 55
Cdd:smart00052 186 DPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYG-QGYLFSRP 237
YuxH COG3434
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ...
 10-63 2.69e-05

c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction mechanisms];


Pssm-ID: 442660 [Multi-domain]  Cd Length: 407  Bit Score: 39.40  E-value: 2.69e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2158999856  10 LVSVVKGLRGTGKPLVFEGVETPGQFEFACSLGPGYLvQGWYAGKPETISAMNI 63
Cdd:COG3434   147 LAELVARLKRYGIKLLAEKVETREEFELCKELGFDLF-QGYFFSKPEILKGKKL 199
 
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