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Conserved domains on  [gi|527037749|ref|WP_020884402|]
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MULTISPECIES: EAL domain-containing protein [Enterobacter]

Protein Classification

EAL domain-containing protein( domain architecture ID 1000813)

EAL domain-containing protein may act as a cyclic diguanylate phosphodiesterase

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 ...
23-202 1.73e-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.


The actual alignment was detected with superfamily member PRK11596:

Pssm-ID: 453023 [Multi-domain]  Cd Length: 255  Bit Score: 56.16  E-value: 1.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037749  23 GELKGLEVLvnfTGVgTH-----VRIPTELVIPRLSAEEELALFNEKLQLLDTCKLFFIQHQLIAWINITPVIVEFLLSN 97
Cdd:PRK11596  42 GRLMAIELL---TAV-THpsnpsQRLSPERYFAEITVSHRLDVVKEQLDLLAQWADFFVRHGLLASVNIDGPTLIALRQQ 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037749  98 GNAVSILERYPFLEFTVNENYPGLNngkdDLQLARMAIHFPLVLANFGAGAASLKAVYDGLFKRVILDKG-FIQQRASEL 176
Cdd:PRK11596 118 PAILRLIERLPWLRFELVEHIRLPK----DSPFASMCEFGPLWLDDFGTGMANFSALSEVRYDYIKVARElFIMLRQSEE 193
                        170       180
                 ....*....|....*....|....*.
gi 527037749 177 SFEPFMrAILWQITPHCQSVLVGGID 202
Cdd:PRK11596 194 GRNLFS-QLLHLMNRYCRGVIVEGVE 218
 
Name Accession Description Interval E-value
PRK11596 PRK11596
cyclic-di-GMP phosphodiesterase; Provisional
23-202 1.73e-09

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183222 [Multi-domain]  Cd Length: 255  Bit Score: 56.16  E-value: 1.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037749  23 GELKGLEVLvnfTGVgTH-----VRIPTELVIPRLSAEEELALFNEKLQLLDTCKLFFIQHQLIAWINITPVIVEFLLSN 97
Cdd:PRK11596  42 GRLMAIELL---TAV-THpsnpsQRLSPERYFAEITVSHRLDVVKEQLDLLAQWADFFVRHGLLASVNIDGPTLIALRQQ 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037749  98 GNAVSILERYPFLEFTVNENYPGLNngkdDLQLARMAIHFPLVLANFGAGAASLKAVYDGLFKRVILDKG-FIQQRASEL 176
Cdd:PRK11596 118 PAILRLIERLPWLRFELVEHIRLPK----DSPFASMCEFGPLWLDDFGTGMANFSALSEVRYDYIKVARElFIMLRQSEE 193
                        170       180
                 ....*....|....*....|....*.
gi 527037749 177 SFEPFMrAILWQITPHCQSVLVGGID 202
Cdd:PRK11596 194 GRNLFS-QLLHLMNRYCRGVIVEGVE 218
EAL COG2200
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
84-236 8.35e-03

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: 37.07  E-value: 8.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037749  84 INITPV------IVEFLLSngnavsILERYPF----LEFTVNENYPGLNNGKDDLQLARM-AIHFPLVLANFGAGAASLK 152
Cdd:COG2200  418 VNLSARslldpdFLERLLE------LLAEYGLpperLVLEITESALLEDLEAAIELLARLrALGVRIALDDFGTGYSSLS 491
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037749 153 AVYDGLFKRVILDKGFIQQRASELSFEPFMRAILWQITPHCQSVLVGGIDDHGLLQRVLSFNFGAMQGALW-PAVSAEHV 231
Cdd:COG2200  492 YLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFgRPLPLEEL 571

                 ....*
gi 527037749 232 TTLVQ 236
Cdd:COG2200  572 EALLR 576
 
Name Accession Description Interval E-value
PRK11596 PRK11596
cyclic-di-GMP phosphodiesterase; Provisional
23-202 1.73e-09

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183222 [Multi-domain]  Cd Length: 255  Bit Score: 56.16  E-value: 1.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037749  23 GELKGLEVLvnfTGVgTH-----VRIPTELVIPRLSAEEELALFNEKLQLLDTCKLFFIQHQLIAWINITPVIVEFLLSN 97
Cdd:PRK11596  42 GRLMAIELL---TAV-THpsnpsQRLSPERYFAEITVSHRLDVVKEQLDLLAQWADFFVRHGLLASVNIDGPTLIALRQQ 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037749  98 GNAVSILERYPFLEFTVNENYPGLNngkdDLQLARMAIHFPLVLANFGAGAASLKAVYDGLFKRVILDKG-FIQQRASEL 176
Cdd:PRK11596 118 PAILRLIERLPWLRFELVEHIRLPK----DSPFASMCEFGPLWLDDFGTGMANFSALSEVRYDYIKVARElFIMLRQSEE 193
                        170       180
                 ....*....|....*....|....*.
gi 527037749 177 SFEPFMrAILWQITPHCQSVLVGGID 202
Cdd:PRK11596 194 GRNLFS-QLLHLMNRYCRGVIVEGVE 218
EAL COG2200
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
84-236 8.35e-03

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: 37.07  E-value: 8.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037749  84 INITPV------IVEFLLSngnavsILERYPF----LEFTVNENYPGLNNGKDDLQLARM-AIHFPLVLANFGAGAASLK 152
Cdd:COG2200  418 VNLSARslldpdFLERLLE------LLAEYGLpperLVLEITESALLEDLEAAIELLARLrALGVRIALDDFGTGYSSLS 491
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037749 153 AVYDGLFKRVILDKGFIQQRASELSFEPFMRAILWQITPHCQSVLVGGIDDHGLLQRVLSFNFGAMQGALW-PAVSAEHV 231
Cdd:COG2200  492 YLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFgRPLPLEEL 571

                 ....*
gi 527037749 232 TTLVQ 236
Cdd:COG2200  572 EALLR 576
 
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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