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Conserved domains on  [gi|1724176689|ref|WP_146983530|]
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EAL domain-containing protein, partial [Lujinxingia vulgaris]

Protein Classification

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 ...
 108-158 2.80e-14

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 cd01948:

Pssm-ID: 453023 [Multi-domain]  Cd Length: 240  Bit Score: 67.96  E-value: 2.80e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1724176689 108 LQEALRGQWLEFWYQPKIDLETLDVVGAESLARIRHPERGVLAPAVFLPEA 158
Cdd:cd01948     3 LRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLA 53
REC super family cl19078
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
 28-87 4.91e-03

phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response regulators (PRRs); Two-component systems (TCSs) involving a sensor and a response regulator are used by bacteria to adapt to changing environments. Processes regulated by two-component systems in bacteria include sporulation, pathogenicity, virulence, chemotaxis, and membrane transport. Response regulators (RRs) share the common phosphoacceptor REC domain and different effector/output domains such as DNA, RNA, ligand-binding, protein-binding, or enzymatic domains. Response regulators regulate transcription, post-transcription or post-translation, or have functions such as methylesterases, adenylate or diguanylate cyclase, c-di-GMP-specific phosphodiesterases, histidine kinases, serine/threonine protein kinases, and protein phosphatases, depending on their output domains. The function of some output domains are still unknown. TCSs are found in all three domains of life - bacteria, archaea, and eukaryotes, however, the presence and abundance of particular RRs vary between the lineages. Archaea encode very few RRs with DNA-binding output domains; most are stand-alone REC domains. Among eukaryotes, TCSs are found primarily in protozoa, fungi, algae, and green plants. REC domains function as phosphorylation-mediated switches within RRs, but some also transfer phosphoryl groups in multistep phosphorelays.


The actual alignment was detected with superfamily member cd17530:

Pssm-ID: 473134 [Multi-domain]  Cd Length: 123  Bit Score: 35.11  E-value: 4.91e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724176689  28 VEIFQMLSQRSFIGRTILMSGHGAPVLEHARRIGQRSGIMIGGILRKPFRQQDLRDLLSS 87
Cdd:cd17530    61 IEFLRHLAESHSNAAVILMSGLDGGILESAETLAGANGLNLLGTLSKPFSPEELTELLTK 120
 
Name Accession Description Interval E-value
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 108-158 2.80e-14

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: 67.96  E-value: 2.80e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1724176689 108 LQEALRGQWLEFWYQPKIDLETLDVVGAESLARIRHPERGVLAPAVFLPEA 158
Cdd:cd01948     3 LRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLA 53
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 108-158 2.10e-13

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: 66.72  E-value: 2.10e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1724176689 108 LQEALRGQWLEFWYQPKIDLETLDVVGAESLARIRHPERGVLAPAVFLPEA 158
Cdd:COG5001   430 LRRALERGELELHYQPQVDLATGRIVGAEALLRWQHPERGLVSPAEFIPLA 480
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 108-169 1.35e-12

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: 63.11  E-value: 1.35e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1724176689 108 LQEALRGQWLEFWYQPKIDLETLDVVGAESLARIRHPERGVLAPAVFLPEA-GTDALHALTLQ 169
Cdd:pfam00563   4 LRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAeELGLIAELDRW 66
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
 107-158 6.29e-11

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


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 58.77  E-value: 6.29e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1724176689  107 LLQEAL-RGQwLEFWYQPKIDLETLDVVGAESLARIRHPERGVLAPAVFLPEA 158
Cdd:smart00052   3 ELRQALeNGQ-FLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLA 54
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 106-158 4.61e-06

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 45.53  E-value: 4.61e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1724176689 106 ALLQEALRGQWLEFWYQPKIDLETLDVVGAESLARIRHPERGVLAPAVFLPEA 158
Cdd:PRK11359  546 AALKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLA 598
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
 28-87 4.91e-03

phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR from some pathogens contains an N-terminal phosphoreceiver (REC) domain and a C-terminal EAL domain that possesses c-di-GMP specific phosphodiesterase activity. The RocR REC domain is phosphorylated and modulates its EAL domain enzymatic activity, regulating the local level of c-di-GMP. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381086 [Multi-domain]  Cd Length: 123  Bit Score: 35.11  E-value: 4.91e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724176689  28 VEIFQMLSQRSFIGRTILMSGHGAPVLEHARRIGQRSGIMIGGILRKPFRQQDLRDLLSS 87
Cdd:cd17530    61 IEFLRHLAESHSNAAVILMSGLDGGILESAETLAGANGLNLLGTLSKPFSPEELTELLTK 120
 
Name Accession Description Interval E-value
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 108-158 2.80e-14

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: 67.96  E-value: 2.80e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1724176689 108 LQEALRGQWLEFWYQPKIDLETLDVVGAESLARIRHPERGVLAPAVFLPEA 158
Cdd:cd01948     3 LRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLA 53
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 108-158 2.10e-13

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: 66.72  E-value: 2.10e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1724176689 108 LQEALRGQWLEFWYQPKIDLETLDVVGAESLARIRHPERGVLAPAVFLPEA 158
Cdd:COG5001   430 LRRALERGELELHYQPQVDLATGRIVGAEALLRWQHPERGLVSPAEFIPLA 480
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 108-169 1.35e-12

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: 63.11  E-value: 1.35e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1724176689 108 LQEALRGQWLEFWYQPKIDLETLDVVGAESLARIRHPERGVLAPAVFLPEA-GTDALHALTLQ 169
Cdd:pfam00563   4 LRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAeELGLIAELDRW 66
EAL COG2200
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
 106-158 1.03e-11

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: 62.11  E-value: 1.03e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1724176689 106 ALLQEALRGQWLEFWYQPKIDLETLDVVGAESLARIRHPERGVLAPAVFLPEA 158
Cdd:COG2200   331 SELREALEEGELRLYYQPIVDLRTGRVVGYEALLRWRHPDGGLISPAEFIPAA 383
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
 107-158 6.29e-11

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


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 58.77  E-value: 6.29e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1724176689  107 LLQEAL-RGQwLEFWYQPKIDLETLDVVGAESLARIRHPERGVLAPAVFLPEA 158
Cdd:smart00052   3 ELRQALeNGQ-FLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLA 54
YjcC COG4943
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ...
 105-158 9.58e-09

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: 53.38  E-value: 9.58e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1724176689 105 PALLQEALRGQWLEFWYQPKIDLETLDVVGAESLARIRHPERGVLAPAVFLPEA 158
Cdd:COG4943   273 RRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRDPDGSVISPDIFIPLA 326
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 106-158 4.61e-06

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 45.53  E-value: 4.61e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1724176689 106 ALLQEALRGQWLEFWYQPKIDLETLDVVGAESLARIRHPERGVLAPAVFLPEA 158
Cdd:PRK11359  546 AALKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLA 598
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
108-158 2.49e-05

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 43.52  E-value: 2.49e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1724176689 108 LQEALRGQWLEFWYQPKIDLeTLDVVGAESLARIRHPERGVLAPAVFLPEA 158
Cdd:PRK10060  413 LRKALENDQLVIHYQPKITW-RGEVRSLEALVRWQSPERGLIPPLEFISYA 462
PRK11829 PRK11829
biofilm formation regulator HmsP; Provisional
 91-158 3.62e-04

biofilm formation regulator HmsP; Provisional


Pssm-ID: 183329 [Multi-domain]  Cd Length: 660  Bit Score: 39.93  E-value: 3.62e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1724176689  91 PARSDETEATSSGEPALLQeALRGQWLEFWYQPKIDLETLDVVGAESLARIRHPERGVLAPAVFLPEA 158
Cdd:PRK11829  394 PHLIEKTHKRLTQENDLLQ-AIENHDFTLFLQPQWDMKRQQVIGAEALLRWCQPDGSYVLPSGFVHFA 460
PRK10551 PRK10551
cyclic di-GMP phosphodiesterase;
118-158 9.51e-04

cyclic di-GMP phosphodiesterase;


Pssm-ID: 182541 [Multi-domain]  Cd Length: 518  Bit Score: 38.82  E-value: 9.51e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1724176689 118 EFW--YQPKIDLETLDVVGAESLARIRHPERGVLAPAVFLPEA 158
Cdd:PRK10551  276 QFYveYQPVVDTQTLRVTGLEALLRWRHPTAGEIPPDAFINYA 318
PRK13561 PRK13561
putative diguanylate cyclase; Provisional
 108-145 3.77e-03

putative diguanylate cyclase; Provisional


Pssm-ID: 184143 [Multi-domain]  Cd Length: 651  Bit Score: 37.00  E-value: 3.77e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1724176689 108 LQEALRGQWLEFWYQPKIDLETLDVVGAESLARIRHPE 145
Cdd:PRK13561  405 ILNALENHQFAIWLQPQVEMRSGKLVSAEALLRMQQPD 442
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
 28-87 4.91e-03

phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR from some pathogens contains an N-terminal phosphoreceiver (REC) domain and a C-terminal EAL domain that possesses c-di-GMP specific phosphodiesterase activity. The RocR REC domain is phosphorylated and modulates its EAL domain enzymatic activity, regulating the local level of c-di-GMP. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381086 [Multi-domain]  Cd Length: 123  Bit Score: 35.11  E-value: 4.91e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724176689  28 VEIFQMLSQRSFIGRTILMSGHGAPVLEHARRIGQRSGIMIGGILRKPFRQQDLRDLLSS 87
Cdd:cd17530    61 IEFLRHLAESHSNAAVILMSGLDGGILESAETLAGANGLNLLGTLSKPFSPEELTELLTK 120
 
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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