1DCF,2RJN,3CRN,3GL9,2V0N,3LUF,1W25,3I5A,2WB4,1DZ3,2QR3,2RDM,3GT7,4HNR,2JVK,1M5T,3A0U,3CNB,5TE9,3EQZ,3KHT,4EUK,3HDG,3LTE,3F7A,4D6X,1L5Z,3EOD,1DBW,3CU5,3RQI,1A2O,2ZAY,3N53,4G97,4ML3,3KTO,5IEB,2QV0,3JTE,5LWK,3LUF,2NT4,3NHM,3ILH,1P6U,2GKG,2NT3,2JBA,1DJM,1A04,3CG0,1KRX,5U8M,5WLP,4L4U,3CG4,3C3M,2PLN,2QZJ,3LUA,2QXY,1XHF,3HDV


Conserved Protein Domain Family
REC

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cd00156: REC 
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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.
Statistics
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PSSM-Id: 381085
View PSSM: cd00156
Aligned: 239 rows
Threshold Bit Score: 42.2143
Threshold Setting Gi: 586500296
Created: 1-Nov-2000
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
Conserved site includes 3 residues -Click on image for an interactive view with Cn3D
Feature 1: metal binding site [ion binding site], 3 residue positions
Conserved feature residue pattern:[ED] [ED] [ED]Click to see conserved feature residue pattern help
Evidence:
  • Comment:signal transduction in two-component systems is mediated by metal ion dependent phosphorelay reactions between protein histidine kinases and phosphoaccepting receiver domains in response regulator proteins
  • Comment:for many receivers, Mg2+ is the preferred metal ion, but other divalent ions such as Mn2+ are also used
  • Structure:3HDG: Mg2+ is coordinated by two water molecules and Asp/Glu residues from REC domain of Wolinella succinogenes Ws1339
    View structure with Cn3D
  • Structure:2V0N: Mg2+ is coordinated by one water molecule and two Asp residues from the REC domain of Caulobacter vibrioides response regulator PleD
    View structure with Cn3D
  • Structure:3I5A: Sr2+ is coordinated by one water molecule and two Asp residues from REC domain of Pseudomonas syringae diguanylate cyclase response regulator WspR
    View structure with Cn3D

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                       ##                                                      #                    
1DCF_A                    11 LVMDENgvSRMVTKGLLVhlg-------ceVTTVSSNeeclr------vvsheHKVVFMDVCmpgvenYQIALRIHekft 77   th...
3HDG_A                    11 LIVEDDtdAREWLSTIISnhf-------peVWSAGDGeegerl-----fglhaPDVIITDIRxpklggLEXLDRIKagg- 77   Wo...
3C3M_A                     7 LVVDDSpxIVDVFVTXLErgg-------yrPITAFSGeeclea-----lnatpPDLVLLDIXxepxdgWETLERIKtdpa 74   Me...
WP_055446392               5 ILVDDNqsVLESVKAKIDtlpkd--yglqhVKSYDSSkqafqe-----ineddFDLLIVDFEmpvyngLELAKKIGe--- 74   La...
PRJNA295643:AOC36_03600    5 ALVDDNpsIHSIIRKLLNdsfavhkfelksYYSAEDLledy--------snshFSFLLLDIEmpetngIELSEKLQfln- 75   Er...
WP_015925587               8 IIIDDEqgVIDAIKANLSseys-----vdgFVTSKEGidai--------kennYDLLILDYFidsmngKQITEKIRktd- 73   [C...
WP_058495594              67 PIIDDNvdARDYRILGFDisk-------tlELIYDKGrf------------ehTPVLVVDYEmpiingIELCKKIKgn-- 125  Le...
P70955                     5 GLVDDYrvDLEKLEAIVSrmqd-----veiVFSTDSAkeayrr-----vkngdIDLLLADIEmphmsgYELADLIKshs- 73   Ba...
XP_647665                956 LVIDDNpyARDSVGFIFSsvfn-----saiVKSANSSvegvrdlkyaiatdsnFKLLLVDYHmpgcdgIEAIQMIVdnpa 1030 Di...
YP_001086808               5 LICDDDkiVRDDIANIAKesgy-----vdyVKKVKDGieaief-----iknekIDLLIIDIDmpykngIDSAEEILsid- 73   Cl...
Feature 1                                                         
1DCF_A                    78 kqrhqrPLLVALSGntdkstk-ekcmsfGLDGVLLKP 113  thale cress
3HDG_A                    78 ----akPYVIVISAfsexkyf-ikaielGVHLFLPKP 109  Wolinella succinogenes
3C3M_A                    75 ---trdIPVLXLTAkpltpee-aneygsYIEDYILKP 107  Methanoculleus marisnigri JR1
WP_055446392              75 -----gKKIIFLTSttgntk--lvinslDISGYLSKP 104  Lacinutrix mariniflava
PRJNA295643:AOC36_03600   76 ----hkIPIIFLTSyehymk---dafglNVYSYILKD 105  Erysipelothrix sp. LV19
WP_015925587              74 ----deLYIMLLTGkaeeapgletlknlDIQMYCEKS 106  [Clostridium] cellulolyticum
WP_058495594             126 -----kSYKIMLTAeadkdtv-ieafnnGLIDKFILK 156  Legionella drozanskii
P70955                    74 ----ldVDVIFVTGhggyav---hafdlNVHDYIMKP 103  Bacillus subtilis subsp. subtilis str. 168
XP_647665               1031 f-sdikIILMILPSdsfah----mnektKNITTLIKP 1062 Dictyostelium discoideum AX4
YP_001086808              74 ----kdIHIVFVTGfadysl---esfkvHPIDFVVKP 103  Clostridioides difficile 630

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