2ETJ,3O3G


Conserved Protein Domain Family
RNase_HII_bacteria_HII_like

?
cd07182: RNase_HII_bacteria_HII_like 
Click on image for an interactive view with Cn3D
Bacterial Ribonuclease HII-like
This family includes mostly bacterial type 2 RNases H, with some eukaryotic members. Bacterial RNase HII has a role in primer removal based on its involvement in ribonucleotide-specific catalytic activity in the presence of RNA/DNA hybrid substrates. Several bacteria, such as Bacillus subtilis, have two different type II RNases H, RNases HII and HIII; double deletion of these leads to cellular lethality. It appears that type I and type II RNases H also have overlapping functions in cells, as over-expression of Escherichia coli RNase HII can complement an RNase HI deletion phenotype. In Leishmania mitochondria, of the four distinct RNase H genes (H1, HIIA, HIIB, HIIC), HIIC is essential for the survival of the parasite and thus can be a potential target for anti-leishmanial chemotherapy. Ribonuclease H (RNase H) is classified into two families, type I (prokaryotic RNase HI, eukaryotic RNase H1 and viral RNase H) and type II (prokaryotic RNase HII and HIII, and eukaryotic RNase H2). RNase H endonucleolytically hydrolyzes an RNA strand when it is annealed to a complementary DNA strand in the presence of divalent cations, in DNA replication and repair.
Statistics
?
PSSM-Id: 260003
Aligned: 489 rows
Threshold Bit Score: 143.28
Created: 23-Jan-2009
Updated: 2-Oct-2020
Structure
?
Program:
Drawing:
Aligned Rows:
 
active siteRNA/DNA hybrid
Conserved site includes 4 residues -Click on image for an interactive view with Cn3D
Feature 1: active site [active site], 4 residue positions
Conserved feature residue pattern:D E D [DE]Click to see conserved feature residue pattern help
Evidence:
  • Comment:The four conserved carboxylates are directly involved in coordinating the metal ion
  • Structure:2ETJ; Thermotoga maritima RNase HII binds magnesium ion.
  • Structure:3O3G: Thermotoga maritima RNase HII binds 3 calcium ions.
  • Comment:This structure was solved in presence of Ca2+ ions, which also interact with the same active site residues.

Sequence Alignment
?
Format: Row Display: Color Bits: Type Selection:
Feature 1          ##                                                                           
2ETJ_A       27 AGVDEAGRGCLAGPVVAAAVVLEKEIe--GINDSKQLSPAKRERLLDEIXE-KAAVGIGIASPEEIDLyNIFNATKLAXN 103 Thermotoga maritima
ZP_02077392  20 VGIDEAGRGPIAGPLVVAAVSFPDDYdddEIYDSKKLSEKKRELLFRKIIKeAREYHILIVDTKTIDTeNIYRATQNAMQ 99  Eubacterium doli...
ADN69376     16 VGLDEAGRGCCAGPLVVGCVIMPQNFnhpLIKDSKQLSQKQREEALEIILEnAIETVTTIINAQEVDQlNPKQASRIGMQ 95  Mycoplasma ferme...
EGV00198     16 LGLDEAGRGCCAGPLVVAGVIFNKNYvnlDINDSKKLNSKKREELFKIIKRdALAYKIVVYDANYVDLfNPKQTSRNGML 95  Mycoplasma colum...
ADE19425     16 LGMDEAGRGALAGPLVVAGVIFPANYkndEINDSKKLTSKQRENLFFKIQEdAIAYEIIELSNFEVDElNPKKASIVGME 95  Mycoplasma croco...
EFW03887     20 IGLDEAGRGPMAGPLVVAGVIFEKGYyheAINDSKQLSEKKRESLYDLIIRdALAYQIEIIDVEDVDRlNVYQASKKGMI 99  Coprobacillus sp...
EFY09304     20 VGIDEAGRGPMAGPCVVSGVIFPKGYydaRINDSKQLSEKQRDELVSNIESnALWTFTEIIPVDIIDRdNIYRATQNAMK 99  Erysipelothrix r...
EFE46786     20 IGIDEAGRGPIAGPLVVAAVSFPVGFsheSIYDSKKLSEKKRKALFQEIIQlASEYHIKIVSPQIIDEqNIYRATQLAML 99  Erysipelotrichac...
EGS29246     23 IGVDEVGRGCIAGPMVVASVILPKNYvnnNIDDSKKLTKNKREAIYQQILKdCLFYKIVFIDVEQVEKlNPKQSSIFGMQ 102 Mycoplasma anati...
EFF41260     16 LGLDEVGRDSLAGPIVVACVMFPKNYhnpLIKDSKELTKDQRDIAYKEIIKdAITYKYIFLDKDFVDLhNPKKSSIIGME 95  Mycoplasma allig...
Feature 1                       #                   #                                           
2ETJ_A      104 RALENLs-vKPSFVLVDGKGIELs---VPGTCLVKGDQKSKLIGAASIVAKVFRDRLXSEFHrxYPQFSFHKHKGYATKE 179 Thermotoga maritima
ZP_02077392 100 RLCDEFq--MIDGVLTDAMPLPFc--kQDCISLVKGDQKSVSIAAASILAKVTRDHIMMAYDlqYPQYGFAKHKGYPTKV 175 Eubacterium doli...
ADN69376     96 RCINKLn-tKPELVITDFEKINDi--nIPQINLVKGDQLSINVAAASILAKVTRDLIMVGIDkkFPMYNFKKNKGYCTKE 172 Mycoplasma ferme...
EGV00198     96 KIVKEIe-lRPNLIITDFEKIDQt--dIKQINLVKGDSKSISVAAASILAKVFRDQLMENYDqkYPQYNFKRHKGYATKD 172 Mycoplasma colum...
ADE19425     96 KIANLLa-dKYDVVITDFEKLNLq--dKKQINLVKGDTISISVAAASILAKHYRDQVMRKLHlkYPMFSWDKNKGYGTKL 172 Mycoplasma croco...
EFW03887    100 DAIHHIa-iQPDFALSDAMPLGDe---IAHNAIIKGDSLSMSIGAASILAKVTRDRIMKKYDlqYPEYGFAQHKGYPTKQ 175 Coprobacillus sp...
EFY09304    100 KIAIES---KADIVLTDAMPLDDi--aIPVEAIVKGDARSLSIAAASILAKTVRDGLMKVYDleFPEYGFAKHKGYGTKQ 174 Erysipelothrix r...
EFE46786    100 ELSNSFh--DADGVLTDAMPLPNa--sLDVISLVKGDQKSVSIAAASILAKVTRDCIMCAYDkqYPQYGFAKHKGYPTKG 175 Erysipelotrichac...
EGS29246    103 KAIIPFl-dKIDLILTDFEKINLgndnIKEINLVKGDSKSLTIAAASILAKVTRDNFMSELSktYPEFKWDDNYGYGTKA 181 Mycoplasma anati...
EFF41260     96 KLIDSYeldQIDYVITDYEKVNTk---FQSRAIKFGDKYSITIAAASIVAKVIRDEYMDKMSleYPIYAFDKNKGYGTKV 172 Mycoplasma allig...
Feature 1                            
2ETJ_A      180 HLNEIRKNGVLP-IHRLSFEP 199 Thermotoga maritima
ZP_02077392 176 HLEALHRYGVIDgLYRHSYGP 196 Eubacterium dolichum DSM 3991
ADN69376    173 HEAAMSQYGICE-FHRKSYKN 192 Mycoplasma fermentans JER
EGV00198    173 HQNVLEAFGPSP-IHRLTYKN 192 Mycoplasma columbinum SF7
ADE19425    173 HLEGLRKNGVSP-FHRLSYKP 192 Mycoplasma crocodyli MP145
EFW03887    176 HKELLKMYGVTP-IHRRSFQP 195 Coprobacillus sp. 29_1
EFY09304    175 HKEAILKFGRCP-IHRKSFRF 194 Erysipelothrix rhusiopathiae ATCC 19414
EFE46786    176 HLEAMHTYGVINdIYRKSYGP 196 Erysipelotrichaceae bacterium 5_2_54FAA
EGS29246    182 HIEAIKKHGYTQ-FHRKTFEP 201 Mycoplasma anatis 1340
EFF41260    173 HLEALKKYGPSP-IHRISYKP 192 Mycoplasma alligatoris A21JP2

| Disclaimer | Privacy statement | Accessibility |
NCBI Home NCBI Search NCBI SiteMap