3RHI,1P51,1P51,1B8Z,1HUE,2O97,2O97,3C4I,1MUL,1RIY,4DKY


Conserved Protein Domain Family
HU

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cd13831: HU 
Click on image for an interactive view with Cn3D
histone-like DNA-binding protein HU
This subfamily includes HU and HU-like domains. HU is a conserved nucleoid-associated protein (NAP) which binds non-specifically to duplex DNA with a particular preference for targeting nicked and bent DNA. It is highly basic and contributes to chromosomal compaction and maintenance of negative supercoiling, thus often referred to as histone-like protein. HU can induce DNA bends, condense DNA in a fiber and also interact with single stranded DNA. It contains two homologous subunits, alpha and beta, typically forming homodimers (alpha-alpha and beta-beta), except in E. coli and other enterobacteria, which form heterodimers (alpha-beta). In E. coli, HU binds uniformly to the chromosome, with a preference for damaged or distorted DNA structures and can introduce negative supercoils into closed circular DNA in the presence of topoisomerase I. Anabaena HU (AHU) shows preference for A/T-rich region in the center of its DNA binding site.
Statistics
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PSSM-Id: 259853
Aligned: 359 rows
Threshold Bit Score: 82.0538
Created: 8-Feb-2013
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
dimer interfaceDNA binding
Conserved site includes 29 residues -Click on image for an interactive view with Cn3D
Feature 1:dimer interface [polypeptide binding site]
Evidence:

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1           #  ##  #        #### ### ### ##   #####  #                           ### # #
3RHI_A        5 NKTELIKNVAQNaeISQKEATVVVQTVVESITNTLaaGEKVQLIGFGTFEVRERAARtGRNPqTGEEMqIAASKVPAFKA 84  Bacillus anthrac...
YP_002731364  2 TKAELVAKVAAEagVTKASAERCVNAFVKALTEALekGERVALPGLGVFNVKERKARkGRNPrTGEEItIPARKVVTFHA 81  Persephonella ma...
EAT05028      2 NKGELVDKVAAEgkITKADADRLVKVVLGSMTDSLtnGEKITIPGFGTFEVRERAAKqGRNPqTGATVeIPARKAVAFKP 81  delta proteobact...
ACG57737      2 TKTELVSYVAQQadITKAKAEKCVNAVFSALAESLkkKERTTIPGFGTFTVSTRKARtGRNPkTGQEIkIPARTTAVWRP 81  Hydrogenobaculum...
BAI68977      2 TKAELVSAVAKGagITKKQADAALKSAISAIAGSLkkGERVAIPGFGIFTVRKRAARkGRNPrTGAVInIPARKVVTFRP 81  Hydrogenobacter ...
ABK99521      2 TKAEFVAAIAAEldVPKNVAAETVEAFLKVTTDLLkaGDKITFPGFGTFGVSERAARtGRNPqTGAEIqIAASKSGKFTA 81  Pelobacter propi...
YP_002219739  2 NKLEFVAALAQHgaMSKVDAEKMFQVFRHTLETELptAGKIVFPGFCTFEVAEKPARkGRNPaTGQEIdIPAKKSIKFKA 81  Acidithiobacillu...
YP_002220512  5 GVTQMVSTLCPEd-VIWSYAARFLEAFARTIRAEMhsAEKILIPEVDTLHFTNRSARkGRNLaTGEKIqIPARRVVTFKA 83  Acidithiobacillu...
EGQ62201      4 KKSELVAALAYHaeSSKAEAERFLEAFGKTIHAEItkVVKIVVPEVGTFQLSRKEARkGRNPqTGEEIqIAARNGVTFKV 83  Acidithiobacillu...
YP_004750266  2 NKSEFIAAMAEQsnMTKAEAERAFGAFRSTLESALprSGKITLPGVGTFAVHERPARkGRNPaTGAEItIAAKQTIRFKP 81  Acidithiobacillu...
Feature 1          ## 
3RHI_A       85 GKeLKE 90  Bacillus anthracis str. Sterne
YP_002731364 82 AKaLKE 87  Persephonella marina EX-H1
EAT05028     82 GKtLKD 87  delta proteobacterium MLMS-1
ACG57737     82 SKeLKK 87  Hydrogenobaculum sp. Y04AAS1
BAI68977     82 AKdLRE 87  Hydrogenobacter thermophilus TK-6
ABK99521     82 GKnLKN 87  Pelobacter propionicus DSM 2379
YP_002219739 82 GKeFAD 87  Acidithiobacillus ferrooxidans ATCC 53993
YP_002220512 84 TKtFQD 89  Acidithiobacillus ferrooxidans ATCC 53993
EGQ62201     84 AKsLQD 89  Acidithiobacillus sp. GGI-221
YP_004750266 82 AKdLVD 87  Acidithiobacillus caldus SM-1

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