1PVO


Conserved Protein Domain Family
Rho_CSD

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cd04459: Rho_CSD 
Click on image for an interactive view with Cn3D
Rho_CSD: Rho protein cold-shock domain (CSD). Rho protein is a transcription termination factor in most bacteria. In bacteria, there are two distinct mechanisms for mRNA transcription termination. In intrinsic termination, RNA polymerase and nascent mRNA are released from DNA template by an mRNA stem loop structure, which resembles the transcription termination mechanism used by eukaryotic pol III. The second mechanism is mediated by Rho factor. Rho factor terminates transcription by using energy from ATP hydrolysis to forcibly dissociate the transcripts from RNA polymerase. Rho protein contains an N-terminal S1-like domain, which binds single-stranded RNA. Rho has a C-terminal ATPase domain which hydrolyzes ATP to provide energy to strip RNA polymerase and mRNA from the DNA template. Rho functions as a homohexamer.
Statistics
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PSSM-Id: 239906
Aligned: 25 rows
Threshold Bit Score: 89.6068
Created: 15-Jun-2006
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
RNA binding
Conserved site includes 11 residues -Click on image for an interactive view with Cn3D
Feature 1:RNA binding site [nucleic acid binding site]
Evidence:
  • Comment:Mutagenic studies suggest these residues participate in RNA-protein interactions.
  • Citation:PMID 9587002
  • Structure:1PVO_F, Escherichia coli Rho Transcription Termination Factor bound with ssRNA, contacts defined at 3.5A.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1          #       #   # # #           # #                        #  ###          
1PVO_F     51 GDGVLE------ILQdgFGFLRsadssylagpDDIYVSPSQIRRFNLRTGDTISGKIRPPKEGERY--FALLKVNE 118 Escherichia coli
AAZ56454  273 VAGILD------ILDn-YAFVRttgy--lpgpNDVYVSLAQVRKYGLRKGDAITGAVRQPREGERRekFNALVRLD 339 Thermobifida fusca YX
AAT83002  263 CSGILD------IRDq-YAFVRtsgy--lpgaNDAYVSMAIVRRHRLRKGDVIVGQMRAHREGERRekFAPLVKIE 329 Propionibacterium acne...
AAA71920   23 FTGVLD------VLSdgYGFLRtasnsylsggNDVYVSPSQIRLFNLRTGDILYGQIRSPRDGERF--FAMVKIKS 90  Lyme disease spirochete
NP_904646 283 FDGILEcmgvleIMPddYGFLRssdynylsspDDVYVSQQQIKHNGLKTGDVVAGTIRPPREGEKY--FPFVQLRS 356 Porphyromonas gingival...
AAC06989   68 VKGVLE------ILPegYGFLRmpennympswNDVYVAPSQIKKFGLRTGDTIEGFARLPRENEKY--KALIRMES 135 Aquifex aeolicus VF5
YP_004675  62 VKGYLE------ISQdgYGFLTenlh--nlesRVAIVSAGLIKQYALRAGDYVVGQARPPRENERY--ATLLKVEA 127 Thermus thermophilus HB27
AAA59208   60 ARGYLD------ITSdgYGFLQadll--dpgsRSVLVTAGIIKQYHLRTGDEVIGRARKPRENERY--GSLVRVEA 125 Deinococcus radiodurans
YP_644428 132 QSGVLD------VLPdgFGFLRtsgy--sqskNDVYISTSQIKRFNLRRGDYIVGQIRPARNGEKY--PAMVRIET 197 Rubrobacter xylanophil...
YP_505968  62 SSGVAE------VLNegFAFMRssvynylanqDDIYISPGQVRRLGIRTGDLIYGEVRAPKKGERY--FALSKALE 129 Neorickettsia sennetsu...

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