1V32


Conserved Protein Domain Family
SWIB-MDM2_like

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cd10567: SWIB-MDM2_like 
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SWIB/MDM2 domain found in SWIB/MDM2 homologous proteins
This family includes Schizosaccharomyces pombe upstream activation factor subunit spp27, Saccharomyces cerevisiae upstream activation factor subunit UAF30, Chlamydiae DNA topoisomerase/SWIB domain fusion protein, Arabidopsis thaliana zinc finger CCCH domain-containing proteins, AtC3H19 and AtC3H44, and similar proteins. S. pombe spp27, also termed upstream activation factor 27 KDa subunit (p27), or upstream activation factor 30 KDa subunit (p30), or upstream activation factor subunit uaf30, is a component of the UAF (upstream activation factor) complex which interacts with the upstream element of the RNA polymerase I promoter and forms a stable preinitiation complex. S. cerevisiae UAF30, also termed upstream activation factor 30 KDa subunit (p30), is a non-essential component of the UAF. It seems to play a role in silencing transcription by RNA polymerase II. The SWIB domain found in Chlamydiae DNA topoisomerase may play a role in chromatin condensation-decondensation, which is characteristic of the chlamydial developmental cycle and not found in any other types of bacteria. AtC3H19, also termed protein needed for RDR2-independent DNA methylation (NERD), is a plant-specific GW repeat- and PHD finger-containing protein that plays a central role in integrating RNA silencing and chromatin signals in 21 nt small-interfering RNA (siRNA)-dependent DNA methylation on the cytosine pathway, leading to transcriptional gene silencing of specific sequences. This family also includes many uncharacterized proteins containing two copies of SWIB/MDM2 domain.
Statistics
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PSSM-Id: 349489
Aligned: 210 rows
Threshold Bit Score: 45.6121
Created: 26-Jun-2017
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
putative
Conserved site includes 13 residues -Click on image for an interactive view with Cn3D
Feature 1:putative peptide binding site [polypeptide binding site]
Evidence:
  • Comment:The SWIB domain and the MDM2 domain share a common evolutionary origin and thus adopt similar structures, which suggests the SWIB domain may interact with a helical peptide through a cleft on the surface.
  • Comment:Based on the structural evidence that MDM2 domain binds p53 or other peptides.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                                 #  ## ##  ##    #     ## #                   ##       
1V32_A         14 GWGSRQLIEFLHslgkdtsemISRYDVSDTIAKYISKEGLLDps-nKKKVVCDkRLVLLFGTRTIfrmkVYDLLEKHY 90   thale cress
ETW31931       67 CEIKSPLKEFLNad------tASRVFVLKYAWKYIKDNNLQNpn-mKRKIIPDdKLKQVLDKDEVdileVPKLLFKHM 137  Plasmodium falc...
XP_012650267   66 CKVKGPLFDLLQee------eLTRSEAVKLVWKYIKDQGLQNpe-nRRIIMSDhKLYPLFGKEEVtfgeVGKAIHKHL 136  Babesia microti...
XP_001767040  302 YPISDQLAKFLDved----gkVSRAEAAKRMWAYIKDHNLQDpt-nKKKILCDqPLQDLLDCDHFvgfdLSKLLKRHF 374  Physcomitrella ...
NP_001332307  261 RWGSKPLIDFLTsigedtreaMSQHSVESVIRRYIREKNLLDre-kKKKVHCDeKLYSIFRKKSInqkrIYTLLNTHL 337  thale cress
Q9SD34        318 SWATKELLEFVSfmkngdtsvLSQFDVQGLLLDYIKKKNLRDpl-qKSQVLCDqMLVKLFGKQRVghfeMLKLLESHV 394  thale cress
XP_002970972  408 GWASKEMISFIKfmkedpktpMKRPAVNKLLWDHIKANKLQNpr-kKTIIRCDeQLRSLFGKKAVtqrsLMKYLHNHF 484  Selaginella moe...
Q9SIV5        806 EWASKELLDLVVhmrrgdrsfLPMLEVQTLLLAYIKRYNLRDpr-rKSQVICDsRLQNLFGKSHVghfeMLNLLDSHF 882  thale cress
XP_001778499  133 DWASRELKAFLKnmkedvmkpLSRFAIHKLLWIYIKQNKLQNpk-kMNEIICDqQLRLIFEKDSVgqfeMFKLLNKHF 209  Physcomitrella ...
XP_011462024  155 GWGSEPLIGFLKsvkkdtskqLSQRELGSAIYEYVMDRHLLEytnkKTKVRCDwRLNKIFRKEEVdvvdVFSFLDQHL 232  Fragaria vesca ...

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