3NW0,2CT0,5HVQ


Conserved Protein Domain Family
RING-CH-C4HC3_NSE1
?
cd16493: RING-CH-C4HC3_NSE1 
Click on image for an interactive view with Cn3D
RING-CH finger, H2 subclass (C4HC3-type), found in non-structural maintenance of chromosomes (SMC) element 1 homolog (NSE1) and similar proteins
NSE1, also known as non-SMC element 1 homolog (NSMCE1), is an E3 ubiquitin ligase that contains a C4HC3-type RING-CH finger, also known as vRING or RINGv, a variant of C3H2C3-type RING-H2 finger. Together with its partner proteins NSE3 and NSE4, it forms a tight subcomplex of the SMC5-6 complex, which includes another two subcomplexes, SMC6-SMC5-NSE2 and NSE5-NSE6. The vRING finger is essential for normal NSE1-NSE3-NSE4 trimer formation in vitro and for damage-induced recruitment of NSE4 and SMC5 to subnuclear foci in vivo. Thus it functions as a protein-protein interaction domain required for SMC5-6 holocomplex integrity and recruitment to, or retention at, DNA lesions. The C-terminal half of NSE1, including the vRING finger, is required for DNA damage resistance and mitotic fidelity of SMC5-6 complex in the fission yeast Schizosaccharomyces pombe. The RING-CH finger may play an important role in Rad52-dependent post-replication repair of UV-damaged DNA in Saccharomyces cerevisiae.
Links
?
Statistics
?
PSSM-Id: 438156
Aligned: 30 rows
Threshold Bit Score: 58.2267
Created: 22-Dec-2011
Updated: 17-Oct-2022
Structure
?
Program:
Drawing:
Aligned Rows:
Download Cn3D
 
Zn binding site
Conserved site includes 8 residues -Click on image for an interactive view with Cn3D
Feature 1: Zn binding site [ion binding site], 8 residue positions
Conserved feature residue pattern:C C C C H C C CClick to see conserved feature residue pattern help
Evidence:
  • Structure:3NW0; Homo sapiens NES1 binds two Zn2+ ions through its RING-CH finger.
  • Comment:RING-CH finger (C4HC3-type)
  • Comment:A RING finger typically binds two zinc atoms, with its Cys and/or His side chains in a unique "cross-brace" arrangement.
  • Comment:The RING fingers found in NSE1 and its homologs have an unusual arrangement of zinc-coordinating residues: the cysteines and histidines are arranged in the sequence as C4HC3-type, rather than the typical C3H2C3-type in RING-H2 finger.
Scroll to Sequence Alignment Display
Sequence Alignment
?
Format: Row Display: Color Bits: Type Selection: 
Feature 1          #  #         #            #                #  #             #     #    
3NW0_A       181 KICNICHSLlIQGQSCEt----------CGIr------------MHLPCVAKYFqsna-eprCPH---CNDYW 227 human
Q07913       269 NTCQNCHKLaIQGVRCGne--------sCREeneetgenslsqiWHVDCFKHYIthv--sknCDR---CGSSL 328 Saccharomyces cerevisi...
Q6BH78       199 FSCHQCNEInTLGIGCPvv--------dCQIn------------FHYKCLDIYMrnesnkgrCPNysnCSYNW 251 Debaryomyces hansenii
Q6FPU2       323 SSCERCKDIvAQGVQCStr--------dCNSv------------WHVDCYEHDIlhe--nriCRS---CGESI 370 Candida glabrata
Q7SAF8       235 KFCESCKEIvTYGQRCSer--------dCTVr------------LHDICEDRYWrtrrgekkCPK---CETEW 284 Neurospora crassa
Q759D3       253 MPCSTCEHVvAQGVLCTgcvakrrdeggCWAa------------WHVDCFDYQVthv--tpqCPS---CEADI 308 Eremothecium gossypii
CCJ29962     180 KRCKACHNVvTQGFRCLni--------dCPIr------------FHEYCSKAYMarqk-dklCPK---CGEIW 228 Pneumocystis jirovecii
XP_023471632 186 KECTICLDIvTMGEYCElg--------nCPVr------------LHKYCADTQFresv-nptCPQ---CSTTW 234
EFX77036     174 GDCVICNKLaVKKFVCPet--------sCGAk------------FHRYCISKLKl------kCPN---CNRVL 217
Q5KC98       206 KSCAQCRRVvTEGLACSnv--------gCDCh------------IHNTCYARNIqqla-npvCPS---CSSSF 254 Cryptococcus neoformans

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