4CVO


Conserved Protein Domain Family
cc_ERCC-6_N

?
cd21397: cc_ERCC-6_N 
coiled-coil domain located near the N-terminus of human Excision Repair Cross Complementing 6 (ERCC-6) and related proteins
This model represents a coiled-coil domain located near the N-terminus of ERCC-6 and related proteins. ERCC-6 (also known as Cockayne syndrome group B, CSB) is a DNA-binding protein important in eukaryotic transcription-coupled repair (TCR). TCR is a well-conserved sub-pathway of nucleotide excision repair (NER) that preferentially removes DNA lesions from the template strand blocking translocation of RNA polymerase II (Pol II). In a model for TCR, the processing Pol II encounters the lesion on the transcribed DNA strand and stalls; it is then displaced by the TCR-initiation complex which includes ERCC-6, ERCC-8, UVSSA and USP7; TCR-specific factors then access the lesion for the DNA damage incision process. The N-terminal region, the ATPase domain and the C-terminal region of ERCC-6 all directly contribute to DNA association and catalytic activity. The ATPase domain functions in concert with either the N- or C-terminal region to mediate UV-induced chromatin association. The N-terminal region prevents ERCC-6 from stably associating with chromatin under normal growth conditions, and the C-terminal region of ERCC-6 promotes stable chromatin association in the presence of lesion-stalled transcription. In addition to this coiled-coil domain, the N-terminal region of ERCC-6 includes two lysine residues subject to SUMOylation, a nucleolar localization signal NoLS1, and a nuclear localization signal NLS1. ERCC-6 also includes a SWI/SNF-like ATPase domain, a nucleotide-binding domain and a ubiquitin-binding domain. This coiled-coil domain binds magnesium. This domain family does not include Saccharomyces cerevisiae RAD26, and Schizosaccharomyces pombe Rhp26.
Statistics
?
PSSM-Id: 411064
Aligned: 45 rows
Threshold Bit Score: 71.0862
Created: 17-Aug-2020
Updated: 25-Oct-2021
Structure
?
Program:
Drawing:
Aligned Rows:
 
Mg binding site
Conserved site includes 2 residues -Click on image for an interactive view with Cn3D
Feature 1:Mg binding site [ion binding site]
Evidence:
  • Structure:4CVO_A; Human ERCC-6 N-terminal coiled-coil domain binds magnesium at 4A
    View structure with Cn3D
  • Citation:PMID 2172786
  • Comment:the N-terminal region of ERCC-6 negatively regulates the enzymatic activity of ERCC-6 in addition to chromatin association, it includes one of two N-terminal Lysine residues subject to SUMOylation, this coiled-coil domain, the second of two N-terminal lysine resides subject to SUMOylation, a nucleolar localization signal NoLS1, and a nuclear localization signal NLS1

Sequence Alignment
?
Format: Row Display: Color Bits: Type Selection:
Feature 1                                        #   #                                         
4CVO_A          2 MEPSAQALELQGLGVDVYDQDVLEQGVLQQVDnAIHEASRASQLVDVEKEYRSVLDDLTSCTTSLRQINKIIEQLSP 78   human
XP_007442226   86 VAPNDQALELRGLGVDVYDQDVLEHGVLQQIDkAINEAAKVDRIDDAETEQQPKSEDVGTCTSSLKPYATVLEQFTP 162  Burmese python
XP_029141334   85 VALKDQALELRGLGVEVYDQEVLEHGVLQQIDkAISEATKVGPAQDGDGDGAAAETDGQAEWEDVGPCTSSPKPSAT 161  Protobothrops mu...
XP_029825550   44 IPESDQADELRGLGISVYDQVDLERGIMGAVDrMVQQKEKEQQQKAAEKELAAVRKEIGLLRQKMARIERTTSLYKL 120  black-legged tick
TRY63996       38 GDEAEDASALEQLSIRAYDQDQLEAEVFRQADqALEQQERQRQTEICLKELRPVILELQSLRQSLGKLELELKRLYG 114  Tigriopus califo...
KZS17136       36 VPIENQSEELRALGITVYDQSKFEEGILRQVDdALEEQERQKKAVAAKKLLVSKDVAKEKVADVPPKVQQETEREKM 112  Daphnia magna
EFX89871      495 VALENQSEELRSLGITVYDQSKFEESILRQVDdALEEQERHKKVINAKKILASKDGDKEKTVADKPLKIRKETEKEK 571  common water flea
XP_023717737  123 VQLSDQAAELQVLGLSVYDQDTLEKGILQQVDhAFEQLDKKQLEEQMKTVADEITTCKQELKKSEILLKALKVTGIA 199  Cryptotermes sec...
PSN50701       72 VQLSDEAKELQTLGLSVYDQDTLEKGILHQVDqALEKLDQQKLEQQMKAIADDIVLKRVQESEIERKIRLGEMTPFG 148  German cockroach
CDM26849        1 MSTNEEASRLRDLQADVRDQDDLERDITRQADkALADKAEENDIKRLEKTLVDRERVDSQVRQAQQRLTQPVGAATR 77   Penicillium roqu...

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