4CCG,3K1L,3K1L


Conserved Protein Domain Family
RING-CH-C4HC3_FANCL

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cd16490: RING-CH-C4HC3_FANCL 
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RING-CH finger, H2 subclass (C4HC3-type), found in Fanconi anemia group L protein (FANCL) and similar proteins
FANCL, also known as fanconi anemia-associated polypeptide of 43 kDa (FAAP43) or PHF9, is a monomeric RING E3 ubiquitin-protein ligase that monoubiquitinates FANCD2 and FANCI. The monoubiquitinated FANCD2-FANCI heterodimer complex in turn recruits key proteins involved in homologous recombination and DNA repair. FANCL is also one of seven components in Fanconi anemia (FA) nuclear core complex, which provides the essential E3 ligase function for spatially defined FANCD2 ubiquitination and FA pathway activation. In the FA core complex, FANCL associates with FANCB and FAAP100 to constitute a catalytic subcomplex that functions as the monoubiquitination module. FANCL specifically interacts with the E2 ubiquitin-conjugating (UBC) enzyme Ube2T to make an E3-E2 pair, which is the catalytic center of the Fanconi Anemia (FA) pathway required for DNA interstrand crosslink repair. Moreover, FANCL has a noncanonical function to regulate the Wnt/beta-catenin signaling, a pathway involved in hematopoietic stem cell self-renewal. It functionally enhances beta-catenin activity through ubiquitinating beta-catenin, with atypical ubiquitin chains (K11 linked). FANCL contains an N-terminal E2-like fold (ELF) domain, a novel double-RWD (DRWD) domain with a clear hydrophobic core, and a C-terminal C4HC3-type RING-CH finger. The DRWD domain is required for substrate binding. The RING-CH finger, also known as vRING or RINGv, is predicted to facilitate E2 binding. It has an unusual arrangement of zinc-coordinating residues. Its cysteines and histidines are arranged in the sequence as C4HC3-type, rather than the C3H2C3-type in canonical RING-H2 finger.
Statistics
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PSSM-Id: 319404
View PSSM: cd16490
Aligned: 34 rows
Threshold Bit Score: 70.7664
Threshold Setting Gi: 86171075
Created: 31-Jul-2013
Updated: 18-Aug-2016
Structure
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Program:
Drawing:
Aligned Rows:
 
Conserved site includes 8 residues -Click on image for an interactive view with Cn3D
Feature 1:Zn binding site [ion binding site]
Evidence:

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
Feature 1          #  #                         #    #    #  #                      #  # 
4CCG_X         19 DCGICYAYQLDg------------tIPDQVCDnsqCGQPFHQICLYEWLRglltsrq-sfniifGECPYCS 76
3K1L_A        310 RCNICFAYRLDgg-----------eVPLVSCDnakCVLKCHAVCLEEWFKtlmdgkt-flevsfGQCPFCK 368
3K1L_B        310 RCNICFAYRLDgg-----------eVPLVSCDnakCVLKCHAVCLEEWFKtlmdgkt-flevsfGQCPFCK 368
gi 167517767 1974 DCGICYSMELEd------------eLPSETCHnaqCGRSYHASCLLAWLQalpttrk-sfdslfGQCPFCQ 2031
gi 190581541  275 PCGICCGYRLNa------------tLPDKVCDyslCEKQFHSLCLLEWLKtlpssrt-sfsvihGQCPYCK 332
gi 284096145  146 NCGVCYSYRLNm------------kIPDKVCDnvkCGMPFHSECLIEWLRsipgthq-sfdtvfGSCPYCS 203
gi 307111175  127 DCAICYAYRLPpaegqlpaggeegeSPDINCDnaaCGKPFHRRCLVEWLNsdtstrq-sfntlfGACPYCS 196
gi 321463057  308 TCCICYSERLNg------------eVPSRTCDnshCGQSFHIYCLYEWLRslretirkqgnkvfGACPYCD 366
gi 546326841  312 ECGICYAYRLEe------------sTPDVTCDlaeCSKPYHRGCLVEWLRalpgtre-sfgmitGNCVYCE 369
gi 761905933  269 ECGICYTHRHYen----------grAPDFTCDnkqCSQPYHVSCLYEWLTsltstrk-sfgflfGECLYCN 328

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