{PDOC51905} {PS51905; ZF_UBZ1} {PS51906; ZF_UBZ2} {PS51907; ZF_UBZ3} {PS51908; ZF_UBZ4} {BEGIN} *********************************************************** * Zinc finger UBZ1-, UBZ2-, UBZ3-, and UBZ4-type profiles * *********************************************************** The ubiquitin-binding zinc finger (UBZ) is a type of zinc-coordinating beta- beta-alpha fold domain found mainly in proteins involved in DNA repair and transcriptional regulation. UBZ domains coordinate a zinc ion with cysteine or histidine residues; depending on their amino acid sequence, UBZ domains are classified into several families [1,2]. Type 1 UBZs are CCHH-type zinc fingers found in tandem UBZ domains of TAX1-binding protein 1 (TAX1BP1) [3,4,5], type 2 UBZs are CCHC-type zinc fingers found in FAAP20 which is a subunit of the Fanconi anemia (FA) core complex [6,7], type 3 UBZs are CCHH-type zinc fingers found only in the Y-family translesion polymerase eta [8,9,10], and type 4 UBZs are CCHC-type zinc fingers found in Y-family translesion polymerase kappa, Werner helicase-interacting protein 1 (WRNIP1), and Rad18 [11,12,13]. The UBZ domain consists of two short antiparallel beta-strands followed by one alpha-helix. The alpha-helix packs against the beta-strands with a zinc ion sandwiched between the alpha-helix and the beta-strands. The zinc ion is coordinated by two cysteines located on the fingertip formed by the beta- strands and two histidines (see ) [1,8] or one hisidine and one cysteine (see ) [6] on the alpha-helix [2]. The profiles we developed cover the entire UBZ1-, UBZ2-, UBZ3-, and UBZ4-type zinc fingers. -Sequences known to belong to this class detected by the profile: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Sequences known to belong to this class detected by the profile: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Sequences known to belong to this class detected by the profile: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Sequences known to belong to this class detected by the profile: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Last update: April 2022 / Profile revised. [ 1] Hofmann K. "Ubiquitin-binding domains and their role in the DNA damage response." DNA Repair. (Amst). 8:544-556(2009). PubMed=19213613; DOI=10.1016/j.dnarep.2009.01.003 [ 2] Suzuki N., Rohaim A., Kato R., Dikic I., Wakatsuki S., Kawasaki M. "A novel mode of ubiquitin recognition by the ubiquitin-binding zinc finger domain of WRNIP1." FEBS. J. 283:2004-2017(2016). PubMed=27062441; DOI=10.1111/febs.13734 [ 3] Ceregido M.A., Spinola Amilibia M., Buts L., Rivera-Torres J., Garcia-Pino A., Bravo J., van Nuland N.A.J. "The structure of TAX1BP1 UBZ1+2 provides insight into target specificity and adaptability." J. Mol. Biol. 426:674-690(2014). PubMed=24239949; DOI=10.1016/j.jmb.2013.11.006 [ 4] Xie X., Li F., Wang Y., Wang Y., Lin Z., Cheng X., Liu J., Chen C., Pan L. "Molecular basis of ubiquitin recognition by the autophagy receptor CALCOCO2." Autophagy 11:1775-1789(2015). PubMed=26506893; DOI=10.1080/15548627.2015.1082025 [ 5] Thurston T.L.M., Boyle K.B., Allen M., Ravenhill B.J., Karpiyevich M., Bloor S., Kaul A., Noad J., Foeglein A., Matthews S.A., Komander D., Bycroft M., Randow F. "Recruitment of TBK1 to cytosol-invading Salmonella induces WIPI2-dependent antibacterial autophagy." EMBO. J. 35:1779-1792(2016). PubMed=27370208; DOI=10.15252/embj.201694491 [ 6] Wojtaszek J.L., Wang S., Kim H., Wu Q., D'Andrea A.D., Zhou P. "Ubiquitin recognition by FAAP20 expands the complex interface beyond the canonical UBZ domain." Nucleic. Acids. Res. 42:13997-14005(2014). PubMed=25414354; DOI=10.1093/nar/gku1153 [ 7] Toma A., Takahashi T.S., Sato Y., Yamagata A., Goto-Ito S., Nakada S., Fukuto A., Horikoshi Y., Tashiro S., Fukai S. "Structural basis for ubiquitin recognition by ubiquitin-binding zinc finger of FAAP20." PLoS One. 10:E0120887-E0120887(2015). PubMed=25799058; DOI=10.1371/journal.pone.0120887 [ 8] Bomar M.G., Pai M.-T., Tzeng S.-R., Li S.S.-C., Zhou P. "Structure of the ubiquitin-binding zinc finger domain of human DNA Y-polymerase eta." EMBO. Rep. 8:247-251(2007). PubMed=17304240; DOI=10.1038/sj.embor.7400901 [ 9] Garcia-Ortiz M.V., Roldan-Arjona T., Ariza R.R. "The noncatalytic C-terminus of AtPOLK Y-family DNA polymerase affects synthesis fidelity, mismatch extension and translesion replication." FEBS. J. 274:3340-3350(2007). PubMed=17550419; DOI=10.1111/j.1742-4658.2007.05868.x [10] Woodruff R.V., Bomar M.G., D'Souza S., Zhou P., Walker G.C. "The unusual UBZ domain of Saccharomyces cerevisiae polymerase eta." DNA Repair. (Amst). 9:1130-1141(2010). PubMed=20837403; DOI=10.1016/j.dnarep.2010.08.001 [11] Yang K., Moldovan G.-L., D'Andrea A.D. "RAD18-dependent recruitment of SNM1A to DNA repair complexes by a ubiquitin-binding zinc finger." J. Biol. Chem. 285:19085-19091(2010). PubMed=20385554; DOI=10.1074/jbc.M109.100032 [12] Rizzo A.A., Salerno P.E., Bezsonova I., Korzhnev D.M. "NMR structure of the human Rad18 zinc finger in complex with ubiquitin defines a class of UBZ domains in proteins linked to the DNA damage response." Biochemistry 53:5895-5906(2014). PubMed=25162118; DOI=10.1021/bi500823h [13] Lachaud C., Castor D., Hain K., Munoz I., Wilson J., MacArtney T.J., Schindler D., Rouse J. "Distinct functional roles for the two SLX4 ubiquitin-binding UBZ domains mutated in Fanconi anemia." J. Cell. Sci. 127:2811-2817(2014). PubMed=24794496; DOI=10.1242/jcs.146167 -------------------------------------------------------------------------------- PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html -------------------------------------------------------------------------------- {END}