ID A0A1B1JH81_TRYCR Unreviewed; 516 AA. AC A0A1B1JH81; DT 02-NOV-2016, integrated into UniProtKB/TrEMBL. DT 02-NOV-2016, sequence version 1. DT 14-DEC-2022, entry version 25. DE SubName: Full=Deacetylase 2 {ECO:0000313|EMBL:ANS13799.1}; OS Trypanosoma cruzi. OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina; OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum. OX NCBI_TaxID=5693 {ECO:0000313|EMBL:ANS13799.1}; RN [1] {ECO:0000313|EMBL:ANS13799.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Dm28 {ECO:0000313|EMBL:ANS13799.1}; RA Picchi G., Zulkievicz V., Alcantara M., Zanchin N., Pierce R., RA Goldenberg S.; RT "a-Paraddise: Anti-Parasitic Drug Discovery in Epigenetics."; RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0007829|PDB:7Q1B, ECO:0007829|PDB:7Q1C} RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 3-481. RX PubMed=34936867; DOI=10.1016/j.celrep.2021.110129; RA Marek M., Ramos-Morales E., Picchi-Constante G.F.A., Bayer T., Norstrom C., RA Herp D., Sales-Junior P.A., Guerra-Slompo E.P., Hausmann K., RA Chakrabarti A., Shaik T.B., Merz A., Troesch E., Schmidtkunz K., RA Goldenberg S., Pierce R.J., Mourao M.M., Jung M., Schultz J., Sippl W., RA Zanchin N.I.T., Romier C.; RT "Species-selective targeting of pathogens revealed by the atypical RT structure and active site of Trypanosoma cruzi histone deacetylase DAC2."; RL Cell Rep. 37:110129-110129(2021). CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; KX359371; ANS13799.1; -; Genomic_DNA. DR PDB; 7Q1B; X-ray; 1.75 A; A=3-481. DR PDB; 7Q1C; X-ray; 2.30 A; A/B=3-481. DR AlphaFoldDB; A0A1B1JH81; -. DR SMR; A0A1B1JH81; -. DR VEuPathDB; TriTrypDB:BCY84_18227; -. DR VEuPathDB; TriTrypDB:C3747_135g72; -. DR VEuPathDB; TriTrypDB:C4B63_9g487; -. DR VEuPathDB; TriTrypDB:Tc_MARK_2797; -. DR VEuPathDB; TriTrypDB:TcBrA4_0102540; -. DR VEuPathDB; TriTrypDB:TcCL_ESM08349; -. DR VEuPathDB; TriTrypDB:TcCLB.504159.80; -. DR VEuPathDB; TriTrypDB:TcCLB.506821.140; -. DR VEuPathDB; TriTrypDB:TCDM_10100; -. DR VEuPathDB; TriTrypDB:TcG_08673; -. DR VEuPathDB; TriTrypDB:TCSYLVIO_004050; -. DR VEuPathDB; TriTrypDB:TcYC6_0051300; -. DR Gene3D; 3.40.800.20; -; 1. DR InterPro; IPR000286; His_deacetylse. DR InterPro; IPR023801; His_deacetylse_dom. DR InterPro; IPR037138; His_deacetylse_dom_sf. DR InterPro; IPR023696; Ureohydrolase_dom_sf. DR Pfam; PF00850; Hist_deacetyl; 1. DR PRINTS; PR01270; HDASUPER. DR SUPFAM; SSF52768; Arginase/deacetylase; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:7Q1B, ECO:0007829|PDB:7Q1C}. FT DOMAIN 79..385 FT /note="Hist_deacetyl" FT /evidence="ECO:0000259|Pfam:PF00850" FT REGION 113..132 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 464..516 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 474..516 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 516 AA; 56358 MW; 16F060C779D5161A CRC64; MVFTDAVAGK TSLPPPVAII VGHNIDASAM PLTYERNRFV IDMLQHYACP VFSHKKSGDA MNTVSSDVFE WVLEPLPVVG VEDMTAFHDR AYLNYLSIRE ALSEVDERAS TVKRSRAEGI QPPVSRRSSA QTQPPLRVLP DLVPIPADEE YGLVNENMPF VGMWRTIQAT VSGTLLAARL LAQPGRFAAI HWFGGRHHAK KSTAGGFCFA NDVVLGVLEL KKLLSSDKNG ILVVDVDAHH GDGTQSAFLH DNSVLTLSMH AHGVGIFPGT GGIEEIGAGL GRGFTMNVPL PEGATDILAV TLMYRSIHFA FKKLGEGLAA IVIVCGSDAL SGDPLGALNL TVGGMQSIIR LLLKEAARRS LKVLLLGAGG YVDTSCARLA GVVTKDVLSC AAAMRLGKTE YFGDSANLGD NLGVAVPEGC EYFTRYGPSF LMHGLPPARV SKLYRLPYGS PLFMRMQRAA TKEALRRRLN QEQDEEEDAE DDEEEEEEEE EEEEEEEEEE EEEEEEEEEE EEEEEP //