#=GF ID bCoV_SUD_C
#=GF AC PF12124.12
#=GF DE Betacoronavirus SUD-C domain
#=GF PI Nsp3_PL2pro; bCoV_PL2pro;
#=GF AU Mistry J;0000-0003-2479-5322
#=GF AU Gavin OL;
#=GF AU Chuguransky S;0000-0002-0520-0736
#=GF AU Bateman A;0000-0002-6982-4660
#=GF AU Richardson L;0000-0002-3655-5660
#=GF SE pdb_2kaf
#=GF GA 25.00 25.00;
#=GF TC 105.80 103.30;
#=GF NC 24.60 21.20;
#=GF BM hmmbuild HMM.ann SEED.ann
#=GF SM hmmsearch -E 1000 --cpu 4 -Z 75585367 HMM pfamseq
#=GF TP Domain
#=GF RN [1]
#=GF RM 29128390
#=GF RT Nsp3 of coronaviruses: Structures and functions of a large
#=GF RT multi-domain protein.
#=GF RA Lei J, Kusov Y, Hilgenfeld R;
#=GF RL Antiviral Res. 2018;149:58-74.
#=GF RN [2]
#=GF RM 19436709
#=GF RT The SARS-unique domain (SUD) of SARS coronavirus contains two
#=GF RT macrodomains that bind G-quadruplexes.
#=GF RA Tan J, Vonrhein C, Smart OS, Bricogne G, Bollati M, Kusov Y,
#=GF RA Hansen G, Mesters JR, Schmidt CL, Hilgenfeld R;
#=GF RL PLoS Pathog. 2009;5:e1000428.
#=GF RN [3]
#=GF RM 20493876
#=GF RT SARS coronavirus unique domain: three-domain molecular
#=GF RT architecture in solution and RNA binding.
#=GF RA Johnson MA, Chatterjee A, Neuman BW, Wuthrich K;
#=GF RL J Mol Biol. 2010;400:724-742.
#=GF DR INTERPRO; IPR022733;
#=GF DR SO; 0000417; polypeptide_domain;
#=GF CC This domain is found in betacoronavirus non-structural protein
#=GF CC NSP3, and is about 65 amino acids in length. It was originally
#=GF CC thought to exist only in SARS-coronaviruses, and so was termed
#=GF CC the SARS-unique domain (SUD), however this has since been shown
#=GF CC to be incorrect. The domain is also known as DPUP (domain
#=GF CC preceding Ubl2 and PL2pro). NSP3 is the product of ORF1a,
#=GF CC proteolytically released from the pp1a/1ab polyprotein [1,2].
#=GF CC The SUD domain has three globular domains, SUD-N (N-terminal),
#=GF CC SUD-M (middle region of SUD), and SUD-C (C-terminal). SUD-C
#=GF CC adopts a fold consisting of seven beta-strands arranged in an
#=GF CC anti-parallel beta-sheet, and two alpha-helices which are packed
#=GF CC against the same side of the beta-sheet. It adopts a frataxin
#=GF CC like fold with structural similarities to DNA-binding domains.
#=GF CC It has been shown that SUD-C binds to single-stranded RNA and
#=GF CC recognises purine bases more strongly than pyrimidine bases,
#=GF CC but these interactions are stabilised in the presence of SUD-M.
#=GF CC The function of this domain is not clear but studies of
#=GF CC structural homologues of SUD-C suggest that it could be related
#=GF CC to metal, adenylate and nucleic acid binding [3].
#=GF SQ 10
#=GS A0A0K1Z0N1_SARS/1473-1538 AC A0A0K1Z0N1.1
#=GS R1A_SARS/1473-1538 AC P0C6U8.1
#=GS Q0Q485_SARS/1469-1534 AC Q0Q485.1
#=GS R9QTB2_SARS/1465-1530 AC R9QTB2.1
#=GS Q6UZF5_SARS/1473-1538 AC Q6UZF5.1
#=GS R1A_SARS2/1497-1561 AC P0DTC1.1
#=GS R1AB_SARS/1473-1538 AC P0C6X7.1
#=GS A0A0K1YZY7_SARS/1473-1538 AC A0A0K1YZY7.1
#=GS R1AB_SARS2/1497-1561 AC P0DTD1.1
#=GS Q6UZF1_SARS/1473-1538 AC Q6UZF1.1
A0A0K1Z0N1_SARS/1473-1538 p-EEHFVETVSLAGSYRDWSYSGQRTELGVEFLKRGDKIVYHTLESPIEFHLDGEVQPLDKLKSLLS
R1A_SARS/1473-1538 .SEEHFVETVSLAGSYRDWSYSGQRTELGVEFLKRGDKIVYHTLESPVEFHLDGEVLSLDKLKSLLS
Q0Q485_SARS/1469-1534 p-EEHFIETISLAGTYRDWSYSGQRTELGVEFLKRGDKIVYHTIEKPTEFYLDGEVLPLDKLKSLLS
R9QTB2_SARS/1465-1530 p-EEHFIETISLAGTYRDWSYSGQRTELGVEFLKRGDKIVYHTIESPVEFHLDGEVLPLDKLKSLLS
Q6UZF5_SARS/1473-1538 .SEEHFVETVSLAGSYRDWSYSGQRTELGVEFLKRGDKIVYHTLESPVEFHLDGEVLSLDKLKSLLS
R1A_SARS2/1497-1561 p-EEHFIETISLAGSYKDWSYSGQSTQLGIEFLKRGDKSVYYTS-NPTTFHLDGEVITFDNLKTLLS
R1AB_SARS/1473-1538 .SEEHFVETVSLAGSYRDWSYSGQRTELGVEFLKRGDKIVYHTLESPVEFHLDGEVLSLDKLKSLLS
A0A0K1YZY7_SARS/1473-1538 p-EEHFVETVSLAGSYRDWSYSGQRTELGVEFLKRGDKIVYHTLESPIEFHLDGEVQPLDKLKSLLS
R1AB_SARS2/1497-1561 p-EEHFIETISLAGSYKDWSYSGQSTQLGIEFLKRGDKSVYYTS-NPTTFHLDGEVITFDNLKTLLS
Q6UZF1_SARS/1473-1538 .SEEHFVETVSLAGSYRDWSYSGQRTELGVEFLKRGDKIVYHTLESPVEFHLDGEVLSLDKLKSLLS
#=GC seq_cons P.EEHFVETVSLAGSYRDWSYSGQRTELGVEFLKRGDKIVYHTLESPlEFHLDGEVLoLDKLKSLLS
//
