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Database: Pfam
Entry: bCoV_SUD_C
LinkDB: bCoV_SUD_C
Original site: bCoV_SUD_C 
#=GF ID   bCoV_SUD_C
#=GF AC   PF12124.9
#=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   25.30 133.30;
#=GF NC   24.60 20.10;
#=GF BM   hmmbuild HMM.ann SEED.ann
#=GF SM   hmmsearch -Z 47079205 -E 1000 --cpu 4 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   15
#=GS A0A096XNP3_CVHSA/1464-1529  AC A0A096XNP3.1
#=GS B8Q8Q2_CVHSA/1473-1538      AC B8Q8Q2.1
#=GS B8Q8Q1_CVHSA/1473-1538      AC B8Q8Q1.1
#=GS A0A0K1Z0N1_CVHSA/1473-1538  AC A0A0K1Z0N1.1
#=GS D5HJV7_BCHK3/1464-1529      AC D5HJV7.1
#=GS Q6RD33_CVHSA/1473-1538      AC Q6RD33.1
#=GS R9QTB2_CVHSA/1465-1530      AC R9QTB2.1
#=GS R9QTH2_CVHSA/1474-1539      AC R9QTH2.1
#=GS R1A_CVHSA/1473-1538         AC P0C6U8.1
#=GS R1A_CVHSA/1473-1538         DR PDB; 2KAF A; 2-67;
#=GS R1A_CVHSA/1473-1538         DR PDB; 2KQW A; 133-198;
#=GS A0A166ZL34_9NIDO/1468-1533  AC A0A166ZL34.1
#=GS Q6UZF5_CVHSA/1473-1538      AC Q6UZF5.1
#=GS Q6RD32_CVHSA/1473-1538      AC Q6RD32.1
#=GS A0A0K1YZY7_CVHSA/1473-1538  AC A0A0K1YZY7.1
#=GS R1AB_CVHSA/1473-1538        AC P0C6X7.1
#=GS A0A0U1WHG0_CVHSA/1468-1533  AC A0A0U1WHG0.1
A0A096XNP3_CVHSA/1464-1529             p-EEHFVETTSLAGSYRDWSYSGQHTELGVEFLKRGDKIVYHNTGSPIEFHLDGEVLPLDKLKSLLS
B8Q8Q2_CVHSA/1473-1538                 .SEEHFVETVSLAGSYRDWSYSGQRTELGVEFLKRGDKIVYHTLESPVEFHLDGEVLSLDKLKSLLS
B8Q8Q1_CVHSA/1473-1538                 .SEEHFVETVSLAGSYRDWSYSGQRTELGVEFLKRGDKIVYHTLESPVEFHLDGEVLSLDKLKSLLS
A0A0K1Z0N1_CVHSA/1473-1538             p-EEHFVETVSLAGSYRDWSYSGQRTELGVEFLKRGDKIVYHTLESPIEFHLDGEVQPLDKLKSLLS
D5HJV7_BCHK3/1464-1529                 p-EEYFVETTSLAGSYRDWSYSGQRTELGVEFLKRGDKIVYHTTGSPIEFHLDGEVLPLDKLKSLLS
Q6RD33_CVHSA/1473-1538                 .SEEHFVETVSLAGSYRDWSYSGQRTELGVEFLKRGDKIVYHTLESPVEFHLDGEVLSLDKLKSLLS
R9QTB2_CVHSA/1465-1530                 p-EEHFIETISLAGTYRDWSYSGQRTELGVEFLKRGDKIVYHTIESPVEFHLDGEVLPLDKLKSLLS
R9QTH2_CVHSA/1474-1539                 .SEEHFVETVSLAGSYRDWSYSGQRTELGVEFLKRGDKIVYHTLESPVEFHLDGEVLPLDKLKSLLS
R1A_CVHSA/1473-1538                    .SEEHFVETVSLAGSYRDWSYSGQRTELGVEFLKRGDKIVYHTLESPVEFHLDGEVLSLDKLKSLLS
#=GR R1A_CVHSA/1473-1538         SS    .HHHHHHHHHHHHTEETTEE----EETTEEEEEEETTEEEEE-SSSS--EEETTEEE-HHHHHHHH-
A0A166ZL34_9NIDO/1468-1533             p-EEHFIETISLAGTYRDWSYSGQRTELGVEFLKRGDKIVYHTIEKPIEFHLDGEVLPLDKLKSLLS
Q6UZF5_CVHSA/1473-1538                 .SEEHFVETVSLAGSYRDWSYSGQRTELGVEFLKRGDKIVYHTLESPVEFHLDGEVLSLDKLKSLLS
Q6RD32_CVHSA/1473-1538                 .SEEHFVETVSLAGSYRDWSYSGQRTELGVEFLKRGDKIVYHTLESPVEFHLDGEVLSLDKLKSLLS
A0A0K1YZY7_CVHSA/1473-1538             p-EEHFVETVSLAGSYRDWSYSGQRTELGVEFLKRGDKIVYHTLESPIEFHLDGEVQPLDKLKSLLS
R1AB_CVHSA/1473-1538                   .SEEHFVETVSLAGSYRDWSYSGQRTELGVEFLKRGDKIVYHTLESPVEFHLDGEVLSLDKLKSLLS
A0A0U1WHG0_CVHSA/1468-1533             p-EEHFIETISLAGTYRDWSYSGQRTELGVEFLKRGDKIVYHTIEKPIEFHLDGEVLPLDKLKSLLS
#=GC SS_cons                           .HHHHHHHHHHHHTEETTEE----EETTEEEEEEETTEEEEE-SSSS--EEETTEEE-HHHHHHHH-
#=GC seq_cons                          ..EEHFVETVSLAGSYRDWSYSGQRTELGVEFLKRGDKIVYHTLESPVEFHLDGEVLsLDKLKSLLS
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