GenomeNet

Database: Pfam
Entry: Herpes_gp350_A
LinkDB: Herpes_gp350_A
Original site: Herpes_gp350_A 
#=GF ID   Herpes_gp350_A
#=GF AC   PF05109.20
#=GF DE   Herpes virus envelope glycoprotein gp350, N-terminal A domain
#=GF PI   Herpes_BLLF1;
#=GF AU   Moxon SJ;0000-0003-4644-1816
#=GF SE   Pfam-B_6348 (release 7.7)
#=GF GA   27.00 27.00;
#=GF TC   31.40 261.70;
#=GF NC   26.30 24.60;
#=GF BM   hmmbuild  HMM.ann SEED.ann
#=GF SM   hmmsearch -E 1000 --cpu 8 -Z 81514348 HMM pfamseq
#=GF TP   Domain
#=GF CL   CL0159
#=GF RN   [1]
#=GF RM   11024143
#=GF RT   Infectious Epstein-Barr virus lacking major glycoprotein BLLF1
#=GF RT   (gp350/220) demonstrates the existence of additional viral
#=GF RT   ligands.
#=GF RA   Janz A, Oezel M, Kurzeder C, Mautner J, Pich D, Kost M,
#=GF RA   Hammerschmidt W, Delecluse HJ;
#=GF RL   J Virol. 2000;74:10142-10152.
#=GF RN   [2]
#=GF RM   17072314
#=GF RT   Structure of the Epstein-Barr virus major envelope glycoprotein.
#=GF RA   Szakonyi G, Klein MG, Hannan JP, Young KA, Ma RZ, Asokan R,
#=GF RA   Holers VM, Chen XS;
#=GF RL   Nat Struct Mol Biol. 2006;13:996-1001.
#=GF DR   INTERPRO; IPR007796;
#=GF DR   SO; 0000417; polypeptide_domain;
#=GF CC   This entry consists of the envelope glycoprotein gp350 from
#=GF CC   Epstein-Barr virus (also known as BLLF1 viral late
#=GF CC   glycoprotein). It is the most abundantly expressed glycoprotein
#=GF CC   in the viral envelope of Herpesviruses and is the major antigen
#=GF CC   responsible for  stimulating the production of neutralising
#=GF CC   antibodies in vivo [1]. It is a 907 residues long gp350
#=GF CC   polypeptide containing an 18-residue peptide at the C-terminal
#=GF CC   that is located inside the viral membrane, a membrane-spanning
#=GF CC   domain and a large N-terminal segment (860 residues) predicted
#=GF CC   to extend outside the viral membrane. The extreme N-terminal
#=GF CC   region (1-470) is sufficient to bind receptor CR2 (also known as
#=GF CC   CD21) and fold into three distinct domains (denoted as A, B and
#=GF CC   C) which organise into am "L-shape" structure. This is domain A,
#=GF CC   which is located in the middle, bridging domain B on one side
#=GF CC   and domain C on the other [2].
#=GF SQ   5
#=GS A0A0C7SXC8_EBVG/1-159  AC A0A0C7SXC8.1
#=GS GP350_EBVA8/1-159      AC P68343.1
#=GS O91331_9GAMA/1-158     AC O91331.1
#=GS GP350_EBVB9/1-159      AC P03200.1
#=GS Q993G4_9GAMA/1-157     AC Q993G4.1
A0A0C7SXC8_EBVG/1-159             MEAALLVCQYTIQSLIHLTGEDPGFFNVEIPEFPFYPTCNVCTADVNVTINFDVGGKKHQLDLDFGQ.LTPHTKAVYQPRGAFGGSENATNLFLLELLGAGELALTMRSKKLPINVTTGEEqQVSLESVDVYFQDVFGTMWCHHAEMQNPVYLIPETVPY
GP350_EBVA8/1-159                 MEAALLVCQYTIQSLIQLTRDDPGFFNVEILEFPFYPACNVCTADVNATINFDVGGKKHKLNLDFGL.LTPHTKAVYQPRGAFGGSENATNLFLLELLGAGELALTMRSKKLPINITTGEEqQVSLESVDVYFQDVFGTMWCHHAEMQNPVYLIPETVPY
O91331_9GAMA/1-158                MEAAFLLCQYTLQSVFHFAGEDPGFFNIEMLQFPFYPKCEVCTADVNISIVFKVGEANRHLDLYFGP.ITPITQNIYQPLHASGGIENVTSLFSLELLGARTMALTMRSIIFPINVSRDEE.HVSMEALYIYFLDAFDILWCQRVQMKEPVYLIPKKMPP
GP350_EBVB9/1-159                 MEAALLVCQYTIQSLIHLTGEDPGFFNVEIPEFPFYPTCNVCTADVNVTINFDVGGKKHQLDLDFGQ.LTPHTKAVYQPRGAFGGSENATNLFLLELLGAGELALTMRSKKLPINVTTGEEqQVSLESVDVYFQDVFGTMWCHHAEMQNPVYLIPETVPY
Q993G4_9GAMA/1-157                METALLLCSYVYYSVVNLPSDETGFLNVELPNFPFYPHCRACDPKLNVTFIIGSGTETETVEVAFGSlLVNQNKSIYTPVHVTGGKDGADRLFVMELLGGGLMAITIDVNQSPVSGSEGNK.--PVTAFLVRFTDFMDVTRCHLVNITDPIVLYPNLIPP
#=GC seq_cons                     MEAALLVCQYTIQSLIHLTGEDPGFFNVEIPEFPFYPsCNVCTADVNVTINFDVGGKKHpLDLDFGp.LTPHTKAVYQPRGAFGGSENATNLFLLELLGAGELALTMRSKKLPINVTTGEEQQVSLESVDVYFQDVFGTMWCHHAEMQNPVYLIPETVPY
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