SCP_EBVB9
ID SCP_EBVB9 Reviewed; 176 AA.
AC P14348; Q777G5;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 23-FEB-2022, entry version 73.
DE RecName: Full=Small capsomere-interacting protein {ECO:0000255|HAMAP-Rule:MF_04022};
GN Name=SCP {ECO:0000255|HAMAP-Rule:MF_04022}; ORFNames=BFRF3;
OS Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Lymphocryptovirus.
OX NCBI_TaxID=10377;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=6087149; DOI=10.1038/310207a0;
RA Baer R., Bankier A.T., Biggin M.D., Deininger P.L., Farrell P.J.,
RA Gibson T.J., Hatfull G., Hudson G.S., Satchwell S.C., Seguin C.,
RA Tuffnell P.S., Barrell B.G.;
RT "DNA sequence and expression of the B95-8 Epstein-Barr virus genome.";
RL Nature 310:207-211(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2998075; DOI=10.1016/0042-6822(85)90230-2;
RA Hudson G.S., Gibson T.J., Barrell B.G.;
RT "The BamHI F region of the B95-8 Epstein-Barr virus genome.";
RL Virology 147:99-109(1985).
CC -!- FUNCTION: Participates in the assembly of the infectious particles by
CC decorating the outer surface of the capsid shell and thus forming a
CC layer between the capsid and the tegument. Complexes composed of the
CC major capsid protein and small capsomere-interacting protein/SCP
CC assemble together in the host cytoplasm and are translocated to the
CC nucleus, where they accumulate and participate in capsid assembly.
CC {ECO:0000255|HAMAP-Rule:MF_04022}.
CC -!- SUBUNIT: Interacts with the major capsid protein/MCP.
CC {ECO:0000255|HAMAP-Rule:MF_04022}.
CC -!- INTERACTION:
CC P14348; P0C703: MCP; Xeno; NbExp=2; IntAct=EBI-2620158, EBI-9645180;
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04022}. Host
CC nucleus {ECO:0000255|HAMAP-Rule:MF_04022}.
CC -!- SIMILARITY: Belongs to the herpesviridae small capsomere-interacting
CC protein family. {ECO:0000255|HAMAP-Rule:MF_04022}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA24838.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; V01555; CAA24838.1; ALT_INIT; Genomic_DNA.
DR EMBL; M11923; AAA45870.1; -; Genomic_DNA.
DR EMBL; AJ507799; CAD53401.1; -; Genomic_DNA.
DR RefSeq; YP_401651.1; NC_007605.1.
DR PDB; 6W19; EM; 5.50 A; Q/R/S/T/U/V/W/X/Y/Z/a/b/c/d/e/u=1-176.
DR PDB; 6W2D; EM; 4.00 A; Z/a/d/e/u=1-176.
DR PDB; 6W2E; EM; 4.40 A; Z/a/d/e=1-176.
DR PDB; 7BQX; EM; 4.20 A; 2/Y/Z/y=1-176.
DR PDB; 7BR7; EM; 4.30 A; 2/Y/Z/m/y=1-176.
DR PDB; 7BR8; EM; 3.80 A; 2/Y/Z/m/y=1-176.
DR PDB; 7BSI; EM; 4.10 A; 0/1/G/H/I/J/K/L/P/Q/R/X/Y/Z/m/y=1-176.
DR PDBsum; 6W19; -.
DR PDBsum; 6W2D; -.
DR PDBsum; 6W2E; -.
DR PDBsum; 7BQX; -.
DR PDBsum; 7BR7; -.
DR PDBsum; 7BR8; -.
DR PDBsum; 7BSI; -.
DR SMR; P14348; -.
DR IntAct; P14348; 8.
DR MINT; P14348; -.
DR DNASU; 3783701; -.
DR GeneID; 3783701; -.
DR KEGG; vg:3783701; -.
DR Proteomes; UP000153037; Genome.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-UniRule.
DR GO; GO:0016032; P:viral process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_04022; HSV_SCP_gammahv; 1.
DR InterPro; IPR009299; Herpes_capsid.
DR Pfam; PF06112; Herpes_capsid; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Capsid protein; Host nucleus; Reference proteome; Virion.
FT CHAIN 1..176
FT /note="Small capsomere-interacting protein"
FT /id="PRO_0000115739"
FT REGION 75..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 176 AA; 18147 MW; DAB605ED00F1A656 CRC64;
MARRLPKPTL QGRLEADFPD SPLLPKFQEL NQNNLPNDVF REAQRSYLVF LTSQFCYEEY
VQRTFGVPRR QRAIDKRQRA SVAGAGAHAH LGGSSATPVQ QAQAAASAGT GALASSAPST
AVAQSATPSV SSSISSLRAA TSGATAAASA AAAVDTGSGG GGQPHDTAPR GARKKQ