SCP_HHV8P
ID SCP_HHV8P Reviewed; 170 AA.
AC Q2HR63;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 29-SEP-2021, entry version 52.
DE RecName: Full=Small capsomere-interacting protein {ECO:0000255|HAMAP-Rule:MF_04022};
GN Name=SCP {ECO:0000255|HAMAP-Rule:MF_04022}; OrderedLocusNames=ORF65;
OS Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's
OS sarcoma-associated herpesvirus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Rhadinovirus.
OX NCBI_TaxID=868565;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10400794; DOI=10.1128/jvi.73.8.6953-6963.1999;
RA Glenn M., Rainbow L., Aurade F., Davison A., Schulz T.F.;
RT "Identification of a spliced gene from Kaposi's sarcoma-associated
RT herpesvirus encoding a protein with similarities to latent membrane
RT proteins 1 and 2A of Epstein-Barr virus.";
RL J. Virol. 73:6953-6963(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16760382; DOI=10.1099/vir.0.81919-0;
RA Rezaee S.A.R., Cunningham C., Davison A.J., Blackbourn D.J.;
RT "Kaposi's sarcoma-associated herpesvirus immune modulation: an overview.";
RL J. Gen. Virol. 87:1781-1804(2006).
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 -!- 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}.
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DR EMBL; AF148805; ABD28922.1; -; Genomic_DNA.
DR RefSeq; YP_001129422.1; NC_009333.1.
DR PDB; 6CGR; EM; 4.20 A; A=1-170.
DR PDB; 6PPB; EM; 4.30 A; 0/1/2/3=1-170.
DR PDB; 6PPD; EM; 3.70 A; 0/1/2/3/A=1-170.
DR PDB; 6PPH; EM; 3.80 A; 0/1/2/3/A=1-170.
DR PDBsum; 6CGR; -.
DR PDBsum; 6PPB; -.
DR PDBsum; 6PPD; -.
DR PDBsum; 6PPH; -.
DR SMR; Q2HR63; -.
DR PRIDE; Q2HR63; -.
DR DNASU; 4961451; -.
DR GeneID; 4961451; -.
DR KEGG; vg:4961451; -.
DR Proteomes; UP000000942; 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..170
FT /note="Small capsomere-interacting protein"
FT /id="PRO_0000423790"
FT REGION 76..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 170 AA; 18569 MW; 0B8620E9547FF42A CRC64;
MSNFKVRDPV IQERLDHDYA HHPLVARMNT LDQGNMSQAE YLVQKRHYLV FLIAHHYYEA
YLRRMGGIQR RDHLQTLRDQ KPRERADRVS AASAYDAGTF TVPSRPGPAS GTTPGGQDSL
GVSGSSITTL SSGPHSLSPA SDILTTLSST TETAAPAVAD ARKPPSGKKK
