ID A1BM55_9GAMA Unreviewed; 211 AA.
AC A1BM55;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Small capsomere-interacting protein {ECO:0000256|HAMAP-Rule:MF_04022};
GN Name=SCP {ECO:0000256|HAMAP-Rule:MF_04022};
GN ORFNames=OvHV-2gp64 {ECO:0000313|EMBL:ABB22284.1};
OS Ovine gammaherpesvirus 2.
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Orthoherpesviridae; Gammaherpesvirinae; Macavirus;
OC Macavirus ovinegamma2.
OX NCBI_TaxID=10398 {ECO:0000313|EMBL:ABB22284.1, ECO:0000313|Proteomes:UP000152762};
RN [1] {ECO:0000313|EMBL:ABB22284.1, ECO:0000313|Proteomes:UP000152762}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17170434; DOI=10.1099/vir.0.82285-0;
RA Taus N.S., Herndon D.R., Traul D.L., Stewart J.P., Ackermann M., Li H.,
RA Knowles D.P., Lewis G.S., Brayton K.A.;
RT "Comparison of ovine herpesvirus 2 genomes isolated from domestic sheep
RT (Ovis aries) and a clinically affected cow (Bos bovis).";
RL J. Gen. Virol. 88:40-45(2007).
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:0000256|HAMAP-Rule:MF_04022}.
CC -!- SUBUNIT: Interacts with the major capsid protein/MCP.
CC {ECO:0000256|HAMAP-Rule:MF_04022}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000256|HAMAP-Rule:MF_04022}. Host
CC nucleus {ECO:0000256|HAMAP-Rule:MF_04022}.
CC -!- SIMILARITY: Belongs to the herpesviridae small capsomere-interacting
CC protein family. {ECO:0000256|HAMAP-Rule:MF_04022}.
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DR EMBL; DQ198083; ABB22284.1; -; Genomic_DNA.
DR Proteomes; UP000152762; 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 3: Inferred from homology;
KW Capsid protein {ECO:0000256|ARBA:ARBA00022561, ECO:0000256|HAMAP-
KW Rule:MF_04022}; Host nucleus {ECO:0000256|HAMAP-Rule:MF_04022};
KW Reference proteome {ECO:0000313|Proteomes:UP000152762};
KW Virion {ECO:0000256|HAMAP-Rule:MF_04022}.
FT REGION 70..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..122
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 211 AA; 22002 MW; 54BEB403477B17B7 CRC64;
MSYARPRLPR IHVRLEQDYP HDPRVQQLQV QVLNNPNYAN NVRAPYTYLV FLTAQQTYDA
YVRQARGVNK KKLPPSNKPP PQPNNQPNNQ QANNLPPVPP HPSGAGSGGG PPNAPPLPDK
PDPQQGGGAN NQSQGSGGGN PLPPDPGCLP QPRDDRGGLG PGIPGLPPGL PKGLPLQLGL
VGSDGGGPPA SPVDSPPTKP VAPKKGSKGA R
//
