ID   PORTL_HHV8P             Reviewed;         605 AA.
AC   F5HGK9;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 35.
DE   RecName: Full=Portal protein {ECO:0000255|HAMAP-Rule:MF_04012};
GN   Name=ORF43;
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: Forms a portal in the viral capsid through which viral DNA is
CC       translocated during DNA packaging. Assembles as a dodecamer at a single
CC       fivefold axe of the T=16 icosahedric capsid. Binds to the molecular
CC       motor that translocates the viral DNA, termed terminase.
CC       {ECO:0000255|HAMAP-Rule:MF_04012}.
CC   -!- SUBUNIT: Homododecamerizes. Interacts with terminase subunits TRM1 and
CC       TRM3. {ECO:0000255|HAMAP-Rule:MF_04012}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04012}. Host
CC       nucleus {ECO:0000255|HAMAP-Rule:MF_04012}.
CC   -!- SIMILARITY: Belongs to the herpesviridae portal protein family.
CC       {ECO:0000255|HAMAP-Rule:MF_04012}.
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DR   EMBL; AF148805; ABD28893.1; -; Genomic_DNA.
DR   RefSeq; YP_001129395.1; NC_009333.1.
DR   PDB; 6PPI; EM; 4.70 A; A/B/C/D/E/F/G/H/I/J/K/L=1-605.
DR   PDBsum; 6PPI; -.
DR   SMR; F5HGK9; -.
DR   BioGRID; 1777000; 2.
DR   PRIDE; F5HGK9; -.
DR   DNASU; 4961497; -.
DR   GeneID; 4961497; -.
DR   KEGG; vg:4961497; -.
DR   Proteomes; UP000000942; Genome.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0044423; C:virion component; IEA:UniProtKB-UniRule.
DR   GO; GO:0051276; P:chromosome organization; IEA:InterPro.
DR   GO; GO:0019076; P:viral release from host cell; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_04012; HSV_PORTL; 1.
DR   InterPro; IPR002660; Herpes_Portal.
DR   Pfam; PF01763; Herpes_UL6; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Coiled coil; Host nucleus; Reference proteome;
KW   Viral genome packaging; Viral release from host cell; Virion.
FT   CHAIN           1..605
FT                   /note="Portal protein"
FT                   /id="PRO_0000423761"
FT   REGION          583..605
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   605 AA;  68014 MW;  5AE7010A4C7646AD CRC64;
     MLRMNPGLGS SISVHPSELS ISLFEILQGK YSYVRGQTLH CSLRNPGVFF RQLFIHLYKN
     ALANCSYDHV LSDWRTYESS AKTRWPEKEA QWGSYRRSTF DSWAQTMRMT LDHLLLNAIN
     RVLYAKTQLS YERYVDWVVT VGMVPVVKHT PDHKLVNSIQ EQLMKDCQRL ASGEKTIGRI
     LTSVTQEISN LVSSLSALYI PGYSEVSIDY DCVKNTFVGL YKQKRVHVEV ITMPAILAGR
     VIFDSPIQRM YTSIMSCHRT AEHAKLCQLL NTAPTKALVG SACNNVYKDI MTHLEQASQR
     TDPKRELLNL LMKLAENKTV SGVTDVVEDF VTDVSQNIVD KNKLFGTGQE TTTQGLRRQV
     SNSVFKCLTN QINEQFDTIT QLEKERELCM KRLKCIETQL SHQQPGDAKG PGSVNLLTAN
     TFQSLGRLQD PSLQLTSSHI PSGSAVLNSF FSSYIPPVRE SMKDLTNLWE SEMFQTYKLA
     PVVDNQGQRL SVTYSQDTIS ILLGPFTYVI ADLLQMELIS HSFVSSSLQD IAAYLYQTSR
     LFVYITDVGQ KYCLVTPPFE NVPGKGPGET DWSANEYSCP EDSRVRRGLS RIPPPCGAPP
     CPGSA