ID   PORTL_EBVB9             Reviewed;         613 AA.
AC   P03213; Q777D6;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Portal protein {ECO:0000255|HAMAP-Rule:MF_04012};
GN   ORFNames=BBRF1;
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   SUBCELLULAR LOCATION.
RX   PubMed=15534216; DOI=10.1073/pnas.0407320101;
RA   Johannsen E., Luftig M., Chase M.R., Weicksel S., Cahir-McFarland E.,
RA   Illanes D., Sarracino D., Kieff E.;
RT   "Proteins of purified Epstein-Barr virus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:16286-16291(2004).
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,
CC       ECO:0000269|PubMed:15534216}. Host nucleus {ECO:0000255|HAMAP-
CC       Rule:MF_04012, ECO:0000269|PubMed:15534216}.
CC   -!- SIMILARITY: Belongs to the herpesviridae portal protein family.
CC       {ECO:0000255|HAMAP-Rule:MF_04012}.
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DR   EMBL; V01555; CAA24820.1; -; Genomic_DNA.
DR   EMBL; AJ507799; CAD53432.1; -; Genomic_DNA.
DR   PIR; E43043; QQBE33.
DR   RefSeq; YP_401682.1; NC_007605.1.
DR   PDB; 7BQT; EM; 4.80 A; A/B/C/D/E/F/G/H/I/J/K/L=1-613.
DR   PDBsum; 7BQT; -.
DR   SMR; P03213; -.
DR   BioGRID; 3509104; 3.
DR   PRIDE; P03213; -.
DR   DNASU; 3783764; -.
DR   GeneID; 3783764; -.
DR   KEGG; vg:3783764; -.
DR   Proteomes; UP000153037; 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; Host nucleus; Reference proteome; Viral genome packaging;
KW   Viral release from host cell; Virion.
FT   CHAIN           1..613
FT                   /note="Portal protein"
FT                   /id="PRO_0000115912"
FT   REGION          577..613
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   613 AA;  68457 MW;  E6E65BB078FBD9AD CRC64;
     MFNMNVDESA SGALGSSAIP VHPTPASVRL FEILQGKYAY VQGQTIYANL RNPGVFSRQV
     FTHLFKRAIS HCTYDDVLHD WNKFEACIQK RWPSDDSCAS RFRESTFESW STTMKLTVRD
     LLTTNIYRVL HSRSVLSYER YVDWICATGM VPAVKKPITQ ELHSKIKSLR DRCVCRELGH
     ERTIRSIGTE LYEATKEIIE SLNSTFIPQF TEVTIEYLPR SDEYVAYYCG RRIRLHVLFP
     PAIFAGTVTF DSPVQRLYQN IFMCYRTLEH AKICQLLNTA PLKAIVGHGG RDMYKDILAH
     LEQNSQRKDP KKELLNLLVK LSENKTISGV TDVVEEFITD ASNNLVDRNR LFGQPGETAA
     QGLKKKVSNT VVKCLTDQIN EQFDQINGLE KERELYLKKI RSMESQLQAS LGPGGNNPAA
     SAPAAVAAEA ASVDILTGST ASAIEKLFNS PSASLGARVS GHNESILNSF VSQYIPPSRE
     MTKDLTELWE SELFNTFKLT PVVDNQGQRL YVRYSSDTIS ILLGPFTYLV AELSPVELVT
     DVYATLGIVE IIDELYRSSR LAIYIEDLGR KYCPASATGG DHGIRQAPSA RGDTEPDHAK
     SKPARDPPPG AGS