ID   PORTL_EHV1B             Reviewed;         753 AA.
AC   P28944; Q6S6U8;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Portal protein {ECO:0000255|HAMAP-Rule:MF_04012};
GN   OrderedLocusNames=56;
OS   Equine herpesvirus 1 (strain Ab4p) (EHV-1) (Equine abortion virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=31520;
OH   NCBI_TaxID=9796; Equus caballus (Horse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=1318606; DOI=10.1016/0042-6822(92)90706-u;
RA   Telford E.A.R., Watson M.S., McBride K., Davison A.J.;
RT   "The DNA sequence of equine herpesvirus-1.";
RL   Virology 189:304-316(1992).
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; AY665713; AAT67313.1; -; Genomic_DNA.
DR   PIR; B36801; WZBEE8.
DR   RefSeq; YP_053100.1; NC_001491.2.
DR   SMR; P28944; -.
DR   GeneID; 2948564; -.
DR   KEGG; vg:2948564; -.
DR   Proteomes; UP000001189; 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   3: Inferred from homology;
KW   Disulfide bond; Host nucleus; Reference proteome; Viral genome packaging;
KW   Viral release from host cell; Virion.
FT   CHAIN           1..753
FT                   /note="Portal protein"
FT                   /id="PRO_0000115905"
FT   REGION          1..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          454..475
FT                   /note="Putative leucine zipper motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04012"
FT   REGION          498..523
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          668..753
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..30
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        498..512
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        671..706
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        707..722
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        727..743
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        192
FT                   /note="Interchain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04012"
FT   DISULFID        293
FT                   /note="Interchain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04012"
SQ   SEQUENCE   753 AA;  83993 MW;  C5E118F78BBED203 CRC64;
     MSADSIEPKQ KRLRYADANK GRKVERKNTP RFEATTGLQS PGEEEQISAD GGWVLIHPTP
     KTMLFKEILM GELGYTEGQG VYNAIRSTEA AIRQIQTTIL TNTLNATRYE DLAKDWQTHL
     DSRGVSAEEI AATYGMYSEG EAVRVAEQIF ATWHRTLQMS LLDFVRSITA CFSASEPDGT
     ASFAKYIDWI ACLGLIPLQR LKRAPGATVH PKLWRKLPTD VPSLESCVDE RDLAGKLYVA
     NSLLREGLEA VVELARCTAS VAIMDYDRVN IFYHYTRREV VAIDSTTGKR GECLVLWQPI
     WKDGSVLFDS PLQRICGEVC NCHALREHAK LCQLLNTVPV KILVGRKKDE AQGPGWASKA
     VDKLMGEGEE LHSSSAASRL VKLIVNMKSM RHIGDITETV RSYLNETSTN LLSGAQVDTS
     LPGFGQSGKT KQGGNMPVQE AFRTSVINGI NGMLEGYVNN LFKTIEDLRT GNSGLLDQLR
     DRESEITHLR EQLLRVSQAA ADGSTQPGAS SAALPGSGAK SGAGGLGHEV IDIRNLMGDD
     GYVANSFQSR YIPAYTADME RLSRLWDQEL LRCFKMNRIT NNQGQEMSVS YSNSSISLLL
     APYFFSILRA RHLGFLITHQ EAYRSEEELC VAVFKKTRLE AYLTELSTLF VARVRNSIAA
     LNSTKRDLPV NDNEAQSDEE QLGKPSDERY YEGRDRSASP QRDRGRNGRG YHKRRRFSNN
     YRRRSGLARD SSIRDRSQRG SRPTPLLHDH VGH