ID   PORTL_VZVD              Reviewed;         769 AA.
AC   P09302;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Portal protein {ECO:0000255|HAMAP-Rule:MF_04012};
GN   Name=54;
OS   Varicella-zoster virus (strain Dumas) (HHV-3) (Human herpesvirus 3).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=10338;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=3018124; DOI=10.1099/0022-1317-67-9-1759;
RA   Davison A.J., Scott J.E.;
RT   "The complete DNA sequence of varicella-zoster virus.";
RL   J. Gen. Virol. 67:1759-1816(1986).
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; X04370; CAA27937.1; -; Genomic_DNA.
DR   PIR; B27215; WZBE54.
DR   PRIDE; P09302; -.
DR   Proteomes; UP000002602; 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..769
FT                   /note="Portal protein"
FT                   /id="PRO_0000115910"
FT   REGION          458..479
FT                   /note="Putative leucine zipper motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04012"
FT   REGION          654..675
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          750..769
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        203
FT                   /note="Interchain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04012"
FT   DISULFID        294
FT                   /note="Interchain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04012"
SQ   SEQUENCE   769 AA;  86780 MW;  5ABD7EDA6D783ECF CRC64;
     MAEITSLFNN SSGSEEKRIA SSVSIDQGLN GSNPNDQYKN MFDIYWNEYA PDIGFCTFPE
     EDGWMLIHPT TQSMLFRKIL AGDFGYTDGQ GIYSAVRSTE TVIRQVQATV LMNALDATRY
     EDLAADWEHH IQQCNLHAGA LAERYGLCGE SEAVRLAHQV FETWRQTLQS SLLEFLRGIT
     GCLYTSGLNG RVGFAKYVDW IACVGIVPVV RKVRSEQNGT PAPLNTYMGQ AAELSQMLKV
     ADATLARGAA VVTSLVECMQ NVAIMDYDRT RLYYNYNRRL IMAKDDVTGM KGECLVVWPP
     VVCGEGVVFD SPLQRLSGEV LACYALREHA RVCQVLNTAP LRVLIGRRNE DDRSHSTRAV
     DRIMGENDTT RAGSAASRLV KLIVNLKNMR HVGDITETVR SYLEETGNHI LEGSGSVDTS
     QPGFGKANQS FNGGAMSGTT NVQSAFKTSV VNSINGMLEG YVNNLFKTIE GLKDVNSDLT
     ERLQFKEGEL KRLREERVKI KPSKGSHITM AEETRIADLN HEVIDLTGII GDDAYIANSF
     QSRYIPPYGD DIKRLSELWK QELVRCFKLH RVNNNQGQEI SVSYSNASIS LLVAPYFSFI
     LRATRLGFLV TQSEVHRSEE ELCQAIFKKA RTESYLSQIR ILYEMQVRAE VIKRGPRRTP
     SPSWGLPDPT EDDERIPEPN KINNQYMHVG YKNLSHFMKG HPPERLRVHK VNAADSTLLD
     KIRANRRRGD GRWDVRNKYT QHFRLQRNDR QLTNTSRRGV GCERRDRRS