PORTL_HHV2H
ID PORTL_HHV2H Reviewed; 678 AA.
AC P89429;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Portal protein {ECO:0000255|HAMAP-Rule:MF_04012};
GN Name=UL6;
OS Human herpesvirus 2 (strain HG52) (HHV-2) (Human herpes simplex virus 2).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX NCBI_TaxID=10315;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=9499055; DOI=10.1128/jvi.72.3.2010-2021.1998;
RA Dolan A., Jamieson F.E., Cunningham C., Barnett B.C., McGeoch D.J.;
RT "The genome sequence of herpes simplex virus type 2.";
RL J. Virol. 72:2010-2021(1998).
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; Z86099; CAB06766.1; -; Genomic_DNA.
DR SMR; P89429; -.
DR PRIDE; P89429; -.
DR Proteomes; UP000001874; 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..678
FT /note="Portal protein"
FT /id="PRO_0000115904"
FT REGION 376..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..443
FT /note="Putative leucine zipper motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04012"
FT REGION 459..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 622..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..678
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 166
FT /note="Interchain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04012"
FT DISULFID 254
FT /note="Interchain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04012"
SQ SEQUENCE 678 AA; 74902 MW; B2974CA22AADB1F4 CRC64;
MAAQRARAPA MRTRGGDAAL CAPEDGWVKV HPTPGTMLFR EILLGQMGYT EGQGVYNVVR
SSEAATRQLQ AAIFHALLNA TTYRDLEEDW RRHVVARGLQ PQRLVRRYRN AREGDIAGVA
ERVFDTWRCT LRTTLLDFAH GVVDCFAPGG PSGPTSFPKY IDWLTCLGLV PILRKTREGE
ATQRLGAFLR QHTLPRQLAT VAGAAERAGP GLLDLAVAFD STRMAEYDRV HIYYNHRRGE
WLVRDPVSGQ RGECLVLCPP LWTGDRLVFD SPVQRLCPEI VACHALREHA HICRLRNTAS
VKVLLGRKSD SERGVAGAAR VVNKALGEDD ETKAGSAASR LVRLIINMKG MRHVGDINDT
VRAYLDEAGG HLIDTPAVDH TLPGFGKGGT GRGSRPQDPG ARPQQLRQAF QTAVVNNING
MLEGYINNLF GTIERLRETN AGLATQLQAR DRELRRAQAG ALEREQRAAD RAAGGGAGRP
AEADLLRADY DIIDVSKSMD DDTYVANSFQ HQYIPAYGQD LERLSRLWEH ELVRCFKILR
HRNKQGQETS ISYSSGAIAS FVAPYFEYVL RAPRAGALIT GSDVILGEEE LWEAVFKKTR
LQTYLTDVAA LFVADVQHAA LPRPPSPTPA DFRASASPRG GSRSRTRTRS RSPGRTPRGA
PDQGWGVERR DGRPHARR