ID PORTL_HHV11 Reviewed; 676 AA. AC P10190; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1989, sequence version 1. DT 04-NOV-2026, entry version 101. DE RecName: Full=Portal protein {ECO:0000255|HAMAP-Rule:MF_04012}; GN Name=UL6; OS Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1). OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes; OC Herpesvirales; Orthoherpesviridae; Alphaherpesvirinae; Simplexvirus; OC Simplexvirus humanalpha1; Human herpesvirus 1. OX NCBI_TaxID=10299; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2839594; DOI=10.1099/0022-1317-69-7-1531; RA McGeoch D.J., Dalrymple M.A., Davison A.J., Dolan A., Frame M.C., McNab D., RA Perry L.J., Scott J.E., Taylor P.; RT "The complete DNA sequence of the long unique region in the genome of RT herpes simplex virus type 1."; RL J. Gen. Virol. 69:1531-1574(1988). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-80. RX PubMed=2826807; DOI=10.1128/jvi.62.2.444-453.1988; RA McGeoch D.J., Dalrymple M.A., Dolan A., McNab D., Perry L.J., Taylor P., RA Challberg M.D.; RT "Structures of herpes simplex virus type 1 genes required for replication RT of virus DNA."; RL J. Virol. 62:444-453(1988). RN [3] RP FUNCTION. RX PubMed=11602732; DOI=10.1128/jvi.75.22.10923-10932.2001; RA Newcomb W.W., Juhas R.M., Thomsen D.R., Homa F.L., Burch A.D., Weller S.K., RA Brown J.C.; RT "The UL6 gene product forms the portal for entry of DNA into the herpes RT simplex virus capsid."; RL J. Virol. 75:10923-10932(2001). RN [4] RP INTERACTION WITH UL15 AND UL28, AND SUBCELLULAR LOCATION. RX PubMed=12743292; DOI=10.1128/jvi.77.11.6351-6358.2003; RA White C.A., Stow N.D., Patel A.H., Hughes M., Preston V.G.; RT "Herpes simplex virus type 1 portal protein UL6 interacts with the putative RT terminase subunits UL15 and UL28."; RL J. Virol. 77:6351-6358(2003). RN [5] RP HOMODODECAMERIZATION. RX PubMed=15507654; DOI=10.1128/jvi.78.22.12668-12671.2004; RA Trus B.L., Cheng N., Newcomb W.W., Homa F.L., Brown J.C., Steven A.C.; RT "Structure and polymorphism of the UL6 portal protein of herpes simplex RT virus type 1."; RL J. Virol. 78:12668-12671(2004). RN [6] RP SUBCELLULAR LOCATION. RX PubMed=16920825; DOI=10.1128/jvi.01364-06; RA Wills E., Scholtes L., Baines J.D.; RT "Herpes simplex virus 1 DNA packaging proteins encoded by UL6, UL15, UL17, RT UL28, and UL33 are located on the external surface of the viral capsid."; RL J. Virol. 80:10894-10899(2006). RN [7] RP INTERACTION WITH TRM1 AND TRM3. RX PubMed=19224991; DOI=10.1128/jvi.00026-09; RA Yang K., Wills E., Baines J.D.; RT "The putative leucine zipper of the UL6-encoded portal protein of herpes RT simplex virus 1 is necessary for interaction with pUL15 and pUL28 and their RT association with capsids."; RL J. Virol. 83:4557-4564(2009). RN [8] RP MUTAGENESIS OF CYS-145; CYS-166 AND CYS-254. RX PubMed=21593161; DOI=10.1128/jvi.00123-11; RA Albright B.S., Nellissery J., Szczepaniak R., Weller S.K.; RT "Disulfide bond formation in the herpes simplex virus 1 UL6 protein is RT required for portal ring formation and genome encapsidation."; RL J. Virol. 85:8616-8624(2011). 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, ECO:0000269|PubMed:11602732}. CC -!- SUBUNIT: Homododecamerizes. Interacts with terminase subunits TRM1 and CC TRM3. {ECO:0000255|HAMAP-Rule:MF_04012, ECO:0000269|PubMed:12743292, CC ECO:0000269|PubMed:19224991}. CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04012, CC ECO:0000269|PubMed:16920825}. Host nucleus {ECO:0000255|HAMAP- CC Rule:MF_04012, ECO:0000269|PubMed:12743292}. CC -!- SIMILARITY: Belongs to the herpesviridae portal protein family. CC {ECO:0000255|HAMAP-Rule:MF_04012}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X14112; CAA32342.1; -; Genomic_DNA. DR EMBL; AH002360; AAA45818.2; -; Genomic_DNA. DR PIR; F28133; WMBEX6. DR PDB; 9OP4; EM; 3.60 A; a/b/c/d/e/f/g/h/i/j/k/l=1-676. DR PDB; 9OP5; EM; 3.50 A; a/b/c/d/e/f/g/h/i/j/k/l=1-676. DR PDB; 9OP8; EM; 3.80 A; a/b/c/d/e/f/g/h/i/j/k/l=1-676. DR PDB; 9OPB; EM; 3.60 A; M/N/O/P/Q/R/S/T/U/V=1-676. DR PDB; 9OPC; EM; 4.20 A; a/b/c/d/e/f/g/h/i/j/k/l=1-676. DR PDB; 9OPV; EM; 3.40 A; M/N/O/P/Q/R/S/T/U/V=1-676. DR SMR; P10190; -. DR BioGRID; 971454; 1. DR IntAct; P10190; 2. DR TCDB; 1.W.4.1.1; the viral portal protein 4 (ppp4) family. DR HAMAP; MF_04012; HSV_PORTL; 1. DR InterPro; IPR002660; Herpes_Portal. DR Pfam; PF01763; Herpes_UL6; 1. 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:UniProtKB-UniRule. DR GO; GO:0019076; P:viral release from host cell; IEA:UniProtKB-UniRule. DR Proteomes; UP000009294; Segment. PE 1: Evidence at protein level; KW 3D-structure; Disulfide bond; Host nucleus; Reference proteome; KW Viral genome packaging; Viral release from host cell; Virion. FT CHAIN 1..676 FT /note="Portal protein" FT /id="PRO_0000115903" FT REGION 383..404 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 ECO:0000305|PubMed:19224991" FT REGION 627..676 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 666..676 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 ECO:0000269|PubMed:21593161" FT DISULFID 254 FT /note="Interchain" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04012, FT ECO:0000269|PubMed:21593161" FT MUTAGEN 145 FT /note="C->A: Complete loss of nuclear localization." FT /evidence="ECO:0000269|PubMed:21593161" FT MUTAGEN 166 FT /note="C->A: Complete loss of portal ring formation." FT /evidence="ECO:0000269|PubMed:21593161" FT MUTAGEN 254 FT /note="C->A: Complete loss of portal ring formation." FT /evidence="ECO:0000269|PubMed:21593161" FT STRAND 27..29 FT /evidence="ECO:0007829|PDB:9OP5" FT STRAND 31..33 FT /evidence="ECO:0007829|PDB:9OP5" FT HELIX 34..44 FT /evidence="ECO:0007829|PDB:9OP5" FT HELIX 52..55 FT /evidence="ECO:0007829|PDB:9OP5" FT HELIX 56..59 FT /evidence="ECO:0007829|PDB:9OP5" FT HELIX 63..79 FT /evidence="ECO:0007829|PDB:9OP5" FT HELIX 83..97 FT /evidence="ECO:0007829|PDB:9OP5" FT HELIX 101..108 FT /evidence="ECO:0007829|PDB:9OP5" FT HELIX 113..143 FT /evidence="ECO:0007829|PDB:9OP5" FT TURN 144..146 FT /evidence="ECO:0007829|PDB:9OP5" FT HELIX 147..149 FT /evidence="ECO:0007829|PDB:9OP5" FT STRAND 152..155 FT /evidence="ECO:0007829|PDB:9OP5" FT HELIX 157..166 FT /evidence="ECO:0007829|PDB:9OP5" FT STRAND 168..174 FT /evidence="ECO:0007829|PDB:9OP5" FT HELIX 180..189 FT /evidence="ECO:0007829|PDB:9OP5" FT HELIX 193..197 FT /evidence="ECO:0007829|PDB:9OP5" FT HELIX 199..221 FT /evidence="ECO:0007829|PDB:9OP5" FT STRAND 222..224 FT /evidence="ECO:0007829|PDB:9OP5" FT TURN 227..229 FT /evidence="ECO:0007829|PDB:9OP5" FT STRAND 231..235 FT /evidence="ECO:0007829|PDB:9OP5" FT TURN 236..239 FT /evidence="ECO:0007829|PDB:9OP5" FT STRAND 240..245 FT /evidence="ECO:0007829|PDB:9OP5" FT TURN 246..249 FT /evidence="ECO:0007829|PDB:9OP5" FT STRAND 250..258 FT /evidence="ECO:0007829|PDB:9OP5" FT HELIX 272..296 FT /evidence="ECO:0007829|PDB:9OP5" FT STRAND 300..304 FT /evidence="ECO:0007829|PDB:9OP5" FT HELIX 338..347 FT /evidence="ECO:0007829|PDB:9OPV" FT HELIX 357..365 FT /evidence="ECO:0007829|PDB:9OPV" FT HELIX 408..457 FT /evidence="ECO:0007829|PDB:9OPV" FT HELIX 459..472 FT /evidence="ECO:0007829|PDB:9OPV" FT STRAND 495..498 FT /evidence="ECO:0007829|PDB:9OP5" FT TURN 501..503 FT /evidence="ECO:0007829|PDB:9OP5" FT STRAND 505..514 FT /evidence="ECO:0007829|PDB:9OP5" FT HELIX 522..539 FT /evidence="ECO:0007829|PDB:9OP5" FT STRAND 542..545 FT /evidence="ECO:0007829|PDB:9OP5" FT STRAND 553..557 FT /evidence="ECO:0007829|PDB:9OP5" FT HELIX 562..566 FT /evidence="ECO:0007829|PDB:9OP5" FT HELIX 569..573 FT /evidence="ECO:0007829|PDB:9OP5" FT TURN 587..589 FT /evidence="ECO:0007829|PDB:9OP5" FT HELIX 592..602 FT /evidence="ECO:0007829|PDB:9OP5" FT HELIX 604..622 FT /evidence="ECO:0007829|PDB:9OP5" SQ SEQUENCE 676 AA; 74092 MW; 8CF9D73C6313FAE9 CRC64; MTAPRSRAPT TRARGDTEAL CSPEDGWVKV HPSPGTMLFR EILHGQLGYT EGQGVYNVVR SSEATTRQLQ AAIFHALLNA TTYRDLEADW LGHVAARGLQ PQRLVRRYRN AREADIAGVA ERVFDTWRNT LRTTLLDFAH GLVACFAPGG PSGPSSFPKY IDWLTCLGLV PILRKRQEGG VTQGLRAFLK QHPLTRQLAT VAEAAERAGP GFFELALAFD STRVADYDRV YIYYNHRRGD WLVRDPISGQ RGECLVLWPP LWTGDRLVFD SPVQRLFPEI VACHSLREHA HVCRLRNTAS VKVLLGRKSD SERGVAGAAR VVNKVLGEDD ETKAGSAASR LVRLIINMKG MRHVGDINDT VRSYLDEAGG HLIDAPAVDG TLPGFGKGGN SRGSAGQDQG GRAPQLRQAF RTAVVNNING VLEGYINNLF GTIERLRETN AGLATQLQER DRELRRATAG ALERQQRAAD LAAESVTGGC GSRPAGADLL RADYDIIDVS KSMDDDTYVA NSFQHPYIPS YAQDLERLSR LWEHELVRCF KILCHRNNQG QETSISYSSG AIAAFVAPYF ESVLRAPRVG APITGSDVIL GEEELWDAVF KKTRLQTYLT DIAALFVADV QHAALPPPPS PVGADFRPGA SPRGRSRSRS PGRTARGAPD QGGGIGHRDG RRDGRR //