PAP_HHV11
ID PAP_HHV11 Reviewed; 488 AA.
AC P10226; B9VQH0; Q09I91;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=DNA polymerase processivity factor;
DE AltName: Full=DNA-binding protein UL42;
DE AltName: Full=Polymerase accessory protein;
DE Short=PAP;
GN ORFNames=UL42;
OS Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX NCBI_TaxID=10299;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE 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].
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nonneuroinvasive mutant HF10;
RX PubMed=17218138; DOI=10.1016/j.micinf.2006.10.019;
RA Ushijima Y., Luo C., Goshima F., Yamauchi Y., Kimura H., Nishiyama Y.;
RT "Determination and analysis of the DNA sequence of highly attenuated herpes
RT simplex virus type 1 mutant HF10, a potential oncolytic virus.";
RL Microbes Infect. 9:142-149(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17 syn+;
RA Cunningham C., Davison A.J.;
RT "Herpes simplex virus type 1 bacterial artificial chromosome.";
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, AND INTERACTION WITH UL30.
RX PubMed=2173776; DOI=10.1128/jvi.64.12.5976-5987.1990;
RA Gottlieb J., Marcy A.I., Coen D.M., Challberg M.D.;
RT "The herpes simplex virus type 1 UL42 gene product: a subunit of DNA
RT polymerase that functions to increase processivity.";
RL J. Virol. 64:5976-5987(1990).
RN [6]
RP INTERACTION WITH UL9.
RX PubMed=15673714; DOI=10.1093/nar/gki196;
RA Trego K.S., Zhu Y., Parris D.S.;
RT "The herpes simplex virus type 1 DNA polymerase processivity factor, UL42,
RT does not alter the catalytic activity of the UL9 origin-binding protein but
RT facilitates its loading onto DNA.";
RL Nucleic Acids Res. 33:536-545(2005).
RN [7]
RP NUCLEAR LOCALIZATION SIGNAL.
RX PubMed=19053255; DOI=10.1021/bi800869y;
RA Alvisi G., Avanzi S., Musiani D., Camozzi D., Leoni V., Ly-Huynh J.D.,
RA Ripalti A.;
RT "Nuclear import of HSV-1 DNA polymerase processivity factor UL42 is
RT mediated by a C-terminally located bipartite nuclear localization signal.";
RL Biochemistry 47:13764-13777(2008).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-319.
RX PubMed=15048824; DOI=10.1002/prot.10630;
RA Hicks J.M., Hsu V.L.;
RT "The extended left-handed helix: a simple nucleic acid-binding motif.";
RL Proteins 55:330-338(2004).
CC -!- FUNCTION: Plays an essential role in viral DNA replication by acting as
CC the polymerase accessory subunit. Associates with the viral polymerase
CC to increase its processivity and forms high-affinity direct
CC interactions with DNA. Facilitates the origin-binding protein UL9
CC loading onto DNA thus increasing its ability to assemble into a
CC functional complex capable of unwinding duplex DNA.
CC {ECO:0000269|PubMed:2173776}.
CC -!- SUBUNIT: Interacts with the DNA polymerase catalytic subunit UL30.
CC Interacts with the origin-binding protein.
CC {ECO:0000269|PubMed:15673714, ECO:0000269|PubMed:2173776}.
CC -!- INTERACTION:
CC P10226; P04293: UL30; NbExp=3; IntAct=EBI-1029310, EBI-8615017;
CC P10226; P10193: UL9; NbExp=3; IntAct=EBI-1029310, EBI-8596799;
CC P10226; P19838: NFKB1; Xeno; NbExp=4; IntAct=EBI-1029310, EBI-300010;
CC P10226; PRO_0000030311 [P19838]: NFKB1; Xeno; NbExp=2; IntAct=EBI-1029310, EBI-697771;
CC P10226; Q04206: RELA; Xeno; NbExp=6; IntAct=EBI-1029310, EBI-73886;
CC -!- SUBCELLULAR LOCATION: Host nucleus.
CC -!- SIMILARITY: Belongs to the herpesviridae DNA polymerase processivity
CC factor family. {ECO:0000305}.
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DR EMBL; X14112; CAA32305.1; -; Genomic_DNA.
DR EMBL; M19121; AAA45824.1; -; Genomic_DNA.
DR EMBL; DQ889502; ABI63504.1; -; Genomic_DNA.
DR EMBL; FJ593289; ACM62265.1; -; Genomic_DNA.
DR PIR; D29890; WMBE42.
DR RefSeq; YP_009137117.1; NC_001806.2.
DR PDB; 1DML; X-ray; 2.70 A; A/C/E/G=1-319.
DR PDBsum; 1DML; -.
DR SMR; P10226; -.
DR BioGRID; 971437; 3.
DR IntAct; P10226; 6.
DR MINT; P10226; -.
DR PRIDE; P10226; -.
DR GeneID; 24271471; -.
DR KEGG; vg:24271471; -.
DR EvolutionaryTrace; P10226; -.
DR Proteomes; UP000009294; Genome.
DR Proteomes; UP000180652; Genome.
DR GO; GO:0042575; C:DNA polymerase complex; IDA:GO_Central.
DR GO; GO:0042025; C:host cell nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0030337; F:DNA polymerase processivity factor activity; IDA:GO_Central.
DR GO; GO:0039686; P:bidirectional double-stranded viral DNA replication; IDA:UniProtKB.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR InterPro; IPR003202; Herpes_UL42.
DR Pfam; PF02282; Herpes_UL42; 2.
PE 1: Evidence at protein level;
KW 3D-structure; DNA replication; DNA-binding; Host nucleus;
KW Reference proteome.
FT CHAIN 1..488
FT /note="DNA polymerase processivity factor"
FT /id="PRO_0000116061"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 394..413
FT /note="Bipartite nuclear localization signal"
FT COMPBIAS 331..356
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..409
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 349
FT /note="S -> N (in strain: Nonneuroinvasive mutant HF10)"
FT STRAND 31..36
FT /evidence="ECO:0007829|PDB:1DML"
FT HELIX 37..47
FT /evidence="ECO:0007829|PDB:1DML"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:1DML"
FT TURN 51..54
FT /evidence="ECO:0007829|PDB:1DML"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:1DML"
FT STRAND 65..72
FT /evidence="ECO:0007829|PDB:1DML"
FT STRAND 75..82
FT /evidence="ECO:0007829|PDB:1DML"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:1DML"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:1DML"
FT STRAND 96..103
FT /evidence="ECO:0007829|PDB:1DML"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:1DML"
FT STRAND 120..129
FT /evidence="ECO:0007829|PDB:1DML"
FT STRAND 135..142
FT /evidence="ECO:0007829|PDB:1DML"
FT STRAND 150..153
FT /evidence="ECO:0007829|PDB:1DML"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:1DML"
FT STRAND 166..169
FT /evidence="ECO:0007829|PDB:1DML"
FT STRAND 175..180
FT /evidence="ECO:0007829|PDB:1DML"
FT HELIX 182..191
FT /evidence="ECO:0007829|PDB:1DML"
FT STRAND 200..204
FT /evidence="ECO:0007829|PDB:1DML"
FT STRAND 208..213
FT /evidence="ECO:0007829|PDB:1DML"
FT STRAND 218..222
FT /evidence="ECO:0007829|PDB:1DML"
FT HELIX 228..233
FT /evidence="ECO:0007829|PDB:1DML"
FT HELIX 248..251
FT /evidence="ECO:0007829|PDB:1DML"
FT STRAND 257..260
FT /evidence="ECO:0007829|PDB:1DML"
FT STRAND 265..271
FT /evidence="ECO:0007829|PDB:1DML"
FT HELIX 274..280
FT /evidence="ECO:0007829|PDB:1DML"
FT STRAND 285..291
FT /evidence="ECO:0007829|PDB:1DML"
FT STRAND 293..296
FT /evidence="ECO:0007829|PDB:1DML"
FT STRAND 298..307
FT /evidence="ECO:0007829|PDB:1DML"
FT STRAND 310..315
FT /evidence="ECO:0007829|PDB:1DML"
SQ SEQUENCE 488 AA; 51159 MW; 432974563DF0A81B CRC64;
MTDSPGGVAP ASPVEDASDA SLGQPEEGAP CQVVLQGAEL NGILQAFAPL RTSLLDSLLV
MGDRGILIHN TIFGEQVFLP LEHSQFSRYR WRGPTAAFLS LVDQKRSLLS VFRANQYPDL
RRVELAITGQ APFRTLVQRI WTTTSDGEAV ELASETLMKR ELTSFVVLVP QGTPDVQLRL
TRPQLTKVLN ATGADSATPT TFELGVNGKF SVFTTSTCVT FAAREEGVSS STSTQVQILS
NALTKAGQAA ANAKTVYGEN THRTFSVVVD DCSMRAVLRR LQVGGGTLKF FLTTPVPSLC
VTATGPNAVS AVFLLKPQKI CLDWLGHSQG SPSAGSSASR ASGSEPTDSQ DSASDAVSHG
DPEDLDGAAR AGEAGALHAC PMPSSTTRVT PTTKRGRSGG EDARADTALK KPKTGSPTAP
PPADPVPLDT EDDSDAADGT AARPAAPDAR SGSRYACYFR DLPTGEASPG AFSAFRGGPQ
TPYGFGFP
