PAP_HHV2H
ID PAP_HHV2H Reviewed; 470 AA.
AC P89463;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 02-JUN-2021, entry version 69.
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 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: 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 loading
CC onto DNA thus increasing its ability to assemble into a functional
CC complex capable of unwinding duplex DNA (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with the DNA polymerase catalytic subunit. Interacts
CC with the origin-binding protein (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the herpesviridae DNA polymerase processivity
CC factor family. {ECO:0000305}.
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DR EMBL; Z86099; CAB06728.1; -; Genomic_DNA.
DR RefSeq; YP_009137194.1; NC_001798.2.
DR SMR; P89463; -.
DR PRIDE; P89463; -.
DR DNASU; 1487329; -.
DR GeneID; 1487329; -.
DR KEGG; vg:1487329; -.
DR Proteomes; UP000001874; Genome.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR InterPro; IPR003202; Herpes_UL42.
DR Pfam; PF02282; Herpes_UL42; 2.
PE 3: Inferred from homology;
KW DNA replication; DNA-binding; Host nucleus; Reference proteome.
FT CHAIN 1..470
FT /note="DNA polymerase processivity factor"
FT /id="PRO_0000385147"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 385..404
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 329..352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..367
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..399
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 470 AA; 49884 MW; 73D2433B210669CB CRC64;
MAHLPGGAAA APLSEDAIPS PRERTEDWPP CQIVLQGAEL NGILQAFAPL RTSLLDSLLV
VGDRGILVHN AIFGEQVFLP LDHSQFSRYR WGGPTAAFLS LVDQKRSLLS VFRANQYPDL
RRVELTVTGQ APFRTLVQRI WTTASDGEAV ELASETLMKR ELTSFAVLLP QGDPDVQLRL
TKPQLTKVVN AVGDETAKPT TFELGPNGKF SVFNARTCVT FAAREEGASS STSAQVQILT
SALKKAGQAA ANAKTVYGEN THRTFSVVVD DCSMRAVLRR LQVGGGTLKF FLTADVPSVC
VTATGPNAVS AVFLLKPQRV CLNWLGRSPG SSTGSLASQD SRAGPTDSQD SSSEPDAGDR
GAPEEEGLEG QARVPPAFPE PPGTKRRHPG AEVVPADDAT KRPKTGVPAA PTRAESPPLS
ARYGPEAAEG GGDGGRYACY FRDLQTGDAS PSPLSAFRGP QRPPYGFGLP