ID   PAP_EHV1B               Reviewed;         405 AA.
AC   P28958; Q6S6Q3;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   23-FEB-2022, entry version 78.
DE   RecName: Full=DNA polymerase processivity factor;
DE   AltName: Full=DNA-binding gene 18 protein;
DE   AltName: Full=Polymerase accessory protein;
DE            Short=PAP;
GN   OrderedLocusNames=18;
OS   Equine herpesvirus 1 (strain Ab4p) (EHV-1) (Equine abortion virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=31520;
OH   NCBI_TaxID=9796; Equus caballus (Horse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=1318606; DOI=10.1016/0042-6822(92)90706-u;
RA   Telford E.A.R., Watson M.S., McBride K., Davison A.J.;
RT   "The DNA sequence of equine herpesvirus-1.";
RL   Virology 189:304-316(1992).
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; AY665713; AAT67275.1; -; Genomic_DNA.
DR   PIR; A36797; WZBEB2.
DR   RefSeq; YP_053063.1; NC_001491.2.
DR   SMR; P28958; -.
DR   IntAct; P28958; 1.
DR   GeneID; 1487522; -.
DR   KEGG; vg:1487522; -.
DR   Proteomes; UP000001189; 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   GO; GO:1900264; P:positive regulation of DNA-directed DNA polymerase activity; IDA:AgBase.
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..405
FT                   /note="DNA polymerase processivity factor"
FT                   /id="PRO_0000116062"
FT   REGION          354..376
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           358..373
FT                   /note="Bipartite nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        358..375
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   405 AA;  45087 MW;  24CC7D018D53DF8E CRC64;
     MALPRAMRPG GSHPNNFLFN TLPVIDNPVE RQRAMAVFER ESLRDAFEML TPIAPSLKNA
     FLIFNEDGLL IHTSVGGEQV YIPIQTNNME SYSWKKAPPA VFLANVDGRR GLLDAFKAKT
     QTNVSKVVFE IENYSPSRIL TQTVFSARDQ TEEDTEMGSD AEGATQTVSS RLVKHEFNNY
     ALMLPTRQPD VSMSLSKAQL NKILGVCKQA GDPITFQCLF DDTLQVRSGD RQVVFSVDYQ
     HADNCGVESS SSLLEKMPMK TKKSAPEPIR GISGRRLFTL VLDEDTNFKQ LIQKLKLKNA
     GAVLNFFLDP DSIPMIGLST KQPFSVMMFF MCSYPTQPCQ VGFSPAAFSS TPMGAGVKRR
     ASEEEESDQP PKKLFPDGKL FKSNFVLLMD KTGAKIPCPE QPMHF