ID   DPOL_PSHV1              Reviewed;        1081 AA.
AC   Q6UDK1;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   23-FEB-2022, entry version 90.
DE   RecName: Full=DNA polymerase catalytic subunit;
DE            EC=2.7.7.7;
DE            EC=3.1.26.4;
GN   Name=UL30;
OS   Psittacid herpesvirus 1 (isolate Amazon parrot/-/97-0001/1997) (PsHV-1)
OS   (Pacheco's disease virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Iltovirus.
OX   NCBI_TaxID=670426;
OH   NCBI_TaxID=152276; Amazona oratrix (yellow-headed parrot).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16873243; DOI=10.1128/jvi.00134-06;
RA   Thureen D.R., Keeler C.L. Jr.;
RT   "Psittacid herpesvirus 1 and infectious laryngotracheitis virus:
RT   Comparative genome sequence analysis of two avian alphaherpesviruses.";
RL   J. Virol. 80:7863-7872(2006).
CC   -!- FUNCTION: Replicates viral genomic DNA. The replication complex is
CC       composed of six viral proteins: the DNA polymerase, processivity
CC       factor, primase, primase-associated factor, helicase, and ssDNA-binding
CC       protein. Additionally, the polymerase contains an intrinsic
CC       ribonuclease H (RNase H) activity that specifically degrades RNA/DNA
CC       heteroduplexes or duplex DNA substrates in the 5' to 3' direction.
CC       Therefore, it can catalyze the excision of the RNA primers that
CC       initiate the synthesis of Okazaki fragments at a replication fork
CC       during viral DNA replication (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC         diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC         Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC         ChEBI:CHEBI:173112; EC=2.7.7.7;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC   -!- SUBUNIT: Forms a complex with the ssDNA-binding protein UL29, the DNA
CC       polymerase processivity factor, and the alkaline exonuclease. Interacts
CC       with the putative helicase-primase complex subunit UL8; this
CC       interaction may coordinate leading and lagging strand DNA synthesis at
CC       the replication fork (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000305}. Note=The protein is
CC       present at discrete sites in nuclei, called replication compartments
CC       where viral DNA replication occurs. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-B family. {ECO:0000305}.
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DR   EMBL; AY372243; AAQ73709.1; -; Genomic_DNA.
DR   RefSeq; NP_944403.1; NC_005264.1.
DR   SMR; Q6UDK1; -.
DR   PRIDE; Q6UDK1; -.
DR   GeneID; 2656967; -.
DR   KEGG; vg:2656967; -.
DR   Proteomes; UP000006840; 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:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:UniProtKB-EC.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0039693; P:viral DNA genome replication; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.132.60; -; 1.
DR   Gene3D; 3.30.420.10; -; 1.
DR   Gene3D; 3.90.1600.10; -; 1.
DR   InterPro; IPR006172; DNA-dir_DNA_pol_B.
DR   InterPro; IPR017964; DNA-dir_DNA_pol_B_CS.
DR   InterPro; IPR006133; DNA-dir_DNA_pol_B_exonuc.
DR   InterPro; IPR006134; DNA-dir_DNA_pol_B_multi_dom.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR042087; DNA_pol_B_thumb.
DR   InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   Pfam; PF00136; DNA_pol_B; 1.
DR   Pfam; PF03104; DNA_pol_B_exo1; 1.
DR   PRINTS; PR00106; DNAPOLB.
DR   SMART; SM00486; POLBc; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
DR   PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE   3: Inferred from homology;
KW   DNA replication; DNA-binding; DNA-directed DNA polymerase; Endonuclease;
KW   Host nucleus; Hydrolase; Multifunctional enzyme; Nuclease;
KW   Nucleotidyltransferase; Reference proteome; Transferase;
KW   Viral DNA replication.
FT   CHAIN           1..1081
FT                   /note="DNA polymerase catalytic subunit"
FT                   /id="PRO_0000406797"
SQ   SEQUENCE   1081 AA;  121296 MW;  42EB37A2C55FAA27 CRC64;
     MAAFDNPVFN KTLTPVAGAG PNFRATYYTS VTEFTHVCPR SLIDGERLGT SVGKVADPPR
     FTVDDRTVDM FSHDHGAWPM RMEHWPGTSA ERRRDKNALR FHEFHVYDII EAHETAQSCS
     AWLHPRFMET LRPSGTVVTL LGMSACGKRV AVHVYGQQPY FYAKKSEIDA SIGISTPGEL
     AHAMAASLRS AASRRSTFVE ATAESFVIDV VQRRDIYYYE SREEEYYRVK SCSAKYISFL
     CDNFCRGVKK YEGGIDATTR FAVDNELFTF GWYRFKPCAG AIQIRDVTRH STSANVEVNC
     TVENLEVIRG RADWPDYKLL SFDIECKAGG ANDLAFPTAE RIEDVVIQIS AVVSSLLTRR
     VEHEILFSLG TCQLPEDIAD HVKVCECGSE FELLLCFMTF LKQFSPEFVT GYNILGFDWG
     FMYNKMVNIY GMRLDGYGKA NAWGTFKVQD MPHSGRGKFR NVKINGIVNF DMFSIIYQKI
     KLCSYKLNSV AETVLGEKKH DLSYKDLPRL FALGPEERGK IGAYCLQDSR LATKLFFKLV
     PHMELSAVAQ LACITLTRAV FDGQQVRVFT CLLQRARKIG VVLPEKSDRF TFSAHAAGDQ
     DDGGRSVGYQ GAKVLDPDVG FHVNPVMVFD FASLYPSIIQ SNNLCYSTMT HNPAAIAHLE
     EGTDYLRVEV QGRVFFFVRE HVRRSLLAEL LTDWLNMRKA LRAQIPLAAT EDEKVLLDMQ
     QIAIKVICNS VYGFTGVMNG MLPCLEVAAT VTAIGRDMLL KTKQYIEENW REYSNIRERF
     FPAMAHEGVP QYSVAVIYGD TDSVFVSFKG VPVACLVASG DAMAAEITNA LFRRPVKLEC
     EKVFTKLLMI AKKKYIGVIH TGKMMMRGVD MVRKSNCRFV NDTAKALLNL VFYDEDVATA
     AASSALVDVS ALPRGLSKLG ARVREAHAAL SSPALDVRDF VMTSELSKAP KYYASSKLAH
     LTVYRKKIAR NEEPPQVKDR IEYVIIAPGQ RIQGDPFREK ETDLVSSLAE DPNWVTAHKL
     RLNADYYFSA LLQTLSVTFN AVFGDAKTAH IVMRSFIPDT LRYPAAVRKI LAENTKTLTP
     M