ID A2TIW3_9ALPH Unreviewed; 1206 AA.
AC A2TIW3;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 24-JAN-2024, entry version 90.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN Name=UL30 {ECO:0000313|EMBL:ABM92130.1};
GN Synonyms=DEVCV32 {ECO:0000313|EMBL:AGA17822.1}, ORF30
GN {ECO:0000313|EMBL:AGS78690.1}, ORF32 {ECO:0000313|EMBL:AJG04899.1};
OS Anatid alphaherpesvirus 1.
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Orthoherpesviridae; Alphaherpesvirinae; Mardivirus.
OX NCBI_TaxID=104388 {ECO:0000313|EMBL:ABM92130.1};
RN [1] {ECO:0000313|EMBL:ABM92130.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=17706377; DOI=10.1016/j.gene.2007.06.022;
RA Liu S., Chen S., Li H., Kong X.;
RT "Molecular characterization of the herpes simplex virus 1 (HSV-1)
RT homologues, UL25 to UL30, in duck enteritis virus (DEV).";
RL Gene 401:88-96(2007).
RN [2] {ECO:0000313|EMBL:ABO26217.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VAC {ECO:0000313|EMBL:ABO26217.1};
RA Li Y.F., Huang B.;
RT "Sequence analysis of a 41-kb segment of the duck enteritis virus genome.";
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ABU46133.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CHv {ECO:0000313|EMBL:ABU46133.1};
RA Cheng A., Wang M.S., Zheng S.;
RT "Discovery and functional identification of novel duck enteritis virus
RT virulent strain CHv UL30 gene.";
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:ACT83543.1, ECO:0000313|Proteomes:UP000164963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VAC {ECO:0000313|EMBL:ACT83543.1};
RX PubMed=19595405; DOI=10.1016/j.virol.2009.06.018;
RA Li Y., Huang B., Ma X., Wu J., Li F., Ai W., Song M., Yang H.;
RT "Molecular characterization of the genome of duck enteritis virus.";
RL Virology 391:151-161(2009).
RN [5] {ECO:0000313|EMBL:ACT83543.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VAC {ECO:0000313|EMBL:ACT83543.1};
RA Li Y.F., Huang B.;
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000313|EMBL:AEN80095.1, ECO:0000313|Proteomes:UP000168285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2085 {ECO:0000313|EMBL:AEN80095.1};
RX PubMed=21802458; DOI=10.1016/j.virusres.2011.07.004;
RA Wang J., Hoper D., Beer M., Osterrieder N.;
RT "Complete genome sequence of virulent duck enteritis virus (DEV) strain
RT 2085 and comparison with genome sequences of virulent and attenuated DEV
RT strains.";
RL Virus Res. 160:316-325(2011).
RN [7] {ECO:0000313|EMBL:AFC61852.1, ECO:0000313|Proteomes:UP000135812}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHv {ECO:0000313|EMBL:AFC61852.1};
RX PubMed=22532531; DOI=10.1128/JVI.00529-12;
RA Wu Y., Cheng A., Wang M., Yang Q., Zhu D., Jia R., Chen S., Zhou Y.,
RA Wang X., Chen X.;
RT "Complete genomic sequence of chinese virulent duck enteritis virus.";
RL J. Virol. 86:5965-5965(2012).
RN [8] {ECO:0000313|EMBL:AGS78690.1, ECO:0000313|Proteomes:UP000112239}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K {ECO:0000313|EMBL:AGS78690.1};
RX PubMed=24009119;
RA Yang C., Li J., Li Q., Li H., Xia Y., Guo X., Yu K., Yang H.;
RT "Complete genome sequence of an attenuated duck enteritis virus obtained by
RT in vitro serial passage.";
RL Genome Announc. 1:e00685-13(2013).
RN [9] {ECO:0000313|EMBL:AGW24824.1, ECO:0000313|Proteomes:UP000114267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C-KCE {ECO:0000313|EMBL:AGW24824.1};
RA Zou Z., Hu Y.;
RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
RN [10] {ECO:0000313|EMBL:AGA17822.1, ECO:0000313|Proteomes:UP000180937}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CV {ECO:0000313|EMBL:AGA17822.1};
RX PubMed=24287923; DOI=10.1007/s11262-013-1009-9;
RA Yang C., Li Q., Li J., Zhang G., Li H., Xia Y., Yang H., Yu K.;
RT "Comparative genomic sequence analysis between a standard challenge strain
RT and a vaccine strain of duck enteritis virus in China.";
RL Virus Genes 48:296-303(2014).
RN [11] {ECO:0000313|Proteomes:UP000098628}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Yang C., Li Q., Li J., Liu D., Li L., Li H., Xia Y., Yang H., Yu K.;
RT "Protective efficacy and genomic characteristics of a duck enteritis virus
RT attenuated by serial passage in chick embryo fibroblast.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [12] {ECO:0000313|EMBL:AJG04899.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CV p80 {ECO:0000313|EMBL:AJG04899.1};
RX PubMed=25392272; DOI=10.1007/s00705-014-2275-0;
RA Yang C., Li J., Li Q., Li L., Sun M., Li H., Xia Y., Yang H., Yu K.;
RT "Biological properties of a duck enteritis virus attenuated via serial
RT passaging in chick embryo fibroblasts.";
RL Arch. Virol. 160:267-274(2015).
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. {ECO:0000256|ARBA:ARBA00025601}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC Evidence={ECO:0000256|ARBA:ARBA00000077};
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 Evidence={ECO:0000256|ARBA:ARBA00024632,
CC ECO:0000256|RuleBase:RU000442};
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000256|ARBA:ARBA00004147}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC {ECO:0000256|ARBA:ARBA00005755, ECO:0000256|RuleBase:RU000442}.
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DR EMBL; EF203709; ABM92130.1; -; Genomic_DNA.
DR EMBL; EF417996; ABO26217.1; -; Genomic_DNA.
DR EMBL; EF643560; ABU46133.1; -; Genomic_DNA.
DR EMBL; EU082088; ACT83543.1; -; Genomic_DNA.
DR EMBL; JF999965; AEN80095.1; -; Genomic_DNA.
DR EMBL; JQ647509; AFC61852.1; -; Genomic_DNA.
DR EMBL; JQ673560; AGA17822.1; -; Genomic_DNA.
DR EMBL; KF487736; AGS78690.1; -; Genomic_DNA.
DR EMBL; KF263690; AGW24824.1; -; Genomic_DNA.
DR EMBL; KJ549663; AJG04899.1; -; Genomic_DNA.
DR RefSeq; YP_003084391.1; NC_013036.1.
DR SMR; A2TIW3; -.
DR GeneID; 8223356; -.
DR KEGG; vg:8223356; -.
DR Proteomes; UP000098628; Genome.
DR Proteomes; UP000112239; Genome.
DR Proteomes; UP000114267; Genome.
DR Proteomes; UP000135812; Genome.
DR Proteomes; UP000164963; Genome.
DR Proteomes; UP000168285; Genome.
DR Proteomes; UP000180937; Genome.
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; DNA polymerase family B, C-terminal domain; 1.
DR Gene3D; 3.30.342.10; DNA Polymerase, chain B, domain 1; 1.
DR Gene3D; 1.10.287.690; Helix hairpin bin; 1.
DR Gene3D; 3.90.1600.10; Palm domain of DNA polymerase; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 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; IPR021639; DNAPolymera_Pol_C.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR PANTHER; PTHR10322; DNA POLYMERASE CATALYTIC SUBUNIT; 1.
DR PANTHER; PTHR10322:SF23; DNA POLYMERASE DELTA CATALYTIC SUBUNIT; 1.
DR Pfam; PF00136; DNA_pol_B; 1.
DR Pfam; PF03104; DNA_pol_B_exo1; 1.
DR Pfam; PF11590; DNAPolymera_Pol; 1.
DR PRINTS; PR00106; DNAPOLB.
DR SMART; SM00486; POLBc; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE 3: Inferred from homology;
KW DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW ECO:0000256|RuleBase:RU000442};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU000442};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW ECO:0000256|RuleBase:RU000442};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW Host nucleus {ECO:0000256|ARBA:ARBA00022562};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU000442};
KW Reference proteome {ECO:0000313|Proteomes:UP000135812};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000442};
KW Viral DNA replication {ECO:0000256|ARBA:ARBA00023109}.
FT DOMAIN 230..527
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 593..1135
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 1160..1200
FT /note="DNA polymerase catalytic subunit Pol C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11590"
FT REGION 626..670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1069..1092
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1206 AA; 134708 MW; 6DDF1AB2C70CD650 CRC64;
MAESGRNFFN PYLDGSAGRG NRKGPVRGNR YSYYTDISEF KFIAPRSLDE EAEDSKRKGT
NIGVLRRKPI AYCNGATFEF LNYDQCMELW TQRTHVWGER SFLANDFNPR FARFHVYDMV
EYVETISSSS GRDAERFVKL LSPMGTIVTM LGLSECGKKV AVHVYGICQY FYMKKSETDA
ACGSRCPRDL AEHMATALRS SSCGGSDGHS GEFSSAGKGG RNFGYRNASP ECFEIDIVER
CDIYYFDTTP CEFYRIKARS SRHVSFLSEN FLPNVTKYES NVDATTRLIL DNIGFSTFGW
YRLKIGNNGE RIQVRAPEHH TTSCDVEINC TVDNLVGDSE DGAIPDYKLL CFDIECKSGG
QNELAFPVAS NEDDLVIQIS CILYSLSTRC MEHALLFSLG SCDLPEIELN GKDGAAIKPE
VLEFDSEYEL LLCFLTFLKQ YSPEFVSGYN IVNFDWAFLY NKLTTVYGIK LDGYGAMNKG
GMFRVWELGG GHFQKRSKVK INGIISLDMY SVATEKLKLS SYKLETVASA ALGEHKRDLS
YKDIPVYYAS GPSKRGLIGE YCIQDSVLVG KLFFKYLPHL ELSAVAKLAG ILLPRVVFDG
QQVRVYTCLL RLAGQHGFVL PENKSRFSGK GGDSEHLAPA LQAEDLEDSD EDEEKDETDN
TKMTSGSAMK GGRSVGYRGA KVLDPCTGFH VDPVTVFDFA SLYPSIIQAH NLCFTTLTLK
EEAVSHLNAD DYLDITVAGQ RLFFVKPHIR VSLLSVLLRD WLAMRKAIRA KIPTSTEEQA
LLLDKQQLAI KVVCNSVYGF CGVSNGLLPC LHVAATVTTV GRNMLLSVRD YIHTHWTTCD
MLVQAFPELV DHVKDKQAYS AMVIYGDTDS VFVRIKGIAP EGLVAVGDAM ASMITRELFT
SPIKLECEKT FFRLLLITKK KYIGTIVGGK MMMKGVDLVR KNNCKFINYY AKRLVDLLFG
NDEVAAAAAA ISKEPAKTWL ERSLPPGLGE FGATLAEAYS KIRARELNVP DFVMTAELSR
APEAYVNKRI PHLTVYYKLC MREEQPPAIK ERIPYVIVAQ IPSVERDAER VATMRGDKRP
SNSTGKADGP AAKRRKLLVS ELAEDPGYVL ANHIPLNTDY YFSHLLGTLS VTFKALFGND
HKTSEAVLKR FIPETYCESD ETAALLSSAG FAEVRLYPGM PLSEEEENRQ KLRRAFDILA
EVPHRN
//
