ID A0A0U1ZCX7_9ALPH Unreviewed; 1250 AA.
AC A0A0U1ZCX7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN ORFNames=CoHVHLJ_044 {ECO:0000313|EMBL:ARD71355.1};
OS Columbid alphaherpesvirus 1.
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Orthoherpesviridae; Alphaherpesvirinae; Mardivirus;
OC Mardivirus columbidalpha1.
OX NCBI_TaxID=93386 {ECO:0000313|EMBL:AJT58581.1};
RN [1] {ECO:0000313|EMBL:AJT58581.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BJ {ECO:0000313|EMBL:AJT58581.1};
RA Zhang L., Hu X., Li Z., Li S., Sun H., Xia M., Yang X., Bai R., Guo J.,
RA Yong W., Su J.;
RT "Characterization of the columbid herpesvirus 1 isolated from domestic
RT pigeons in China.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ARD71355.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLJ {ECO:0000313|EMBL:ARD71355.1};
RX PubMed=28316016; DOI=10.1007/s00705-017-3329-x;
RA Guo Y., Li S., Sun X., He Y., Zhao H., Wang Y., Zhao P., Xing M.;
RT "Complete genome sequence and evolution analysis of a columbid herpesvirus
RT type 1 from feral pigeon in China.";
RL Arch. Virol. 162:2131-2133(2017).
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; KJ995972; AJT58581.1; -; Genomic_DNA.
DR EMBL; KX589235; ARD71355.1; -; Genomic_DNA.
DR Proteomes; UP000202345; 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; 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:UP000202345};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000442};
KW Viral DNA replication {ECO:0000256|ARBA:ARBA00023109}.
FT DOMAIN 251..548
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 615..1179
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 1206..1244
FT /note="DNA polymerase catalytic subunit Pol C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11590"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 68..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 654..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1107..1136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1250 AA; 139253 MW; B1C9EDFC1A90F198 CRC64;
MEGTTSRTFF NPFLARRSSS GDGLPRGPGT ANWGAGTNAN ASRYSRQRYT YVSEQEEFKF
IAPECLDERD GDEGVSSGDD DQPRSYPKGT HVGTLKRSPL AYRDGEVVEF LDFEKSGKLW
PRRSRTWGAK TFREDDFDPR FNRFHVYDMV ETVETADGAL GRDSERFLEL IRPLGTVITM
LGMTECGKRV AVHVYGVNPY FYMGKDQVDA ACGSRCPRDV AEKMAASIRN SITGGGQKQF
YGHGFRGASA DCFDVDVVQK TDVYFYGTPQ KPYYRVKARS GRFVSSVCDN FCQTVTKYEG
AVDSVTRMVL DNANFITFGW YRLKIGEQGR RVQVRRPEYH TTSCDVEINC TVDNLEGEPG
ADEWPDYKLL CFDIECKSSG HNELAFPEAT NEEDLVIQIS CLLYSLQTRR LEHIILFSLG
SCDLSSEFLE GLREKQLPEP TVLEFESEYE LLLAFMTFVK QYAPEFATGY NIVNFDWAFI
HNKLTTVYDM RLDGYGVLNK GGMFKIWDAG INRFQKKSKV KITGIISLDM YSVATEKAKL
PNYKLNTVAA AVLGERKKDL SYKEIPGHFA AGPVKRGVIG EYCLQDSLLV GKLFFKYLPH
LELSAVAKLA GILLPRAIYD GQQLRVFTCL LRLASSRGFL LPDNTKRFTD AAMAPVPAGG
EDSNPALDGA EGSDDDDERA DRDAGSEPAA PKTKSSSSRQ VGYQGAKVLE PETGFHVNPV
VVFDFASLYP SIIQAHNLCF TTLTLDRSAV DDLRPGDDYL QINVNGKTLY FVKKHVRESL
LSILLTDWLA MRKAIRAKIP GSPEDQAVLL DKQQAAIKVV CNSVYGFCGV VNGLLPCLNV
AATVTTIGRN MLLAVRDYIH RRWASWDALI KEFPQLDGHA KAGEDYSVSV IYGDTDSVFV
KITGVDTAAL VSTGDVMGKR ISSELFLPPI KLECEKTFDK LLLITKKKYM GTIFGGKMMM
KGVDLVRKNN CKFINAYAKR LVDLLFLNDD VAKAAAVITS EPPSTWLERP LPDGLKPFGE
VLVEAYDKVA GNKPLDVSEF VMSAELSRPP NAYANKRIAH LTVYYKLCMR ADQPPMVKDR
ISYVIAAECD EIERDAARVA EIRGDAVKDA SPASDPVDGD DPSAPQPAKR RRAAAPKKRK
LLVSELAEDP GYLMSAGLKL NIDYYFTHLL GTLSVTFKAL FGNDTKVTES VLKRFIPESF
KESDEDAERL AKAGFAVVRT GAGLDPSEEE ESRQRWSTAF RILTAVRRRY
//
