ID Q6QXG1_GVAS Unreviewed; 1145 AA.
AC Q6QXG1;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE RecName: Full=DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012417};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN Name=ORF101,DNA polymerase {ECO:0000313|EMBL:AAS82637.1};
GN ORFNames=AsGVgp101 {ECO:0000313|EMBL:AAS82637.1};
OS Agrotis segetum granulosis virus (AsGV) (Agrotis segetum granulovirus).
OC Viruses; Naldaviricetes; Lefavirales; Baculoviridae; Betabaculovirus;
OC Betabaculovirus agsegetum.
OX NCBI_TaxID=10464 {ECO:0000313|EMBL:AAS82637.1, ECO:0000313|Proteomes:UP000202635};
OH NCBI_TaxID=47767; Agrotis segetum (Turnip moth).
RN [1] {ECO:0000313|EMBL:AAS82637.1, ECO:0000313|Proteomes:UP000202635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Ai X.L., Wang Z.F., Wang B., Zhang W., Li F., Fu J.H., Cui C.S., Shi Y.H.,
RA He M.;
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Replicates the viral genome, host DNA polymerases cannot
CC substitute for the viral enzyme in this process.
CC {ECO:0000256|ARBA:ARBA00002701}.
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 -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC {ECO:0000256|ARBA:ARBA00005755}.
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DR EMBL; AY522332; AAS82637.1; -; Genomic_DNA.
DR RefSeq; YP_006243.1; NC_005839.2.
DR Proteomes; UP000202635; 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: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; 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; 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 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 PRINTS; PR00106; DNAPOLB.
DR SMART; SM00486; POLBc; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
PE 3: Inferred from homology;
KW DNA replication {ECO:0000256|ARBA:ARBA00023109};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Viral DNA replication {ECO:0000256|ARBA:ARBA00023109}.
FT DOMAIN 235..414
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 580..929
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT REGION 529..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..550
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1145 AA; 133045 MW; 5B2B2182C2CB437A CRC64;
MDDDYLYCDY DEIDIPPIIR SSPKRKLYDE HETTPVLKKE RDNSSVEKDG ECSSKYKKEP
VCETSEDFEV CSNLLEKVVK SDRETAHYSA NCVFKITKLH YSSSFLYIFL TGNDNVQYYF
KTYCPIYSYK LCTHRFQSCR FNCQSYKSLV VTGLKSRECH RVNVIKMERS KCSGEKYLLD
EMCNDVNRVQ MQTGIYEGDY VRFKDGITVD ENGCATGAVS ELVKVTMEEL TQPIDPIVGS
YDLETFTDGM RFSNSEVDPI ITISYVLRKQ NNNMSRYCFI NTNGKRFRLN DVYLANAEYC
DGKVIVAPFN NERDMLVTFL EVLWRTNPDE ILDYNGDKFD IPYIIGRMKK LNIDEQFIQR
YDLPKVSFKV TNIRTKFGYG FNSHSMVYYN HLDIYQFIKS SYDASKMENM KLDTAATFYL
NVGKVELSVK EMMTLYHEGS FGKVVKYNVR DSILPLEIFF KCQVANKLYA DAGIMYLCRD
DYLRTISHKI NLALFSRSIY NRNENGDADP YFYNKFDLNK IMGRKKSMAR VNDDDDDDGQ
EAAAAEEEGE EIDFTNLSRS HVPLHLIPPD ARKLCPLKTR MKYTGGKVLS PNPGYYETTF
TLDFSQLYTS IMIYITACLS NLFFGSDGYL YLQHNENAVT TKFLKEMASK RAIWKQEMKK
HAPGSFTYNL YDSWQNAAKL VCNSQYGWFG MFCKPLANLI TQIGREKLGE AKEKIECLSG
NEEIMKKWNL TKMKLSVVYG DTDSNFVAID LEPEEFKRLG VDGLKKMILQ DILAPVNAVW
GGSFKMELEN IMKCMLIKGK KMYMCLKENG SLYKRGFNVK KDSPPFLRII FDNVIKRILT
NHSLDCVLKN MLSELKTKRD EFCAKKCDQY SFSQTLNEDK KTTIAYKLYM ELKESSNTKY
IPASGDRIPY ILEDKRSNNV KDKAWPTQIF EDQNPSWNKH LGIVCTFLND IMSMLRNDTL
FVYTFQIICD YYQKDQVYDI VYPVLKVMTQ SKIKDIMCKE LNVKDKKKLD EKQMEDCFER
GVHKYIHTHE FTMSKTPPKY RINVEGFNDD CPACNGRGIS AVKKNMSLEL IENEVSKKGK
KKIVNKVEEK QAVVVDKKKL VKEEVVILKK RKEKKSVVGG KTKLIDKYDL KEEDEWWLKP
KNKGN
//
