DPOL_ASFL6
ID DPOL_ASFL6 Reviewed; 1244 AA.
AC P43139; Q89937; Q89938; Q89939;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 23-FEB-2022, entry version 93.
DE RecName: Full=DNA polymerase beta {ECO:0000250|UniProtKB:P42489};
DE EC=2.7.7.7;
GN Name=DPOL;
OS African swine fever virus (isolate Pig/Portugal/Lis 60/1960) (ASFV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Asfuvirales; Asfarviridae; Asfivirus.
OX NCBI_TaxID=82815;
OH NCBI_TaxID=6937; Ornithodoros (relapsing fever ticks).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8121806; DOI=10.1093/nar/22.2.208;
RA Martins A., Ribeiro G., Marques M.I., Costa J.V.;
RT "Genetic identification and nucleotide sequence of the DNA polymerase gene
RT of African swine fever virus.";
RL Nucleic Acids Res. 22:208-213(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Isolate PAAR-100;
RX PubMed=8525640; DOI=10.1006/viro.1995.9953;
RA Marques M.I., Costa J.V.;
RT "Functional and molecular characterization of African swine fever virus
RT mutants resistant to phosphonoacetic acid.";
RL Virology 214:72-81(1995).
CC -!- FUNCTION: DNA-directed DNA polymerase involved in viral DNA
CC replication.
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 -!- INDUCTION: Expressed in the early phase of the viral replicative cycle.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: Consistent with its intracellular location, ASFV encodes
CC its own replicative DNA polymerase and three base excision repair
CC enzymes: a class II AP endonuclease, the repair polymerase Pol X, and
CC an ATP-dependent DNA ligase.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family. {ECO:0000305}.
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DR EMBL; X73330; CAA51757.1; -; Genomic_DNA.
DR EMBL; U27573; AAB60596.1; -; Genomic_DNA.
DR EMBL; U27574; AAB60597.1; -; Genomic_DNA.
DR EMBL; U27575; AAB60598.1; -; Genomic_DNA.
DR PIR; S37034; S37034.
DR SMR; P43139; -.
DR PRIDE; P43139; -.
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: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; Early protein;
KW Nucleotidyltransferase; Repeat; Transferase; Viral DNA replication.
FT CHAIN 1..1244
FT /note="DNA polymerase beta"
FT /id="PRO_0000046503"
FT REPEAT 1069..1072
FT /note="1"
FT REPEAT 1073..1076
FT /note="2"
FT REPEAT 1077..1080
FT /note="3"
FT REPEAT 1081..1084
FT /note="4"
FT REPEAT 1085..1088
FT /note="5"
FT REPEAT 1089..1092
FT /note="6"
FT REPEAT 1093..1096
FT /note="7"
FT REPEAT 1097..1100
FT /note="8"
FT REPEAT 1101..1104
FT /note="9"
FT REPEAT 1105..1108
FT /note="10"
FT REPEAT 1109..1112
FT /note="11"
FT REPEAT 1113..1116
FT /note="12"
FT REPEAT 1117..1120
FT /note="13"
FT REGION 1069..1120
FT /note="13 X 4 AA tandem repeats of A-G-N-P"
FT REGION 1069..1118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 436
FT /note="D -> G (in strain: Isolate PAAR-100;
FT phosphonoacetate-resistant)"
FT VARIANT 512
FT /note="L -> F (in strain: Isolate PAAR-463;
FT phosphonoacetate-resistant)"
FT VARIANT 515
FT /note="A -> V (in strain: Isolate PAAR-20;
FT phosphonoacetate-resistant)"
SQ SEQUENCE 1244 AA; 142534 MW; 3689D15732B0A19E CRC64;
MDRSEIVARE NPVITQRVTN LLRTNAPLLF MPIDIHEVRY GAYMLFMYGS LENGYKAEVR
IENIPVFFDV QIESDNTNQL FLKSLLAAEN ITYERLETLT QRPVMGYREK EKEFAPYIRI
FFKSLYERRK AITYLNNMGY NTAADDTTCY YRMVSRELKL PLTTWIQLQH YSYEPRGLVH
RFSVTPEDLV SYQDDGPTDH SIVMAYDIET YSPVKGTVPD PNQANDVVFM ICMRIFWIHS
TEPLASTCIT MAPCKKSPEW TTIVCSSEKN LLLSFAEQFS RWAPDICTGF NDSRYDWPFI
VEKSMQHGIL EEVFNKMSLF WPQKLDTILK CYYVKEKRVK ISAEKSIISS FLHTPGCLPI
DVRNMCMQLY PKAEKTSLKA FLENCGLDSK VDLPYHLMWK YYETRDSEKM ADVAYYCIID
AQRCQDLLVR HNVIPDRREV GILSYTSLYD CIYYAGGHKV CNMLIAYAIH DEYGRIACST
IARGKREHGK YPGAFVIDPV KGLEQDKPTT GLDFASLYPS LIMAYNFSPE KFVASRDEAN
SLMAKGESLH YVSFHFNNRL VEGWFVRHNN VPDKMGLYPK VLIDLLNKRT ALKQELKKLG
EKKECIHESH PGFKELQFRH AMVDAKQKAL KIFMNTFYGE AGNNLSPFFL LPLAGGVTSS
GQYNLKLVYN FVINKGYGIK YGDTDSLYIT CPDSLYTEVT DAYLNSQKTT KHYEQLCHEK
VLLSMKAMST LCAEVNEYLR QDNGTSYLRM AYEEVLFPVC FTGKKKYYGI AHVNTPNFNT
KELFIRGIDI IKQGQTKLTK TIGTRIMEES MKLRRPEDHR PPLIEIVKTV LKDAVVNMKQ
WNFEDFIQTD AWRPDKDNKA VQIFMSRMHA RREQLKKHGA AATSQFAEPE PGERFSYVIV
EKQVQFDIQG HRTDTTRKGD KMEYVSEAKA KNLPIDILFY INNYVLGLCA RFINENEEFQ
PPGNVSNKDE YAQRRAKSYL QKFVQSIHPK DKSVIKQGIV HRQCYKYVHQ EIKKKIGIFA
DLYKEFFNNT TNPIESFIQS TQFMIHYFDE EQKVNHSMKK MVEQHAALAG NPAGNPAGNP
AGNPAGNPAG NPAGNPAGNP AGNPAGNPAG NPAGNPAGNP ASNALMRAIF TQLITEEKKI
VQALYNKGDE IHDLLTYIIN NINYKIATFQ TKQMLTFELS STHVELLLKL NKTWLILVGI
RVAKKHLHAL LGLHNNEPPS KTFIQQAIEE ECGSIKPSCY DFIS
