ID W8QF12_9VIRU Unreviewed; 1120 AA.
AC W8QF12;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012417};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=AMIV_049 {ECO:0000313|EMBL:AHL67544.1};
OS Anopheles minimus iridovirus.
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC Pimascovirales; Iridoviridae; Betairidovirinae; Chloriridovirus.
OX NCBI_TaxID=1465751 {ECO:0000313|EMBL:AHL67544.1, ECO:0000313|Proteomes:UP000110868};
RN [1] {ECO:0000313|EMBL:AHL67544.1, ECO:0000313|Proteomes:UP000110868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AMIV {ECO:0000313|EMBL:AHL67544.1};
RA Tong Y., Zhang J., Huang Y., Li S., Pei G., Zhang Z., Mi Z., An X.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
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; KF938901; AHL67544.1; -; Genomic_DNA.
DR RefSeq; YP_009021128.1; NC_023848.1.
DR GeneID; 18938210; -.
DR KEGG; vg:18938210; -.
DR OrthoDB; 5091at10239; -.
DR Proteomes; UP000110868; 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; 2.40.50.730; -; 1.
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; 2.
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 Coiled coil {ECO:0000256|SAM:Coils};
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 Reference proteome {ECO:0000313|Proteomes:UP000110868};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Viral DNA replication {ECO:0000256|ARBA:ARBA00023109}.
FT DOMAIN 91..383
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 454..872
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 912..1001
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT COILED 632..659
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1120 AA; 130106 MW; 9BD7F69CC212E32D CRC64;
MATLQTIDIY AYSWHIDEEE QDSTFIRVYG LNNLNENICV SINGFRPHVY VELPTHINWV
DFKPQLYSFF QQLSSGLKCT LTFARKLYGA NLKKKDEKFV HKKFPFLKCT FNSKRDAHFL
AHKLKNRQYV PGIGQLKFNV HHLDACPRLQ LTSKYNLPTA GWIRFKGTKI LQDEDKFTER
CDEFMIDLSD KRYKPEDLMK RCDAVGTVKP LILSFDLEVN SEDGITMPKA TRPGDVVFQI
SCVFSRLGEP AESFDKYLLS LGNPSPELVG AKVLSYPSES KLLMGFTNLI KEKNPNCIIG
YNIFSFDIPY LMDRANYKHI YPEWSVQGFP RDRCGISREI KWSSSAYKNQ EFKYLDCEGR
LYIDLLPIVQ RDFKLNDYKL KTVSTQFIGE TKDDLDAKGI FKCYREGIKN TSVAYKYMSV
CGKYCMQDSL LVTKLFDKLN VWHGLSEMAA VCNVPMITLF TKGQQVKVYS QVYKHCVENK
IVVEKDGYVT RENERYVGAF VFPPKPGLYE NVVPMDFSSL YPSLIIAYNI DYSTLAADPH
IPDEMCHVME WEDHISCKHD PKVIEKARLT KLIDELVNKK GYDKALVSKY RKERSEITKS
LNKNVMCEKR RYRFLDPNKL GKESVGVLPT IIQNLLEARK NTRKEIVVLK DKLKTTTNDK
EKINLETTIS VLNQRQLAYK VSANSMYGIT GVKAGMLPCM PIAMSVTFMG RTNILKAAKY
LQEIYGGFLV YGDTDSNYVS FNHKNFSYAE LWDYALKVAD EVSSLFPPPM RLEFEEAIYK
KFLILTKKRY MYQTCLRNGS IKPEIGKRGV ILNRRDNSGF IRNIYEKMVK IIFEEDDPTR
LQTRVLHALT NDINNMFCGA IPVQDFVITK STGDYGNLEP QFFLNEKGLK RAMLGQYNVP
FLTDEAKMEE EITNEKQEKE WYLSKLPAHI QLLEKIKRRG QIKNEGSRLE YVILETNDHK
DKQCVKIEAL DYYLKNKDVL KLDYLYYLQR CINPIDQILE VLFKLPHFTK QVYDYHFNKK
KLIGQMNLLF APTLNIDKTN VLLYRDLDKY YIQLGQAADN NTLHLVAQFQ TTEDTKNLYL
KLRHKCTKLK TKFTFKCGYI KLNGFAEQKL ISALKRLCKA
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