ID   A0A142CKD4_9VIRU        Unreviewed;      1130 AA.
AC   A0A142CKD4;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
OS   Brazilian marseillevirus.
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Pimascovirales; Marseilleviridae; Marseillevirus.
OX   NCBI_TaxID=1813599 {ECO:0000313|EMBL:AMQ10896.1, ECO:0000313|Proteomes:UP000203790};
RN   [1] {ECO:0000313|EMBL:AMQ10896.1, ECO:0000313|Proteomes:UP000203790}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BH2014 {ECO:0000313|EMBL:AMQ10896.1,
RC   ECO:0000313|Proteomes:UP000203790};
RX   PubMed=26978387; DOI=10.3390/v8030076;
RA   Dornas F.P., Assis F.L., Aherfi S., Arantes T., Abrahao J.S., Colson P.,
RA   La Scola B.;
RT   "A Brazilian Marseillevirus Is the Founding Member of a Lineage in Family
RT   Marseilleviridae.";
RL   Viruses 8:76-76(2016).
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   -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC       {ECO:0000256|ARBA:ARBA00005755, ECO:0000256|RuleBase:RU000442}.
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DR   EMBL; KT752522; AMQ10896.1; -; Genomic_DNA.
DR   RefSeq; YP_009238893.1; NC_029692.1.
DR   GeneID; 27112301; -.
DR   KEGG; vg:27112301; -.
DR   OrthoDB; 165at10239; -.
DR   Proteomes; UP000203790; 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: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; 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.
DR   PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE   3: Inferred from homology;
KW   DNA replication {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   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU000442};
KW   Reference proteome {ECO:0000313|Proteomes:UP000203790};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000442};
KW   Viral DNA replication {ECO:0000256|ARBA:ARBA00023109}.
FT   DOMAIN          91..369
FT                   /note="DNA-directed DNA polymerase family B exonuclease"
FT                   /evidence="ECO:0000259|Pfam:PF03104"
FT   DOMAIN          489..965
FT                   /note="DNA-directed DNA polymerase family B
FT                   multifunctional"
FT                   /evidence="ECO:0000259|Pfam:PF00136"
SQ   SEQUENCE   1130 AA;  130262 MW;  6A1273402C9EC3A5 CRC64;
     MAQRTHNFKI SKWDFCDSEE GLVFYAYGRD ELSQTVCAKI EGFHPYVYIQ LPKKRNLKWG
     KREARILFEH LKTKVCKKYP PVSFELKKKS FLKGRVPVQT LRLEFLNIAG AKMCANAMEN
     RENRVEGLGV FAAKELRSHE QNIDVYTKFF THRVLDSTGW IKVVEEKGLA YEKNSKADKE
     YVCDWRNVSK GEDMGLINTK KLSFDIEAYS AHHSAFPDPN IKENAITQIA YTVEETNGGI
     WKEVISLGNC LRIRGAKVLN ARTEKELLLL FFRRVSDIDP DLVIGYNIIK FDWNYLMTRA
     KRHGIFQRMC ELLTRIFAVP ASEDKMSWSS SAYGTQKFVF TKIPGVSQID MYVEFERNHK
     LDKNTLDHVS ELFLGEKKKD VTAKELFKIM ETSMILESFQ KTSVPFRERR RAVYTAINRK
     HSTSYLLDFR QRVKRCRSLL ELDLLVRSGV TKLADYCIQD TVLPLRLLKH FDVELNMDML
     AGVFCVPREY LQTRGQQVKV FSMLYREMQS EDLIVEFLGY DKEVSNVKYK GATVFDAKTG
     FWEDVLVWDF ESLYPSEIIS RNIDYTSFCT NDESVPDEEC NIVEWDQHEF CKCPLDSKAG
     KNKKKDQEVV CGHFKQRFKK SKVLENGEIQ EGVLPRMLRH VLARRKAVKG EMGQAARNAD
     KEVDPEKKAQ FKTKEKVANA SQLALKIAAN SAYGALGATQ GISPLVEAAA AVTTAGRQDI
     VKVVDRILER WPEGILVYGD TDSCMIHFPG GRTPKDLIEF GVFVGKEISK HLVSPMNLQF
     EKLCKKFIIF SKKRYYTFIV DENGKVIAID KKGIVLTRRD NCLLVRDLFG ATVKQVIEKE
     DTQKILQGVY DGIYGMMSRS IPDQKYVITA SIKALDEYKN DGKGLVNVAL ARKMKKRGEE
     VIPNTRLEFV FLTVPDKKKG EKTLQAEQVE DFTWYIDNKK RLGLKIDTHL YLTKKVMEPL
     AELLNIWEKK TIEYEKLDER IKRLKSLMSP EDKDCVTKLE FLFRKTKLSD SIPEKSQSTI
     DSFFGKRESK REPQSLLHRA RVIANQALAS DKKVVSLLIE SYNREKHIKT LNARRKMFGL
     QAVRQRLPKR GAKILVQDEK ILKTLAKAHL AHSETALQLK RLFARPIVVE
//