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Database: UniProt
Entry: A0A076FCW3_9VIRU
LinkDB: A0A076FCW3_9VIRU
Original site: A0A076FCW3_9VIRU 
ID   A0A076FCW3_9VIRU        Unreviewed;      1091 AA.
AC   A0A076FCW3;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012417};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   ORFNames=PmNV_005 {ECO:0000313|EMBL:AII15793.1};
OS   Penaeus monodon nudivirus.
OC   Viruses; Naldaviricetes; Lefavirales; Nudiviridae; Gammanudivirus;
OC   Gammanudivirus pemonodonis.
OX   NCBI_TaxID=1529056 {ECO:0000313|EMBL:AII15793.1, ECO:0000313|Proteomes:UP000203413};
RN   [1] {ECO:0000313|EMBL:AII15793.1, ECO:0000313|Proteomes:UP000203413}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Indonesia {ECO:0000313|EMBL:AII15793.1};
RX   PubMed=25063321; DOI=10.1186/1471-2164-15-628;
RA   Yang Y.T., Lee D.Y., Wang Y., Hu J.M., Li W.H., Leu J.H., Chang G.D.,
RA   Ke H.M., Kang S.T., Lin S.S., Kou G.H., Lo C.F.;
RT   "The genome and occlusion bodies of marine Penaeus monodon nudivirus (PmNV,
RT   also known as MBV and PemoNPV) suggest that it should be assigned to a new
RT   nudivirus genus that is distinct from the terrestrial nudiviruses.";
RL   BMC Genomics 15:628-628(2014).
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; KJ184318; AII15793.1; -; Genomic_DNA.
DR   RefSeq; YP_009051843.1; NC_024692.1.
DR   GeneID; 20098311; -.
DR   KEGG; vg:20098311; -.
DR   OrthoDB; 9861at10239; -.
DR   Proteomes; UP000203413; 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; 3.90.1600.10; Palm domain of DNA polymerase; 2.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR   InterPro; IPR006172; DNA-dir_DNA_pol_B.
DR   InterPro; IPR006134; DNA-dir_DNA_pol_B_multi_dom.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
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   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   Reference proteome {ECO:0000313|Proteomes:UP000203413};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Viral DNA replication {ECO:0000256|ARBA:ARBA00023109}.
FT   DOMAIN          780..896
FT                   /note="DNA-directed DNA polymerase family B
FT                   multifunctional"
FT                   /evidence="ECO:0000259|Pfam:PF00136"
FT   REGION          678..715
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        687..715
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1091 AA;  127272 MW;  E945664B2EA5C39F CRC64;
     MSVRYVNSNW KEWLSQVPDT PKSNYLYITD WQVDGDDYFG VGINKMTRKL EKFKVANLSS
     GLYVWALNQQ TLKELLVNFT ISDITYVKQN TEYMNNHVTV LDDIMKSGRY QPKWKLFKLH
     TTSFNESKSL HYSISNSTGF LQHIAVLGQW NLSTFMMMEF HVKGMDYIYG KYINERLQYL
     ENIESNFNLF TTVYDIETVS NYDHRIPTGN FFADHIMSVT FIKGTEIITL FNIPLTFDHQ
     LDAAKSIIDK ISAKDYYKME TRTTLVYNTE WDLLAKLFEL FESIDEAYIC LGYNSRNYDM
     PFLLTRAIYL GMPQVSKFYY VNGILSYGMN MIHVDLNQVL VKYFAQELSS FSLKNVAKAL
     LEDDDTQKVD FNARNLRYIY QFMIESGHLN NGKYDNVLCR QPNPWSISLD IMAKYNEMDC
     LVVLALWDKL QYEHFITYAS RVFFLPLVRL GLSKLNEYLS TNMIYEGLQQ NTIFAHHTNS
     SLTMNSQMMY TLNIENISSD ANKAFHGGFN ERKNRGCYHE VHAMDARAYY PELISGMNLS
     HETASLLRIK DLKLIARGCT NFDESFKIMK FCTHKAINQN IKPPSTTCEN IINAIASAAY
     VHCMVDNCPT IKFEDLDKYN DMDKVVVLHK THRGILSKII EQRNTLRNIA KSSKKEISSH
     IDACQTLLSE YKLKNRMGSN KYNDDEEEEI SYSDDDDNND DNEEEISYDD YDDDDEDDMI
     INKVYSIEDF KIPKDKHTEE AVYMVTKHIR LLEKKDFNKF EDAIKSLELY IEDLKLEFTR
     LNSHYRNMKL LNNSIYGLLG ASYGTIKAKN LAAIVTMLGR HFIVEASRIG NMINANMIYS
     DTDSVFFSIS NAIVKNSANR IISGVNRLNA NVVLNDKVYK DMFVLGKKTY IATCNDMIFS
     RGINKNGPNL WKTMMDRFYV QFIKNRESLN FSGVYDILFD MYMDTYKLLY DNRNAILRLV
     SIRTRESYKM NTVVTKLIDR ISLEKPDYKF DSKVYCFYRI FGDISNTHLA LDIEMDDTPI
     EEINLYKFYS NIVSTYYLIF AYAIEQTNQE KLGYVIKYPM QEFNKANKYS FIKALAAIKE
     MPTRDNDKQP T
//
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