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DPOL_NPVLD
ID   DPOL_NPVLD              Reviewed;        1014 AA.
AC   P30318; Q9YMP4;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 2.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=DNA polymerase;
DE            EC=2.7.7.7;
GN   Name=POL; OrderedLocusNames=LdOrf-83;
OS   Lymantria dispar multicapsid nuclear polyhedrosis virus (LdMNPV).
OC   Viruses; Naldaviricetes; Lefavirales; Baculoviridae; Alphabaculovirus.
OX   NCBI_TaxID=10449;
OH   NCBI_TaxID=7088; Lepidoptera (butterflies and moths).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1469355; DOI=10.1099/0022-1317-73-12-3177;
RA   Bjoernson R.M., Glocker B., Rohrmann G.F.;
RT   "Characterization of the nucleotide sequence of the Lymantria dispar
RT   nuclear polyhedrosis virus DNA polymerase gene region.";
RL   J. Gen. Virol. 73:3177-3183(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9887315; DOI=10.1006/viro.1998.9469;
RA   Kuzio J., Pearson M.N., Harwood S.H., Funk C.J., Evans J.T., Slavicek J.M.,
RA   Rohrmann G.F.;
RT   "Sequence and analysis of the genome of a baculovirus pathogenic for
RT   Lymantria dispar.";
RL   Virology 253:17-34(1999).
CC   -!- FUNCTION: Replicates the viral genome, host DNA polymerases cannot
CC       substitute for the viral enzyme in this process. {ECO:0000250}.
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   -!- SIMILARITY: Belongs to the DNA polymerase type-B family. {ECO:0000305}.
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DR   EMBL; D11476; BAA02036.1; -; Genomic_DNA.
DR   EMBL; AF081810; AAC70269.1; -; Genomic_DNA.
DR   PIR; JQ1920; JQ1920.
DR   PIR; T30431; T30431.
DR   RefSeq; NP_047720.1; NC_001973.1.
DR   SMR; P30318; -.
DR   PRIDE; P30318; -.
DR   GeneID; 1488540; -.
DR   KEGG; vg:1488540; -.
DR   Proteomes; UP000203997; 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   GO; GO:0019079; P:viral genome replication; ISS:UniProtKB.
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;
KW   Nucleotidyltransferase; Transferase; Viral DNA replication.
FT   CHAIN           1..1014
FT                   /note="DNA polymerase"
FT                   /id="PRO_0000046529"
FT   REGION          956..983
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        462..463
FT                   /note="AA -> RRP (in Ref. 1; BAA02036)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        483..493
FT                   /note="RKRAFNEPAPS -> ASAPSTSRP (in Ref. 1; BAA02036)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        565
FT                   /note="S -> SS (in Ref. 1; BAA02036)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        701..725
FT                   /note="LAPDRRQTAIRSIVQDHVCKTLNDS -> WRRTAARPRSAPSCRTTCAKRST
FT                   TL (in Ref. 1; BAA02036)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        783..799
FT                   /note="LLRGHSTACALGLLAEQ -> FSAATRRVRARPARRE (in Ref. 1;
FT                   BAA02036)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1014 AA;  115823 MW;  F6AE184DBCE4CBF3 CRC64;
     MSSVNLMEWS ALKTQLQAGR DAGKARVSIG PADTARITRM TYADNHLIVF MNARLAKENH
     RLYQFYAEVR CDLYSYKSCY GTHASATCHR NCTSYKTFVM PGLRDVHTDK LHVVKFKRSD
     EKRDKNCLDG YLADVNRVHM QTSLLEGQYV RFKNAHACRD YRLSHTAKDV HEFESMLERV
     QVSALSHEIL PVVACYDIET HSDGQRFSAP DADFIISIAV VVRRDAADTR ICLFYSPDDP
     VDLSSSSSSP PAAPDTAAVH FRAERDMIAA FFQLLPLLNA DVVLDFNGDK FDLPFLTGRA
     NKLCGPAEAA RATKIARYDL SPVNVVTQQS YDKFSNKLHS HYLTYYIHID LYQFLSTDSE
     HNDLENFQLN TVAEHYLKKS KVDLPIHDML QMYGEKRLSR IVEYNVQDCV LPVELFLKLE
     IADYMYTQCM LLYLCTDDLL RNISHKITVA YFHLALTNTV AAADPTPDPY FFNKYDLSVT
     SGRKRAFNEP APSANAIDLS QLKRTPVDAA RIPPSAVKLC STRQSCTYKG GKVLSPKPGF
     NRWVATLDFN ALYPTIMMWE GVCMSNVFIA SDGNVYLDKN VNAVNPKLLK TLSEMRVRYK
     GLRDQCEYNS FYYKLYDKIQ NALKRIANSI YGYYGIFFKP LANYITKMGR GKLKEVVGKV
     EAMSDDPRIL REFGLSKINF SVIYGDTDSC FIRVLFDEAE LAPDRRQTAI RSIVQDHVCK
     TLNDSWCGYK MSLENIMLSL ILLKKKKYCY LNNEQRTKYK GWLIKRDMPL FMRKAFRATV
     DSLLRGHSTA CALGLLAEQM LRYYREFGAP RENLVDYCFS MSYNETSTTA KRRKEEDPAR
     KPVITIAKHC RELLANPGVD FLPGNGDRIQ YVLVDVKEKI TQKAFPLKLF DPDSPTLQIS
     WLKHMNILCT FMNELIQVFG NRPEFEHYFG AIVDEYTSAQ MYDVRYPVLV PTRRAKAGKS
     AKKNDSDSDS DSDDDDDPAT TPVNYHSLFS MHLKKPKRQA VGEFEPCPQC VARA
 
 
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