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Database: UniProt
Entry: Q98207_MCV1
LinkDB: Q98207_MCV1
Original site: Q98207_MCV1 
ID   Q98207_MCV1             Unreviewed;      1004 AA.
AC   Q98207;
DT   01-FEB-1997, integrated into UniProtKB/TrEMBL.
DT   01-FEB-1997, sequence version 1.
DT   24-JAN-2024, entry version 114.
DE   RecName: Full=DNA polymerase {ECO:0000256|ARBA:ARBA00015749, ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417, ECO:0000256|RuleBase:RU000442};
GN   Name=MC039L {ECO:0000313|EMBL:AAC55167.1};
OS   Molluscum contagiosum virus subtype 1 (MOCV) (MCVI).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Molluscipoxvirus;
OC   Molluscum contagiosum virus.
OX   NCBI_TaxID=10280 {ECO:0000313|EMBL:AAC55167.1};
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1] {ECO:0000313|EMBL:AAC55167.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=8670425; DOI=10.1126/science.273.5276.813;
RA   Senkevich T.G., Bugert J.J., Sisler J.R., Koonin E.V., Darai G., Moss B.;
RT   "Genome sequence of a human tumorigenic poxvirus: prediction of specific
RT   host response-evasion genes.";
RL   Science 273:813-816(1996).
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; U60315; AAC55167.1; -; Genomic_DNA.
DR   PIR; T30641; T30641.
DR   RefSeq; NP_043990.1; NC_001731.1.
DR   SMR; Q98207; -.
DR   GeneID; 1487060; -.
DR   KEGG; vg:1487060; -.
DR   OrthoDB; 165at10239; -.
DR   Proteomes; UP000000869; 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; 1.10.287.690; Helix hairpin bin; 1.
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; 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; IPR013617; DNA-dir_DNA_pol_B_vir_insert.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR   InterPro; IPR013660; DNApol_B_exo_N.
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; PF08408; DNA_pol_B_3; 1.
DR   Pfam; PF03104; DNA_pol_B_exo1; 1.
DR   Pfam; PF08452; DNAP_B_exo_N; 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:UP000000869};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000442};
KW   Viral DNA replication {ECO:0000256|ARBA:ARBA00023109}.
FT   DOMAIN          1..22
FT                   /note="DNA polymerase B exonuclease N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08452"
FT   DOMAIN          109..344
FT                   /note="DNA-directed DNA polymerase family B exonuclease"
FT                   /evidence="ECO:0000259|Pfam:PF03104"
FT   DOMAIN          345..472
FT                   /note="DNA-directed DNA polymerase family B viral insert"
FT                   /evidence="ECO:0000259|Pfam:PF08408"
FT   DOMAIN          486..984
FT                   /note="DNA-directed DNA polymerase family B
FT                   multifunctional"
FT                   /evidence="ECO:0000259|Pfam:PF00136"
SQ   SEQUENCE   1004 AA;  115103 MW;  050EBD03FE967517 CRC64;
     MEIRCLNWFE ARGEERALYL KAKTRAGDTL FVRFPHYYYY VVDGGTLSTL APPPRAASAL
     GEFELACIDE TLARADALHA PTRPRSQLWL LEEAQPRQIA GALLAEFMHI TWFFLRNEIE
     PNGCYRVPDA ELEPVCARCF HCAAPRRAFA TRVPLFEVTH TYLFFDIECQ FDKKFPSVFS
     NPVSHISFCY VDRLGTEVRF SLLNSDLLSE DSLRGCRRIA TPDEFALEPG VTFCSEVVLL
     QLTKRLLERH FDFIVTFNGN NFDIRYVSNR LQLLTQSSVC FRLPDQREPV KLVIYERSLA
     SHRGAGGMAN TSFHVNNNNG TIFFDLYTFI QKAERLDSYK LDSISKNVFH CRARVLDAGA
     GECTLAGGPD ANAEDRLRLF CEVLQTGNYV TLDTVHVCRI LGKRFFEHGF ALRVRCAESY
     APGSLCELAF GKDDVDLREL YRHYSLAAAL EMERYCMHDA CLCKYLWSYY RVPSKIDAAA
     ATYLLPQCLA LEYRASTLIK GPLLRLMLRE RVVYVRTQEP ARYTYGGGKV FLPRQKLFDT
     NVMVFDYNSL YPNVCIFGNL SPETLVGVVA NAHRLDAEIN MQELRRRFPE PAFLHVLCEA
     RARDGYSEIA VFDRRRQGII PKLLGTFMEQ RARYKALMRA ASSGLERTLY DSMQYVYKVV
     ANSVYGLMGF YNSSLYSYSS AKCCTTIGRV MITYLDRVVD GATLCAGVLR LAAEPRNPLL
     ASAPPRARDV DVSAALGHEL ELRFRSVYGD TDSIFLELNL REVQTTLAVA RTLERVLNEH
     VLFENFRVEF EAIYQNLILQ SKKKYSTTKY AADHRAGDAP EHVSKGTSET RRDVSRFHKL
     MISRYKAQLV ALLAEARLSS RQVCIEMLRS LEVDLFAEFA ARAQPLEMFL LSRMHHRNYK
     APDNPNVELV NRYNRENLEP IELGERYYYA YVCASELPWQ LAVANVRNHE RIVDASYVLP
     ERERVFYEIY FRRLATELVN LLDNKPLCAE FFTRLFGVRP VFSN
//
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