ID A0A0A1ERQ5_9ADEN Unreviewed; 907 AA.
AC A0A0A1ERQ5;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=DNA polymerase {ECO:0000256|PIRNR:PIRNR000788, ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|PIRNR:PIRNR000788, ECO:0000256|RuleBase:RU000442};
OS Rhesus adenovirus 53.
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus; Human mastadenovirus G.
OX NCBI_TaxID=1574629 {ECO:0000313|EMBL:AIY35096.1, ECO:0000313|Proteomes:UP000105286};
RN [1] {ECO:0000313|EMBL:AIY35096.1, ECO:0000313|Proteomes:UP000105286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Stool {ECO:0000313|EMBL:AIY35096.1};
RX PubMed=25410856; DOI=10.1128/JVI.02950-14;
RA Abbink P., Maxfield L.F., Ng'ang'a D., Borducchi E.N., Iampietro M.J.,
RA Bricault C.A., Teigler J.E., Blackmore S., Parenteau L., Wagh K.,
RA Handley S.A., Zhao G., Virgin H.W., Korber B., Barouch D.H.;
RT "Construction and evaluation of novel rhesus monkey adenovirus vaccine
RT vectors.";
RL J. Virol. 89:1512-1522(2015).
CC -!- FUNCTION: Eukaryotic-type DNA polymerase involved in viral genomic
CC replication. DNA synthesis is protein primed, and acts in a strand
CC displacement replication. Assembles in complex with viral pTP, DBP,
CC host NFIA and host POU2F1/OCT1 on viral origin of replication. The
CC polymerase covalently transfers dCMP onto pTP, thereby initiating
CC complementary strand synthesis. {ECO:0000256|ARBA:ARBA00003123}.
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|PIRNR:PIRNR000788, ECO:0000256|RuleBase:RU000442};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC {ECO:0000256|ARBA:ARBA00005755, ECO:0000256|PIRNR:PIRNR000788,
CC ECO:0000256|RuleBase:RU000442}.
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DR EMBL; KM591903; AIY35096.1; -; Genomic_DNA.
DR Proteomes; UP000105286; Genome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0039693; P:viral DNA genome replication; IEA:UniProtKB-KW.
DR InterPro; IPR006172; DNA-dir_DNA_pol_B.
DR InterPro; IPR014382; DNA-dir_DNA_pol_B_adenovir.
DR InterPro; IPR017964; DNA-dir_DNA_pol_B_CS.
DR InterPro; IPR004868; DNA-dir_DNA_pol_B_mt/vir.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR012337; RNaseH-like_sf.
DR Pfam; PF03175; DNA_pol_B_2; 1.
DR PIRSF; PIRSF000788; DPol_ADV; 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|PIRNR:PIRNR000788,
KW ECO:0000256|RuleBase:RU000442};
KW DNA-binding {ECO:0000256|PIRNR:PIRNR000788, ECO:0000256|RuleBase:RU000442};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW ECO:0000256|PIRNR:PIRNR000788};
KW Nucleotidyltransferase {ECO:0000256|PIRNR:PIRNR000788,
KW ECO:0000256|RuleBase:RU000442};
KW Transferase {ECO:0000256|PIRNR:PIRNR000788, ECO:0000256|RuleBase:RU000442};
KW Viral DNA replication {ECO:0000256|ARBA:ARBA00023109}.
FT DOMAIN 155..630
FT /note="DNA-directed DNA polymerase family B
FT mitochondria/virus"
FT /evidence="ECO:0000259|Pfam:PF03175"
SQ SEQUENCE 907 AA; 102967 MW; 6EDE5C2B594C1A74 CRC64;
MGAFGKQLVP FMLVMHVSGE ETLVRQACEL ARELKWDVWN DRSATFYVVT PEKMAVGKKF
REFRDRLQTL LASELWNSFL AANPQLADWA RAELGLASPE SLTYEELKKA PALKGQPRFI
ELYIVGHNIN GFDEIVLAAQ VINNRSDVPG PFRISRNFMP RAGKILFNDV TFALPNPRQK
KRTDFSLWEQ GSCDDTDFKH QYLKVMVRDT FALTHTSLRK AAQAYALPVE KGCCPYKAVN
EFYMLGSYRA DEKGFPAEEY WKDREEYLLN RELWEKKQES SYNLVRETLD YCALDVLVTA
ALVNKLQESY AQFIEDSVGL PRANFNVFQR PTISSNSHAI FRQILYRAEK PHKTHLGEGL
LAPSHEMYDY VRASIRGGRC YPTYIGVLRE PLYVYDICGM YASALTHPMP WGAPLNPYER
ALAVKRWEEA LQDVETEIDY FNKVLLPGIF TIDADPPHAN LLDPLPPFCS RKGGRLCWTN
EPLRGEVATS VDMITLHNRG WRVRILPDER TAVFPEWRCV AREYVQLNIA AKERADREKN
QTLRSIAKLL SNALYGSFAT KLDNKKIVFS DQMDHSTIKS IAAGHVNIKS SSFVETDNLS
AEVMPAFERA YSPEQLALVH SDAEESDGEG GHAPFYTPPG GAGHVTYTYK PITFVDAEED
DLCLHTLEKV DPLIENDRYP SQIASFVLAW TRAFVSEWSQ FLYAEDRGTP LEERPLKSVY
GDTDSLFVTE AGHRLMETQG KKRIKKNGGN LVFDPDKPEL TWLVECETVC AECGADAYSP
ESVFLAPKLY ALKCLHCTRC QHVSKGKLRA KGHAAESLSY DLMLRCYLAD SQGDDARFST
SRMSLKRTLA SAQPGAHPFT VTETTLTRTL RPWKDKTLAA LDAHRLVPYS ESRPNPRNQE
VCWIEIP
//
