DPOL_ADEG1
ID DPOL_ADEG1 Reviewed; 1121 AA.
AC Q64751;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=DNA polymerase {ECO:0000255|HAMAP-Rule:MF_04055};
DE EC=2.7.7.7 {ECO:0000255|HAMAP-Rule:MF_04055};
GN Name=POL {ECO:0000255|HAMAP-Rule:MF_04055};
OS Fowl adenovirus A serotype 1 (strain CELO / Phelps) (FAdV-1) (Avian
OS adenovirus gal1 (strain Phelps)).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Aviadenovirus; Fowl aviadenovirus A.
OX NCBI_TaxID=10553;
OH NCBI_TaxID=8976; Galliformes.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=8627769; DOI=10.1128/jvi.70.5.2939-2949.1996;
RA Chiocca S., Kurzbauer R., Schaffner G., Baker A., Mautner V., Cotten M.;
RT "The complete DNA sequence and genomic organization of the avian adenovirus
RT CELO.";
RL J. Virol. 70:2939-2949(1996).
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:0000250|UniProtKB:P03261,
CC ECO:0000250|UniProtKB:P04495, ECO:0000255|HAMAP-Rule:MF_04055}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_04055};
CC -!- SUBUNIT: Heterodimer with the terminal protein; this heterodimer binds
CC to bp 9 to 18 of the genome. Forms a complex with viral pTP, DBP and
CC hosts NFIA and POU2F1/OCT1 for initiation of replication.
CC {ECO:0000250|UniProtKB:P04495, ECO:0000255|HAMAP-Rule:MF_04055}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000250|UniProtKB:P03261,
CC ECO:0000255|HAMAP-Rule:MF_04055}.
CC -!- MISCELLANEOUS: This DNA polymerase requires a protein as a primer.
CC {ECO:0000255|HAMAP-Rule:MF_04055}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC {ECO:0000255|HAMAP-Rule:MF_04055, ECO:0000305}.
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DR EMBL; U46933; AAC54904.1; -; Genomic_DNA.
DR RefSeq; NP_043878.1; NC_001720.1.
DR PRIDE; Q64751; -.
DR GeneID; 1733477; -.
DR KEGG; vg:1733477; -.
DR Proteomes; UP000001594; Genome.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:UniProtKB-UniRule.
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:0006261; P:DNA-templated DNA replication; IEA:UniProtKB-UniRule.
DR GO; GO:0039693; P:viral DNA genome replication; IEA:UniProtKB-UniRule.
DR Gene3D; 3.90.1600.10; -; 1.
DR HAMAP; MF_04055; ADV_DPOL; 1.
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; IPR023211; DNA_pol_palm_dom_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; SSF53098; SSF53098; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS00116; DNA_POLYMERASE_B; 1.
DR PROSITE; PS00119; PA2_ASP; 1.
PE 3: Inferred from homology;
KW DNA replication; DNA-binding; DNA-directed DNA polymerase; Host nucleus;
KW Nucleotidyltransferase; Reference proteome; Transferase;
KW Viral DNA replication.
FT CHAIN 1..1121
FT /note="DNA polymerase"
FT /id="PRO_0000046500"
FT REGION 443..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 736..775
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..757
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1121 AA; 129396 MW; A55B9B6A54D3BDE1 CRC64;
MLIAKNVTGE WVWITSRTPV QQCPTCGRHW VRRHSCNERR SAFYYHAVQG SGSDLWQHVH
FSCPAQHPHI RQLYITYDIE TYTVFEKKGK RMHPFMLCFM LSGDPQLVSR AERLARQDDR
LKALDEGFYW LDSHPGEVAR RFRNFRSRLQ IEFAQNLVDR YAAANRDYCD QLVKDGKYGS
VHKIPYELFE KPTSPLSLPD NFYSVDIVVL GHNICKFDEL LLATELVERR DLFPEACKCD
RSFMPRVGRL LFNDIIFRMP NPNYVKKDAS RVERWSRGIV SHQDARSVFV RFMVRDTLQL
TSGAKLSKAA AAYALDLCKG HCPYEAINEF ISTGRFHADA DGFPVERYWE DPSVIAEQKN
LWQKEHPGQQ YDIVQACLEY CMQDVRVTQK LAHTLHDSYD AYFQRELGME GHFNIFVRPT
IPSNTHAFWK QLTFSNYVRE QRATCPPSVP EPPKKKGRTK KKKQPSPDYV AEVYAPHRPM
FKYIRQALRG GRCYPNVLGP YLKPVYVFDI CGMYASALTH PMPHGMPLDP KFTAQHVEEL
NRLLTNESHL SYFDARIKPS ILKIEAYPPP PEMLDPLPPI CSRRGGRLVW TNEALYDEVV
TVIDILTLHN RGWRVQVLHD EMNIVFPEWK TLCADYVTKN ILAKEKADRE KNEVIRSISK
MLSNALYGAF ATNMDTTRII FEQDLSEADK KNIYEGTEIV KHVTLLNDDS FNGTEVTLEN
APNPFSEESL RQQFRYADDP EQEEPEAEED GEEEGDDSDR ESARKPKNAL TEDDPLVAVD
LEVEATLATG PYIPEGELSS AHYARANETR FKPMRLLEAT PEALTVLHLE SLDKQVANKR
YATQIACFVL GWSRAFFSEW CDILYGPDRG VHILRREEPR SLYGDTDSLF VTETGYHRMK
SRGAHRIKTE STRLTFDPEN PGLYWACDCD IKCKACGSDT YSSETIFLAP KLYGLKNSIC
VNEQCRTVGP GKIRSKGHRQ SELIYDTLLR CWRRHEDVQF GAQSNIPELH TRRTIFKTTL
LNKVSRYDPF TIHNEQLTRV LRPWKDLTLY EHGDYLYPYD NEHPNPRTTG DVRPVPIVGH
EDPLAPLRWE PYAFLSEEEC GQVHDLLFAD DSSQEAESLG V
