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Database: UniProt
Entry: A0A1D8QM89_9ADEN
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ID   A0A1D8QM89_9ADEN        Unreviewed;      1176 AA.
AC   A0A1D8QM89;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 33.
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};
GN   Name=pol {ECO:0000313|EMBL:AOW42059.1};
OS   Pigeon adenovirus 2.
OC   Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC   Rowavirales; Adenoviridae; Aviadenovirus; Pigeon aviadenovirus B.
OX   NCBI_TaxID=1907767 {ECO:0000313|EMBL:AOW42059.1, ECO:0000313|Proteomes:UP000201673};
RN   [1] {ECO:0000313|EMBL:AOW42059.1, ECO:0000313|Proteomes:UP000201673}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YPDS-Y-V1.A19.11-2013 {ECO:0000313|EMBL:AOW42059.1};
RX   PubMed=27697452; DOI=10.1016/j.virusres.2016.09.024;
RA   Teske L., Rubbenstroth D., Meixner M., Liere K., Bartels H.,
RA   Rautenschlein S.;
RT   "Identification of a novel aviadenovirus, designated pigeon adenovirus 2 in
RT   domestic pigeons (Columba livia).";
RL   Virus Res. 227:15-22(2016).
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; KX121164; AOW42059.1; -; Genomic_DNA.
DR   RefSeq; YP_009310429.1; NC_031503.1.
DR   GeneID; 29997534; -.
DR   KEGG; vg:29997534; -.
DR   OrthoDB; 529at10239; -.
DR   Proteomes; UP000201673; 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   Reference proteome {ECO:0000313|Proteomes:UP000201673};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000788, ECO:0000256|RuleBase:RU000442};
KW   Viral DNA replication {ECO:0000256|ARBA:ARBA00023109}.
FT   DOMAIN          368..826
FT                   /note="DNA-directed DNA polymerase family B
FT                   mitochondria/virus"
FT                   /evidence="ECO:0000259|Pfam:PF03175"
FT   REGION          828..857
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1176 AA;  134960 MW;  75B44F5D83DCBA74 CRC64;
     MSLVLPPTLL GEDARLLKLT KSTQRFFRGD GKERYLSKSV FYLNEQPIKL TPSPFSIGLR
     KFLRTHRFLI GRSNYSLYYN KIDYTYYSLD PVRRLSVFRP RYIGVLVFKG YSVSIKKKHE
     TDNAVLPPMY LTRHADGTWI WIASITPVNR CPRCGSTWSS NHSCNETVAA FHHIVMGKGK
     DLWQHVYFRC PAMQPNTRLL FVTYDIETYT SFELKGKRLQ PFMLCFKLSG HPDLVETGHE
     IARQDDTIGM LSGGYYWIDP RPGEVARRFR TFRHRLQLHF ARDLVRRFYR CNEDYCRQVM
     RDGQYASIYD IPHELFTHPI APLSLSESFF SVDIVILGHN ICKFDELLLA TELLEQRHEF
     PQAVRCVRAF MPRVGRLLFN DIRFSLPNPL YKRKDASRVT RWASGRVSVV DDADVYVRFM
     VRDTCQLTSG AKLSRAATAY ALDLGKGTCP YEAINEHFSF GDFEKDEDGF PVSRYWEQPS
     VLLEQKNLWQ QAHPGQAYDI VQACLEYCMQ DVLVTEKLAH VLYENYDAYF SNELEMAGPF
     NIFERPTIPS NTHALWKQIA FTAYVNEQKR KGRRKIHPDY LAELYSPHKT MFRYIRQALR
     GGRCYPTVLG PFSAPVYVFD ICGMYASALT HPMPHGMPLH PDHVRQEVDK LNELLRSTDH
     LSYFDSRIKP SILKIDAHPP RLEYLDPLPP LCSRRGGRLV WTNESLYDEV VVILDVITLH
     NRGWRVTVRQ DPMNVVFPEW KTLCAEYVGK NIAAKEKADR DKNEVLRSIS KMLSNALYGA
     FATNMDATSI KFEQDLTEGD LADIYDGTKV VKHVTLLNDP SLMSRELPIP NSPWSADGDV
     TTNPLLTDDA ESDEGPSLSE VDEQLEAAVG GEVYIPSDDH AHYAKASETV FKPLRLVDAD
     GAALTVLHLE RLDKLVDNHR YATQLACFVL GWSRAFFSEW SDIVHGPDRG IHPHSRPPRS
     LYGDTDSLFV TASGYERMRT LGAHRLKTPT TRLTFDPEKP DLYWACECDI KCKKCGSDTY
     SSEAVFLAPK LYGLKDAVCV NPVCGHVGVG KIRSKGHRQA ELIYETLMKC WYRHEAETLG
     AHPKEPDLYT RRTIFKTTLL NKVSRYDPFT IHTEQLVRIL RPWKDLTLYE HNGLLHPYNN
     LNPNPRTVGE KIYREDASAQ DPLAPLSLLR SDGSQA
//
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