ID A0A249Y230_9CAUD Unreviewed; 708 AA.
AC A0A249Y230;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=DNA-directed DNA polymerase {ECO:0000256|HAMAP-Rule:MF_04101};
DE EC=2.7.7.7 {ECO:0000256|HAMAP-Rule:MF_04101};
DE EC=3.1.11.- {ECO:0000256|HAMAP-Rule:MF_04101};
GN ORFNames=RU60_022 {ECO:0000313|EMBL:ASZ78289.1};
OS Klebsiella phage 2044-307w.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Autographiviridae; Studiervirinae; Przondovirus; Przondovirus 2044307w.
OX NCBI_TaxID=2024247 {ECO:0000313|EMBL:ASZ78289.1, ECO:0000313|Proteomes:UP000221535};
RN [1] {ECO:0000313|Proteomes:UP000221535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Zhao X.;
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Replicates viral genomic DNA. This polymerase possesses two
CC enzymatic activities: DNA synthesis (polymerase) and an exonucleolytic
CC activity that degrades single-stranded DNA in the 3'- to 5'-direction.
CC {ECO:0000256|HAMAP-Rule:MF_04101}.
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, ECO:0000256|HAMAP-
CC Rule:MF_04101};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_04101};
CC -!- SIMILARITY: Belongs to the DNA polymerase type-A family.
CC {ECO:0000256|HAMAP-Rule:MF_04101}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MF285615; ASZ78289.1; -; Genomic_DNA.
DR Proteomes; UP000221535; Genome.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006261; P:DNA-templated DNA replication; IEA:InterPro.
DR GO; GO:0039693; P:viral DNA genome replication; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.370; -; 2.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR HAMAP; MF_04101; DPOL_T7; 1.
DR InterPro; IPR019760; DNA-dir_DNA_pol_A_CS.
DR InterPro; IPR001098; DNA-dir_DNA_pol_A_palm_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR002298; DNA_polymerase_A.
DR InterPro; IPR034699; DPOL_T7.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR PANTHER; PTHR10133; DNA POLYMERASE I; 1.
DR PANTHER; PTHR10133:SF62; DNA POLYMERASE THETA; 1.
DR Pfam; PF00476; DNA_pol_A; 1.
DR PRINTS; PR00868; DNAPOLI.
DR SMART; SM00482; POLAc; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS00447; DNA_POLYMERASE_A; 1.
PE 3: Inferred from homology;
KW DNA replication {ECO:0000256|HAMAP-Rule:MF_04101};
KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_04101};
KW DNA-directed DNA polymerase {ECO:0000256|HAMAP-Rule:MF_04101};
KW Exonuclease {ECO:0000256|HAMAP-Rule:MF_04101};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_04101};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_04101};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_04101};
KW Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_04101};
KW Nuclease {ECO:0000256|HAMAP-Rule:MF_04101};
KW Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_04101};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_04101};
KW Viral DNA replication {ECO:0000256|ARBA:ARBA00023109, ECO:0000256|HAMAP-
KW Rule:MF_04101}.
FT DOMAIN 452..668
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
FT REGION 1..187
FT /note="3'-5'exonuclease"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04101"
FT REGION 202..708
FT /note="Polymerase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04101"
FT BINDING 5
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic; for 3'-5' exonuclease activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04101"
FT BINDING 5
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic; for 3'-5' exonuclease activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04101"
FT BINDING 7
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic; for 3'-5' exonuclease activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04101"
FT BINDING 174
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic; for 3'-5' exonuclease activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04101"
FT BINDING 479
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /ligand_note="catalytic; for polymerase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04101"
FT BINDING 479
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /ligand_note="catalytic; for polymerase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04101"
FT BINDING 480
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /ligand_note="catalytic; for polymerase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04101"
FT BINDING 510
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04101"
FT BINDING 522
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04101"
FT BINDING 526
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04101"
FT BINDING 530
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04101"
FT BINDING 658
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /ligand_note="catalytic; for polymerase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04101"
FT BINDING 658
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /ligand_note="catalytic; for polymerase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04101"
SQ SEQUENCE 708 AA; 80109 MW; 7718CF8C46C75C9D CRC64;
MLVTDIEANN LLEKVTQFHC GVIYDYSTDE YVSYRPWDFS AYLDALEAEV ARGGLIVFHN
GHKYDAPVLT KLAKLQLNRE FHLPRENVVD TLVLSRLLFA NIKDSDMALL RSGKLPGKRF
GSHALEAWGY RLGEMKGEYK DDFKKLLEEQ GEDYVDGAEW ISFNEPMMAY NVQDVVVTKA
LLEKLLSDKH YFPPEDGCGD NWWMHDAVTF WQYSCEAVWL EHRAAWLLAK QERNGFPFNT
KAIEELYVEL AGRRSELLQT LTDTFGTWYQ PKGGTELFLH PRTGKPLGKY PRVKYPKQGG
IYKKPKNKAQ REGREPCELD TRDYVEGAPY TPVEHVVFNP SSRDHIALKL KEAGWVPTEF
TDKGAPKVDD EVLEHVRVED PEKQRCIDLI KEYLMIQKRI GQAAEGDKAW LRYVQEDGKI
HGSVNPNGAV TGRATHSFPN LGQVPGVRSP YGEPCRAAFG AEHHLDGLTG LPWVQAGIDA
SGLELRCLAH FMSKYDGGAY ADVILNGDIH TVNQQAAELP TRDNAKTFIY GFLYGAGDEK
IGQIVGAGKE RGKELKKKFL ENTPAIAALR EGIQQTLVES SRWVAGEQKV KWKRRWIKGL
DGRKVHVRSP HAALNTLLQS AGALICKLWI VETEELLLKA GLKHGWDGDF AYMAWVHDEI
QVACRTPEIA QQVIDIAQQA MRNVGEHFKF RCRLDTEGKM GPNWAVCH
//
