ID A0A419A5X7_9RHOB Unreviewed; 938 AA.
AC A0A419A5X7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=DNA polymerase I {ECO:0000256|ARBA:ARBA00020311, ECO:0000256|RuleBase:RU004460};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417, ECO:0000256|RuleBase:RU004460};
GN Name=polA {ECO:0000256|RuleBase:RU004460,
GN ECO:0000313|EMBL:RJL12786.1};
GN ORFNames=D3P05_12230 {ECO:0000313|EMBL:RJL12786.1};
OS Paracoccus siganidrum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=1276757 {ECO:0000313|EMBL:RJL12786.1, ECO:0000313|Proteomes:UP000283587};
RN [1] {ECO:0000313|Proteomes:UP000283587}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26381 {ECO:0000313|Proteomes:UP000283587};
RA Jurado V., Gutierrez-Patricio S., Gonzalez-Pimentel J.L., Miller A.Z.,
RA Laiz L., Saiz-Jimenez C.;
RT "Paracoccus onubensis nov. sp. a moderate halophilic bacterium isolated
RT from Gruta de las Maravillas (Aracena, Spain).";
RL Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: In addition to polymerase activity, this DNA polymerase
CC exhibits 5'-3' exonuclease activity. {ECO:0000256|RuleBase:RU004460}.
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:RU004460};
CC -!- SUBUNIT: Single-chain monomer with multiple functions.
CC {ECO:0000256|ARBA:ARBA00011541}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-A family.
CC {ECO:0000256|ARBA:ARBA00007705, ECO:0000256|RuleBase:RU004460}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RJL12786.1}.
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DR EMBL; QZEW01000047; RJL12786.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A419A5X7; -.
DR OrthoDB; 9806424at2; -.
DR Proteomes; UP000283587; Unassembled WGS sequence.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
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:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:0006261; P:DNA-templated DNA replication; IEA:UniProtKB-UniRule.
DR CDD; cd08637; DNA_pol_A_pol_I_C; 1.
DR CDD; cd06139; DNA_polA_I_Ecoli_like_exo; 1.
DR CDD; cd09898; H3TH_53EXO; 1.
DR CDD; cd09859; PIN_53EXO; 1.
DR Gene3D; 3.30.70.370; -; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 2.
DR Gene3D; 3.40.50.1010; 5'-nuclease; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR InterPro; IPR002562; 3'-5'_exonuclease_dom.
DR InterPro; IPR020046; 5-3_exonucl_a-hlix_arch_N.
DR InterPro; IPR002421; 5-3_exonuclease.
DR InterPro; IPR036279; 5-3_exonuclease_C_sf.
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; IPR020045; DNA_polI_H3TH.
DR InterPro; IPR018320; DNA_polymerase_1.
DR InterPro; IPR002298; DNA_polymerase_A.
DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR InterPro; IPR008918; HhH2.
DR InterPro; IPR029060; PIN-like_dom_sf.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR NCBIfam; TIGR00593; pola; 1.
DR PANTHER; PTHR10133; DNA POLYMERASE I; 1.
DR PANTHER; PTHR10133:SF62; DNA POLYMERASE THETA; 1.
DR Pfam; PF01367; 5_3_exonuc; 1.
DR Pfam; PF02739; 5_3_exonuc_N; 1.
DR Pfam; PF00476; DNA_pol_A; 1.
DR Pfam; PF01612; DNA_pol_A_exo1; 1.
DR PRINTS; PR00868; DNAPOLI.
DR SMART; SM00474; 35EXOc; 1.
DR SMART; SM00475; 53EXOc; 1.
DR SMART; SM00479; EXOIII; 1.
DR SMART; SM00279; HhH2; 1.
DR SMART; SM00482; POLAc; 1.
DR SUPFAM; SSF47807; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF88723; PIN domain-like; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS00447; DNA_POLYMERASE_A; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU004460};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU004460};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW ECO:0000256|RuleBase:RU004460};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004460};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW ECO:0000256|RuleBase:RU004460};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nuclease {ECO:0000256|ARBA:ARBA00022839};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU004460};
KW Reference proteome {ECO:0000313|Proteomes:UP000283587};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT DOMAIN 10..270
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 326..526
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00474"
FT DOMAIN 346..527
FT /note="Exonuclease"
FT /evidence="ECO:0000259|SMART:SM00479"
FT DOMAIN 695..898
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
SQ SEQUENCE 938 AA; 101889 MW; A38C760EC0E46FF5 CRC64;
MTPTGFGKGS HLHLIDGSAF IFRAYHALPP LTRKSDGLPV GAVAGFCNML WKYVTDERGQ
DAPTHAAVIF DHSAKTFRNE IYPAYKANRP EPPEDLRPQF PLTREATRAF NIACIETEGF
EADDIIAAFA CQARDAGGRV TIVSSDKDLM QLVGGGVDML DPIKGKTIGP EEVAEKFGVG
PDRVVDVQAL AGDSVDNVPG APGIGIKTAA QLINEYGDLE TLLERAAEIK QPKRRQTLID
HAEQIRVSKR LVTLDCDTPL DASLESLEIR APDPQALLGF LADMEFRTLT ARVAERLGAE
PPAVVSAPPS EAPAAPELPA IDHAGYETVT DRAALDAWIA RIREAGHVAI DTETTSLDEM
QAALVGISLA VEPGRACYVP VGHVQGSDDL FGQAALVEGQ LPLDQVLAAL KPVLEDPAIL
KIGQNLKYDW KILARQIPEL GGIRMAPLTD TMLMSYALNA GSHNHGMDEL AERYLGHRCI
PIKDLIGSGK SQIRFDQVPI DKAAPYAAED AEITLRLYRH FAPMLPVEQV TTAYEVLERP
MIPVLADMEL AGIRVETDTL KRMSNAFAQK LAGLEDEIHE LAGERFNVGS PKQLGEILFD
KMGLAGGKQG KTGAFSTSAD VLEDLAAEGH DLPARILDWR QVAKLKSTYT DALQTHVDPD
TGRVHTSYSI TGAQTGRLAS TDPNLQNIPV RTEEGRRIRE AFVAAEGHRL VSLDYSQIEL
RILAHVADIP ALKQAFRDGI DIHAMTASQM FGVPVEGMDP MIRRRAKAIN FGVIYGISGF
GLSRNLRIPR AEAQQFIDTY FERFPEIRAY MDKTVADAKQ DGFVRTLFGR RINTPGINQS
GPAAGGARRA AINAPIQGAA ADIIRRAMIR MPEAIRGLPA RMLLQVHDEL VFEVQESAVE
DLIAAARKVM EGAAEPAVKL NVPLIVDAGH GMNWAEAH
//
