ID A0A1T4KQ58_9ACTN Unreviewed; 923 AA.
AC A0A1T4KQ58;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
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 ORFNames=SAMN02745673_00487 {ECO:0000313|EMBL:SJZ44569.1};
OS Marinactinospora thermotolerans DSM 45154.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Marinactinospora.
OX NCBI_TaxID=1122192 {ECO:0000313|EMBL:SJZ44569.1, ECO:0000313|Proteomes:UP000190637};
RN [1] {ECO:0000313|EMBL:SJZ44569.1, ECO:0000313|Proteomes:UP000190637}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45154 {ECO:0000313|EMBL:SJZ44569.1,
RC ECO:0000313|Proteomes:UP000190637};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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 -!- SIMILARITY: Belongs to the DNA polymerase type-A family.
CC {ECO:0000256|ARBA:ARBA00007705, ECO:0000256|RuleBase:RU004460}.
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DR EMBL; FUWS01000001; SJZ44569.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T4KQ58; -.
DR STRING; 1122192.SAMN02745673_00487; -.
DR OrthoDB; 9806424at2; -.
DR Proteomes; UP000190637; 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; cd06140; DNA_polA_I_Bacillus_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; 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; 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; 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.
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}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU004460};
KW Reference proteome {ECO:0000313|Proteomes:UP000190637};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT DOMAIN 24..284
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 333..512
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00474"
FT DOMAIN 679..886
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 923 AA; 99762 MW; 33F153D630B82124 CRC64;
MVKTQATPEQ SGSPSARKEG SGVPRLLLLD GHSMAFRAFF ALPVDKFATS TGQSTNAVYG
FTSMLIKLLR DERPTHVAVA WDRSEPTFRH EVYDAYKAGR AETPPEFPGQ VALLQELLGL
MGVASLSVAG FEADDLIATL AVEGGAKGME VLIASGDRDA FQLVTDTCTV LYPGKSLSDL
TRMTPSAVET KYGVSPQRYR DLAALVGEKS DNLPGVPGVG PKTAAKWIAK YGSLDDLIAR
ADEITGKAGQ SFRDHLDDVL RNQRLNALST DVEIGVPVEE LTMGAWDRPG INTLFDTLEF
AGTLRERLFS VLGEEDAAGS GEGSPASDEG FEVELVSPVA GELGAWLERH AGPDGRCGLA
VTGSWGRGTG EITGLAIATP AGTAVHVDPA GLDAADESAL AAWLADPDRT KAVHDAKGPM
LALAAHGWDL AGLTADTALA AYLALPGQRN VGLGDLCLRY LNRELSPQEE GGRQLALDID
GGGDAAEALR RDLALRARAT LELADALDAD LERRGATRLL REVELPLVRV LAAMERTGIA
ADRAYLDELE AEFAAAVRQA VQEAHRVVGR EFNLGSPKQL QQILFTELDL PKTKRIKTGY
TTDADALAWL ATRTDNELPV ILLRHRDQTK LRTTVEGLIK TIADDGRIHT TFNQMIAATG
RLSSTDPNLQ NIPVRTDAGR RIRRAFVVGE GYEHLLTADY SQIELRIMAH LSGDESLIEA
FETGHDFHSE IAARVFGVPA GQVGGEERAR IKAMNYGLAY GLSAFGLSQQ LGTTPEEARR
LMDDYFAQFG RVRDYLHEVV EQARRAGYTE TMLGRRRYLP DLTSDNRQRR EMAERMALNA
PIQGSAADII KVAMLDVDAA LREGGFSSRL LLQVHDELVL EVVADELDAV RKLVSENMAN
AYDLRVPLAV SVGVGPNWHD AAH
//
