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Database: UniProt
Entry: A0A0T2IBI9_9MICO
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ID   A0A0T2IBI9_9MICO        Unreviewed;       890 AA.
AC   A0A0T2IBI9;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 41.
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=ASD62_00505 {ECO:0000313|EMBL:KQZ88026.1};
OS   Phycicoccus sp. Root563.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Phycicoccus.
OX   NCBI_TaxID=1736562 {ECO:0000313|EMBL:KQZ88026.1, ECO:0000313|Proteomes:UP000051641};
RN   [1] {ECO:0000313|Proteomes:UP000051641}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root563 {ECO:0000313|Proteomes:UP000051641};
RA   Garrido-Oter R., Bai Y.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQZ88026.1, ECO:0000313|Proteomes:UP000051641}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root563 {ECO:0000313|EMBL:KQZ88026.1,
RC   ECO:0000313|Proteomes:UP000051641};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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}.
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:KQZ88026.1}.
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DR   EMBL; LMGM01000001; KQZ88026.1; -; Genomic_DNA.
DR   RefSeq; WP_056914286.1; NZ_LMGM01000001.1.
DR   AlphaFoldDB; A0A0T2IBI9; -.
DR   STRING; 1736562.ASD62_00505; -.
DR   OrthoDB; 9806424at2; -.
DR   Proteomes; UP000051641; 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; 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; 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   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.
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}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU004460};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051641};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT   DOMAIN          2..262
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00475"
FT   DOMAIN          303..478
FT                   /note="3'-5' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00474"
FT   DOMAIN          646..853
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
SQ   SEQUENCE   890 AA;  97450 MW;  5E80A3281D77116B CRC64;
     MSRLLLLDGH SLAYRAFFAL PVENFSTSTG QHTNAVYGFT SMLINVLRDE QPTHLAVAFD
     VSRKTFRSEE YAEYKATRSA TPSEFQGQVA LVREVLDALK IKHVQLDGFE ADDVIATLTT
     QATAQGMDVV ICTGDRDAFQ LVTDKVTLLY PVRGVSEVWR MDPKAVEEKY LVAPERYSDL
     AALVGETSDN LPGVPGVGPK TAAKWLGLYG DLQGVVAHAD EIKGKAGESL REHLNGVLRN
     RRLNHLLTDL ELPVTIDELE RQNWDRDQVH TVFDSLEFRV LRDRLFEYLE APQEEAEHGF
     DLEGSVLAPD EVAGWLQEYA AAGARVGVHV VGSWGRGTGD ATALALATDG DAAAYVDLAA
     LDPAGEATVG AWLADPMRPK VLHDAKGPLL ALAARGWAVD GIETDTALAA YLVRPDQRSY
     DLSDLVLRHL GRELRAETAD SGQGLLDFGD DQDTGAQESM VRARAVLDLA ASLAEQLEAT
     GGTSLQRDVE LPLEHVLAGM ERTGIGADTE TMTGLEADFA AKVREAQEDA YDAIGGDQIN
     LGSPKQLQVV LFETLGLPKT RRTKTGYTTD ADALTDLFTK TEHPFLEALL RHRDASRLRV
     TVEGLLKSVA DDGRIHTTYQ QTIAATGRLS STDPNLQNIP IRTDEGRRIR EVFVVGEGYE
     SLMSADYSQI EMRIMAHLSG DEGLIEAFRT GEDLHRFVGS RVFHVEPQDV TSAMRSKVKA
     MSYGLAYGLS AFGLSKQLTI STGEAQGLMD EYFARFGGVR DYLTEVVAEA RGTGYTQTML
     GRRRYLPDLT SDNRQRREMA ERMALNAPIQ GSAADIIKLA MLRVDKALTE SGARSRQLLQ
     VHDELVLEIA PGERDDVEAL VRREMGGAME MDVPLEVSVG VGRSWHDAAH
//
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