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Database: UniProt
Entry: A0A370F096_9FLAO
LinkDB: A0A370F096_9FLAO
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ID   A0A370F096_9FLAO        Unreviewed;       944 AA.
AC   A0A370F096;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
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=DEU42_10194 {ECO:0000313|EMBL:RDI15804.1};
OS   Flavobacterium sp. AG291.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=2184000 {ECO:0000313|EMBL:RDI15804.1, ECO:0000313|Proteomes:UP000254305};
RN   [1] {ECO:0000313|EMBL:RDI15804.1, ECO:0000313|Proteomes:UP000254305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AG291 {ECO:0000313|EMBL:RDI15804.1,
RC   ECO:0000313|Proteomes:UP000254305};
RA   Venturi V.;
RT   "Genome sequencing of rice bacterial endophytes.";
RL   Submitted (JUL-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   -!- 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:RDI15804.1}.
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DR   EMBL; QQAR01000001; RDI15804.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A370F096; -.
DR   OrthoDB; 9806424at2; -.
DR   Proteomes; UP000254305; 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; 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.
DR   PROSITE; PS00447; DNA_POLYMERASE_A; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
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:UP000254305};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT   DOMAIN          5..266
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00475"
FT   DOMAIN          346..531
FT                   /note="3'-5' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00474"
FT   DOMAIN          701..908
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
FT   REGION          293..333
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          562..589
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   944 AA;  106244 MW;  1E7B679D223B6FDF CRC64;
     MSQQKRLFLL DAYALIFRGY YAFIKNPRIN SKGMDTSAIM GFMNSLLDVI KREKPDHLAV
     AFDKGGSHVR TEMFTEYKAN RDETPEAIKV AVPYIQELLK AMHIPVIELE GCEADDLIGT
     LAKQAEKQNY QVFMVTPDKD FAQLVSENIF MYRPARMGNG IEIWGVPEVL ERFEIERPEQ
     VIDFLGMMGD AVDNIPGLPG VGEKTAKKFL KDYGTMENLL ANTHELKGKM KENIEANKEK
     GLMSKVLATI ITDCDVTFHE EDFELSTPDI EKVEAIFNEL EFRRMAEQFQ KLFDDSTQPE
     SGAPKAATPK ASSKNDQQFS LFGGGEPDSE TAETTTTGFY NTIANTDHFY QAVQGTMAIN
     FLMRDLMKQT SVSFDTETTG VNPLIAELVG MSFSWEKGKG FYVPVPANRE EAQQVINLFL
     PFFEDENIEK VGQNLKYDLE VLAQYGVTVK GKIFDTMIAH YLINPDMRHG MDILSETYLK
     YSPVSIETLI GKKGKGQKSM RDVELDLIKE YAVEDADITL QLKEVFAPML ESTDTRKLFD
     EIEIPLMPVL AAMEQEGINL DVPYLKELAA ELSADIKKLE QQIYETAGES FNLASPKQLG
     DILFDKLKIG GAKQKKTKTG QYATGEEVLS YLAAENPIVA DILEWRQLVK LLNTYVEALP
     LQVEPSTGRV HTDYMQTVAA TGRLSSNNPN LQNIPVRTER GRQIRKAFIA RNEDYTILSA
     DYSQIELRII AALSGDPEMV SAFQKGEDIH ASTAAKVFNV ALNEVTREQR SHAKTVNFGI
     VYGVSAFGLS NQTSLSRSES KELIDAYYKT YPRLKQYISE QVEIAREQGY VQTISGRRRY
     LKDINSQNMV VRGGAERNAV NAPIQGSAAD IIKIAMINIQ KRLVDEGWKS KMLLQVHDEL
     VFDVHNSELE KIKPMIKQEM ESAFKLDVPL EVDMGTGKNW LEAH
//
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