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Database: UniProt
Entry: A0A2Z3I2D1_9GAMM
LinkDB: A0A2Z3I2D1_9GAMM
Original site: A0A2Z3I2D1_9GAMM 
ID   A0A2Z3I2D1_9GAMM        Unreviewed;       924 AA.
AC   A0A2Z3I2D1;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
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=DKL61_15250 {ECO:0000313|EMBL:AWM81582.1};
OS   Gammaproteobacteria bacterium ESL0073.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria.
OX   NCBI_TaxID=2070539 {ECO:0000313|EMBL:AWM81582.1, ECO:0000313|Proteomes:UP000246096};
RN   [1] {ECO:0000313|EMBL:AWM81582.1, ECO:0000313|Proteomes:UP000246096}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ESL0073 {ECO:0000313|EMBL:AWM81582.1,
RC   ECO:0000313|Proteomes:UP000246096};
RA   Ellegaard K.M.;
RT   "Reference genomes for bee gut microbiota database.";
RL   Submitted (MAY-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}.
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DR   EMBL; CP029478; AWM81582.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2Z3I2D1; -.
DR   OrthoDB; 9806424at2; -.
DR   Proteomes; UP000246096; Chromosome.
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   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:UP000246096};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT   DOMAIN          4..266
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00475"
FT   DOMAIN          325..512
FT                   /note="3'-5' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00474"
FT   DOMAIN          682..888
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
SQ   SEQUENCE   924 AA;  102286 MW;  4A643C6E78C12EC0 CRC64;
     MSQAPLVLVD GSSYLYRAYH ALPPLATANG QPTGAIKGVI NMLKSLVKQY PDSPIAVVFD
     AKGGSFRDEL FADYKAHRPP MPDDLRSQIE PLHQCVKAMG FPLLCVDRVE ADDVIGTLAI
     ATAKTERSVV ISTGDKDMAQ LVNHKITLVN TMSGTTLDPQ GVVDKFGVEP KFIIDFLALM
     GDKSDNIPGV PSVGEKTAVG LIQGLQGGLD TIYSHLDQIP NLPIRGAKSL PAKLEEHKEM
     AYLSYQLATI KTDVELDITI DELNRSEEDA TTLIELYRTL EFKQWLDALL RKAPKQEQAK
     MQQGDIFSNE EITPIETETS NTRDYQMITD TATLDAWVEK LNKAELIAFD TETTSVDAQQ
     AELVGLSFSI KPHQAIYIPV AHDYMGAPKQ LSRDDVVAKL KPILENPNKA KVGQHAKYDI
     NVLSHYNIDV QGVKYDTMME SYILDATGSR HDMDTLANNY LNEQTVKFED IAGKGAKQLT
     FNQISLEQAA PYAAEDADIT LRLHETLWAK LQQEPNQAEV LTHIEIPLIP ALARIERNGA
     LVDAKLLAAQ SQELGEKMIA LENKTFELAG QTFNMGSPKQ LGEILYTKLG LPVISKTATG
     QPSTAEAVLA ELASQGYELP EVLMEYRSLS KLKSTYTDRL PEQINPRTGR IHTSYHQAVT
     ATGRLSSSDP NLQNIPIRTP EGRRIRQAFI APKGYKLLAV DYSQIELRIM AHLAQDKGLL
     DAFKHGLDVH KATAAEVFGV SVNQVTADQR RKAKAINFGL IYGMSAFGLA KQIGVDRKEA
     QEYIDKYFTQ YPGVLSYMER TRELAAEKGY VETLFKRRLY LPDIKASNAN TRRGAERTAI
     NAPMQGTAAD IIKRAMISVD AWLQHEKTDA KVILQVHDEL VLEVREDLTQ LVSDKIKILM
     AEAAELSVPL VVDVGIGNNW DEAH
//
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