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Database: UniProt
Entry: A0A0A3B7J9_9PAST
LinkDB: A0A0A3B7J9_9PAST
Original site: A0A0A3B7J9_9PAST 
ID   A0A0A3B7J9_9PAST        Unreviewed;       934 AA.
AC   A0A0A3B7J9;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 46.
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=OA57_10805 {ECO:0000313|EMBL:KGQ69574.1};
OS   Chelonobacter oris.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Chelonobacter.
OX   NCBI_TaxID=505317 {ECO:0000313|EMBL:KGQ69574.1, ECO:0000313|Proteomes:UP000030380};
RN   [1] {ECO:0000313|EMBL:KGQ69574.1, ECO:0000313|Proteomes:UP000030380}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1662 {ECO:0000313|EMBL:KGQ69574.1,
RC   ECO:0000313|Proteomes:UP000030380};
RA   Kudirkiene E., Hansen M.J., Bojesen A.M.;
RT   "Draft genome sequence of Chelonobacter oris 1662T, associated with
RT   respiratory disease in Hermann's Tortoises.";
RL   Submitted (NOV-2014) 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:KGQ69574.1}.
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DR   EMBL; JSUM01000016; KGQ69574.1; -; Genomic_DNA.
DR   RefSeq; WP_034617658.1; NZ_JSUM01000016.1.
DR   AlphaFoldDB; A0A0A3B7J9; -.
DR   STRING; 505317.OA57_10805; -.
DR   OrthoDB; 9806424at2; -.
DR   Proteomes; UP000030380; 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   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:UP000030380};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT   DOMAIN          8..269
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00475"
FT   DOMAIN          338..524
FT                   /note="3'-5' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00474"
FT   DOMAIN          693..898
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
SQ   SEQUENCE   934 AA;  103535 MW;  5D9FB2C6D3625523 CRC64;
     MTAKIAENSL ILVDGSSYLY RAFHAFPPLT NSLGEPTGAM YGVLNMLKSL ISQANPRYLA
     VVFDAKGKTF RDELFEQYKS HRPPMPEDLR KQILPLHSII NALGIPLLVI DGVEADDVIG
     TLAVNASKCG QKVLISTGDK DMAQLVDDNI TLINTMNNTL LDRDGVIEKY GIPPELMIDY
     LALRGDSSDN IPGVAGVGEK TALGLLQGIG SMAQIYANLD KVAELPIRGA KKLGDKLAEA
     KEMADLSYLL ATIKTDVELP LNYDQLTLQA AQNDELIEAF GRYEFKRWLN DILQNGSSSV
     TAAELPTRSF NAYQATADSG QSAVADVLES VQVDRTLYQT ILTDAELAHW LGKLSTAELI
     AVDTETDSLN YMQANLVGIS FALQNGEAAY LPLQHRYLDA PEQLDLSAAL AKLKPILENP
     QIKKIGQNIK YDETIFFRHG IELQGVAYDT MLESYILDST GRHNMDDLAK RYLGHNTITF
     EELAGKGKNQ LTFDQIPIEQ AAEYAAEDAD ITMKLHQTLW KKVQTEPTLG ELFEKLEMPL
     VSVLSRIERN GVLLDSDLLF QQSSEIANRL IQLEQQAHEL AGEPFNLAST KQLQEILFGK
     LGLPVIKKTP KGAPSTNEEV LEELAYEHDL PKILVEHRGL SKLKSTYTDK LPLMVDKDSG
     RVHTSYHQAV TITGRLSSSD PNLQNIPIRT EEGRRIRKAF VAAKGNKIIA ADYSQIELRI
     MAHLSNDSGL GKAFAEGKDI HRATAAEIFG VSLDDVTSEQ RRSAKAINFG LIYGMSAFGL
     ARQLGIARGQ AQQYIDLYFQ RYPGVQTFMS DIQQKAREQG YVETLFKRRL YLPEIKSTNA
     MRRKGAERVA INAPMQGTAA DIIKRAMLAI DDEILNSDEI KMIMQVHDEL VFEVRSDKVE
     HYAARIKTLM EQAAELAVPL IAEVGVGENW DEAH
//
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