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Database: UniProt
Entry: A0A369Q7T3_9SPHN
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ID   A0A369Q7T3_9SPHN        Unreviewed;       946 AA.
AC   A0A369Q7T3;
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=dpo1 {ECO:0000313|EMBL:RDC60943.1};
GN   Synonyms=polA {ECO:0000256|RuleBase:RU004460};
GN   ORFNames=HME9302_02160 {ECO:0000313|EMBL:RDC60943.1};
OS   Alteripontixanthobacter maritimus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Alteripontixanthobacter.
OX   NCBI_TaxID=2161824 {ECO:0000313|EMBL:RDC60943.1, ECO:0000313|Proteomes:UP000253727};
RN   [1] {ECO:0000313|EMBL:RDC60943.1, ECO:0000313|Proteomes:UP000253727}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HME9302 {ECO:0000313|EMBL:RDC60943.1,
RC   ECO:0000313|Proteomes:UP000253727};
RA   Kang H., Kim H., Joh K.;
RT   "Altererythrobacter sp. HME9302 genome sequencing and assembly.";
RL   Submitted (APR-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}.
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:RDC60943.1}.
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DR   EMBL; QBKA01000002; RDC60943.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A369Q7T3; -.
DR   OrthoDB; 9806424at2; -.
DR   Proteomes; UP000253727; 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:UP000253727};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT   DOMAIN          5..270
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00475"
FT   DOMAIN          338..534
FT                   /note="3'-5' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00474"
FT   DOMAIN          703..906
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
FT   REGION          293..331
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   946 AA;  103220 MW;  83E7975FC87CD013 CRC64;
     MAETQHLYLV DGSAYIFRAY HRLPPLTDPE GTPVGAVYGY TTMLWKLADD LDAADGPTHM
     AVILDKDSTS FRNDIYPEYK ANRPEPPEDL RPQFPLIRDA TRAFSLPCIE EGGLEADDLI
     ASYARAAQRE GWNVTIVSSD KDLMQVVGTD TKSGGTIDML DTMKNARIGP AEVEEKFGVP
     PHLVGDVLAL MGDSVDNIPG IYGVGPKTAS KLIAEHGDLT AALDSAPDMK KSKLKERLLE
     GREDAEMSRV LVTLKEDADL PMPIADMKLD GVPPEPLAEF LKKHGFSSLL RRLDAGRGSP
     DRPNQLNPTK AERKGADAAS EGDRQPLPDM PAIDRNAYEC VQTMERLNHW IERAFALREV
     AVDTETSALD AISADLVGVS LALGPNEACY IPLAHGGTDL LSEKPQQIDP AAALAALKPL
     LESDAVVKIG QNIKYDLNIL ARNGIAVAPI EDTMILSFAL DAGRSLDGIG GGHGMDELAQ
     RHLGHTCMTF KEVCGTGKKQ IGFGEVALDV ATKYAAEDAD VTWRLYKHLK PRLPIEGGTR
     VYERVDRPLI PVVAGMERHG IQVDRANLAK LSEEFAKEMA RLESAIHETA GQEFAIGSPK
     QLGEILFDTM GYKGGRKGKS GQYSTDQTTL EKLEAQGAPI ARQVLEWRQL SKLKSTYTDA
     LQAAINPRTG RVHTSYSLVG AQTGRLSSTD PNLQNIPIRT EIGRQIRDAF VADDGNVLLA
     ADYSQIELRL AAHMADVGPL KEAFAEGEDI HARTAREMFG EVTRDTRAQA KTINFAILYG
     ISRWGLAGRL GVEADEAQEM IDTYFKRFPG IQRYILETTE SVKQRGYSET LFGRKTWFPR
     INSKNPSERQ GSERAAINAP IQGTSADIIK RAMARMNPAL AAAGLPDVRM LLQVHDELVF
     ELPESDVEDA SPIIERIMAD AARPSVELSV PLGIEIGTGK SWGAAH
//
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