ID A0A1I6CQE6_9RHOB Unreviewed; 932 AA.
AC A0A1I6CQE6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=SAMN04515673_101201 {ECO:0000313|EMBL:SFQ95416.1};
OS Poseidonocella sedimentorum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Poseidonocella.
OX NCBI_TaxID=871652 {ECO:0000313|EMBL:SFQ95416.1, ECO:0000313|Proteomes:UP000199302};
RN [1] {ECO:0000313|EMBL:SFQ95416.1, ECO:0000313|Proteomes:UP000199302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KMM 9023,NRIC 0796,JCM 17311,KCTC 23692
RC {ECO:0000313|Proteomes:UP000199302};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOYI01000001; SFQ95416.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6CQE6; -.
DR STRING; 871652.SAMN04515673_101201; -.
DR Proteomes; UP000199302; 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:UP000199302};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT DOMAIN 4..267
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 324..521
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00474"
FT DOMAIN 689..892
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
SQ SEQUENCE 932 AA; 102589 MW; E3FBD3C1D852E736 CRC64;
MAFGKGCHLH LIDGSAFIFR AYHALPPLTR KSDGLPIGAV AGFCNMIFRY VEANEGPDAP
THVAVIFDKG SHTFRNDLYD QYKANRDAMP EDLRPQMPLT REATRAFNIA CKEIEGYEAD
DIIATLSRQA QAAGGRVTII SSDKDLMQLV GDGVEMLDAM KNRRIDREGV LEKFGVYPER
VVDVQALAGD SVDNVPGAPG IGIKTAAQLI NEYGTLEELL DSAEQIKQPK RRQTLIEKRE
QIELSKRLVQ LDEATPLDFT LDDLEVLEPD PEVLLPFLAE MEFRTLTKRI ADKLGVESPE
IQIAAPAPEE GPSLADLPFD PDSYTCVRSA EDLAPWIAQI HARGWVAVDT ETTGLNEMTA
DLVGISLCIE PGEACYIPLA HKAPGAADDL FTEDAPVEGQ MPMADALALL KPVLEDPAVL
KIGQNMKYDA KIFARQGIEI APIDDTMLMS YAMHAGLHGH GMDALSDKYL GHTPIPIKSL
LGSGKSQITF DRVPLDEAVK YAAEDADITL RLWQMFRPRL HTAQVTRVYE RLERPLVPVL
ARMEMAGIKV DRETLSRMSG AFAQKMAQLE EEIHGLAGRT FNVGSPKQLG EILFDEMGLE
GGKRGKTGAY ATGADVLEDL ATLHELPARV LDWRQLSKLK STYTDALQEH INSETGRVHT
SYSIAGASTG RLASTDPNLQ NIPIRTEEGR RIREAFVAEP GKQLIALDYS QIELRILAHI
AQIDALKEAF REGQDIHAAT ASEMFGVPLD EMTPDVRRQA KAINFGVIYG ISAFGLARNL
RIPREEAKAF IDRYFERFPG IRDYMDATKG FAKEHGHVAT LFGRKIHTPE INARGPRAGF
AQRAAINAPI QGTAADIIRR AMIRMEDAIR DLPATMLLQV HDELLFEVEE GAEDALIAAA
RRVMEEAAEP VIKLDVPLVV DAGTGANWAE AH
//
