ID A0A1G5QRQ9_9GAMM Unreviewed; 897 AA.
AC A0A1G5QRQ9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=SAMN03097708_02656 {ECO:0000313|EMBL:SCZ64564.1};
OS Thiohalomonas denitrificans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiohalomonadales;
OC Thiohalomonadaceae; Thiohalomonas.
OX NCBI_TaxID=415747 {ECO:0000313|EMBL:SCZ64564.1, ECO:0000313|Proteomes:UP000199648};
RN [1] {ECO:0000313|EMBL:SCZ64564.1, ECO:0000313|Proteomes:UP000199648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLD2 {ECO:0000313|EMBL:SCZ64564.1,
RC ECO:0000313|Proteomes:UP000199648};
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; FMWD01000008; SCZ64564.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G5QRQ9; -.
DR STRING; 415747.SAMN03097708_02656; -.
DR OrthoDB; 9806424at2; -.
DR Proteomes; UP000199648; 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:UP000199648};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT DOMAIN 7..261
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 300..487
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00474"
FT DOMAIN 655..861
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
SQ SEQUENCE 897 AA; 99109 MW; 1DB1C915C6FDB0A8 CRC64;
MTERSNKPLV LVDGSSYLYR AFHALPALTN SRGEPTGAVY GVANMLRRLL KDYDPEYMAV
VFDAKGKTFR DELYDQYKAH RPPMPDELRG QVQVLHELVR AMGLPLLIID GVEADDVIGT
LARQAEAVDM EVVVSTGDKD MAQLVSKRVT LVNTMTGTVT DADHVEEKFG VPVENIVDWL
ALVGDVVDNV PGVPKCGPKT AVKWLQQYGS LDGVMEHAGA IKGKVGENLR ASFDQLPLSR
ELVTIRCDVP LDQGPFDLRR GEPDREALRE IYTRLEFRAW LSELLDGTEP EEQVPEGTEY
ELVLDEAGLD AWIKRLEGAD LFAFDTETTN LDYMLAEVVG VSLAVEPGHA AYIPVGHDYP
GAPDQLDKET VFQRLAPLLL DPNRVKLAQN LKYDMSVLAA AGIHLEGPVH DTMLESYVLN
STAARHDMDS LSLKYLGRKT VTYEEVAGKG AKQLGFNEVD LEQAAPYAAE DADVTLQLHR
KLWPQLEAIP SLAKLYTGIE LPLVAVLSRL ERNGVLVDVG KLRRQSTELA KRMGEIELLA
HQEAGGPFNL GSPKQLQVIL FEQKGLPVVK KTPKGQPSTA EEVLQELALD YELPRLILEY
RSLSKLKSTY TDKLPGQVSH DGRVHTSYHQ AVAATGRLSS SDPNLQNIPI RTPEGRRIRQ
AFVASDGYKL LAADYSQIEL RIMAHLSQDE GLLGAFAEGQ DIHTATAAEV FGMPLEEVTV
AQRRSAKAIN FGLIYGMSAF GLARQLGIDR AAAQTYVDLY FRRYPGVKAY MDASRRKAKD
DGFVETVFGR RLYIPDIKAS NAQRRQYAER TAINAPMQGT AADIIKRAMI AVDGWLLKGS
VDARMIMQVH DELVFEVAEE DLDIVRTTVI RCMSGAADLS VPLEVEAGVG DNWDEAH
//
