ID A0A1I1K0J8_9GAMM Unreviewed; 918 AA.
AC A0A1I1K0J8;
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=SAMN02745724_01937 {ECO:0000313|EMBL:SFC54469.1};
OS Pseudoalteromonas denitrificans DSM 6059.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=1123010 {ECO:0000313|EMBL:SFC54469.1, ECO:0000313|Proteomes:UP000198862};
RN [1] {ECO:0000313|EMBL:SFC54469.1, ECO:0000313|Proteomes:UP000198862}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6059 {ECO:0000313|EMBL:SFC54469.1,
RC ECO:0000313|Proteomes:UP000198862};
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; FOLO01000011; SFC54469.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1K0J8; -.
DR STRING; 1123010.SAMN02745724_01937; -.
DR OrthoDB; 9806424at2; -.
DR Proteomes; UP000198862; 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:UP000198862};
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 320..507
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00474"
FT DOMAIN 676..882
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
SQ SEQUENCE 918 AA; 102473 MW; 6EF15A13EAC5C0B9 CRC64;
MAQIPENPLI LVDGSSYLFR AYHSPPHFVN SKGEPTGAIY GVVNMLKSLV KQFDPSHVAV
IFDAKGKTFR NDMYSDYKAN RPSMPDDLRC QIEPLHKIIK AMGFPLISIG GVEADDVIGT
FARIATENKR DVLISTGDKD MAQLVNEHVT LINTMTDEVL DSDAVVEKFG VAPDRIIDYL
SLMGDKVDNI PGVEGCGPKT AVKWIEKYDT LIGVIDNAKS IKGKIGEKLA AAIPHLPLSY
ELATIKLDVA LDEDLESLKI VDPDKDLLIQ YYAESEFRRW IADLLKNKPT KTKAKKVAKT
ETVESSEETP VEVPNVDADY TTILTEEALD IWIEKLNASE LFAFDTETTS LDYMQADLVG
MSFAVKVGEA AYLPLAHDYL DAPEQLDKEL VFKKLGPILA DENKAKVGQN LKYDKSVLAR
AGYELNGIAF DTMLESYTLN SVSTRHNMDA LALKFLNHTN ISFEEIAGKG KKQLTFNQIS
LEQAAHYAAE DADITLRLHQ EIWPQLDKDP ELKSVFTDIE LPLLSVLSDI ERTGVKIDSQ
MLTAQSQQLG ERLIELEKAA HDLAEEPFNL SSPKQLQAIL FEKMQLPVIK KTPKGAPSTA
EEVLKELALT YSLPKIIMEY RGLSKLKSTY TDKLPQMVNE ESGRVHTSYH QAVTATGRLS
STDPNLQNIP IRTEEGRRIR QAFIADEGHK IMAADYSQIE LRIMAHLSQD KGLLTAFASG
KDVHSATASE VFSVPLDEVT TDMRRKAKAV NFGLIYGMSA FGLANQLDIP RSEAQHYMDT
YFERFPGVLT YMETTREKAT EQGYVETLFG RRLYLPDITK NGPRKKAAER AAINAPMQGT
AADIIKKAML IVHQWVKQQP KDTIKILMQV HDELVFEIKE DCLEAYTTKI CELMSQAAKL
DVPLIADSDF GDNWDQAH
//
