ID A0A239TZW1_9STAP Unreviewed; 876 AA.
AC A0A239TZW1;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=SPI02_07010 {ECO:0000313|EMBL:GEP84116.1};
OS Staphylococcus piscifermentans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=70258 {ECO:0000313|EMBL:GEP84116.1, ECO:0000313|Proteomes:UP000321736};
RN [1] {ECO:0000313|EMBL:GEP84116.1, ECO:0000313|Proteomes:UP000321736}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 109625 {ECO:0000313|EMBL:GEP84116.1,
RC ECO:0000313|Proteomes:UP000321736};
RA Hosoyama A., Uohara A., Ohji S., Ichikawa N.;
RT "Whole genome shotgun sequence of Staphylococcus piscifermentans NBRC
RT 109625.";
RL Submitted (JUL-2019) 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, ECO:0000256|RuleBase:RU004460}.
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:GEP84116.1}.
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DR EMBL; BKAR01000005; GEP84116.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239TZW1; -.
DR OrthoDB; 9806424at2; -.
DR Proteomes; UP000321736; 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; cd06140; DNA_polA_I_Bacillus_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 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}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU004460};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT DOMAIN 2..262
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 287..467
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00474"
FT DOMAIN 633..840
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
SQ SEQUENCE 876 AA; 99837 MW; AF481D8F85D18586 CRC64;
MEKLVLIDGN SLSFRAFYAL PLLTNRAGIH TNAIYGFAML LEKIKKEEKP THFLVAFDAG
KTTFRHQTFS DYKGGRQKTP PELSEQFPLI RQLLDAYQIK HYELENYEAD DIIGTLSKQA
DKAGIKTIIV TGDRDLTQLA SENVTIYYTK KGVTDVDHYT PEFIAEKYNG LQPSQIIDMK
GLMGDTSDNI PGIAGVGEKT AIKLLNQYDS VENLYQHIDE VSGKKLKEKL ENGHDDALMS
KQLATIKRDS PIEVTLKDTK LPEEVDQTAK IDLFKELDFK QMLNQIDVDA EDKTEEKREY
EVEHDFNNIN FNDLSEAAVH FEVDEGDYLT ADILKFGMKA DGHFVVIDAD TIQDYPELVK
WLEDKNTRKL VYDAKKTYAE AHRLNINIQN ITFDIMLASY ILDPSRSIDD VYSVVQHYGQ
NYVAEAVNIY GKGRKRQIPD DEVMNPYIAA ILDAVSESTP LMYDQLEEYN QLELFKSLEL
PLARILGEME ELGIYTDVDE LQEMEKEIQG KLDTLIERIH EAAGEEFNIN SPKQLGVVLF
EKLELPVIKK TKTGYSTAVD VLEQLQGEHP IIDDILEYRQ LSKLQSTYIE GLQKVIQKDH
RIHTHFNQTL AQTGRLSSVD PNLQNIPVRL EEGRRIRKAF KPAEPGNVIL SADYSQIELR
VLAHITQDES MIKAFREGHD IHTATAMKVF GVEPDEVDGL MRRQAKAVNF GIVYGISDYG
LSQSLGISRK AAKQFIDDYL ASFPGVKQYM SDIVKDAKAK GYVETLLHRR RYIPDITSRN
FNRRSFAERT AMNTPIQGSA ADIIKLAMVN FDKEIQNQDF HVHLLLQVHD ELIFELPEAE
VEAFSKFIED IMDNAIDLDV PLQVDTNYGP TWYDAK
//
