ID R2RXU1_9ENTE Unreviewed; 879 AA.
AC R2RXU1;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 60.
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=UAS_00871 {ECO:0000313|EMBL:EOH88110.1};
OS Enterococcus asini ATCC 700915.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1158606 {ECO:0000313|EMBL:EOH88110.1, ECO:0000313|Proteomes:UP000013777};
RN [1] {ECO:0000313|EMBL:EOH88110.1, ECO:0000313|Proteomes:UP000013777}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700915 {ECO:0000313|EMBL:EOH88110.1,
RC ECO:0000313|Proteomes:UP000013777};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A.M., Gilmore M.S., Lebreton F., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Enterococcus asini ATCC_700915.";
RL Submitted (FEB-2013) 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:EOH88110.1}.
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DR EMBL; AJAP01000010; EOH88110.1; -; Genomic_DNA.
DR RefSeq; WP_010753520.1; NZ_KB946293.1.
DR AlphaFoldDB; R2RXU1; -.
DR STRING; 57732.RU94_GL001892; -.
DR GeneID; 78365915; -.
DR PATRIC; fig|1158606.3.peg.829; -.
DR eggNOG; COG0258; Bacteria.
DR eggNOG; COG0749; Bacteria.
DR HOGENOM; CLU_004675_0_0_9; -.
DR OrthoDB; 9806424at2; -.
DR Proteomes; UP000013777; 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 Reference proteome {ECO:0000313|Proteomes:UP000013777};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT DOMAIN 3..266
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 302..469
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00474"
FT DOMAIN 635..843
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
SQ SEQUENCE 879 AA; 100423 MW; 3FF994F70247D9B5 CRC64;
MKKKLLLIDG NSVAFRAFFA LHNSLERFKN ANGLHTNAIY AFHNMFDNVM KLEEPTHVLV
AFDAGKTTFR TELYEEYKGG RAKTPSEFRE QLPFIRELIH NLGVKTYELP NYEADDIIGT
LATEAKDQYE VVILSGDRDL LQLVSDDVTV DITVKGVSEI EVYTPEKVAE RYDGLTPAQV
VDLKGLAGDT SDNIPGVTKV GEKTAIKLLK EYDTVEGVYE HVDEMKKSKL KENLQNDRDI
AFLSKELATI NRKAPVTIKL EDLAYQGKDL ERLIPFYQEM NFKSFLDKLN VTEEVPEMED
ILFEVVREFT PEMFTDDMAL YVEMLGENYH TEAIQGVAWG TSEKIYVTDE LALFENEHFV
NWLAQGKNKK VFDAKRTYVA LNRYCEKKLA GVHFDVLLAA YLLDTNDNSN DIAGVARQYD
YQEIQSDEAI YGKGAKKGLP EDEETFFAHL ARKIKGIHWL SQRLDEDLAA KDQSKLFYDM
ELPLSFILGD MEIAGITVDP TRLHQMKGDF SKRLQEIEKK IYAEAGEEFN INSPKQLGVI
LFEKMGLPVI KKTKTGYSTA VDVLEQLREQ APIVDDILNY RQIAKIQSTY VEGLLRVIAN
DGKVHTRYVQ TLTQTGRLSS VDPNLQNIPI RLEEGRQIRA AFVPRHKDWL IYSSDYSQIE
LRVLAHISQD EHLRAAFIEG QDIHASTAMR VFGIEKAEDV TPNMRRQAKA VNFGIVYGIS
DYGLSQNLGI TRKAAQQYID TYFEKYPGVK NYMEEIVREA KEQGFVETLY HRRRYLPEIN
SRNFNLRSFA ERTAINTPIQ GSAADILKIA MIELNQRMKE EGLEAVMLLQ VHDELVFEVP
ESELETLDKL VKEVMEHAVS LEVPLITDSS WGATWYEAK
//
