ID A0A1G2BKQ2_9BACT Unreviewed; 789 AA.
AC A0A1G2BKQ2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
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};
DE Flags: Fragment;
GN Name=polA {ECO:0000256|RuleBase:RU004460};
GN ORFNames=A2927_02900 {ECO:0000313|EMBL:OGY89246.1};
OS Candidatus Komeilibacteria bacterium RIFCSPLOWO2_01_FULL_45_10.
OC Bacteria; Candidatus Komeilibacteria.
OX NCBI_TaxID=1798550 {ECO:0000313|EMBL:OGY89246.1, ECO:0000313|Proteomes:UP000178849};
RN [1] {ECO:0000313|EMBL:OGY89246.1, ECO:0000313|Proteomes:UP000178849}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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 -!- 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:OGY89246.1}.
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DR EMBL; MHKL01000023; OGY89246.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2BKQ2; -.
DR STRING; 1798550.A2927_02900; -.
DR Proteomes; UP000178849; 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 Gene3D; 3.30.70.370; -; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 2.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR InterPro; IPR002562; 3'-5'_exonuclease_dom.
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; 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; 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; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS00447; DNA_POLYMERASE_A; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|RuleBase:RU004460};
KW DNA repair {ECO:0000256|RuleBase:RU004460};
KW DNA replication {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 1..134
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 201..379
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00474"
FT DOMAIN 547..753
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
FT REGION 161..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OGY89246.1"
SQ SEQUENCE 789 AA; 89502 MW; 874D58C326B2819F CRC64;
IVTGDLDTLQ LVDANTEIFT LKKGISETIT YDERAVKERY GLEPEQLIDF KALRGDPSDN
IPGVKGIGEK TAAELIKEFG SLEELYKNLD SKKIKDRVRE LLQNQEKDAF LSKKLVTIQT
DLPTNFKLAE TGLTGFNQKK IVELFRKLEF KSLLNKIPSE LNGQQPVSGE PGSPLPKTDS
GQSQMGFLKI KNEQLKTKFK YALINDKKSF AEFLHLLKKQ EEFAIDSETT SLNVWQARLL
GLSFSWTPDE AFYLNINDHP EWLDELKPIL ENPQIKKIGH HLKYDYEMLM QNNINLAGIE
FDTLLAAYLL TSANRNLDLD SLVFSYLGYQ MQPIEELIGP KGKKQISMAE VPLEKVSWYA
GEDADFSLKL YQKLRPELEK ISDLGLLKKV ELPLIPVLAK MEQAGIKIDT AFLKKLDQKF
TKKIKVLEEK IYQLSGRHFN IASPLQLKEV LFEKMGIAIK GLKRTKTGIS TAAGELEKLW
NAHPIIPLIS EFREYSKLQN TYTRALPKEA DKSGRIHTSF NQTITATGRL SSSEPNLQNI
PIRTEIGKEI RRGFIAERGY RLISADYSQI ELRIIASLAE DKKMIEYFKN GEDIHARTAA
NINKIELKDV TRQQRTAAKE VNFGVIYGLG HVGLSQRTGI SREEAKKFIE AYFELYPQIK
KWLAETKEQA SKRGYVETLL GRRRYLPDIN SGVQLIKAGA ERMAVNAPIQ GTAADLLKMA
MVKIDGELPK ISPQSKMLLT VHDELVFEAP EKDVAKVSDF VKKTMENIYK LKVPIEAEVK
AARNWGECK
//
