ID A0A0G0DRS1_9BACT Unreviewed; 897 AA.
AC A0A0G0DRS1;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 42.
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=UR51_C0011G0037 {ECO:0000313|EMBL:KKP57782.1};
OS Candidatus Moranbacteria bacterium GW2011_GWF1_34_10.
OC Bacteria; Candidatus Moranbacteria.
OX NCBI_TaxID=1618715 {ECO:0000313|EMBL:KKP57782.1, ECO:0000313|Proteomes:UP000034605};
RN [1] {ECO:0000313|EMBL:KKP57782.1, ECO:0000313|Proteomes:UP000034605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKP57782.1}.
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DR EMBL; LBPM01000011; KKP57782.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0DRS1; -.
DR STRING; 1618715.UR51_C0011G0037; -.
DR PATRIC; fig|1618715.3.peg.979; -.
DR Proteomes; UP000034605; 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; 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:SF27; DNA POLYMERASE NU; 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.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA damage {ECO:0000256|RuleBase:RU004460};
KW DNA repair {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 Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU004460};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT DOMAIN 9..274
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 320..478
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00474"
FT DOMAIN 657..862
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
FT COILED 520..547
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 897 AA; 102663 MW; 66A06240AE3017BB CRC64;
MKNNQEKNKK IVLLDGNAII HRSFHALPPF TTKKGELVNA VYGFSSTLLA VIDKFKPEYI
VATFDLKGQT FRAAQFDGYK AKRVKAPDEL YNQIERVKEI VKTFNIPIYE KEGYEADDMI
GTIAKKFSVP GSQFTDNMEV IIVTGDLDTL QLVDERIKVY TMSRGLSKAV LYDKEAVMAR
FGGLEPMQLK DYKGLRGDAS DNIPGVKGIG EKGAINLLKE YQNLEGVYKN INDIKGSLRD
KLEKDKMMAF TSRDLGTIMI NVPFEFKLEE CHTHDFDRKK LIDLFKELGF FSLIKRLQKE
GEEPKDKGEK KIKNGIKDFE YQILENEKVA GFIEEMKTKK EIALSINEKE IAFSSKTGRA
YSLELNAKNL ENLKFILEDK NIKKVGWNLK KDYKFLKERN IELRGIYFDV MLADYLIRSG
EKIELDRLIL AELGEEFNEK GSGQISLMGF SREEEAKKLC EKVDYIWKLK NILAQKIEEM
SESQKTYSKI KNLKNVFENI EMPLVVILAE MEIMGIKINK EIFKEISQKI DSQLENLEKK
IQEMAGKDFN INSTQQLSEV LFIDLKLPTD GIKKNKSGYS TAAPELAKLK GQHKIIEKIE
TYRELFKLKT TYLDNIPLLI GEDGRIHTTF KQEVTSTGRL SSENPNLQNI PIKSEAGKII
RTAFEAERGH VFVSADYSQI DLRVMAHMSD DKKMREAFWA NEDIHTKTAS EVNKVTLSKV
TQKMRREAKA LNFGIIYGMG SFGFSQSADI SRAEAKKFID EYMENFSSVA QFIKTTKQYA
KENEFVETET GRRRYLAEIN SPNFMVQAGA ERMAINMPIQ GLAADIMKLA MIAVYDYFKH
DLEVKMILQI HDEIILEVAE ARAQEVAQKT KEIMEKVYSL SVPLTVDVKI GNNWGEL
//