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Database: UniProt
Entry: A0A0G0DRS1_9BACT
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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
//
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