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Database: UniProt
Entry: A0A1G6SH69_9BURK
LinkDB: A0A1G6SH69_9BURK
Original site: A0A1G6SH69_9BURK 
ID   A0A1G6SH69_9BURK        Unreviewed;       930 AA.
AC   A0A1G6SH69;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
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=SAMN05444679_10876 {ECO:0000313|EMBL:SDD16290.1};
OS   Variovorax sp. CF079.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=1882774 {ECO:0000313|EMBL:SDD16290.1, ECO:0000313|Proteomes:UP000198763};
RN   [1] {ECO:0000313|EMBL:SDD16290.1, ECO:0000313|Proteomes:UP000198763}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF079 {ECO:0000313|EMBL:SDD16290.1,
RC   ECO:0000313|Proteomes:UP000198763};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-A family.
CC       {ECO:0000256|ARBA:ARBA00007705, ECO:0000256|RuleBase:RU004460}.
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DR   EMBL; FMZU01000008; SDD16290.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G6SH69; -.
DR   STRING; 1882774.SAMN05444679_10876; -.
DR   OrthoDB; 9806424at2; -.
DR   Proteomes; UP000198763; 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   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   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.
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};
KW   Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022839};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU004460};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198763};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT   DOMAIN          4..269
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00475"
FT   DOMAIN          334..520
FT                   /note="3'-5' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00474"
FT   DOMAIN          688..894
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
SQ   SEQUENCE   930 AA;  102260 MW;  15C691BAD8428D9A CRC64;
     MTDKKTLLLV DGSSYLYRAF HAMPDLRAVP GDAGSPATGA IRGMINMMQA LRREVRADYA
     ACVFDAPGKT FRDDWYPQYK ANRSPMPDDL RSQVEPIHQV VKLLGWPVLC VPDIEADDVI
     GTLARTAANQ GIEVIVSSGD KDLSQLVDEH VTIIDTMNGK KRDVAGVTAE FGVPPTLMID
     YQTLVGDSVD NVPGVEKVGP KTAAKWLLEY GSLDALIARA GEVKGQAGEN LRKALDWLPQ
     GKRLVTIRTD CELDGHVSGL PSLAGIAIGP QQIDELKGFY EKYGFKSLVK TLEAHEVSPE
     LIEENKKKKG PEGGTGLFDE PGFEAAAKAT NLAYDTVMNW EAFDAWLAKL QAAELVAIDT
     ETNSLDEMRA EIVGISFSVK PGEAAYIPVA HNYPDAPAQL PRDEVLAKLK PWLEDGTKKK
     LGQHIKYDRH VFANHGIEVQ GYAHDTMLQS YVLEVHKPHG LASLAERHLG RTGIDYEDLC
     GKGAHQIPFS QVSIEKAAEY SCEDSDQTLD VHLALWPKLE ADEKLRYIYE LEMASSEALY
     RVERNGVLID APTLAAQSNE LGKRIMALEQ EAYELAGQPF NLGSPKQIGE VFFTKLGLPV
     VKKTPSGAPS TDEEVLEKLA EDFPLPAKIL EHRGLSKLKG TYTDKLGQLA NPRSGRVHTH
     YAQAVAVTGR LSSNDPNLQN IPIRTAEGRR VREAFVAPAG SVIASSDYSQ IELRIMAHIS
     GDESLLRAFT EGIDVHRATA AEVFGVAVEQ VSSEQRRYAK VINFGLIYGM SSFGLARNLG
     IETKAAASYI DRYFARYPGV KIYMDETKAL AKQKGYVETV FGRRLYLPEI NSPNGPRRGG
     AERAAINAPM QGTAADLIKL SMVKVQEVLD AEKRRTKMIM QVHDELVFEV PEDEVEWVRT
     EIPRLMAGVA ELKVPLLAEI GFGPNWDKAH
//
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