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Database: UniProt
Entry: A0A0Q4SA42_9BURK
LinkDB: A0A0Q4SA42_9BURK
Original site: A0A0Q4SA42_9BURK 
ID   A0A0Q4SA42_9BURK        Unreviewed;       940 AA.
AC   A0A0Q4SA42;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 45.
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=ASF16_02175 {ECO:0000313|EMBL:KQO27888.1};
OS   Acidovorax sp. Leaf78.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=1736237 {ECO:0000313|EMBL:KQO27888.1, ECO:0000313|Proteomes:UP000051234};
RN   [1] {ECO:0000313|Proteomes:UP000051234}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf78 {ECO:0000313|Proteomes:UP000051234};
RA   Garrido-Oter R., Mueller D.B.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000051234}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf78 {ECO:0000313|Proteomes:UP000051234};
RA   Vorholt J.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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}.
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:KQO27888.1}.
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DR   EMBL; LMLZ01000001; KQO27888.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q4SA42; -.
DR   STRING; 1736237.ASF16_02175; -.
DR   Proteomes; UP000051234; 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: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.
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|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          11..270
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00475"
FT   DOMAIN          344..530
FT                   /note="3'-5' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00474"
FT   DOMAIN          698..904
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
SQ   SEQUENCE   940 AA;  102214 MW;  0C89D6826E6B01F8 CRC64;
     MTSAAQPSGG KKTLVLVDGS SYLYRAFHAM PDLRAVPGDP ESPATGAIRG MINMLQVLRR
     EFPSGYAACV FDASGPTFRD DLYPEYKAQR SPMPDDLRAQ IEPIHEVVRL LGWPVVCVPG
     VEADDVIGTL AAVAAAQGVE VIVSSGDKDL SQLVNEHITI IDTMNGKKRD VAGVTAEFGV
     PPSLMVDYQT LVGDTVDNVP GVPKVGPKTA AKWLGEYGSL DALIARAGEI KGVAGENLRG
     ALQWLPTGRQ LVTIKTDCDL AGHVDGLPAM DAIAMRQEDA APLRDFYQKY GFKGLARALE
     SNAPADAKAN SKSKVTLPGA SGDLFESPEA TFVAEAAQGR EVSYETILTW ADFDRWLAKL
     QTAELAAIDT ETTSLDELRA EIVGISFSVE PGAAAYIPLR HAGPDAPEQL PFDEVLAKLK
     PWLEDASRPK LGQHIKYDRH VFANHGINVQ GYAHDTMLQS YVLEVHKPHG LASLAERHTG
     RSGISYEDLC GKGAHQIPFA QVAVDKAAAY SCEDSDQTLD VHRVLWPMLE AEGPLRGIYE
     LEMASSETLF RIERNGVLID AATLANQSHE LGQRILKLEQ DAYEIAGQPF NLGSPKQLGE
     IFFDKLGMPV VKKTATGARS TDEEVLEKLA EDYPLPAKLL EHRSLSKLKG TYTDKLAQLA
     NPRTGRVHTH YAQAVAITGR LSSNDPNLQN IPIRTVEGRR VREAFVAPAG SVIASADYSQ
     IELRIMAHIS GDESLLHAFR NGLDVHRATA AEVFGVEVDQ VSSEQRRYAK VINFGLIYGM
     SSFGLAKNLG IETKAAAAYI DRYFQRYPGV KQYMDETKAS AKARGYVETV FGRRLYLPEI
     NSPNGPRRSG AERAAINAPM QGTAADLIKK AMVAVQQELD ANKPGIKMIM QVHDELVFEL
     PEGEVEWVGT HIPRLMAEVA DLKVPLLAEV GVGPNWDKAH
//
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