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
//