ID A0A0Q4KFA4_9SPHN Unreviewed; 924 AA.
AC A0A0Q4KFA4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-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=ASE86_02630 {ECO:0000313|EMBL:KQN25172.1};
OS Sphingomonas sp. Leaf33.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736215 {ECO:0000313|EMBL:KQN25172.1, ECO:0000313|Proteomes:UP000051455};
RN [1] {ECO:0000313|EMBL:KQN25172.1, ECO:0000313|Proteomes:UP000051455}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf33 {ECO:0000313|EMBL:KQN25172.1,
RC ECO:0000313|Proteomes:UP000051455};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQN25172.1, ECO:0000313|Proteomes:UP000051455}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf33 {ECO:0000313|EMBL:KQN25172.1,
RC ECO:0000313|Proteomes:UP000051455};
RA Schulze-Lefert P.;
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:KQN25172.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LMLB01000001; KQN25172.1; -; Genomic_DNA.
DR RefSeq; WP_056421997.1; NZ_LMLB01000001.1.
DR AlphaFoldDB; A0A0Q4KFA4; -.
DR STRING; 1736215.ASE86_02630; -.
DR OrthoDB; 9806424at2; -.
DR Proteomes; UP000051455; 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:UP000051455};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT DOMAIN 1..262
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 318..508
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00474"
FT DOMAIN 681..884
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
SQ SEQUENCE 924 AA; 100555 MW; 71C0D9449D72CF11 CRC64;
MPHLYLVDGS GYIFRAYHRL PPLTNKHGEP VGAVYGYTTM LWRLADDLHK ADGPTHMAVV
LDKSSVSFRN ELYDKYKAHR PPPPEDLIPQ FPMIRDATRA FSLPCIDEAG WEADDLIASY
AKAALAQGWQ VTIVSSDKDL MQLVEDGSLD MLDTMNNRRI GSAEVFEKFG VPPGKVGEVL
ALMGDSVDNV PGVPGVGPKT AAKLIQEHGD VEAVLAAAET MKKGKLRDNL IEFAESARIS
RKLVELACDV PLPDALEDLE LKGIPDAPLR AFLEHHGFKS LLAKLGTGAS AADAPVETPA
APGMPEVDAD PPCDHDAYET VVDPERLDHW VQIARHQGFV AIDTETTGLD ATRAELVGVS
LALAPNLACY VPIGHGGSDM FAERPPQIDR AVVIKKLKPL LEDPSVLKIG HNLKYDMIVL
GRLGLTVAPY DDTIVMSFDL DAGLHGHGMD ELAATHLSHS CIAYKDVTGT GKKAIGFHEV
DLKAATRYAA EDADVTLRLW RRLKPRLAFE GSTQVYEMVD RPLPAVVATM EMHGIKVDAD
HLARLSADFS TQIAAREEEI HAIAGFKFAI GSPKQLGDVL FDKMGIKGGR KGKSGVYSTD
VNELERIAAD KDSPGREMVV KVLDWRQLSK LKSTYTDALQ AQINPATGRV HTSYSLTGAQ
TGRLSSTDPN LQNIPIRTET GRQIRDAFVA EPGNLILSAD YSQIELRLAA HIADVPQLRE
AFERGDDIHS MTAQELFGTV DRDTRGRAKT INFAILYGIS RWGLAGRLDV TPDEAQAMIS
RYFERFPGIN RYIADTLTEA KARGYTSTLF GRKTHFPRIK ASNPNERAGS ERAAINAPIQ
GTSADIIKRA MTRMGPALAD AGLGHVRMLL QVHDELVFEL PKGDVAAATE VIRRVMETAA
EPAVKLTVPL GVEIGTGPSW GAAH
//