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Database: UniProt
Entry: A0A0N1LFV4_9SPHN
LinkDB: A0A0N1LFV4_9SPHN
Original site: A0A0N1LFV4_9SPHN 
ID   A0A0N1LFV4_9SPHN        Unreviewed;       934 AA.
AC   A0A0N1LFV4;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, 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=IP68_12170 {ECO:0000313|EMBL:KPF74524.1};
OS   Blastomonas sp. AAP25.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Blastomonas.
OX   NCBI_TaxID=1523416 {ECO:0000313|EMBL:KPF74524.1, ECO:0000313|Proteomes:UP000037930};
RN   [1] {ECO:0000313|EMBL:KPF74524.1, ECO:0000313|Proteomes:UP000037930}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AAP25 {ECO:0000313|EMBL:KPF74524.1,
RC   ECO:0000313|Proteomes:UP000037930};
RA   Zeng Y., Feng F., Liu Y., Koblizek M.;
RT   "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT   Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL   Submitted (AUG-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:KPF74524.1}.
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DR   EMBL; LJHP01000016; KPF74524.1; -; Genomic_DNA.
DR   RefSeq; WP_054135265.1; NZ_LJHP01000016.1.
DR   AlphaFoldDB; A0A0N1LFV4; -.
DR   PATRIC; fig|1523416.3.peg.812; -.
DR   OrthoDB; 9806424at2; -.
DR   Proteomes; UP000037930; 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:UP000037930};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT   DOMAIN          5..264
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00475"
FT   DOMAIN          328..522
FT                   /note="3'-5' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00474"
FT   DOMAIN          691..894
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
SQ   SEQUENCE   934 AA;  101456 MW;  E4325CC28271124D CRC64;
     MSQQNHLYLV DGSSYIFRAY HRLPPLTNPE GTPVGAVYGY TTMLWKLADD LHKADGPTHM
     AVILDKSSQS FRNDLYDQYK AHRPAPPEDL VPQFPLIRDA TRAFSMPCIE EDNVEADDII
     ASYALDALAK GWKVTIVSSD KDLMQLIQPG LDMLDTMKNV RMGPEAVMEK FGVTPEQLGD
     VLALMGDAVD NVPGIRGVGP KTASKLIVEH GDLESVLAAA PAMKPSKLRD SLIEQAEMAR
     LSKVLVTLKD DCPLPNELED FLLKDIPPEP LAEFLKLHGF TSLLRKLGAS GPAEVSPASS
     SPATGAQSSS NAIAPLALAM PPIDTDSYVC VQDFETLDDW IARAFAVGTI AVDTETDSLD
     SMQARLVGIS LALAPGEACY VPLGHGGSDM FAEKPKQIAM DVAIARLKPL LEDDSVLKIG
     QNLKYDLNVL ARHGVAVSPI EDTMVMSFTL DAGHEFGSGG HGMDALAQRH LGHECISFKS
     LTGTGKKQIG FNEVPLSDAT RYAAEDADVT LRLWHVLQPR LPIEGATRIY QMVDRPLIPV
     VAAMERNGIK VDREQLAALS HDFATRMAAL ETEIHALAGQ SFSIGSPKQL GEILFEKMGL
     KGGKKGKTGA YSTDVTVLEK LAGEGSEISR KVLDWRQLAK LKSTYTDALQ EQINPDTGRV
     HTSYSLVGAQ TGRLSSTEPN LQNIPIRTEI GRQIRHAFVA EPGNVILAAD YSQIELRLAA
     HMADVETLRD AFAKGEDIHN RTALELFGEV NRDTRGRAKT INFAILYGIS RWGLAGRLEV
     TADEAQAMID TYFQRFPGIN RYIAETMEKA RECGFTETLF GRKTHFPRIN SKNQAERQGS
     ERAAINAPIQ GTSADIIKRA MARMVPALEA AGLGHVRMLL QVHDELVFEL PEADVDAASQ
     VIRAVMEGAA EPAVTLSVPL GVEIGTGPSW GAAH
//
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