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Entry: A0A1Q4UPB1_9PROT
LinkDB: A0A1Q4UPB1_9PROT
Original site: A0A1Q4UPB1_9PROT 
ID   A0A1Q4UPB1_9PROT        Unreviewed;       940 AA.
AC   A0A1Q4UPB1;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 34.
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=LF95_11560 {ECO:0000313|EMBL:OKH87441.1};
OS   Thalassospira sp. TSL5-1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Thalassospiraceae; Thalassospira.
OX   NCBI_TaxID=1544451 {ECO:0000313|EMBL:OKH87441.1, ECO:0000313|Proteomes:UP000186302};
RN   [1] {ECO:0000313|EMBL:OKH87441.1, ECO:0000313|Proteomes:UP000186302}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TSL5-1 {ECO:0000313|EMBL:OKH87441.1,
RC   ECO:0000313|Proteomes:UP000186302};
RA   Zhou H., Wang H.;
RT   "Genome sequencing of Thalassospira sp. TSL5-1.";
RL   Submitted (SEP-2014) 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:OKH87441.1}.
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DR   EMBL; JRJD01000003; OKH87441.1; -; Genomic_DNA.
DR   RefSeq; WP_073955165.1; NZ_KV880638.1.
DR   AlphaFoldDB; A0A1Q4UPB1; -.
DR   STRING; 1544451.LF95_11560; -.
DR   OrthoDB; 9806424at2; -.
DR   Proteomes; UP000186302; 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   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT   DOMAIN          9..264
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00475"
FT   DOMAIN          317..529
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;  103141 MW;  31427865E6FAE68D CRC64;
     MTDTAQPPRR VVLVDGSGFI FRAFHALPPM NSPDGTPVNA VYGFCTMLMK LREDTKPDHM
     AVIFDTKGKS FRNDFYPDYK AHRPPPPEEL VPQFGLIRDA VRAFNLPSIE LEGYEADDLI
     ATYARQAAEQ GADVIIVSSD KDLMQLVTER VEMFDAMKNR TIRSGEVMEK FGVGPDKVID
     VQALAGDPVD NVPGVPGIGV KTAAQLITEY GDLDSLLERA GEIKQPKRRE KLIENADMAR
     ISRDLVRLKT DVPVTHPVDD FDLREPDADV LLSFIATHGF KSLTAKVKAK FGGTVDENGV
     AEAGTGVNDV TVTKAEYELV QDEESLKKWI AKADYEGILA VDTETTSLNA HQARLVGISI
     AVQPGEACYI PLTHGMGDEA TEPKAAQGGF DFGSDPADDK AKAEIPQQIP LKRAIELLKP
     LLEDRGVLKI GQNIKYDKII FARHGIDVAP IDDTMVLSYV LDGTSHGHGM DELADLHLGY
     KTIKFTDVAG TGKNQLTFDQ VPLDKALDYA AEDADITLRL HRLLKPRIAQ EHMASVYETL
     DRPLVPVLAK MEALGVKVDA DKLRELSSDF ASRMEVLEKT IHEMAGETFN LGSPKQLGEI
     LFERMSLPGG KKTKTGAWQT GADVLEGLAA QGHDLPARIL DWRQLSKLKS TYTDALANHI
     NPQTGRVHTS YGQTNVNTGR LSSNDPNLQN IPIRSEEGRK IRTAFIADEG CKLISADYSQ
     IELRLLAHVA EIDALRTAFK NGEDIHASTA SKVFGVPIEG MDPMVRRKAK AINFGIIYGI
     SAFGLANQLG IPQKEAKEFI NAYFEIYPGI RDYMERAKDF AKTHGMVRTL FGRKIFINGI
     NDKNGMRRSF GERAAINAPI QGGAADIIKR AMIAVPDALL DAGLKTRMLL QVHDELIFEA
     PEAETEQAVK VIRDVMENAA HLSVPLIADA GIGDSWADAH
//
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