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Database: UniProt
Entry: A0A1Z5I9V0_9LACO
LinkDB: A0A1Z5I9V0_9LACO
Original site: A0A1Z5I9V0_9LACO 
ID   A0A1Z5I9V0_9LACO        Unreviewed;       886 AA.
AC   A0A1Z5I9V0;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   24-JAN-2024, entry version 31.
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   ECO:0000313|EMBL:GAW98391.1};
GN   ORFNames=IWT30_00336 {ECO:0000313|EMBL:GAW98391.1};
OS   Secundilactobacillus mixtipabuli.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Secundilactobacillus.
OX   NCBI_TaxID=1435342 {ECO:0000313|EMBL:GAW98391.1, ECO:0000313|Proteomes:UP000198374};
RN   [1] {ECO:0000313|EMBL:GAW98391.1, ECO:0000313|Proteomes:UP000198374}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IWT30 {ECO:0000313|EMBL:GAW98391.1,
RC   ECO:0000313|Proteomes:UP000198374};
RA   Tohno M., Tanizawa Y., Arita M.;
RT   "Draft genome sequences of new species of the genus Lactobacillus isolated
RT   from orchardgrass silage.";
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, ECO:0000256|RuleBase:RU004460}.
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:GAW98391.1}.
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DR   EMBL; BCMF01000002; GAW98391.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Z5I9V0; -.
DR   OrthoDB; 9806424at2; -.
DR   Proteomes; UP000198374; 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; cd06140; DNA_polA_I_Bacillus_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   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   Reference proteome {ECO:0000313|Proteomes:UP000198374};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT   DOMAIN          5..268
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00475"
FT   DOMAIN          307..477
FT                   /note="3'-5' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00474"
FT   DOMAIN          644..850
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
SQ   SEQUENCE   886 AA;  100310 MW;  3B2A648E5EC33771 CRC64;
     MTESKRLLLI DGNSVAFRAF FALYTALNSM TNADGLHTNA IFGFNRMLDI MLEDVKPTEA
     LVAFDAGKVT FRTKKYADYK GGRAKTPPEL SEQMPVIRQL LEARGIKSYE LKNYEADDII
     GTMAKQAEAA GYETTIFTGD RDLTQLTSDK TSVAVSKKGV TEVETYTPEH VEEKLGVRPD
     QIIEIKGLQG DNSDNYPGVT GVGPKTAVSL IQKYGTIDGV YENIDKITAK KMKEHLIEDK
     DSAFQSRDLA TIRRDAPIEI KLSDLTYKGD QQDELVKFYQ EMNFQSYLNK MNTDAGDEDV
     LGLKPVKFTV LTTDNLNEVT QFKNHVSFYL EMPEANYHTS TFAGFVIGED DQWFVSRDVD
     LLKQEPLKGL LTSDQIQKDV FDVKRTYVGL NRLGIHLTNV DFDLLLASYL LDTNENSNDL
     GRLAFQHGYH QIQSDEEVYG KGAKRAIPDD DQLFFEHLTR KGITIESLKA SLFKKLDENE
     QTKLYRDLEL PMAYVLAHME IAGITVDTDR LSAMQSEFTE LLAQTQQTIF QEAGEEFNIG
     SPKQLQHILF EKLGLTPIKK TKTGYSTSVD VLEKLAAEAP IVENILKYRQ ISKIQSTYVE
     GLLKVVHSSD QKVHTRYLQT LTQTGRLSSV DPNLQNIPIR TEEGRRIRQA FIPSHKGWQI
     FSSDYSQIEL RVLAHITHDK NLQEAFREGE DIHASTARRI FRLGPDAEVD PNMRRQAKAV
     NFGIVYGISD FGLSQNIGIT RKQARQFIDT YFEEYPGVKQ YMTDIVASAK DKGYVETIAH
     RRRYLPDINA RNFNQRSFAE RTAMNTPIQG SAADIIKIAM IKMEDAIKDL KATMLLQVHD
     ELIFEAPAEE IPTLEKLVPS VMDSAVKLEI PLKVESHYGN TWYEAK
//
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