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Database: UniProt
Entry: A0A1Z5IHK4_9LACO
LinkDB: A0A1Z5IHK4_9LACO
Original site: A0A1Z5IHK4_9LACO 
ID   A0A1Z5IHK4_9LACO        Unreviewed;       886 AA.
AC   A0A1Z5IHK4;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 33.
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:GAX01233.1};
GN   ORFNames=IWT126_01259 {ECO:0000313|EMBL:GAX01233.1};
OS   Secundilactobacillus silagei JCM 19001.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Secundilactobacillus.
OX   NCBI_TaxID=1302250 {ECO:0000313|EMBL:GAX01233.1, ECO:0000313|Proteomes:UP000198402};
RN   [1] {ECO:0000313|EMBL:GAX01233.1, ECO:0000313|Proteomes:UP000198402}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IWT126 {ECO:0000313|EMBL:GAX01233.1,
RC   ECO:0000313|Proteomes:UP000198402};
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:GAX01233.1}.
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DR   EMBL; BCMG01000005; GAX01233.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Z5IHK4; -.
DR   STRING; 1302250.GCA_001313225_01705; -.
DR   OrthoDB; 9806424at2; -.
DR   Proteomes; UP000198402; 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: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   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}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU004460};
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          303..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;  100247 MW;  AC8BC63E56A400BB CRC64;
     MTESKRLLLI DGNSVAFRAF FALYTSLNSF TNADGLHTNA IFGFNRMLDI MLEQVKPTEA
     LVAFDAGKVT FRTKKYADYK GGRSKTPPEL LEQMPVIRQL LTARGIKSYE LKNYEADDII
     GTMAKQAEEA GYETTIFTGD RDLTQLTSDK TSVAVSKKGV TEVETYTPEH VEEKLGVRPN
     QIIEIKGLQG DTSDNYPGVT GVGPKTAVSL IQKYDTIDGV YDNLDKITAK KMKEHLIEDK
     NSAFQSRDLA TIRRDAPIEI KLSDLAYKGD QRDELVEFYQ EMNFQSFLNK MNADSGDEDV
     LGLKPVKFTV LTADHLSDLD QFNDHVSFYL EMPEANYHTS TFAGFVIGEG DKWFVSRDVD
     LLKQAPLKAL LSGEQVQKDV FDVKRTYVGL NRLGIHLAHV DFDLLLASYL LDTNENSNDL
     GRLAFQHGYH QIQSDEEVYG KGAKRAIPDD DQIFFEHLTR KGITIEALKK SLFKQLDNNE
     QTQLYRDLEL PMAYVLAHME IAGIMVDTDR LTAMQSEFTE LLAQTQQTIF QEAGEEFNIG
     SPKQLQHILF EKLGLTPIKK TKTGYSTSVD VLEKLAAEAP IVENILKYRQ ISKIQSTYVE
     GLLKVVHSTD QKVHTRYLQT LTQTGRLSSV DPNLQNIPIR TEEGRRIRQA FIPSHKGWQI
     FSSDYSQIEL RVLAHITHDA NLQEAFREGE DIHASTARRI FHLGPDAEID PNMRRQAKAV
     NFGIVYGISD FGLSQNIGIT RKQARQFIDT YFEEYPGVKK YMTDIVASAK DKGYVETIAH
     RRRYLPDINA RNFNQRSFAE RTAMNTPIQG SAADIIKIAM INMEDAIKDL QATMLLQVHD
     ELIFEAPAEE IPTLEKLVPS VMDSAVKLEI PLKVESHYGN TWYEAK
//
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