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Database: UniProt
Entry: R8ALN7_PLESH
LinkDB: R8ALN7_PLESH
Original site: R8ALN7_PLESH 
ID   R8ALN7_PLESH            Unreviewed;       422 AA.
AC   R8ALN7;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=DNA polymerase I {ECO:0000313|EMBL:EON87251.1};
GN   ORFNames=PLESHI_16867 {ECO:0000313|EMBL:EON87251.1};
OS   Plesiomonas shigelloides 302-73.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Plesiomonas.
OX   NCBI_TaxID=1315976 {ECO:0000313|EMBL:EON87251.1, ECO:0000313|Proteomes:UP000014012};
RN   [1] {ECO:0000313|EMBL:EON87251.1, ECO:0000313|Proteomes:UP000014012}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=302-73 {ECO:0000313|EMBL:EON87251.1,
RC   ECO:0000313|Proteomes:UP000014012};
RX   PubMed=23814109;
RA   Pique N., Aquilini E., Alioto T., Minana-Galbis D., Tomas J.M.;
RT   "Genome Sequence of Plesiomonas shigelloides Strain 302-73 (Serotype O1).";
RL   Genome Announc. 1:e00404-13(2013).
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   -!- 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}.
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:EON87251.1}.
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DR   EMBL; AQQO01000371; EON87251.1; -; Genomic_DNA.
DR   AlphaFoldDB; R8ALN7; -.
DR   PATRIC; fig|1315976.3.peg.3229; -.
DR   HOGENOM; CLU_004675_2_1_6; -.
DR   Proteomes; UP000014012; Unassembled WGS sequence.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006261; P:DNA-templated DNA replication; IEA:InterPro.
DR   CDD; cd08637; DNA_pol_A_pol_I_C; 1.
DR   Gene3D; 3.30.70.370; -; 1.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
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; IPR002298; DNA_polymerase_A.
DR   PANTHER; PTHR10133; DNA POLYMERASE I; 1.
DR   PANTHER; PTHR10133:SF62; DNA POLYMERASE THETA; 1.
DR   Pfam; PF00476; DNA_pol_A; 1.
DR   PRINTS; PR00868; DNAPOLI.
DR   SMART; SM00482; POLAc; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   PROSITE; PS00447; DNA_POLYMERASE_A; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000014012}.
FT   DOMAIN          179..386
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
SQ   SEQUENCE   422 AA;  46589 MW;  2CBA53B1FEC0D721 CRC64;
     MHEVLWPQLE QEAGLASVLQ EMEVPLLSVL SRMERNGVLI DPALLGRHSM ELTARLAELE
     SKAHELAGEP FNLASTKQLQ GILFEKLGLP VLKKTPGGAP STNEEVLAEL ALDYPLPAVL
     LEYRGLAKLK STYTDKLPQM INPATGRVHT SYHQAVTATG RLSSTDPNLQ NIPVRNEEGR
     RIRQAFIAGA GNQIIAADYS QIELRIMAHL SGDAGLLRAF SEGKDIHRAT AAEVFGLPLE
     QVSAEQRRSA KAINFGLIYG MSAFGLARQL GIGRNDAQRY MDLYFERYPG VLTYMERTRE
     QAHAQGYVET LFGRRLQLPD IRSRNAMRRK GAERAAINAP MQGTAADIIK RAMLAVDAWL
     ATPEADGIRM IMQVHDELVF EVPQEKVALC SAKVRELMQQ SAALDVPLLV EVGVGDNWDQ
     AH
//
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