GenomeNet

Database: UniProt
Entry: A0A1Y1R0C3_9GAMM
LinkDB: A0A1Y1R0C3_9GAMM
Original site: A0A1Y1R0C3_9GAMM 
ID   A0A1Y1R0C3_9GAMM        Unreviewed;       913 AA.
AC   A0A1Y1R0C3;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-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   ORFNames=B0D91_14940 {ECO:0000313|EMBL:OQX33199.1};
OS   Oceanospirillales bacterium LUC14_002_19_P2.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales.
OX   NCBI_TaxID=1940822 {ECO:0000313|EMBL:OQX33199.1, ECO:0000313|Proteomes:UP000192421};
RN   [1] {ECO:0000313|EMBL:OQX33199.1, ECO:0000313|Proteomes:UP000192421}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LUC14_002_19_P2 {ECO:0000313|EMBL:OQX33199.1};
RA   Lim S.J., Davis B.G., Gill D.E., Engel A.S., Anderson L.C., Campbell B.J.;
RT   "Novel co-symbiosis in the unique lucinid bivalve Phacoides pectinatus.";
RL   Submitted (FEB-2017) 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:OQX33199.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; MUIA01000442; OQX33199.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y1R0C3; -.
DR   Proteomes; UP000192421; 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:UP000192421};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT   DOMAIN          8..269
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00475"
FT   DOMAIN          315..502
FT                   /note="3'-5' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00474"
FT   DOMAIN          671..877
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
SQ   SEQUENCE   913 AA;  100759 MW;  3FCEC845E3926ECE CRC64;
     MPAANTSAPL VLVDGSSYLY RAFHALPPLV SSKGQPTGAI KGVVNMLRRM QSDYPDSEVV
     VVFDAKGKTF RDDIYPEYKA HRPPMPDDLR SQIEPLHTVV RAMGFPLLVI EGVEADDVIG
     TLAAMATEAG RDCVVSTGDK DMAQLVNQHV TLVNTMTDTV MDIPGVQSKF GIGPELIIDF
     LALMGDKVDN IPGVPGVGEK TALALLQNLG GLEAIYANLD KVPTLTFRGA KTMPKKLEEN
     KEQAFLSYEL ATIKTDVALS LTLSDLRNET PDRDTLLHWF QELEFKGWIN QLQKEGDEDT
     GVEPASAPAA VERVYETVLT EADFTRWMDQ LKQASLFAFD TETTSLDYMQ AELVGVSFSV
     EPGKAAYVPF AHDYLDAPVQ LERAYVLGAL KPLLESEKHL KVGQNLKYDK SVLARYDITL
     RGIAFDTMLE SYVLDSTGTR HDMDSLSLKY LGESTVSFED IAGKGVKQLT FNQISLEQAG
     PYAAEDADIT LRLHQALWPK LEADAPLKSV FESIELPLVG ILSRMERTGA LVNANLLGEQ
     SIELADRLQV LEREAFDLAG QEFNLSSPKQ LQELLFNKLG LPVIKKTPKG QPSTAEEVLE
     ELALSHELPR LILEHRSLSK LKSTYTDKLP RMVNPASGRI HTSYHQAVTA TGRLSSSEPN
     LQNIPVRTGE GRRIRQAFIA PKGYKVVAAD YSQIELRIMA HLSKDEGLLN AFAHGLDVHK
     ATAAEVFGVP LDSVTGDQRR SAKAINFGLI YGMSAFGLAK QLGIFRQSAQ EYVDLYFERY
     PGVKDYMERT RKQAHEQGYV ETLFGRRLHL PEINARNKMR QQAAERTAIN APMQGTAADI
     IKKAMIGVDQ WLAESGLDAR MVMQVHDELV LEVAEGCLET VVDGLREHMT AAAELAIPLL
     VDVGIGDNWD EAH
//
DBGET integrated database retrieval system