DPO1_SYNY3
ID DPO1_SYNY3 Reviewed; 986 AA.
AC Q55971;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=DNA polymerase I;
DE Short=POL I;
DE EC=2.7.7.7;
GN Name=polA; OrderedLocusNames=slr0707;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX PubMed=8590279; DOI=10.1093/dnares/2.4.153;
RA Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N.,
RA Sugiura M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region
RT from map positions 64% to 92% of the genome.";
RL DNA Res. 2:153-166(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
CC -!- FUNCTION: In addition to polymerase activity, this DNA polymerase
CC exhibits 3'-5' and 5'-3' exonuclease activity. {ECO:0000250}.
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 -!- SUBUNIT: Single-chain monomer with multiple functions. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-A family. {ECO:0000305}.
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DR EMBL; BA000022; BAA10748.1; -; Genomic_DNA.
DR PIR; S77056; S77056.
DR AlphaFoldDB; Q55971; -.
DR SMR; Q55971; -.
DR IntAct; Q55971; 3.
DR STRING; 1148.1006595; -.
DR PaxDb; Q55971; -.
DR EnsemblBacteria; BAA10748; BAA10748; BAA10748.
DR KEGG; syn:slr0707; -.
DR eggNOG; COG0258; Bacteria.
DR eggNOG; COG0749; Bacteria.
DR InParanoid; Q55971; -.
DR OMA; NRPPMPD; -.
DR PhylomeDB; Q55971; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IBA:GO_Central.
DR GO; GO:0006261; P:DNA-templated DNA replication; IEA:InterPro.
DR GO; GO:0006302; P:double-strand break repair; IBA:GO_Central.
DR CDD; cd09898; H3TH_53EXO; 1.
DR Gene3D; 3.30.420.10; -; 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; 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 PANTHER; PTHR10133; PTHR10133; 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; SSF47807; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR SUPFAM; SSF88723; SSF88723; 1.
DR TIGRFAMs; TIGR00593; pola; 1.
PE 3: Inferred from homology;
KW DNA damage; DNA repair; DNA replication; DNA-binding;
KW DNA-directed DNA polymerase; Exonuclease; Hydrolase; Nuclease;
KW Nucleotidyltransferase; Reference proteome; Transferase.
FT CHAIN 1..986
FT /note="DNA polymerase I"
FT /id="PRO_0000101255"
FT DOMAIN 1..303
FT /note="5'-3' exonuclease"
FT DOMAIN 304..592
FT /note="3'-5' exonuclease"
FT REGION 308..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 593..986
FT /note="Polymerase"
SQ SEQUENCE 986 AA; 110287 MW; C87852AD07487FB3 CRC64;
MFMSAKSPLL LLVDGHSLAF RAYYAFGLSK KGPLRTTAGI PTSVCFGFLN SLMQVMESQK
PAAIAIAFDR REPTFRHEAD GAYKSNRQET PEDFAEDLSY LQQLLEALNL QTITYAGYEA
DDILGTLACQ GSDAGYQVKI LSGDRDLFQL VSPEKNISVL YLTRNPFSSN TGYDELDWQG
VVDKMGVTPA QIVDFKALCG DKSDCIPGIN GIGEKTAIKL LAEYETLEKV YENLAQIKGA
LKTRLDNGKD DAMHSQMLAR IVVDVPLPVT WEDLQLTGFS TDRLVPLLEK LELRTFIDKI
QAFHRNFSDN QSPVPMGNEA DNGEPKKTVK AKKSKEKVNP DDSQQLSLFD GVPVVNQEDG
LITIQLPKQI QPQIITTIAQ LEALVEELKK HTDADFPVAW DTETDSLDPL VANLVGIGCA
WGQEPNQVAY IPLKHHQGEQ LSLGIIKDLL GEILGNAIYP KVLQNAKFDR RVLAHHGIEL
GGVVLDTMLA SYVLQPEETH NLTDLCRRYN LGLVALSYKD LGLKKDQTIA DLPLETAGQY
CGLDCYATYL LASKLQKELD QYPELKEILK EIEQPLEKIL AAMEDRGIRI DCDYLQTLSQ
QLAENLLTIE TAAYEAAGES FNLSSPKQLG TILFDKLGLD RKKSRKTKTG YSTDHATLEK
LQGDHPIIDA ILEHRTLAKL KSTYVDALPE LVNGQTQRIH TDFNQAVTST GRLSSSNPNL
QNIPIRSDFS RQIRRAFLPQ KDWLLVSADY SQIELRILAH LSQEPVLLQA YGDRQDVHGV
TAKLLFGKED ITPAERNLGK TINFGVIYGM GAQRFARETG ISAVEGREFI DRYHRTYAQV
FDYLETMKLE AIAKGYVTTI VGRRRYFNFV TEALRQLRGK TVTELDLVDV KMNYNDAQLL
RSAANAPIQG SSADIIKIAM VKLAKLLESY QTRMLLQVHD ELIFEMPPEE WEELAPLIQN
TMEQALTLSV PLVVEMHRGS NWMEAK
