DPO1_CHLAA
ID DPO1_CHLAA Reviewed; 942 AA.
AC O08307; A9WD23;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=DNA polymerase I;
DE Short=POL I;
DE EC=2.7.7.7;
GN Name=polA; OrderedLocusNames=Caur_0341;
OS Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl).
OC Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Chloroflexineae;
OC Chloroflexaceae; Chloroflexus.
OX NCBI_TaxID=324602;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9526698; DOI=10.1016/s1050-3862(97)10002-x;
RA Tvermyr M., Kristiansen B.E., Kristensen T.;
RT "Cloning, sequence analysis and expression in E. coli of the DNA polymerase
RT I gene from Chloroflexus aurantiacus, a green nonsulfur eubacterium.";
RL Genet. Anal. 14:75-83(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29366 / DSM 635 / J-10-fl;
RX PubMed=21714912; DOI=10.1186/1471-2164-12-334;
RA Tang K.H., Barry K., Chertkov O., Dalin E., Han C.S., Hauser L.J.,
RA Honchak B.M., Karbach L.E., Land M.L., Lapidus A., Larimer F.W.,
RA Mikhailova N., Pitluck S., Pierson B.K., Blankenship R.E.;
RT "Complete genome sequence of the filamentous anoxygenic phototrophic
RT bacterium Chloroflexus aurantiacus.";
RL BMC Genomics 12:334-334(2011).
CC -!- FUNCTION: In addition to polymerase activity, this DNA polymerase
CC exhibits 3'-5' and 5'-3' exonuclease activity.
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.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-A family. {ECO:0000305}.
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DR EMBL; Y12328; CAA72997.1; -; Genomic_DNA.
DR EMBL; CP000909; ABY33592.1; -; Genomic_DNA.
DR RefSeq; WP_012256248.1; NC_010175.1.
DR RefSeq; YP_001633981.1; NC_010175.1.
DR AlphaFoldDB; O08307; -.
DR SMR; O08307; -.
DR STRING; 324602.Caur_0341; -.
DR EnsemblBacteria; ABY33592; ABY33592; Caur_0341.
DR KEGG; cau:Caur_0341; -.
DR PATRIC; fig|324602.8.peg.392; -.
DR eggNOG; COG0258; Bacteria.
DR eggNOG; COG0749; Bacteria.
DR HOGENOM; CLU_004675_0_0_0; -.
DR InParanoid; O08307; -.
DR OMA; NRPPMPD; -.
DR Proteomes; UP000002008; 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; 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 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.
DR PROSITE; PS00447; DNA_POLYMERASE_A; 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..942
FT /note="DNA polymerase I"
FT /id="PRO_0000101237"
FT DOMAIN 177..269
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000255"
FT DOMAIN 340..522
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000255"
SQ SEQUENCE 942 AA; 103698 MW; CC424A5103B2408F CRC64;
MAYPLLVLVD GHALAYRAFF ALRESGLRSS RGEPTYAVFG FAQILLTALA EYRPDYAAVA
FDVGRTFRDD LYAEYKAGRA ETPEEFYPQF ERIKQLVQAL NIPIYTAEGY EADDVIGTLA
RQATERGVDT IILTGDSDVL QLVNDHVRVA LANPYGGKTS VTLYDLEQVR KRYDGLEPDQ
LADLRGLKGD TSDNIPGVRG IGEKGAIALL KQFRSLDALL EQIDAAPKRY QTLLREQAEA
ARFSRQLATI VTDVPVQLDL EAARIGVYDR SAVMALFQEL EFGVSSNLIK KLPSVVQAPT
LAELPADLPA APLTTAPTQL SLFAGESEPA QPTAEPPPVT IVRDATALAD LVSRLRNAPA
FAFDTECTSL QPVASDLVGI SIAIAPDTVC YIPVGHQSET QVPCGEVVTA LAPFFANPQQ
PKFAHNAKFD MEVLAGAGIK VSGLAFDTMI AAAMLGKRQG LKDLAFYELK LPEPPTTIED
LIGRGNKQIS FAEVPVEQAA PYAAADALYT LRLTERLQRQ LEAEPALHDL YYRVELPLIE
VLTDMELTGI RLDQEYLREL GRHFAQRIAD LVERIYQQAG GPFNINSGQQ LNDVLFGRLG
IDPRAHGLSK LKSGGYSITA EVLEELSQLY PIAADILTYR QLTKLKSTYI DALPDLVNPR
TGRIHTSYNQ LGAATGRLSS NNPNLQNIPV RTEEGREIRR AFVAEPGWRF VAADYSQIEL
RVLAHMSGDE NLIAAFQQGL DIHAATASRL FGVEPTAVDK NQRRVAKTVV FGVIYGISAF
GLAQRLGIER DLARQLIDNL FAQFPGIRRY IDQTLEFGRQ HGYVQTLFGR RRVMEDLRAS
GARRAAAERE AINAPIQGTA ADLMKMAMVN VHRALREQGL RTRLLLQVHD ELIAEAPEDE
VEPAARLLRD VMSSVYRDLV VPLSVNLEVG PNWDEMSPLA MG
