DPO1_HAEIN
ID DPO1_HAEIN Reviewed; 930 AA.
AC P43741;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=DNA polymerase I;
DE Short=POL I;
DE EC=2.7.7.7;
GN Name=polA; OrderedLocusNames=HI_0856;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
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.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-A family. {ECO:0000305}.
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; L42023; AAC22515.1; -; Genomic_DNA.
DR PIR; E64098; E64098.
DR RefSeq; NP_439016.1; NC_000907.1.
DR RefSeq; WP_005693204.1; NC_000907.1.
DR AlphaFoldDB; P43741; -.
DR SMR; P43741; -.
DR STRING; 71421.HI_0856; -.
DR PRIDE; P43741; -.
DR EnsemblBacteria; AAC22515; AAC22515; HI_0856.
DR KEGG; hin:HI_0856; -.
DR PATRIC; fig|71421.8.peg.897; -.
DR eggNOG; COG0258; Bacteria.
DR eggNOG; COG0749; Bacteria.
DR HOGENOM; CLU_004675_0_0_6; -.
DR OMA; NRPPMPD; -.
DR PhylomeDB; P43741; -.
DR BioCyc; HINF71421:G1GJ1-896-MON; -.
DR Proteomes; UP000000579; 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..930
FT /note="DNA polymerase I"
FT /id="PRO_0000101240"
FT DOMAIN 1..327
FT /note="5'-3' exonuclease"
FT DOMAIN 328..520
FT /note="3'-5' exonuclease"
FT REGION 524..930
FT /note="Polymerase"
SQ SEQUENCE 930 AA; 103741 MW; 226654BB7CFF730B CRC64;
MAQIATNPLV LVDGSSYLYR AFHAFPSLTN AAGEPTSAMY GVLNMLKSLI SQVQPTHIAV
VFDAKGKTFR DEMFEQYKSH RPPMPDDLRK QIQPLHDMIR ALGIPLLVVE GIEADDVIGT
LALQASSLGK KVLISTGDKD MAQLVDDNIM LINTMNNSLL DRKGVIEKYG IPPELIIDYL
ALMGDSADNI PGVAGVGEKT ALGLLQGIGS MAEIYANLEK VAELPIRGAK KLGEKLLAEK
NNADLSYTLA TIKTDVELNV TTDQLLLGES QKDQLIEYFA RYEFKRWLNE VMNGADSITQ
TTEQPVKMNQ YKATSQDQSA VENTPKIQID RTKYETLLTQ ADLTRWIEKL NAAKLIAVDT
ETDSLDYMSA NLVGISFALE NGEAAYLPLQ LDYLDAPKTL EKSTALAAIK PILENPNIHK
IGQNIKFDES IFARHGIELQ GVEFDTMLLS YTLNSTGRHN MDDLAKRYLG HETIAFESLA
GKGKSQLTFN QIPLEQATEY AAEDADVTMK LQQALWLKLQ EEPTLVELYK TMELPLLHVL
SRMERTGVLI DSDALFMQSN EIASRLTALE KQAYALAGQP FNLASTKQLQ EILFDKLELP
VLQKTPKGAP STNEEVLEEL SYSHELPKIL VKHRGLSKLK STYTDKLPQM VNSQTGRVHT
SYHQAVTATG RLSSSDPNLQ NIPIRNEEGR HIRQAFIARE GYSIVAADYS QIELRIMAHL
SGDQGLINAF SQGKDIHRST AAEIFGVSLD EVTSEQRRNA KAINFGLIYG MSAFGLSRQL
GISRADAQKY MDLYFQRYPS VQQFMTDIRE KAKAQGYVET LFGRRLYLPD INSSNAMRRK
GAERVAINAP MQGTAADIIK RAMIKLDEVI RHDPDIEMIM QVHDELVFEV RSEKVAFFRE
QIKQHMEAAA ELVVPLIVEV GVGQNWDEAH