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Description:
DNA polymerase I (EC 2.7.7.7) (POL I).
Molecular weight: 10311
View which proteins in this organism that is involved with DNA Repair;
classified after biological processes (using data from the GOA project):
DNA repair( GO:0006281 )
Important dates:
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
07-MAR-2006, entry version 78.
Phylogenetic order:
Bacteria Proteobacteria Gammaproteobacteria Enterobacteriales Enterobacteriaceae Escherichia.
To calculate the pI (Isoelectric point - the pH where a protein has a neutral charge),
go to this page and enter the protein ID (e.g 3MG_ECOLI): http://us.expasy.org/tools/pi_tool.html
Links to references in other databases for protein DPO1_ECOLI:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | V00317 | CAA23607.1 | - |
| EMBL | L19201 | AAB02998.1 | - |
| EMBL | U00096 | AAC76861.1 | - |
| EMBL | J01663 | AAA24402.1 | - |
| EMBL | J01664 | AAA24404.1 | - |
| PIR | A92360 | DJECI. | |
| PDB | 1D8Y | X-ray | A=325-928. |
| PDB | 1D9D | X-ray | A=325-928. |
| PDB | 1D9F | X-ray | A=325-928. |
| PDB | 1DPI | X-ray | @=324-928. |
| PDB | 1KFD | X-ray | @=324-928. |
| PDB | 1KFS | X-ray | A=325-928. |
| PDB | 1KLN | X-ray | A=324-928. |
| PDB | 1KRP | X-ray | A=325-928. |
| PDB | 1KSP | X-ray | A=325-928. |
| PDB | 1QSL | X-ray | A=325-928. |
| PDB | 2KFN | X-ray | A=325-928. |
| PDB | 2KFZ | X-ray | A=325-928. |
| PDB | 2KZM | X-ray | A=325-928. |
| PDB | 2KZZ | X-ray | A=325-928. |
| SWISS-2DPAGE | P00582 | COLI. | |
| ECO2DBASE | F113.0 | 6TH EDITION. | |
| GenomeReviews | U00096_GR | b3863.1 | |
| EchoBASE | EB0739 | -.1 | |
| EcoGene | EG10746 | polA. | |
| BioCyc | EcoCyc:EG10746-MONOMER | -.1 | |
| LinkHub | P00582 | -.1 | |
| GO | GO:0005515 | F:protein binding | IPI. |
| InterPro | IPR002562 | 3_5_exonuclease. | |
| InterPro | IPR002421 | 5_3_exonuclease. | |
| InterPro | IPR001098 | DNA_pol. | |
| InterPro | IPR002298 | DNA_polI. | |
| InterPro | IPR000513 | Exo_N_I. | |
| InterPro | IPR008918 | HhH2. | |
| InterPro | IPR012337 | RNaseH_fold. | |
| Pfam | PF01612 | 3_5_exonuc | 1. |
| Pfam | PF01367 | 5_3_exonuc | 1. |
| Pfam | PF02739 | 5_3_exonuc_N | 1. |
| Pfam | PF00476 | DNA_pol_A | 1. |
| PRINTS | PR00868 | DNAPOLI. | |
| SMART | SM00474 | 35EXOc | 1. |
| SMART | SM00475 | 53EXOc | 1. |
| SMART | SM00279 | HhH2 | 1. |
| SMART | SM00482 | POLAc | 1. |
| TIGRFAMs | TIGR00593 | pola | 1. |
| PROSITE | PS00447 | DNA_POLYMERASE_A | 1. |
Keywords:
3D-structure; Complete proteome; Direct protein sequencing; DNA damage; DNA repair; DNA replication; DNA-binding; DNA-directed DNA polymerase; Exonuclease; Hydrolase; Nuclease; Nucleotidyltransferase; Transferase.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX MEDLINE=82120160; PubMed=6276402;
RA Joyce C.M., Kelley W.S., Grindley N.D.F.;
RT "Nucleotide sequence of the Escherichia coli polA gene and primary
RT structure of DNA polymerase I.";
RL J. Biol. Chem. 257:1958-1964(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / MG1655;
RX MEDLINE=93347969; PubMed=8346018;
RA Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome. III. DNA sequence of the
RT region from 87.2 to 89.2 minutes.";
RL Nucleic Acids Res. 21:3391-3398(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 918-928.
RC STRAIN=K12;
RX MEDLINE=83056713; PubMed=6183253;
RA Joyce C.M., Grindley N.D.;
RT "Identification of two genes immediately downstream from the polA gene
RT of Escherichia coli.";
RL J. Bacteriol. 152:1211-1219(1982).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 284-350.
RX MEDLINE=83189123; PubMed=6302278;
RA Kelley W.S., Joyce C.M.;
RT "Genetic characterization of early amber mutations in the Escherichia
RT coli polA gene and purification of the amber peptides.";
RL J. Mol. Biol. 164:529-560(1983).
RN [5]
RP AMINO-ACID COMPOSITION, AND PARTIAL PROTEIN SEQUENCE.
RX MEDLINE=82120161; PubMed=7035456;
RA Brown W.E., Stump K.H., Kelley W.S.;
RT "Escherichia coli DNA polymerase I. Sequence characterization and
RT secondary structure prediction.";
RL J. Biol. Chem. 257:1965-1972(1982).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF KLENOW FRAGMENT.
RX MEDLINE=85137890; PubMed=3883192;
RA Ollis D.L., Brick P., Hamlin R., Xuong N.G., Steitz T.A.;
RT "Structure of large fragment of Escherichia coli DNA polymerase I
RT complexed with dTMP.";
RL Nature 313:762-766(1985).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF KLENOW FRAGMENT.
RX MEDLINE=91114709; PubMed=1989886;
RA Beese L.S., Steitz T.A.;
RT "Structural basis for the 3'-5' exonuclease activity of Escherichia
RT coli DNA polymerase I: a two metal ion mechanism.";
RL EMBO J. 10:25-33(1991).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF KLENOW FRAGMENT.
RX MEDLINE=93227044; PubMed=8469987;
RA Beese L.S., Derbyshire V., Steitz T.A.;
RT "Structure of DNA polymerase I Klenow fragment bound to duplex DNA.";
RL Science 260:352-355(1993).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (3.9 ANGSTROMS) OF KLENOW FRAGMENT.
RX MEDLINE=94083412; PubMed=8260491;
RA Beese L.S., Friedman J.M., Steitz T.A.;
RT "Crystal structures of the Klenow fragment of DNA polymerase I
RT complexed with deoxynucleoside triphosphate and pyrophosphate.";
RL Biochemistry 32:14095-14101(1993).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF KLENOW FRAGMENT.
RX MEDLINE=98181033; PubMed=9514742; DOI=10.1006/jmbi.1997.1586;
RA Brautigam C.A., Steitz T.A.;
RT "Structural principles for the inhibition of the 3'-5' exonuclease
RT activity of Escherichia coli DNA polymerase I by phosphorothioates.";
RL J. Mol. Biol. 277:363-377(1998).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF KLENOW FRAGMENT.
RX MEDLINE=99105820; PubMed=9888810; DOI=10.1021/bi981537g;
RA Brautigam C.A., Sun S., Piccirilli J.A., Steitz T.A.;
RT "Structures of normal single-stranded DNA and deoxyribo-3'-S-
RT phosphorothiolates bound to the 3'-5' exonucleolytic active site of
RT DNA polymerase I from Escherichia coli.";
RL Biochemistry 38:696-704(1999).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.08 ANGSTROMS) OF KLENOW FRAGMENT.
RX MEDLINE=20056229; PubMed=10588690; DOI=10.1073/pnas.96.25.14240;
RA Teplova M., Wallace S.T., Tereshko V., Minasov G., Symons A.M.,
RA Cook P.D., Manoharan M., Egli M.;
RT "Structural origins of the exonuclease resistance of a zwitterionic
RT RNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:14240-14245(1999).
RN [13]
RP STRUCTURE BY NMR OF 728-777.
RX MEDLINE=93183012; PubMed=8442659; DOI=10.1006/abbi.1993.1130;
RA Mullen G.P., Vaughn J.B. Jr., Mildvan A.S.;
RT "Sequential proton NMR resonance assignments, circular dichroism, and
RT structural properties of a 50-residue substrate-binding peptide from
RT DNA polymerase I.";
RL Arch. Biochem. Biophys. 301:174-183(1993).
Feature:
CHAIN 1 928 DNA polymerase I.
/FTId=PRO_0000101239.
DOMAIN 1 323 5'-3' exonuclease.
DOMAIN 324 517 3'-5' exonuclease.
REGION 324 928 Klenow fragment.
REGION 521 928 Polymerase.
STRAND 327 332
STRAND 335 335
HELIX 336 347
TURN 348 348
STRAND 349 359
STRAND 361 361
TURN 363 365
STRAND 368 376
TURN 377 378
STRAND 379 384
STRAND 389 389
TURN 390 391
HELIX 398 409
TURN 410 410
TURN 412 413
STRAND 414 414
STRAND 416 420
HELIX 421 429
TURN 430 432
STRAND 438 441
HELIX 442 449
TURN 451 452
STRAND 453 454
STRAND 457 457
HELIX 458 465
STRAND 466 466
HELIX 473 477
STRAND 479 480
TURN 481 482
HELIX 486 488
STRAND 489 489
HELIX 491 515
TURN 516 517
STRAND 518 518
HELIX 520 528
TURN 529 529
HELIX 530 543
STRAND 545 545
STRAND 547 547
HELIX 549 573
STRAND 574 576
STRAND 580 580
TURN 582 585
STRAND 586 586
HELIX 587 590
TURN 591 593
STRAND 594 595
STRAND 597 597
TURN 608 610
HELIX 613 617
TURN 618 620
STRAND 622 622
HELIX 623 639
TURN 640 643
HELIX 644 647
STRAND 648 648
TURN 650 652
STRAND 653 655
STRAND 658 662
STRAND 665 667
STRAND 670 674
HELIX 676 678
STRAND 679 679
STRAND 681 683
HELIX 684 691
TURN 692 692
STRAND 693 694
TURN 697 698
STRAND 699 706
TURN 707 708
HELIX 709 717
TURN 718 719
HELIX 721 728
TURN 729 730
HELIX 733 741
TURN 742 743
HELIX 746 748
HELIX 751 765
TURN 766 767
TURN 770 771
HELIX 772 777
TURN 778 778
TURN 781 783
HELIX 784 794
HELIX 796 812
STRAND 813 816
TURN 818 819
STRAND 822 824
TURN 826 829
STRAND 831 832
HELIX 833 870
STRAND 873 880
TURN 881 882
STRAND 883 889
TURN 890 892
HELIX 893 906
STRAND 907 908
STRAND 910 912
STRAND 916 923
HELIX 924 927
Comments:
-!- FUNCTION: In addition to polymerase activity, this DNA polymerase
exhibits 3' to 5' and 5' to 3' exonuclease activity. It is able to
utilize nicked circular duplex DNA as a template and can unwind
the parental DNA strand from its template.
-!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) =
diphosphate + DNA(n+1).
-!- SUBUNIT: Single-chain monomer with multiple functions.
-!- INTERACTION:
P06959:aceF; NbExp=1; IntAct=EBI-552540, EBI-542707;
P0A6R3:fis; NbExp=1; IntAct=EBI-552540, EBI-550170;
P08936:hns; NbExp=1; IntAct=EBI-552540, EBI-544934;
P43329:hrpA; NbExp=1; IntAct=EBI-552540, EBI-545429;
P10485:hsdS; NbExp=1; IntAct=EBI-552540, EBI-552202;
P02342:hupA; NbExp=1; IntAct=EBI-552540, EBI-547648;
P02341:hupB; NbExp=1; IntAct=EBI-552540, EBI-370411;
P00391:lpdA; NbExp=1; IntAct=EBI-552540, EBI-542856;
P00490:malP; NbExp=1; IntAct=EBI-552540, EBI-551914;
P0A817:metK; NbExp=1; IntAct=EBI-552540, EBI-546295;
P11880:murF; NbExp=1; IntAct=EBI-552540, EBI-554810;
P07012:prfB; NbExp=1; IntAct=EBI-552540, EBI-556176;
P69407:rcsB; NbExp=1; IntAct=EBI-552540, EBI-369670;
P60723:rplD; NbExp=1; IntAct=EBI-552540, EBI-545597;
P0A7K2:rplL; NbExp=1; IntAct=EBI-552540, EBI-543702;
P02410:rplM; NbExp=1; IntAct=EBI-552540, EBI-543801;
P0A7M2:rpmB; NbExp=1; IntAct=EBI-552540, EBI-543024;
P0A7Z4:rpoA; NbExp=1; IntAct=EBI-552540, EBI-544985;
P0A8V2:rpoB; NbExp=1; IntAct=EBI-552540, EBI-544996;
P0A8T7:rpoC; NbExp=1; IntAct=EBI-552540, EBI-543604;
P0A7V0:rpsB; NbExp=1; IntAct=EBI-552540, EBI-543439;
P30856:slyD; NbExp=1; IntAct=EBI-552540, EBI-369251;
P02990:tufA; NbExp=1; IntAct=EBI-552540, EBI-301077;
P77182:yfcK; NbExp=1; IntAct=EBI-552540, EBI-555845;
P31461:yidX; NbExp=1; IntAct=EBI-552540, EBI-553327;
-!- SIMILARITY: Belongs to the DNA polymerase type-A family.
-!- SIMILARITY: Contains 1 3'-5' exonuclease domain.
-!- SIMILARITY: Contains 1 5'-3' exonuclease domain.
-!- DATABASE: NAME=Worthington enzyme manual;
WWW="http://www.worthington-biochem.com/DNAP/".
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Sequence length: 928
MVQIPQNPLI LVDGSSYLYR AYHAFPPLTN SAGEPTGAMY GVLNMLRSLI MQYKPTHAAV
VFDAKGKTFR DELFEHYKSH RPPMPDDLRA QIEPLHAMVK AMGLPLLAVS GVEADDVIGT
LAREAEKAGR PVLISTGDKD MAQLVTPNIT LINTMTNTIL GPEEVVNKYG VPPELIIDFL
ALMGDSSDNI PGVPGVGEKT AQALLQGLGG LDTLYAEPEK IAGLSFRGAK TMAAKLEQNK
EVAYLSYQLA TIKTDVELEL TCEQLEVQQP AAEELLGLFK KYEFKRWTAD VEAGKWLQAK
GAKPAAKPQE TSVADEAPEV TATVISYDNY VTILDEETLK AWIAKLEKAP VFAFDTETDS
LDNISANLVG LSFAIEPGVA AYIPVAHDYL DAPDQISRER ALELLKPLLE DEKALKVGQN
LKYDRGILAN YGIELRGIAF DTMLESYILN SVAGRHDMDS LAERWLKHKT ITFEEIAGKG
KNQLTFNQIA LEEAGRYAAE DADVTLQLHL KMWPDLQKHK GPLNVFENIE MPLVPVLSRI
ERNGVKIDPK VLHNHSEELT LRLAELEKKA HEIAGEEFNL SSTKQLQTIL FEKQGIKPLK
KTPGGAPSTS EEVLEELALD YPLPKVILEY RGLAKLKSTY TDKLPLMINP KTGRVHTSYH
QAVTATGRLS STDPNLQNIP VRNEEGRRIR QAFIAPEDYV IVSADYSQIE LRIMAHLSRD
KGLLTAFAEG KDIHRATAAE VFGLPLETVT SEQRRSAKAI NFGLIYGMSA FGLARQLNIP
RKEAQKYMDL YFERYPGVLE YMERTRAQAK EQGYVETLDG RRLYLPDIKS SNGARRAAAE
RAAINAPMQG TAADIIKRAM IAVDAWLQAE QPRVRMIMQV HDELVFEVHK DDVDAVAKQI
HQLMENCTRL DVPLLVEVGS GENWDQAH