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Description:
DNA polymerase II (EC 2.7.7.7) (Pol II).
Molecular weight: 89921
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:
01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
01-MAY-1991, sequence version 1.
07-MAR-2006, entry version 60.
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 DPO2_ECOLI:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | X54847 | CAA38616.1 | - |
| EMBL | M37727 | AAA23684.1 | - |
| EMBL | M62646 | AAA24406.1 | - |
| EMBL | M35371 | AAA24407.1 | - |
| EMBL | M38283 | AAA63764.1 | - |
| EMBL | D10483 | BAB96628.1 | ALT_FRAME |
| EMBL | D10483 | BAB96629.1 | ALT_FRAME |
| EMBL | U00096 | AAC73171.1 | - |
| PIR | S15943 | JDEC22. | |
| PDB | 1Q8I | X-ray | A=1-782. |
| GenomeReviews | U00096_GR | b0060.1 | |
| EchoBASE | EB0740 | -.1 | |
| EcoGene | EG10747 | polB. | |
| BioCyc | EcoCyc:EG10747-MONOMER | -.1 | |
| InterPro | IPR006172 | DNA_pol_B. | |
| InterPro | IPR006133 | DNA_pol_B_exo. | |
| InterPro | IPR006134 | DNA_pol_B_region. | |
| InterPro | IPR012337 | RNaseH_fold. | |
| Pfam | PF00136 | DNA_pol_B | 1. |
| Pfam | PF03104 | DNA_pol_B_exo | 1. |
| PRINTS | PR00106 | DNAPOLB. | |
| SMART | SM00486 | POLBc | 1. |
| PROSITE | PS00116 | DNA_POLYMERASE_B | 1. |
Keywords:
3D-structure; Complete proteome; Direct protein sequencing; DNA damage; DNA repair; DNA-binding; DNA-directed DNA polymerase; Nucleotidyltransferase; SOS response; Transferase.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-8.
RC STRAIN=K12 / W3110;
RX MEDLINE=91238699; PubMed=2034216; DOI=10.1007/BF00273583;
RA Iwasaki H., Ishino Y., Toh H., Nakata A., Shinagawa H.;
RT "Escherichia coli DNA polymerase II is homologous to alpha-like DNA
RT polymerases.";
RL Mol. Gen. Genet. 226:24-33(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX MEDLINE=91083835; PubMed=2261080;
RA Chen H., Sun Y., Stark T., Beattie W., Moses R.E.;
RT "Nucleotide sequence and deletion analysis of the polB gene of
RT Escherichia coli.";
RL DNA Cell Biol. 9:631-635(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12;
RX MEDLINE=92334977; PubMed=1630901;
RA Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N.,
RA Isono K., Mizobuchi K., Nakata A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the
RT 0-2.4 min region.";
RL Nucleic Acids Res. 20:3305-3308(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655;
RX MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA Mau B., Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1474(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-457, AND PROTEIN SEQUENCE OF
RP 1-27.
RC STRAIN=K12;
RX MEDLINE=91017565; PubMed=2217198;
RA Bonner C.A., Hays S., McEntee K., Goodman M.F.;
RT "DNA polymerase II is encoded by the DNA damage-inducible dinA gene of
RT Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:7663-7667(1990).
RN [6]
RP VARIANT MUTANT ALLELE POLB100.
RX MEDLINE=97236820; PubMed=9079692; DOI=10.1074/jbc.272.13.8611;
RA Qiu Z., Goodman M.F.;
RT "The Escherichia coli polB locus is identical to dinA, the structural
RT gene for DNA polymerase II. Characterization of Pol II purified from a
RT polB mutant.";
RL J. Biol. Chem. 272:8611-8617(1997).
Feature:
INIT_MET 0 0
CHAIN 1 782 DNA polymerase II.
/FTId=PRO_0000046473.
VARIANT 400 400 G -> D (in allele POLB100).
CONFLICT 171 171 G -> A (in Ref. 2).
CONFLICT 256 257 EH -> DD (in Ref. 5).
CONFLICT 259 266 FKNGVFFA -> PAKTASFLP (in Ref. 3).
CONFLICT 271 271 R -> G (in Ref. 5).
CONFLICT 286 286 N -> D (in Ref. 3).
CONFLICT 734 734 N -> T (in Ref. 2).
CONFLICT 739 782 LDYQRSPLDYEHYLTRQLQPVAEGILPFIEDNFATLMTGQL
GLF -> PGLPTFTTGLRTLSDPPATTRGGGNTPFY (in
Ref. 2).
STRAND 2 12
TURN 15 16
STRAND 18 26
TURN 27 28
STRAND 29 34
STRAND 36 36
STRAND 38 38
STRAND 40 45
HELIX 46 55
TURN 56 58
STRAND 61 70
TURN 72 73
STRAND 74 74
STRAND 76 83
HELIX 85 97
TURN 98 99
STRAND 103 104
TURN 105 106
HELIX 109 116
TURN 117 118
STRAND 120 130
TURN 131 132
STRAND 133 141
TURN 143 144
STRAND 151 158
TURN 160 161
STRAND 162 162
STRAND 164 171
TURN 172 173
STRAND 174 182
STRAND 185 185
TURN 188 189
STRAND 191 199
HELIX 200 214
STRAND 217 223
TURN 224 227
HELIX 228 238
TURN 239 240
STRAND 246 249
STRAND 253 257
STRAND 259 261
STRAND 263 268
TURN 269 270
STRAND 271 275
HELIX 276 282
STRAND 283 283
STRAND 288 288
HELIX 292 297
TURN 298 299
TURN 314 314
HELIX 315 322
HELIX 324 345
TURN 346 346
HELIX 347 358
STRAND 360 360
TURN 362 365
HELIX 368 382
TURN 383 384
STRAND 385 385
TURN 390 391
STRAND 393 393
STRAND 404 404
STRAND 409 419
TURN 420 421
HELIX 422 430
HELIX 434 442
STRAND 443 443
STRAND 445 445
TURN 446 448
STRAND 449 451
STRAND 453 453
TURN 454 455
STRAND 457 462
STRAND 464 464
HELIX 465 481
TURN 482 483
HELIX 485 502
TURN 503 503
TURN 505 506
STRAND 507 507
TURN 508 509
HELIX 512 535
TURN 536 537
STRAND 539 543
STRAND 545 551
STRAND 553 554
HELIX 558 581
TURN 582 584
STRAND 591 602
TURN 607 608
TURN 610 611
STRAND 614 614
STRAND 616 622
TURN 623 624
STRAND 625 633
HELIX 642 656
TURN 657 658
HELIX 662 673
TURN 674 677
HELIX 678 681
HELIX 748 754
TURN 755 755
HELIX 756 761
TURN 762 763
HELIX 764 767
TURN 768 768
HELIX 771 779
Comments:
-!- FUNCTION: Thought to be involved in DNA repair and/or mutagenesis.
-!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) =
diphosphate + DNA(n+1).
-!- ENZYME REGULATION: DNA polymerase II activity is regulated by the
lexA gene during the SOS response.
-!- SIMILARITY: Belongs to the DNA polymerase type-B family.
-!- CAUTION: Ref.3 sequence differs from that shown due to a
frameshift in position 238.
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Sequence length: 782
AQAGFILTRH WRDTPQGTEV SFWLATDNGP LQVTLAPQES VAFIPADQVP RAQHILQGEQ
GFRLTPLALK DFHRQPVYGL YCRAHRQLMN YEKRLREGGV TVYEADVRPP ERYLMERFIT
SPVWVEGDMH NGTIVNARLK PHPDYRPPLK WVSIDIETTR HGELYCIGLE GCGQRIVYML
GPENGDASSL DFELEYVASR PQLLEKLNAW FANYDPDVII GWNVVQFDLR MLQKHAERYR
LPLRLGRDNS ELEWREHGFK NGVFFAQAKG RLIIDGIEAL KSAFWNFSSF SLETVAQELL
GEGKSIDNPW DRMDEIDRRF AEDKPALATY NLKDCELVTQ IFHKTEIMPF LLERATVNGL
PVDRHGGSVA AFGHLYFPRM HRAGYVAPNL GEVPPHASPG GYVMDSRPGL YDSVLVLDYK
SLYPSIIRTF LIDPVGLVEG MAQPDPEHST EGFLDAWFSR EKHCLPEIVT NIWHGRDEAK
RQGNKPLSQA LKIIMNAFYG VLGTTACRFF DPRLASSITM RGHQIMRQTK ALIEAQGYDV
IYGDTDSTFV WLKGAHSEEE AAKIGRALVQ HVNAWWAETL QKQRLTSALE LEYETHFCRF
LMPTIRGADT GSKKRYAGLI QEGDKQRMVF KGLETVRTDW TPLAQQFQQE LYLRIFRNEP
YQEYVRETID KLMAGELDAR LVYRKRLRRP LSEYQRNVPP HVRAARLADE ENQKRGRPLQ
YQNRGTIKYV WTTNGPEPLD YQRSPLDYEH YLTRQLQPVA EGILPFIEDN FATLMTGQLG
LF