DPO4_SACS2
ID DPO4_SACS2 Reviewed; 352 AA.
AC Q97W02;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=DNA polymerase IV;
DE Short=Pol IV;
DE EC=2.7.7.7;
GN Name=dbh; Synonyms=dpo4; OrderedLocusNames=SSO2448;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [2]
RP CHARACTERIZATION.
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11713310; DOI=10.1093/nar/29.22.4607;
RA Boudsocq F., Iwai S., Hanaoka F., Woodgate R.;
RT "Sulfolobus solfataricus P2 DNA polymerase IV (Dpo4): an archaeal DinB-like
RT DNA polymerase with lesion-bypass properties akin to eukaryotic pol eta.";
RL Nucleic Acids Res. 29:4607-4616(2001).
RN [3]
RP CHARACTERIZATION.
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11919199; DOI=10.1074/jbc.m202021200;
RA Kokoska R.J., Bebenek K., Boudsocq F., Woodgate R., Kunkel T.A.;
RT "Low fidelity DNA synthesis by a Y family DNA polymerase due to
RT misalignment in the active site.";
RL J. Biol. Chem. 277:19633-19638(2002).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF TERNARY COMPLEX WITH DNA AND AN
RP INCOMING NUCLEOTIDE, AND MUTAGENESIS OF 105-ASP-GLU-106.
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11595188; DOI=10.1016/s0092-8674(01)00515-3;
RA Ling H., Boudsocq F., Woodgate R., Yang W.;
RT "Crystal structure of a Y-family DNA polymerase in action: a mechanism for
RT error-prone and lesion-bypass replication.";
RL Cell 107:91-102(2001).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 1-244 IN COMPLEX WITH PCNA,
RP INTERACTION WITH PCNA1, SUBUNIT, DNA-BINDING, AND MUTAGENESIS OF
RP 342-GLU--THR-352.
RX PubMed=19054331; DOI=10.1111/j.1365-2958.2008.06553.x;
RA Xing G., Kirouac K., Shin Y.J., Bell S.D., Ling H.;
RT "Structural insight into recruitment of translesion DNA polymerase Dpo4 to
RT sliding clamp PCNA.";
RL Mol. Microbiol. 71:678-691(2009).
CC -!- FUNCTION: Poorly processive, error-prone DNA polymerase involved in
CC untargeted mutagenesis. Copies undamaged DNA at stalled replication
CC forks, which arise in vivo from mismatched or misaligned primer ends.
CC These misaligned primers can be extended by PolIV. Exhibits no 3'-5'
CC exonuclease (proofreading) activity. It is involved in translesional
CC synthesis.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Note=Binds 2 magnesium ions per subunit.;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Highly active from 35 to 95 degrees Celsius. Thermostable.;
CC -!- SUBUNIT: Monomer. Interacts with the PCNA heterotrimer via PCNA1.
CC {ECO:0000269|PubMed:19054331}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DOMAIN: The catalytic core consists of fingers, palm and thumb
CC subdomains, but the fingers and thumb subdomains are much smaller than
CC in high-fidelity polymerases; residues from five sequence motifs of the
CC Y-family cluster around an active site cleft that can accommodate DNA
CC and nucleotide substrates with relaxed geometric constraints, with
CC consequently higher rates of misincorporation and low processivity.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-Y family. {ECO:0000305}.
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DR EMBL; AE006641; AAK42588.1; -; Genomic_DNA.
DR PIR; E90416; E90416.
DR RefSeq; WP_009993137.1; NC_002754.1.
DR PDB; 1JX4; X-ray; 1.70 A; A=1-352.
DR PDB; 1JXL; X-ray; 2.10 A; A=1-352.
DR PDB; 1N48; X-ray; 2.20 A; A=1-352.
DR PDB; 1N56; X-ray; 2.40 A; A/B=1-352.
DR PDB; 1RYR; X-ray; 2.28 A; A=1-352.
DR PDB; 1RYS; X-ray; 2.03 A; A/B=1-352.
DR PDB; 1S0M; X-ray; 2.70 A; A/B=1-352.
DR PDB; 1S0N; X-ray; 2.80 A; A=1-352.
DR PDB; 1S0O; X-ray; 2.10 A; A/B=1-352.
DR PDB; 1S10; X-ray; 2.10 A; A=1-352.
DR PDB; 1S97; X-ray; 2.40 A; A/B/C/D=1-352.
DR PDB; 1S9F; X-ray; 2.00 A; A/B/C/D=1-352.
DR PDB; 2AGO; X-ray; 2.85 A; A=1-341.
DR PDB; 2AGP; X-ray; 2.90 A; A/B=1-341.
DR PDB; 2AGQ; X-ray; 2.10 A; A=1-341.
DR PDB; 2ASD; X-ray; 1.95 A; A/B=2-352.
DR PDB; 2ASJ; X-ray; 2.35 A; A/B=2-352.
DR PDB; 2ASL; X-ray; 2.65 A; A/B=2-352.
DR PDB; 2ATL; X-ray; 2.80 A; A/B=2-352.
DR PDB; 2AU0; X-ray; 2.70 A; A/B=2-352.
DR PDB; 2BQ3; X-ray; 2.00 A; A=1-352.
DR PDB; 2BQR; X-ray; 2.37 A; A=1-352.
DR PDB; 2BQU; X-ray; 2.50 A; A=1-352.
DR PDB; 2BR0; X-ray; 2.17 A; A=1-352.
DR PDB; 2C22; X-ray; 2.56 A; A=1-352.
DR PDB; 2C28; X-ray; 2.27 A; A=1-352.
DR PDB; 2C2D; X-ray; 2.57 A; A=1-352.
DR PDB; 2C2E; X-ray; 2.61 A; A=1-352.
DR PDB; 2C2R; X-ray; 2.55 A; A=1-352.
DR PDB; 2IA6; X-ray; 2.50 A; A/B=1-352.
DR PDB; 2IBK; X-ray; 2.25 A; A=1-352.
DR PDB; 2IMW; X-ray; 2.05 A; P=1-348.
DR PDB; 2J6S; X-ray; 2.50 A; A=1-352.
DR PDB; 2J6T; X-ray; 2.60 A; A=1-352.
DR PDB; 2J6U; X-ray; 2.50 A; A=1-352.
DR PDB; 2JEF; X-ray; 2.17 A; A=1-352.
DR PDB; 2JEG; X-ray; 2.38 A; A=1-352.
DR PDB; 2JEI; X-ray; 2.39 A; A=1-352.
DR PDB; 2JEJ; X-ray; 1.86 A; A=1-352.
DR PDB; 2R8G; X-ray; 2.70 A; A=1-352.
DR PDB; 2R8H; X-ray; 2.48 A; A=1-352.
DR PDB; 2R8I; X-ray; 2.38 A; A=1-352.
DR PDB; 2RDI; X-ray; 1.92 A; A=1-341.
DR PDB; 2RDJ; X-ray; 2.20 A; A/B=1-352.
DR PDB; 2UVR; X-ray; 2.90 A; A=1-352.
DR PDB; 2UVU; X-ray; 2.70 A; A=1-352.
DR PDB; 2UVV; X-ray; 2.20 A; A=1-352.
DR PDB; 2UVW; X-ray; 2.09 A; A=1-352.
DR PDB; 2V4Q; X-ray; 2.60 A; A=1-352.
DR PDB; 2V4R; X-ray; 2.50 A; A=1-352.
DR PDB; 2V9W; X-ray; 3.00 A; A/B=1-352.
DR PDB; 2VA2; X-ray; 2.80 A; A/B=1-352.
DR PDB; 2VA3; X-ray; 2.98 A; A=1-352.
DR PDB; 2W8K; X-ray; 3.10 A; A=1-352.
DR PDB; 2W8L; X-ray; 3.00 A; A=1-352.
DR PDB; 2W9A; X-ray; 2.60 A; A=1-352.
DR PDB; 2W9B; X-ray; 2.28 A; A/B=1-352.
DR PDB; 2W9C; X-ray; 2.87 A; A/B=1-352.
DR PDB; 2XC9; X-ray; 2.20 A; A=1-352.
DR PDB; 2XCA; X-ray; 2.50 A; A=1-352.
DR PDB; 2XCP; X-ray; 2.60 A; A/B=1-352.
DR PDB; 3FDS; X-ray; 2.05 A; A=1-352.
DR PDB; 3GII; X-ray; 2.60 A; A=2-341.
DR PDB; 3GIJ; X-ray; 2.40 A; A/B=2-341.
DR PDB; 3GIK; X-ray; 2.90 A; A=2-341.
DR PDB; 3GIL; X-ray; 2.71 A; A/B=2-341.
DR PDB; 3GIM; X-ray; 2.70 A; A=2-341.
DR PDB; 3KHG; X-ray; 2.96 A; A/B=2-341.
DR PDB; 3KHH; X-ray; 2.70 A; A/B=2-341.
DR PDB; 3KHL; X-ray; 2.10 A; A/B=2-341.
DR PDB; 3KHR; X-ray; 2.01 A; A/B=2-341.
DR PDB; 3M9M; X-ray; 2.90 A; B=1-352.
DR PDB; 3M9N; X-ray; 1.93 A; B=1-352.
DR PDB; 3M9O; X-ray; 2.00 A; B=1-352.
DR PDB; 3PR4; X-ray; 2.65 A; A=1-341.
DR PDB; 3PR5; X-ray; 2.40 A; B=1-341.
DR PDB; 3PVX; X-ray; 3.03 A; A=1-341.
DR PDB; 3PW0; X-ray; 2.91 A; A=1-341.
DR PDB; 3PW2; X-ray; 2.74 A; A=1-341.
DR PDB; 3PW4; X-ray; 2.90 A; A=1-341.
DR PDB; 3PW5; X-ray; 3.00 A; A=1-341.
DR PDB; 3PW7; X-ray; 2.90 A; A/E=1-341.
DR PDB; 3QZ7; X-ray; 2.00 A; A=1-352.
DR PDB; 3QZ8; X-ray; 2.00 A; A=1-352.
DR PDB; 3RAQ; X-ray; 2.25 A; A/B=2-341.
DR PDB; 3RAX; X-ray; 1.89 A; A/B=2-341.
DR PDB; 3RB0; X-ray; 3.22 A; A/B=2-341.
DR PDB; 3RB3; X-ray; 2.80 A; A=2-341.
DR PDB; 3RB4; X-ray; 2.80 A; A/B=2-341.
DR PDB; 3RB6; X-ray; 2.70 A; A/B=2-341.
DR PDB; 3RBD; X-ray; 2.50 A; A/B=2-341.
DR PDB; 3RBE; X-ray; 2.80 A; A/B=2-341.
DR PDB; 3T5H; X-ray; 2.35 A; A=1-341.
DR PDB; 3T5J; X-ray; 2.40 A; A=1-341.
DR PDB; 3T5K; X-ray; 2.90 A; A=1-341.
DR PDB; 3T5L; X-ray; 2.90 A; A=1-341.
DR PDB; 3V6H; X-ray; 2.30 A; A/B=1-342.
DR PDB; 3V6J; X-ray; 2.30 A; A/J=1-342.
DR PDB; 3V6K; X-ray; 3.60 A; A/J=1-342.
DR PDB; 4F4W; X-ray; 1.90 A; A/B=231-352.
DR PDB; 4F4X; X-ray; 2.05 A; A=231-352.
DR PDB; 4F4Y; X-ray; 2.34 A; A/B=5-143, A/B=231-247.
DR PDB; 4F4Z; X-ray; 2.30 A; A/B=1-246.
DR PDB; 4F50; X-ray; 2.22 A; A=246-352.
DR PDB; 4FBT; X-ray; 2.00 A; A=1-341.
DR PDB; 4FBU; X-ray; 2.60 A; A/B=1-341.
DR PDB; 4G3I; X-ray; 2.50 A; A/B=1-341.
DR PDB; 4GC6; X-ray; 2.90 A; A=1-352.
DR PDB; 4GC7; X-ray; 2.89 A; A/B=1-352.
DR PDB; 4JUZ; X-ray; 2.65 A; A=1-341.
DR PDB; 4JV0; X-ray; 2.95 A; A=1-341.
DR PDB; 4JV1; X-ray; 2.30 A; A=1-341.
DR PDB; 4JV2; X-ray; 2.74 A; A=1-341.
DR PDB; 4QW8; X-ray; 2.29 A; A=1-341.
DR PDB; 4QW9; X-ray; 2.40 A; A=1-341.
DR PDB; 4QWA; X-ray; 2.20 A; A=1-341.
DR PDB; 4QWB; X-ray; 1.80 A; A=1-343.
DR PDB; 4QWC; X-ray; 2.40 A; A/D=1-342.
DR PDB; 4QWD; X-ray; 2.05 A; A=1-341.
DR PDB; 4QWE; X-ray; 2.20 A; A=1-341.
DR PDB; 4RUA; X-ray; 3.07 A; A=1-341.
DR PDB; 4RUC; X-ray; 2.90 A; A=1-341.
DR PDB; 4RZR; X-ray; 2.20 A; A/D=1-352.
DR PDB; 4TQR; X-ray; 1.58 A; A=1-342.
DR PDB; 4TQS; X-ray; 2.06 A; A/B=1-352.
DR PDB; 5EDW; X-ray; 2.62 A; A=1-341.
DR PDB; 6L84; X-ray; 2.60 A; A=1-352.
DR PDB; 6L97; X-ray; 2.36 A; A/B=1-352.
DR PDB; 6VG6; X-ray; 3.08 A; A/D=1-341.
DR PDB; 6VGM; X-ray; 2.84 A; A/D=1-341.
DR PDB; 6VKP; X-ray; 2.54 A; A/D=1-341.
DR PDB; 6VNP; X-ray; 2.42 A; A/D/G/J=1-341.
DR PDB; 7KLE; X-ray; 3.00 A; A=1-341.
DR PDB; 7KLF; X-ray; 2.30 A; A=1-341.
DR PDBsum; 1JX4; -.
DR PDBsum; 1JXL; -.
DR PDBsum; 1N48; -.
DR PDBsum; 1N56; -.
DR PDBsum; 1RYR; -.
DR PDBsum; 1RYS; -.
DR PDBsum; 1S0M; -.
DR PDBsum; 1S0N; -.
DR PDBsum; 1S0O; -.
DR PDBsum; 1S10; -.
DR PDBsum; 1S97; -.
DR PDBsum; 1S9F; -.
DR PDBsum; 2AGO; -.
DR PDBsum; 2AGP; -.
DR PDBsum; 2AGQ; -.
DR PDBsum; 2ASD; -.
DR PDBsum; 2ASJ; -.
DR PDBsum; 2ASL; -.
DR PDBsum; 2ATL; -.
DR PDBsum; 2AU0; -.
DR PDBsum; 2BQ3; -.
DR PDBsum; 2BQR; -.
DR PDBsum; 2BQU; -.
DR PDBsum; 2BR0; -.
DR PDBsum; 2C22; -.
DR PDBsum; 2C28; -.
DR PDBsum; 2C2D; -.
DR PDBsum; 2C2E; -.
DR PDBsum; 2C2R; -.
DR PDBsum; 2IA6; -.
DR PDBsum; 2IBK; -.
DR PDBsum; 2IMW; -.
DR PDBsum; 2J6S; -.
DR PDBsum; 2J6T; -.
DR PDBsum; 2J6U; -.
DR PDBsum; 2JEF; -.
DR PDBsum; 2JEG; -.
DR PDBsum; 2JEI; -.
DR PDBsum; 2JEJ; -.
DR PDBsum; 2R8G; -.
DR PDBsum; 2R8H; -.
DR PDBsum; 2R8I; -.
DR PDBsum; 2RDI; -.
DR PDBsum; 2RDJ; -.
DR PDBsum; 2UVR; -.
DR PDBsum; 2UVU; -.
DR PDBsum; 2UVV; -.
DR PDBsum; 2UVW; -.
DR PDBsum; 2V4Q; -.
DR PDBsum; 2V4R; -.
DR PDBsum; 2V9W; -.
DR PDBsum; 2VA2; -.
DR PDBsum; 2VA3; -.
DR PDBsum; 2W8K; -.
DR PDBsum; 2W8L; -.
DR PDBsum; 2W9A; -.
DR PDBsum; 2W9B; -.
DR PDBsum; 2W9C; -.
DR PDBsum; 2XC9; -.
DR PDBsum; 2XCA; -.
DR PDBsum; 2XCP; -.
DR PDBsum; 3FDS; -.
DR PDBsum; 3GII; -.
DR PDBsum; 3GIJ; -.
DR PDBsum; 3GIK; -.
DR PDBsum; 3GIL; -.
DR PDBsum; 3GIM; -.
DR PDBsum; 3KHG; -.
DR PDBsum; 3KHH; -.
DR PDBsum; 3KHL; -.
DR PDBsum; 3KHR; -.
DR PDBsum; 3M9M; -.
DR PDBsum; 3M9N; -.
DR PDBsum; 3M9O; -.
DR PDBsum; 3PR4; -.
DR PDBsum; 3PR5; -.
DR PDBsum; 3PVX; -.
DR PDBsum; 3PW0; -.
DR PDBsum; 3PW2; -.
DR PDBsum; 3PW4; -.
DR PDBsum; 3PW5; -.
DR PDBsum; 3PW7; -.
DR PDBsum; 3QZ7; -.
DR PDBsum; 3QZ8; -.
DR PDBsum; 3RAQ; -.
DR PDBsum; 3RAX; -.
DR PDBsum; 3RB0; -.
DR PDBsum; 3RB3; -.
DR PDBsum; 3RB4; -.
DR PDBsum; 3RB6; -.
DR PDBsum; 3RBD; -.
DR PDBsum; 3RBE; -.
DR PDBsum; 3T5H; -.
DR PDBsum; 3T5J; -.
DR PDBsum; 3T5K; -.
DR PDBsum; 3T5L; -.
DR PDBsum; 3V6H; -.
DR PDBsum; 3V6J; -.
DR PDBsum; 3V6K; -.
DR PDBsum; 4F4W; -.
DR PDBsum; 4F4X; -.
DR PDBsum; 4F4Y; -.
DR PDBsum; 4F4Z; -.
DR PDBsum; 4F50; -.
DR PDBsum; 4FBT; -.
DR PDBsum; 4FBU; -.
DR PDBsum; 4G3I; -.
DR PDBsum; 4GC6; -.
DR PDBsum; 4GC7; -.
DR PDBsum; 4JUZ; -.
DR PDBsum; 4JV0; -.
DR PDBsum; 4JV1; -.
DR PDBsum; 4JV2; -.
DR PDBsum; 4QW8; -.
DR PDBsum; 4QW9; -.
DR PDBsum; 4QWA; -.
DR PDBsum; 4QWB; -.
DR PDBsum; 4QWC; -.
DR PDBsum; 4QWD; -.
DR PDBsum; 4QWE; -.
DR PDBsum; 4RUA; -.
DR PDBsum; 4RUC; -.
DR PDBsum; 4RZR; -.
DR PDBsum; 4TQR; -.
DR PDBsum; 4TQS; -.
DR PDBsum; 5EDW; -.
DR PDBsum; 6L84; -.
DR PDBsum; 6L97; -.
DR PDBsum; 6VG6; -.
DR PDBsum; 6VGM; -.
DR PDBsum; 6VKP; -.
DR PDBsum; 6VNP; -.
DR PDBsum; 7KLE; -.
DR PDBsum; 7KLF; -.
DR AlphaFoldDB; Q97W02; -.
DR BMRB; Q97W02; -.
DR SMR; Q97W02; -.
DR DIP; DIP-48855N; -.
DR IntAct; Q97W02; 1.
DR STRING; 273057.SSO2448; -.
DR EnsemblBacteria; AAK42588; AAK42588; SSO2448.
DR GeneID; 44128166; -.
DR KEGG; sso:SSO2448; -.
DR PATRIC; fig|273057.12.peg.2526; -.
DR eggNOG; arCOG04582; Archaea.
DR HOGENOM; CLU_012348_1_2_2; -.
DR InParanoid; Q97W02; -.
DR OMA; CKPDGLL; -.
DR PhylomeDB; Q97W02; -.
DR BRENDA; 2.7.7.7; 6163.
DR EvolutionaryTrace; Q97W02; -.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006261; P:DNA-templated DNA replication; IEA:UniProtKB-UniRule.
DR GO; GO:0042276; P:error-prone translesion synthesis; IBA:GO_Central.
DR CDD; cd03586; PolY_Pol_IV_kappa; 1.
DR Gene3D; 3.30.1490.100; -; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR HAMAP; MF_01113; DNApol_IV; 1.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR036775; DNA_pol_Y-fam_lit_finger_sf.
DR InterPro; IPR017961; DNA_pol_Y-fam_little_finger.
DR InterPro; IPR022880; DNApol_IV.
DR InterPro; IPR024728; PolY_HhH_motif.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR001126; UmuC.
DR Pfam; PF00817; IMS; 1.
DR Pfam; PF11799; IMS_C; 1.
DR Pfam; PF11798; IMS_HHH; 1.
DR SUPFAM; SSF100879; SSF100879; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS50173; UMUC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA damage; DNA repair; DNA replication;
KW DNA-binding; DNA-directed DNA polymerase; Magnesium; Metal-binding;
KW Mutator protein; Nucleotidyltransferase; Reference proteome; Transferase.
FT CHAIN 1..352
FT /note="DNA polymerase IV"
FT /id="PRO_0000173976"
FT DOMAIN 3..187
FT /note="UmuC"
FT ACT_SITE 106
FT BINDING 7
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 105
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT SITE 12
FT /note="Substrate discrimination"
FT MUTAGEN 105..106
FT /note="DE->AA: Loss of function."
FT /evidence="ECO:0000269|PubMed:11595188"
FT MUTAGEN 342..352
FT /note="Missing: Almost complete loss of interaction with
FT PCNA."
FT /evidence="ECO:0000269|PubMed:19054331"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:4TQR"
FT HELIX 11..19
FT /evidence="ECO:0007829|PDB:4TQR"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:4TQR"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:6L97"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:4TQR"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:1JX4"
FT TURN 38..40
FT /evidence="ECO:0007829|PDB:3KHH"
FT STRAND 42..46
FT /evidence="ECO:0007829|PDB:4TQR"
FT HELIX 48..51
FT /evidence="ECO:0007829|PDB:4TQR"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:4TQR"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:2W9B"
FT HELIX 61..67
FT /evidence="ECO:0007829|PDB:4TQR"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:4TQR"
FT HELIX 78..93
FT /evidence="ECO:0007829|PDB:4TQR"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:4TQR"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:4TQR"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:4TQR"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:4QWC"
FT HELIX 118..136
FT /evidence="ECO:0007829|PDB:4TQR"
FT STRAND 140..147
FT /evidence="ECO:0007829|PDB:4TQR"
FT HELIX 148..158
FT /evidence="ECO:0007829|PDB:4TQR"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:4GC7"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:4TQR"
FT HELIX 168..177
FT /evidence="ECO:0007829|PDB:4TQR"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:4TQR"
FT HELIX 188..194
FT /evidence="ECO:0007829|PDB:4TQR"
FT TURN 196..198
FT /evidence="ECO:0007829|PDB:1JX4"
FT HELIX 202..206
FT /evidence="ECO:0007829|PDB:1JX4"
FT HELIX 212..215
FT /evidence="ECO:0007829|PDB:4TQR"
FT HELIX 219..229
FT /evidence="ECO:0007829|PDB:4TQR"
FT STRAND 243..255
FT /evidence="ECO:0007829|PDB:4TQR"
FT HELIX 258..276
FT /evidence="ECO:0007829|PDB:4TQR"
FT STRAND 281..290
FT /evidence="ECO:0007829|PDB:4TQR"
FT TURN 291..293
FT /evidence="ECO:0007829|PDB:2J6S"
FT STRAND 295..301
FT /evidence="ECO:0007829|PDB:4TQR"
FT HELIX 308..325
FT /evidence="ECO:0007829|PDB:4TQR"
FT STRAND 330..340
FT /evidence="ECO:0007829|PDB:4TQR"
FT STRAND 343..346
FT /evidence="ECO:0007829|PDB:2IMW"
SQ SEQUENCE 352 AA; 40193 MW; C0B0AD4B3A3E87D0 CRC64;
MIVLFVDFDY FYAQVEEVLN PSLKGKPVVV CVFSGRFEDS GAVATANYEA RKFGVKAGIP
IVEAKKILPN AVYLPMRKEV YQQVSSRIMN LLREYSEKIE IASIDEAYLD ISDKVRDYRE
AYNLGLEIKN KILEKEKITV TVGISKNKVF AKIAADMAKP NGIKVIDDEE VKRLIRELDI
ADVPGIGNIT AEKLKKLGIN KLVDTLSIEF DKLKGMIGEA KAKYLISLAR DEYNEPIRTR
VRKSIGRIVT MKRNSRNLEE IKPYLFRAIE ESYYKLDKRI PKAIHVVAVT EDLDIVSRGR
TFPHGISKET AYSESVKLLQ KILEEDERKI RRIGVRFSKF IEAIGLDKFF DT
