DPO4_SACSO
ID DPO4_SACSO Reviewed; 354 AA.
AC P96022;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=DNA polymerase IV;
DE Short=Pol IV;
DE EC=2.7.7.7;
GN Name=dbh;
OS Saccharolobus solfataricus (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=2287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 35091 / DSM 1616 / JCM 8930 / NBRC 15331 / P1;
RX PubMed=8876701; DOI=10.1016/0027-5107(96)00164-9;
RA Kulaeva O.I., Koonin E.V., McDonald J.P., Randall S.K., Rabinovich N.,
RA Connaughton J.F., Levine A.S., Woodgate R.;
RT "Identification of a DinB/UmuC homolog in the archeon Sulfolobus
RT solfataricus.";
RL Mutat. Res. 357:245-253(1996).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 2-216.
RC STRAIN=ATCC 35091 / DSM 1616 / JCM 8930 / NBRC 15331 / P1;
RX PubMed=11545744; DOI=10.1016/s1097-2765(01)00310-0;
RA Zhou B.-L., Pata J.D., Steitz T.A.;
RT "Crystal structure of a DinB lesion bypass DNA polymerase catalytic
RT fragment reveals a classic polymerase catalytic domain.";
RL Mol. Cell 8:427-437(2001).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX PubMed=11685247; DOI=10.1038/nsb1101-984;
RA Silvian L.F., Toth E.A., Pham P., Goodman M.F., Ellenberger T.;
RT "Crystal structure of a DinB family error-prone DNA polymerase from
RT Sulfolobus solfataricus.";
RL Nat. Struct. Biol. 8:984-989(2001).
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. May be 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 -!- SUBUNIT: Monomer.
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. It
CC lacks the O helices present in high-fidelity DNA polymerases in the
CC fingers domain.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-Y family. {ECO:0000305}.
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DR EMBL; U52110; AAB38090.1; -; Genomic_DNA.
DR PIR; T46875; T46875.
DR PDB; 1IM4; X-ray; 2.30 A; A=2-216.
DR PDB; 1K1Q; X-ray; 2.80 A; A/B=1-354.
DR PDB; 1K1S; X-ray; 2.80 A; A=1-354.
DR PDBsum; 1IM4; -.
DR PDBsum; 1K1Q; -.
DR PDBsum; 1K1S; -.
DR AlphaFoldDB; P96022; -.
DR SMR; P96022; -.
DR BRENDA; 2.7.7.7; 6163.
DR EvolutionaryTrace; P96022; -.
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; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:0006261; P:DNA-templated DNA replication; IEA:UniProtKB-UniRule.
DR CDD; cd03586; PolY_Pol_IV_kappa; 1.
DR Gene3D; 3.30.1490.100; -; 1.
DR Gene3D; 3.30.70.270; -; 2.
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; 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; 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; Transferase.
FT CHAIN 1..354
FT /note="DNA polymerase IV"
FT /id="PRO_0000173975"
FT DOMAIN 3..188
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 STRAND 3..8
FT /evidence="ECO:0007829|PDB:1IM4"
FT HELIX 11..19
FT /evidence="ECO:0007829|PDB:1IM4"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:1IM4"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:1K1Q"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:1IM4"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:1IM4"
FT HELIX 48..51
FT /evidence="ECO:0007829|PDB:1IM4"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:1IM4"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:1K1Q"
FT HELIX 61..67
FT /evidence="ECO:0007829|PDB:1IM4"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:1IM4"
FT HELIX 78..93
FT /evidence="ECO:0007829|PDB:1IM4"
FT STRAND 97..103
FT /evidence="ECO:0007829|PDB:1IM4"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:1IM4"
FT TURN 112..117
FT /evidence="ECO:0007829|PDB:1IM4"
FT HELIX 119..137
FT /evidence="ECO:0007829|PDB:1IM4"
FT STRAND 141..148
FT /evidence="ECO:0007829|PDB:1IM4"
FT HELIX 149..158
FT /evidence="ECO:0007829|PDB:1IM4"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:1IM4"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:1IM4"
FT HELIX 172..177
FT /evidence="ECO:0007829|PDB:1IM4"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:1IM4"
FT HELIX 189..197
FT /evidence="ECO:0007829|PDB:1IM4"
FT HELIX 203..208
FT /evidence="ECO:0007829|PDB:1K1Q"
FT HELIX 211..215
FT /evidence="ECO:0007829|PDB:1K1Q"
FT HELIX 221..231
FT /evidence="ECO:0007829|PDB:1K1Q"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:1K1Q"
FT STRAND 246..250
FT /evidence="ECO:0007829|PDB:1K1Q"
FT TURN 260..263
FT /evidence="ECO:0007829|PDB:1K1Q"
FT HELIX 264..275
FT /evidence="ECO:0007829|PDB:1K1Q"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:1K1Q"
FT STRAND 281..293
FT /evidence="ECO:0007829|PDB:1K1Q"
FT STRAND 295..301
FT /evidence="ECO:0007829|PDB:1K1Q"
FT HELIX 308..322
FT /evidence="ECO:0007829|PDB:1K1Q"
FT TURN 323..325
FT /evidence="ECO:0007829|PDB:1K1Q"
FT STRAND 331..342
FT /evidence="ECO:0007829|PDB:1K1Q"
SQ SEQUENCE 354 AA; 39986 MW; 0EDDAEB0F30EAD35 CRC64;
MIVIFVDFDY FFAQVEEVLN PQYKGKPLVV CVYSGRTKTS GAVATANYEA RKLGVKAGMP
IIKAMQIAPS AIYVPMRKPI YEAFSNRIMN LLNKHADKIE VASIDEAYLD VTNKVEGNFE
NGIELARKIK QEILEKEKIT VTVGVAPNKI LAKIIADKSK PNGLGVIRPT EVQDFLNELD
IDEIPGIGSV LARRLNELGI QKLRDILSKN YNELEKITGK AKALYLLKLA QNKYSEPVEN
KSKIPHGRYL TLPYNTRDVK VILPYLKKAI NEAYNKVNGI PMRITVIAIM EDLDILSKGK
KFKHGISIDN AYKVAEDLLR ELLVRDKRRN VRRIGVKLDN IIINKTNLSD FFDI
