ID DPO4_SULAC Reviewed; 354 AA. AC Q4JB80; DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot. DT 02-AUG-2005, sequence version 1. DT 27-MAR-2024, entry version 110. DE RecName: Full=DNA polymerase IV {ECO:0000255|HAMAP-Rule:MF_01113}; DE Short=Pol IV {ECO:0000255|HAMAP-Rule:MF_01113}; DE EC=2.7.7.7 {ECO:0000255|HAMAP-Rule:MF_01113}; GN Name=dbh {ECO:0000255|HAMAP-Rule:MF_01113}; GN OrderedLocusNames=Saci_0554; OS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC OS 15157 / NCIMB 11770). OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae; OC Sulfolobus. OX NCBI_TaxID=330779; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770; RX PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005; RA Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E., RA Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.; RT "The genome of Sulfolobus acidocaldarius, a model organism of the RT Crenarchaeota."; RL J. Bacteriol. 187:4992-4999(2005). 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. {ECO:0000255|HAMAP-Rule:MF_01113}. 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; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01113}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01113}; CC Note=Binds 2 magnesium ions per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01113}; CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01113}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01113}. CC -!- SIMILARITY: Belongs to the DNA polymerase type-Y family. CC {ECO:0000255|HAMAP-Rule:MF_01113}. 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; CP000077; AAY79949.1; -; Genomic_DNA. DR RefSeq; WP_011277451.1; NZ_CP046615.1. DR PDB; 3BQ0; X-ray; 2.60 A; A=1-354. DR PDB; 3BQ1; X-ray; 2.70 A; A=1-354. DR PDB; 3BQ2; X-ray; 2.70 A; A=1-354. DR PDB; 4F4W; X-ray; 1.90 A; A/B=1-231. DR PDB; 4F4X; X-ray; 2.05 A; A=1-231. DR PDB; 4F4Y; X-ray; 2.34 A; A/B=1-354. DR PDB; 4F4Z; X-ray; 2.30 A; A/B=248-354. DR PDB; 4F50; X-ray; 2.22 A; A=1-246. DR PDB; 4HYK; X-ray; 2.80 A; A=1-354. DR PDB; 4NLG; X-ray; 2.40 A; A=1-354. DR PDBsum; 3BQ0; -. DR PDBsum; 3BQ1; -. DR PDBsum; 3BQ2; -. DR PDBsum; 4F4W; -. DR PDBsum; 4F4X; -. DR PDBsum; 4F4Y; -. DR PDBsum; 4F4Z; -. DR PDBsum; 4F50; -. DR PDBsum; 4HYK; -. DR PDBsum; 4NLG; -. DR AlphaFoldDB; Q4JB80; -. DR SMR; Q4JB80; -. DR STRING; 330779.Saci_0554; -. DR GeneID; 78440899; -. DR KEGG; sai:Saci_0554; -. DR PATRIC; fig|330779.12.peg.538; -. DR eggNOG; arCOG04582; Archaea. DR HOGENOM; CLU_012348_1_2_2; -. DR BRENDA; 2.7.7.7; 6160. DR EvolutionaryTrace; Q4JB80; -. DR Proteomes; UP000001018; 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; 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; 3.30.70.270; -; 2. DR Gene3D; 3.40.1170.60; -; 1. DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1. DR Gene3D; 3.30.1490.100; DNA polymerase, Y-family, little finger domain; 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; IPR022880; DNApol_IV. DR InterPro; IPR024728; PolY_HhH_motif. DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase. DR InterPro; IPR001126; UmuC. DR PANTHER; PTHR11076:SF33; DNA POLYMERASE KAPPA; 1. DR PANTHER; PTHR11076; DNA REPAIR POLYMERASE UMUC / TRANSFERASE FAMILY MEMBER; 1. DR Pfam; PF00817; IMS; 1. DR Pfam; PF11798; IMS_HHH; 1. DR SUPFAM; SSF56672; DNA/RNA polymerases; 1. DR SUPFAM; SSF100879; Lesion bypass DNA polymerase (Y-family), little finger domain; 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..354 FT /note="DNA polymerase IV" FT /id="PRO_0000173974" FT DOMAIN 3..188 FT /note="UmuC" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01113" FT ACT_SITE 106 FT /evidence="ECO:0000255|HAMAP-Rule:MF_01113" FT BINDING 7 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01113" FT BINDING 105 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01113" FT SITE 12 FT /note="Substrate discrimination" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01113" FT STRAND 3..8 FT /evidence="ECO:0007829|PDB:4F4W" FT HELIX 11..19 FT /evidence="ECO:0007829|PDB:4F4W" FT HELIX 21..23 FT /evidence="ECO:0007829|PDB:4F4W" FT STRAND 28..33 FT /evidence="ECO:0007829|PDB:4F4W" FT STRAND 35..39 FT /evidence="ECO:0007829|PDB:4F4W" FT STRAND 41..46 FT /evidence="ECO:0007829|PDB:4F4W" FT HELIX 48..51 FT /evidence="ECO:0007829|PDB:4F4W" FT TURN 52..54 FT /evidence="ECO:0007829|PDB:4F4W" FT HELIX 61..67 FT /evidence="ECO:0007829|PDB:4F4W" FT STRAND 71..75 FT /evidence="ECO:0007829|PDB:4F4W" FT HELIX 78..93 FT /evidence="ECO:0007829|PDB:4F4W" FT STRAND 97..103 FT /evidence="ECO:0007829|PDB:4F4W" FT STRAND 106..110 FT /evidence="ECO:0007829|PDB:4F4W" FT TURN 112..117 FT /evidence="ECO:0007829|PDB:4F4W" FT HELIX 119..137 FT /evidence="ECO:0007829|PDB:4F4W" FT STRAND 141..148 FT /evidence="ECO:0007829|PDB:4F4W" FT HELIX 149..159 FT /evidence="ECO:0007829|PDB:4F4W" FT STRAND 164..166 FT /evidence="ECO:0007829|PDB:4F4W" FT HELIX 169..171 FT /evidence="ECO:0007829|PDB:4F4W" FT HELIX 172..178 FT /evidence="ECO:0007829|PDB:4F4W" FT HELIX 181..183 FT /evidence="ECO:0007829|PDB:4F4W" FT HELIX 189..197 FT /evidence="ECO:0007829|PDB:4F4W" FT HELIX 203..208 FT /evidence="ECO:0007829|PDB:4F4W" FT HELIX 211..218 FT /evidence="ECO:0007829|PDB:4F4W" FT HELIX 220..230 FT /evidence="ECO:0007829|PDB:4F4W" FT STRAND 240..242 FT /evidence="ECO:0007829|PDB:4F50" FT STRAND 249..256 FT /evidence="ECO:0007829|PDB:4F4Z" FT HELIX 259..276 FT /evidence="ECO:0007829|PDB:4F4Z" FT STRAND 278..280 FT /evidence="ECO:0007829|PDB:3BQ1" FT STRAND 282..290 FT /evidence="ECO:0007829|PDB:4F4Z" FT STRAND 295..301 FT /evidence="ECO:0007829|PDB:4F4Z" FT HELIX 308..325 FT /evidence="ECO:0007829|PDB:4F4Z" FT STRAND 327..329 FT /evidence="ECO:0007829|PDB:4HYK" FT STRAND 331..340 FT /evidence="ECO:0007829|PDB:4F4Z" 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 //