DPO4_SULAC
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 03-AUG-2022, entry version 102.
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}; OrderedLocusNames=Saci_0554;
OS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS 15157 / NCIMB 11770).
OC Archaea; Crenarchaeota; 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;
CC Evidence={ECO:0000255|HAMAP-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}.
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DR EMBL; CP000077; AAY79949.1; -; Genomic_DNA.
DR RefSeq; WP_011277451.1; NC_007181.1.
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 EnsemblBacteria; AAY79949; AAY79949; Saci_0554.
DR GeneID; 3474616; -.
DR KEGG; sai:Saci_0554; -.
DR PATRIC; fig|330779.12.peg.538; -.
DR eggNOG; arCOG04582; Archaea.
DR HOGENOM; CLU_012348_1_2_2; -.
DR OMA; CKPDGLL; -.
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; 3.30.1490.100; -; 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; 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
