ID   DNAE2_RHOPS             Reviewed;        1110 AA.
AC   Q139V1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Error-prone DNA polymerase {ECO:0000255|HAMAP-Rule:MF_01902};
DE            EC=2.7.7.7 {ECO:0000255|HAMAP-Rule:MF_01902};
GN   Name=dnaE2 {ECO:0000255|HAMAP-Rule:MF_01902}; OrderedLocusNames=RPD_1903;
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Pelletier D.A., Kyrpides N., Lykidis A., Oda Y., Harwood C.S.,
RA   Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: DNA polymerase involved in damage-induced mutagenesis and
CC       translesion synthesis (TLS). It is not the major replicative DNA
CC       polymerase. {ECO:0000255|HAMAP-Rule:MF_01902}.
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_01902};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01902}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-C family. DnaE2
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01902}.
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DR   EMBL; CP000283; ABE39138.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q139V1; -.
DR   SMR; Q139V1; -.
DR   STRING; 316057.RPD_1903; -.
DR   PRIDE; Q139V1; -.
DR   EnsemblBacteria; ABE39138; ABE39138; RPD_1903.
DR   KEGG; rpd:RPD_1903; -.
DR   eggNOG; COG0587; Bacteria.
DR   HOGENOM; CLU_001600_4_0_5; -.
DR   OMA; NSWPMGF; -.
DR   OrthoDB; 561611at2; -.
DR   BioCyc; RPAL316057:RPD_RS09555-MON; -.
DR   Proteomes; UP000001818; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.50.140; -; 1.
DR   HAMAP; MF_01902; DNApol_error_prone; 1.
DR   InterPro; IPR011708; DNA_pol3_alpha_NTPase_dom.
DR   InterPro; IPR040982; DNA_pol3_finger.
DR   InterPro; IPR023073; DNA_pol_error_prone.
DR   InterPro; IPR029460; DNAPol_HHH.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR004365; NA-bd_OB_tRNA.
DR   InterPro; IPR003141; Pol/His_phosphatase_N.
DR   InterPro; IPR004805; PolC_alpha.
DR   PANTHER; PTHR32294; PTHR32294; 1.
DR   PANTHER; PTHR32294:SF4; PTHR32294:SF4; 1.
DR   Pfam; PF07733; DNA_pol3_alpha; 1.
DR   Pfam; PF17657; DNA_pol3_finger; 1.
DR   Pfam; PF14579; HHH_6; 1.
DR   Pfam; PF01336; tRNA_anti-codon; 1.
DR   SMART; SM00481; POLIIIAc; 1.
DR   TIGRFAMs; TIGR00594; polc; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; DNA damage; DNA repair; DNA replication;
KW   DNA-directed DNA polymerase; Nucleotidyltransferase; Transferase.
FT   CHAIN           1..1110
FT                   /note="Error-prone DNA polymerase"
FT                   /id="PRO_1000070597"
FT   REGION          1072..1110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1075..1110
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1110 AA;  123650 MW;  CC1D06567E5E3390 CRC64;
     MKVPAYAEIG VTTNFSFLEG GSHPQDYVHE ASRLGLEAIG IADRNTLAGV VRAYSELGNE
     DLIHKPRLLI GARLVFADGT PDVLAYPVDR AAYGRLCRLL SVGKLRGAKG ECHLAVADLE
     AFSQGLSLVL MPPYRFQASA IAAALQRLTA LESGGVWLGL TPYYRGDDKR RLARLKRVAW
     AARVPGIATN DVLYHHPERR ALQDVLSCVR EKTTIDKIGR RLEANAERHL KPAAEMARLF
     RADPDAIAET LRFAAGISFT LDELKYHYPD EPVPPGKTAQ QHLEDLTWEG VAEYFPAGIS
     DKLHATIDKE LGIIAHRGYA QYFLTVHDIV RYARSQDILC QGRGSAANSA VCYVLGITCV
     DPTEIDLLFE RFVSEERDEP PDIDVDFEHS RREEVMQYIY RRYGRHRAAI VATVIHYRPR
     SAIRDVGKAL GLSEDVTAAL ADTVWGSWGK GLNEMQVKQA GLDPHNPLIG RAVELATELI
     GFPRHLSQHV GGYVLTQDRL DSYVPIGNAA MEGRTFIEWD KDDIDAIKMM KVDVLALGML
     TCIRKGFDLI AQHKGVRYAL SDIKSEDDNA VYQMLQRGES IGVFQVESRA QMNMLPRLKP
     KCFYDLVIEV AIVRPGPIQG DMVHPYLRRR NKQEPVVYPA PAGHAGDANE LEVILGKTLG
     VPLFQEQAMR IAIEAAHFTP DEANQLRRAM ATFRNVGTIG KFESKMVGNL VARGYDPVFA
     KNCFEQIKGF GSYGFPESHA ASFAKLVYVS AWMKCEHPDA FCCALLNSQP MGFYAPAQIV
     GDARANEVEV RPVDVSFSDG QCTLEERCGK HHAVRLGFRQ IDGFVWADPD EERVRREAGL
     LPSEDWAARI VAARARGPFN SLERFARLTA LPKRALILLA DADAFRSLGL DRRAALWAVR
     RLPDDVPLPL FEAASASEQL DENAAPLPQM PTAEHVVADY QTVRLSLKGH PMEFLRPLFA
     AERVVTCRSI SESRVSGQRM RCAGVVLVRQ RPGSAKGVVF ITLEDETGIA NLVVWPAVME
     TFRKEVMGAR LLWVEGRIQA SPEGVVHLVA ERLSDRSFEM TRLSDNLAAP RLGELHEPLN
     DDRREHPDNP AQRIRHPRDV RILPPSRDFH