ID DNAE2_RHOP5 Reviewed; 1153 AA.
AC Q07QK9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 93.
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=RPE_1827;
OS Rhodopseudomonas palustris (strain BisA53).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Rhodopseudomonas.
OX NCBI_TaxID=316055;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BisA53;
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., Kim E., Harwood C.S., Oda Y.,
RA Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris BisA53.";
RL Submitted (SEP-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; CP000463; ABJ05775.1; -; Genomic_DNA.
DR AlphaFoldDB; Q07QK9; -.
DR SMR; Q07QK9; -.
DR STRING; 316055.RPE_1827; -.
DR KEGG; rpe:RPE_1827; -.
DR eggNOG; COG0587; Bacteria.
DR HOGENOM; CLU_001600_4_0_5; -.
DR OrthoDB; 9803237at2; -.
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 CDD; cd04485; DnaE_OBF; 1.
DR CDD; cd07434; PHP_PolIIIA_DnaE2; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 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; DnaE2.
DR InterPro; IPR004805; DnaE2/DnaE/PolC.
DR InterPro; IPR029460; DNAPol_HHH.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR InterPro; IPR004013; PHP_dom.
DR InterPro; IPR003141; Pol/His_phosphatase_N.
DR NCBIfam; TIGR00594; polc; 1.
DR PANTHER; PTHR32294; DNA POLYMERASE III SUBUNIT ALPHA; 1.
DR PANTHER; PTHR32294:SF4; ERROR-PRONE DNA POLYMERASE; 1.
DR Pfam; PF07733; DNA_pol3_alpha; 1.
DR Pfam; PF17657; DNA_pol3_finger; 1.
DR Pfam; PF14579; HHH_6; 1.
DR Pfam; PF02811; PHP; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR SMART; SM00481; POLIIIAc; 1.
PE 3: Inferred from homology;
KW Cytoplasm; DNA damage; DNA repair; DNA replication;
KW DNA-directed DNA polymerase; Nucleotidyltransferase; Transferase.
FT CHAIN 1..1153
FT /note="Error-prone DNA polymerase"
FT /id="PRO_1000070596"
FT REGION 1107..1153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1119..1135
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1153 AA; 128709 MW; 85A2C7AC6B3E3148 CRC64;
MTAPRYAEIG VTSNFSFLEG GSHPQEFVQQ ASALGLAAIG IADRNTLAGV VRAYSELDNE
ELFYKPKLLI GARLCFADGT PDILAYPTDR AAYGRLCRLL SAGKLRAGKG ECHLSFADLE
AFTKTSTPSW PGLSRPSTSS SKAVQVSVDA RVKPGHDEAK RAAGESRLLL VLMPPYRFQS
HEITAALTRL TALQGAGVWL ALVPYYRGDD KRRLARLQRI AAAARVPGIA SNDVLYHHES
RRALQDVLTC VRDKTTIDKA GRLLESNAER YLKPTEEMAR LFRADPDAIA ETLRFADRIS
FTLDELKYQY PDEPVPPGKT AQQHLKDLTE QGIAEYFPNG IDAKLRATID KELTIIAHRQ
YAPYFLTVHD IVRYARSQNI LCQGRGSAAN SAVCYVLGIT CVDPTEIDLL FERFVSEERD
EPPDIDVDFE HSRREEVMQY IYRRYGRHRA AIVSTVIHYR PRSAIRDVGK ALGLSEDVTA
ALADTVWGSW GKGLNEMQVR QAGLDPTNPM IVRAIDLATE LIGFPRHLSQ HVGGYVLTQD
RLDEFVPIGN AAMEERTFIE WDKDDIDAVK MMKVDVLALG MLTCIRKGFD LIAQHKGKRY
ELADIKSEDD NEVYKMLQRG ESVGVFQVES RAQMNMLPRL RPRCFYDLVI EVAIVRPGPI
QGDMVHPYLR RRNGQEPVVY PSPAGHAGEA NELKTILGKT LGVPLFQEQA MRIAIEAAHF
TPDEANQLRR AMATFRNVGT IGKFEAKMTG NLVARGYDPV FAQNCFEQIK GFGSYGFPES
HAASFAKLVY VSAWLKHAHP DAFCCALLNS QPMGFYAPAQ IVGDARQNGV EIRGVDVAYS
FSQNTLEERC GQHHAVRLGF RQIDGFRWAD FDEANLWQAR GDAPPEDWGA RIVEAREKSP
FTSLEQFARA TALPKRALIL LADADAFRSL KLDRRAALWA VRRLPDDVPL PLFEVAKARE
QQDENAAPLP LMPLAEHVVA DYQTVRLSLK GHPMQFLRAL FAAEGVNTCR AVSETRRNGR
RARCAGVVLV RQRPGSAKGV VFITLEDETG IANLVVWPAV MEKFRKEVMG ARLLWVEGKI
QASPEGVVHL VAEELVDRSA EMARLSDELI APSASTEREA PLNDDRRDHP DLPAQQIRHP
RNVRILPPSR DFH
//
