ID   DNAE2_COREF             Reviewed;        1073 AA.
AC   Q8FRX6;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 106.
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=CE0632;
OS   Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189
OS   / NBRC 100395).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=196164;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
RX   PubMed=12840036; DOI=10.1101/gr.1285603;
RA   Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S.,
RA   Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.;
RT   "Comparative complete genome sequence analysis of the amino acid
RT   replacements responsible for the thermostability of Corynebacterium
RT   efficiens.";
RL   Genome Res. 13:1572-1579(2003).
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; BA000035; BAC17442.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8FRX6; -.
DR   SMR; Q8FRX6; -.
DR   STRING; 196164.23492469; -.
DR   PRIDE; Q8FRX6; -.
DR   EnsemblBacteria; BAC17442; BAC17442; BAC17442.
DR   KEGG; cef:CE0632; -.
DR   eggNOG; COG0587; Bacteria.
DR   HOGENOM; CLU_001600_4_0_11; -.
DR   OMA; NSWPMGF; -.
DR   Proteomes; UP000001409; 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:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
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; IPR004013; PHP_dom.
DR   InterPro; IPR003141; Pol/His_phosphatase_N.
DR   InterPro; IPR016195; Pol/histidinol_Pase-like.
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; PF02811; PHP; 1.
DR   SMART; SM00481; POLIIIAc; 1.
DR   SUPFAM; SSF89550; SSF89550; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; DNA damage; DNA repair; DNA replication;
KW   DNA-directed DNA polymerase; Nucleotidyltransferase; Reference proteome;
KW   Transferase.
FT   CHAIN           1..1073
FT                   /note="Error-prone DNA polymerase"
FT                   /id="PRO_0000103377"
FT   REGION          41..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1073 AA;  116229 MW;  827F8754ED71EE32 CRC64;
     MVGMEWDTGA RGLTGRPLPW SMVEGILSGR EVGTPRPVLH EAEPECLSTP RPGPGSTEVP
     GERRGSRQGE RSGEIPFVEL HATSSYNFLA GASDPGEMVD RAHELGLSAL ALVDRDGLYG
     AVRFAEAAAE VGLATVFGAE LSLREGVLTV LCRGVEGYRR LSHLITGAAM SAGEKGSVDY
     PLLPQVAEQG AGHWVVLAGV EWQKKIDHLI ECFGRDNVVL EFPARMLPED TDHHDILRSI
     QTRTGLRGIL STMPTAATRD HVRLAGAKCA LALRANLAEA ESSLHPMGGT WLRSGGALAR
     AYPQCGDLLA TTVEIASGCA FTFDLVAPEL PRWDTPDGHT EMTWLTHLVE SRFDRRYRSR
     PAEVRERARA QIRHELGVIE QLGFPGYFLI VDDLVQFCHN ATILCQGRGS AANSAVCFVL
     GITNAEPITA GLLFERFLSR DRDGPPDIDI DIESGRREEV IQYVYTRYGR DNAAQVANVI
     TYRTKGALRD AARALGYPQG TVDAWSRGAS EPPADVVELA GQLKGQPRHL GIHSGGMVIC
     DRPIADVVPT EWARMEGRSV VQWDKDDCAA AGLVKFDLLG LGMLEALHHM MDLVAHHRGI
     TVNLWELDLA DAGVYDMLCR ADAVGVFQVE SRAQMSTLPR LKPRTFFDLV VEVALIRPGP
     IQGGSVHPYL RRRSGEEAVT YDHPVLEKSL GKTLGIPLFQ EQIMQIAVDA AGFTGGEADA
     LRRAMGSKRS PTRMAALRSR FYQGLADTHG IIGDTADKLW NKMVAFAAYG FPESHSQSFA
     TLVYFSAWFK HHYPAEFCAG LLRAQPMGFY SPQSLIADAR RHGVEILPIS INESGVQADA
     PDGHLRLGLD LVKGLGEEAA RRIAEHAPYT SIPDLSRRAD LGVAHIEALA RAGALDCLGV
     GRREALWQAG IAATERPGML PGISAIEAPA LPGMSAFELM ATSIAATGVT HDAQPMALLR
     AHLDALGVVP ADRLLTDVAD GTRVRIAGVV THRQRPQTAS GVTFLGLEDE TGLMNVMVSP
     GLWDRQRVLA RTAKTLIIRG IVQNATGAVN VVADKLEPLP VGEWLSRGSR DFR