ID   DNAE2_BRADU             Reviewed;        1151 AA.
AC   Q89QU8;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 111.
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=blr3026;
OS   Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS   NBRC 14792 / USDA 110).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium.
OX   NCBI_TaxID=224911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX   PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA   Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA   Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT   "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT   Bradyrhizobium japonicum USDA110.";
RL   DNA Res. 9:189-197(2002).
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; BA000040; BAC48291.1; -; Genomic_DNA.
DR   RefSeq; NP_769666.1; NC_004463.1.
DR   RefSeq; WP_011085810.1; NZ_CP011360.1.
DR   AlphaFoldDB; Q89QU8; -.
DR   SMR; Q89QU8; -.
DR   STRING; 224911.27351284; -.
DR   PRIDE; Q89QU8; -.
DR   EnsemblBacteria; BAC48291; BAC48291; BAC48291.
DR   GeneID; 64022776; -.
DR   KEGG; bja:blr3026; -.
DR   PATRIC; fig|224911.44.peg.2653; -.
DR   eggNOG; COG0587; Bacteria.
DR   HOGENOM; CLU_001600_4_0_5; -.
DR   InParanoid; Q89QU8; -.
DR   OMA; NSWPMGF; -.
DR   PhylomeDB; Q89QU8; -.
DR   Proteomes; UP000002526; 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; 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   Pfam; PF01336; tRNA_anti-codon; 1.
DR   SMART; SM00481; POLIIIAc; 1.
DR   SUPFAM; SSF89550; SSF89550; 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; Reference proteome;
KW   Transferase.
FT   CHAIN           1..1151
FT                   /note="Error-prone DNA polymerase"
FT                   /id="PRO_0000103369"
FT   REGION          1108..1151
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1118..1151
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1151 AA;  129582 MW;  2F0563C7FC4625A7 CRC64;
     MNTPAYAEIG ITTNFSFLRG GSDPRAYVHQ ASILGISAIG IADHNTLAGV VRAYKELDND
     KVLHKPKLLI GARIVFIDGT PDILVYPRDR AAYGRLCQLL TRGKRGDDVT RIEKGECRLT
     FSDLLAFSEG QLLVLTLPHR FEPAQALDVL AKLKATRAEG VWLAASLVHR GDDRRRLARL
     DDLATTAKVQ LLATNEVLYH DPARRPLQDV LTCIREKTTI EAVGRKLEAN AERFLKTPRE
     MSRLFRDFPD AIAETMRFAN KIDFSLDQLR YQYPDEPVPP GKTAQGHLED LTWAGVDKYF
     AGKIDDKLRA TLKKELALIA ELKYAHYFLT VHDIVHYARS QNILCQGRGS AANSAVCYVL
     GITSVDPTKV DLLFERFISK ERLEPPDIDV DFEHSRREEV MQYVYRRYGR HRAAIIATII
     HYRPRSAIRD VGKALGLTED VTAALADTVW GSWGSGLNDM QVKQAGLDPQ NPMINLAVEL
     ATELIEFPRH LSQHVGGYVL TQDRLDTYVP IGNAAMDDRT FIEWDKDDVD ALNMMKVDVL
     ALGMLTCIRK CFDLIDQHKG ERWVLASVPQ DDPKVYDMLC DGESLGVFQV ESRAQMNMLP
     RLKPRTFYDL VIEVAIVRPG PIQGDMVHPY LRRRNGQEKV NYPSPSPEHG PADELYKVLH
     KTKGVPLFQE QAMRIAIEAA KFTSEEANGL RRSMATFRNV GTIGKYEDKL IGNMVARGYD
     PNFARSCFDQ IKGFGSYGFP ESHAASFAQL VYISSWLKYH HPDAFCCGLL NSQPMGFYAP
     AQIVGDARKN GVEVRDIDVS YSFAQNTLEQ GSGKYCAVRL GFRQIDGFHW LDEDEEHLKR
     SLLSFRGAPL GANPESIGPH MPGGMDSGLD AGASPRNDKK EDWANRIVAA RNRRPFTSLE
     DFARDTGLPK RALILLADAD AFRSLGLDRR EALWQVRRLP DDVPLPLFEA ATAREQPDEH
     AKPLPLMPRP EQVVADYQTI RLSLKGHPME FLREMLSRER VVACKDVNHQ NERRRVRCAG
     VVLVRQRPGS ASGVVFMTLE DETGIANVVV WPKIMEQYRK EVMGARLILV EGYIQSSPEK
     VTHLIAQRMV DRSHDLIGLA NDSLTRKHPV PSGDALIEPL NDDRRDHADA PAQKIRHPRN
     VRILPPSRDF H