DNAE2_BRASO
ID DNAE2_BRASO Reviewed; 1170 AA.
AC A4YRD9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=BRADO2647;
OS Bradyrhizobium sp. (strain ORS 278).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium; unclassified Bradyrhizobium.
OX NCBI_TaxID=114615;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ORS 278;
RX PubMed=17540897; DOI=10.1126/science.1139548;
RA Giraud E., Moulin L., Vallenet D., Barbe V., Cytryn E., Avarre J.-C.,
RA Jaubert M., Simon D., Cartieaux F., Prin Y., Bena G., Hannibal L.,
RA Fardoux J., Kojadinovic M., Vuillet L., Lajus A., Cruveiller S., Rouy Z.,
RA Mangenot S., Segurens B., Dossat C., Franck W.L., Chang W.-S., Saunders E.,
RA Bruce D., Richardson P., Normand P., Dreyfus B., Pignol D., Stacey G.,
RA Emerich D., Vermeglio A., Medigue C., Sadowsky M.;
RT "Legumes symbioses: absence of nod genes in photosynthetic bradyrhizobia.";
RL Science 316:1307-1312(2007).
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; CU234118; CAL76465.1; -; Genomic_DNA.
DR RefSeq; WP_011925673.1; NC_009445.1.
DR AlphaFoldDB; A4YRD9; -.
DR SMR; A4YRD9; -.
DR STRING; 114615.BRADO2647; -.
DR PRIDE; A4YRD9; -.
DR EnsemblBacteria; CAL76465; CAL76465; BRADO2647.
DR KEGG; bra:BRADO2647; -.
DR eggNOG; COG0587; Bacteria.
DR HOGENOM; CLU_001600_4_0_5; -.
DR OMA; NSWPMGF; -.
DR OrthoDB; 561611at2; -.
DR BioCyc; BSP114615:BRADO_RS12425-MON; -.
DR Proteomes; UP000001994; 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..1170
FT /note="Error-prone DNA polymerase"
FT /id="PRO_1000070589"
FT REGION 867..899
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1129..1170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 882..899
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1137..1152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1170 AA; 131983 MW; 73C24A0B6EA41E32 CRC64;
MTPIPYAEIG VTTNFSFLHG GSHPQAYVHQ AAEYGLTAIG IADHNTLAGI VRAYSELSND
QLGYRPKLLY GARLVFTCGT PDILVYPRDR AAYGRLCQLL TRGKRGSDLD KVAKGDCRLA
FEDLFDFIAG QLLVLMPPHR FDEDALGAIL ARLKDSPAEG VWLAGSLLYR GDDRRRLARL
ARLAASAKVP LIATNDVLYH HPQQRMLQDV LTCIREKASI ESIGRRLQAN AERHLKPGHE
MARLFRDHPE AIAETLRFTD RIVFSLDQLK YQYPDEPVPP GKTAQGHLED LTWAGAKTYF
GDKLDDRLRA VLNKELALIA ELNYAHYFLT VHDIVRYARS EGILCQGRGS AANSAVCYVL
GITSVDPTKI DLLFERFISK ERLEPPDIDV DFEHSRREEV MQYVYHRYGR HRAAIIATVI
HYRPRSAIRD VGKALGLTED VTSVLADTVW GSWGDGLSDM QVRQAGLDPH NPMIRRAVEL
ASELITFPRH LSQHVGGYVL TQDRLDSYVP IGNAAMDDRT FIEWDKDDVD ALSMMKVDVL
ALGMLTCIRK SFDLIADHKG RRYVLSDIKS EDDNEVYQML QRGESLGVFQ VESRAQMNML
PRLKPRTFYD LVIEVAIVRP GPIQGDMVHP YLRRRNKLEK VTYPSPSPDH GPSDELYKVL
HKTLGVPLFQ EQAMRIAIEA AKFSPEEANG LRRAMATFRN VGTIGSYEEK MVSNMIARGY
DPAFAKSCFD QIKGFGSYGF PESHAASFAQ LVYVSSWLKY FHPDAFCCAL LNSQPMGFYA
PAQIVGDARK NGVEIRDIDV SHSFADNTLE KTDGEYCAVR LGFRQIDGFR WIDRDEERIR
KLSEAVRKEA LSVSTRSLPA ISPVSFRGAR SANPESRDSG FALRAPRNDN DRQIPLHNDD
REDDWADRII RARQRRPFTS LEDFARDTAL PKRALLLLAD ADAFRSLGLD RRAALWAVRR
LPDDVPLPLF EAAIAREQPD EGAQPLPEMP LPEHVVADYQ TIRLSLKGHP MEFLRRRFAA
EGVLACRDVN DTNDRRRIRC AGVVLVRQRP GSAKGVVFMT LEDETGIANI VVWPKVMETF
RKEVMGARLV LVEGRIQSSP EKVVHLVAER LVDRTADLTL LSDDRLDAIP HGATPAEPLN
DDRRDHTDNP SQRVSHPRNV RILPRSRDFH
