ID A0A1I3DL07_9BURK Unreviewed; 1049 AA.
AC A0A1I3DL07;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Error-prone DNA polymerase {ECO:0000256|ARBA:ARBA00017273, ECO:0000256|HAMAP-Rule:MF_01902};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417, ECO:0000256|HAMAP-Rule:MF_01902};
GN Name=dnaE2 {ECO:0000256|HAMAP-Rule:MF_01902};
GN ORFNames=SAMN05192543_101387 {ECO:0000313|EMBL:SFH87424.1};
OS Paraburkholderia megapolitana.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=420953 {ECO:0000313|EMBL:SFH87424.1, ECO:0000313|Proteomes:UP000199548};
RN [1] {ECO:0000313|EMBL:SFH87424.1, ECO:0000313|Proteomes:UP000199548}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 23650 {ECO:0000313|EMBL:SFH87424.1,
RC ECO:0000313|Proteomes:UP000199548};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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:0000256|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;
CC Evidence={ECO:0000256|ARBA:ARBA00024632, ECO:0000256|HAMAP-
CC Rule:MF_01902};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_01902}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-C family. DnaE2
CC subfamily. {ECO:0000256|ARBA:ARBA00007391, ECO:0000256|HAMAP-
CC Rule:MF_01902}.
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DR EMBL; FOQU01000001; SFH87424.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I3DL07; -.
DR STRING; 420953.SAMN05192543_101387; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000199548; Unassembled WGS sequence.
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; 1.10.150.870; -; 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 {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01902};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW Rule:MF_01902};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW Rule:MF_01902};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW Rule:MF_01902};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW ECO:0000256|HAMAP-Rule:MF_01902};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_01902}; Reference proteome {ECO:0000313|Proteomes:UP000199548};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01902}.
FT DOMAIN 12..79
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1049 AA; 116686 MW; BC5A23F00C4782B1 CRC64;
MNPVARPLPA YAELFCLSNF SFLHGASHAD ELVARAVQLG YAGLAITDEC SLAGAVRAHI
AAETAKLPLV IGSYFRLVHA DGSPAFGLIL LAQNREGYGN LSELITLART RAPKGQYRLT
PQDLSRPDPQ YGHLRGMPDC LAILVPEFPA QEERLDAQIE WLDETFPGRA WCGLILHQRA
MDDIHRGALE YVSQQHGVPV VALGHVVMHV RSRKPLQDTM TAIRVGRPVH ECGYDLAPNA
EQHLRARLRL ALLYPEAALE QTLAVMARCT FSLREVRYEY PDELIPDGFT PTSWLRQETY
VGAHARFPSG IPYDVQEKLE YELDLIASLE YEPFFITVYD IVLYARSQNI LCQGRGSAAN
SLVCFCLGIT EVDPNRSSML FERFISKERG EPPDIDVDFE HQRREEVIQY IYNKYGRDRA
AIAAAVSTYR PRGALRETGK ALGVDPQIVD AVAKTHHWFD SGTELLKRFE ESGLDPSAPI
IQSWASLAAQ LVGFPRHLSQ HSGGFVISRG KLTRLVPVEN AAMAERSVIQ WDKDDLEALG
LLKVDVLALG MLSVIRRALD FVSEQRGERV QMRDIPDGDD PTFDMICKAD TMGVFQIESR
AQMSMLPRLK PRTYYDLVIE VAIVRPGPIQ GGAVHPYLKR RQKLVPVDYP SDKLEAALER
TLGIPIFQEQ VMQVAIIAAG FTPGEADELR RAMAAWKRKG NLQKYYDRIV TGMLARGYER
TFADAIFEQI KGFGEYGFPE SHAASFALLV YASSWLKCHE PEAFLAALLN SMPMGFYSPS
QLVQDAQRHG VKVLPADVTI SGWDASLEAQ GSELRPAVRL GLSLVLGMRD GAAERIENAR
AVRPFTSVID LARRAQLDRH DLHVLADANA LASLAGNRRE ALWQSVAAVP DRDMLAAART
EDETPQLGTP TEAETVVGDY RSVGLTLERH PLELLRPTLH AQRLMPAATL RTYRNGQLAR
ACGIVTGRQR PGTAKGVIFM TIEDETGNVN VIIWPNLLER QRKETLNASL LAVYGTWQCE
GEVRHLIAKR LVDLSHLLGG LATVSRNFH
//
