ID A0A1Y0EPX2_9BURK Unreviewed; 1245 AA.
AC A0A1Y0EPX2;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Error-prone DNA polymerase {ECO:0000256|HAMAP-Rule:MF_01902};
DE EC=2.7.7.7 {ECO:0000256|HAMAP-Rule:MF_01902};
GN Name=dnaE2 {ECO:0000256|HAMAP-Rule:MF_01902};
GN ORFNames=CCO03_14340 {ECO:0000313|EMBL:ARU05705.1};
OS Comamonas serinivorans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Comamonas.
OX NCBI_TaxID=1082851 {ECO:0000313|EMBL:ARU05705.1, ECO:0000313|Proteomes:UP000196138};
RN [1] {ECO:0000313|EMBL:ARU05705.1, ECO:0000313|Proteomes:UP000196138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26136 {ECO:0000313|EMBL:ARU05705.1,
RC ECO:0000313|Proteomes:UP000196138};
RA Song R., Chenine A.L., Ruprecht R.M.;
RL Submitted (MAY-2017) 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|HAMAP-Rule:MF_01902}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-C family. DnaE2
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01902}.
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DR EMBL; CP021455; ARU05705.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y0EPX2; -.
DR KEGG; cser:CCO03_14340; -.
DR Proteomes; UP000196138; 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 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; IPR004013; PHP_dom.
DR InterPro; IPR003141; Pol/His_phosphatase_N.
DR InterPro; IPR016195; Pol/histidinol_Pase-like.
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 SMART; SM00481; POLIIIAc; 1.
DR SUPFAM; SSF89550; PHP domain-like; 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:UP000196138};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01902}.
FT DOMAIN 26..93
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT REGION 155..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 923..942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 950..979
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 992..1014
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 994..1008
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1245 AA; 135287 MW; CB49132AC032EB88 CRC64;
MDPPLNHLTP TTPVTTPAPD PLPAYAELRC LSNFSFLRGA SHPDELVQRA QALGYRALAL
TDDGSLAGVV RAHVAAKAAG LPLIVGAQFR VQARAPGETP FTLVLLAQTL FGYGNLCAFI
TQLRRAAPKG HYQLTRDQVQ GHALRDCLAL LCPDRQPPAA PDTPGHANRH SSGAAQAWAR
SPGPAAEPTS PADTAQAIES IDPMGPSPAT APPDAAAPAS PLGRQAVQAA DALAELGHWA
LSQFMGRCWI GVDLPRRMDD ALWLHRLREM GMRTALPLVA VGDVHLHVRS RKPLHDVLTA
IRIGQPLTHC GHALQRSAEL HLRSRLRLAQ TFPPELLAET LVVASRCHFS LDEIRYQYPA
EVVPTGTTAL AYLEALTQKG AAERWPDGVP AQVQAQLTRE LGLIGELGYE HYFLTVHDIV
AHARSVHILC QGRGSAANSA VCYCLGITAV NPAQSELLFE RFISKERNEP PDIDVDFEHE
RREEVIQYLY TKYGRDRCAL TATVISYHER SAIRDVGKAL GFDEATLDAI ARQHRRLEGQ
GVQAELLREL GLDVDALAVQ QLMQLVAQIL GFPRHLSQHT GGFVLTQGPL SRLVPIENAA
MRDRTVIQWD KDDLDAAGLL KVDVLALGML TALRRTFDFV AQRRGVRPTL ATLPPDDPAT
YDMICRADTV GVFQIESRAQ MSMLPRLQPR NFYDLVIEVA IVRPGPIQGG MVHPYLRRRQ
GLEKVTYEKP VLQQALARTL GVPIFQEQVM QIAILAAGFS PGEADALRRA MAAWRRTGTL
SKYQQKIIDG MTANGYTPEF AESIFRQIQG FSEYGFPESH AASFAQLVYA SSWLKCHEPA
AFLAALLNSQ PMGFYTPSQL VQDARRHGVR VRPVDVLHSD WDCSLEDLRH PDGPAVRLGL
CQVSGLSQAS GQRIVQARLA AGPTAPTGHA GHGPGSASAT APLDAGVHGL ATQATSSSSD
AEAWRDGQAP EPLASPAGQS AEVCLAQPQQ VFVGHPPADP PEPGGPPPHQ AGRLHASDAT
TTDITHQASQ ADDLPTPSPW PDVEALARSA GLDRREVQLL AAADALRGLA GHRRQQMWAA
AGWHAEPALL HEAPTHEPPL VLPQAPETEA VAWDLAATHL SLRTHPMALL RPRLARWRLR
SSQDLHTAVD GDWVRTAGIV TVRQQPPTAK GTTFVSLEDE FGSLQVIVWR HVRDAQRPIL
QGARLMAVQG RWQREGLVCN LIAHRLADLS ALLAPFATGS SRDFH
//
