ID A0A2S0N2N0_9BURK Unreviewed; 1048 AA.
AC A0A2S0N2N0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=C6571_14870 {ECO:0000313|EMBL:AVO42400.1};
OS Simplicispira suum.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Simplicispira.
OX NCBI_TaxID=2109915 {ECO:0000313|EMBL:AVO42400.1, ECO:0000313|Proteomes:UP000239326};
RN [1] {ECO:0000313|EMBL:AVO42400.1, ECO:0000313|Proteomes:UP000239326}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC1-8 {ECO:0000313|EMBL:AVO42400.1,
RC ECO:0000313|Proteomes:UP000239326};
RA Kim S.-J., Heo J., Kwon S.-W.;
RT "Genome sequencing of Simplicispira sp.";
RL Submitted (MAR-2018) 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; CP027669; AVO42400.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S0N2N0; -.
DR KEGG; simp:C6571_14870; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000239326; 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 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 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 Pfam; PF01336; tRNA_anti-codon; 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};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01902}.
FT DOMAIN 16..83
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1048 AA; 117131 MW; A3D755AC8C0CAC03 CRC64;
MATRTPPGAH ALPAYAELQC LSNFSFLRGA SRPEELVERA KALGYSALAM TDECSMAGVV
RAHVAAKELG LALVLGSQFC IGPADADTDV KEPACTLVVL AQNMNGYGNL CAFITRLRRA
SEKGTYRATM HDVTGAALAD CLVLLCLGRA SSDGELQQLG RWALQEFTGR CWIGVEQLRQ
IDDELWLHRM RELSALTALP LVAVGDVHMH VRSRKPLHDV LTATRIGKPL TECGDALERS
AERHLRSRLR LAQTFPAELL QETLRVAARC SFSLDELRYQ YPDEVVPPDH TATSYLRQAT
YEGAGRRWPA GIPTKVQEQI EYELDLICEL KYEPYFLTVY DIVVFARSRH ILCQGRGSAA
NSVVCYCLGV TEVDPARMSV LFERFISRER NEPPDIDIDF EHQRREEVIQ YLYNKYGRDR
AALTAAVITY RPRSAIRDVG KALGFDLETV DAIAKGQQWF DGKQVRRERF EELGMEPESL
AVRQLVELTG QLIGFPRHLS QHTGGFVLTR DLLCRMVPVE NASMPDRTVI QWDKDDLDAA
GLLKVDVLAL GMLSALRRAL DFISDRRGYA FGMQDIPADD SATFDMICKA DTVGVFQIES
RAQMGMLPRH RPRCFYDLVI QVAIVRPGPI QGGMVHPYLN RRQGKEPVVY PSKDLELALG
RTLGVPVFQE QVMQVAILAA GFTPGEADGL RRAMAAWKRK GGLEKYYSKI VDGMTARGYE
QSFAESIFEQ IKGFSEYGFP ESHSASFALL VYASSWIKCH EPAAFLAALL NSQPLGFYSP
SQLVQDARRH DVQVRPVDVM RSDVDSSLED LPEVPVVRLG LHMVRGLQSR SAERIVQERS
RAPFDSAEDL ARRCHLELHE MKLLAAAGAL QSLAGHRRQQ VWEAAALHAV PELLHDAPVD
EEVLELEEAK EGEEVLWDFA SVGLTLRSHP MALLRARLER YRLRTSEQLR QVPDGRIVRT
AGIVTVRQQP QTAGGTVFVS LEDECGSIQV IVWRGVREAQ REVLLGARLL AVKGRWQREG
EVCNLIAEKL ADLSPLLGRL ATQSRDFR
//
