ID A0A3N4ZL98_9MICO Unreviewed; 1093 AA.
AC A0A3N4ZL98;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=EDD34_2380 {ECO:0000313|EMBL:RPF21745.1};
OS Myceligenerans xiligouense.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC Promicromonosporaceae; Myceligenerans.
OX NCBI_TaxID=253184 {ECO:0000313|EMBL:RPF21745.1, ECO:0000313|Proteomes:UP000280501};
RN [1] {ECO:0000313|EMBL:RPF21745.1, ECO:0000313|Proteomes:UP000280501}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15700 {ECO:0000313|EMBL:RPF21745.1,
RC ECO:0000313|Proteomes:UP000280501};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (NOV-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RPF21745.1}.
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DR EMBL; RKQZ01000001; RPF21745.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N4ZL98; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000280501; 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; cd07431; PHP_PolIIIA; 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}; Reference proteome {ECO:0000313|Proteomes:UP000280501};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01902}.
FT DOMAIN 5..72
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT REGION 483..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1093 AA; 117594 MW; 4D324735A5317F11 CRC64;
MTEYAELHAH SAYSFLDGAS PPEVLAAEGA RLGLRALAIT DHDGLYGVVR FSEAAKHVGL
PTVFGAELHL PAPGPTGPVL DLPTGVPDPR ATHLLVLARG ADGYRSLSSA IGTAHLDAGT
KGAAHYTLGG LGERARGEWL VLTGCRKGAV RRALTGPGTR ADRLDAARRE LDALTDTFGP
AGVAVEITAT GDPRDAGLHE ALALLAAEAG LPLVATTAAH YARPADADLA GALAAVRARS
SLDDMDGFLP GAPVTHLRSG AEMARLHARH PEAVANAARL GAECAFDLDL IAPDLPPHPV
PDGHDEASWL RELTYRGAEE RYGKRPPTPS GTLAARAWEK IDHELRIITE LNFPGYFLVV
HDLVDFCRRR GILCQGRGSA ANSAVCYALG ITAVDAVRHG LLFERFLAPE RDGPPDIDLD
IESVRREEVI QYVYERFGRT HAAQVANVIT YRPRSAVRDA SRALGYDAGQ ADAWSRSIER
WGGLKPEADP APAPGGRTRT DDTHDVVPRH APPSAAEEGR IPSDVIDLAD RMLRLPRHLG
IHSGGMVMCD RPVIEVCPVE WARMDGRTVL QWDKEDCADA GLVKFDLLGL GMLTAIRYAF
EQIAEHTGER LTLHGLPPED ERVYDLLCAA DTVGVFQVES RAQMATLPRL RPRTFYDIVV
EVALIRPGPI QGGSVHPYIE RAQARARGER EIQYPHPLLE NSLRRTLGVP LFQEQLMQMA
IDVAGFTPAE SDRLRRAMGS KRSLERMEAL RARLYAGMAE RGIPEPVRDE IYEKLKAFAD
FGFPESHAYS FAYLVYASAW LKVHHPAAFY AGLLAAQPMG FYSPQSLVAD ARRHGLRVLR
PDVNASRALA CVERTGDDGD RALAVRMGLA EVRGIGEELA EKIVAARAGG FAGLRDLVRG
VDLSTAQLEA LATAGALESL GLTRREALWE AGALGQEGPA TLPGVSGGTE APLLPEMAET
EVVRADAWAT GVTPDSYPTQ YVRDGLTAAG VRTVAEVTAT EPGRRVAVGG VVTHRQRPGT
AGGVTFLSLE DETGLLNVIC TPGLWRRFRQ VARSAPAMVV RGRVESADGA VNLLAEHLAP
LSLTAVGRSR DFR
//
