ID A0A1H3PXE1_9PSEU Unreviewed; 1101 AA.
AC A0A1H3PXE1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=SAMN05216215_104451 {ECO:0000313|EMBL:SDZ05633.1};
OS Saccharopolyspora shandongensis.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharopolyspora.
OX NCBI_TaxID=418495 {ECO:0000313|EMBL:SDZ05633.1, ECO:0000313|Proteomes:UP000199529};
RN [1] {ECO:0000313|EMBL:SDZ05633.1, ECO:0000313|Proteomes:UP000199529}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.3530 {ECO:0000313|EMBL:SDZ05633.1,
RC ECO:0000313|Proteomes:UP000199529};
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; FNOK01000044; SDZ05633.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3PXE1; -.
DR STRING; 418495.SAMN05216215_104451; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000199529; 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};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01902}.
FT DOMAIN 65..132
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT REGION 14..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..44
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1101 AA; 120032 MW; 36CC7904AF16AA11 CRC64;
MSWFNPPQTW SDLEKVLSGR LPPADGSGPR DERHPGDGND SPAWTRRRAR YEADAVAAVA
EVPYAELHAH SNFSFLDGAS HPEELAAEAA RLGLDAIALT DHDGLYGVVR FAEAAAEHGV
RTVFGAELSL GLSVPQNGIP DPEGRHLLVL ARDPAGYASL CRAISEAHLE GKEKGRPVYD
LEKLAGAAAG HWQVLTGCRK GAVPAALAES GPAAAAAELD RLIALFGRDH VTVELTDHGL
PADSARNDAM AELADRAGVS TVAATGAHLA RPDRARLAAV VAAIRARRSL DDMDGWLPGW
AGNYLRSGAE MAEMFARYPG AVQRAAELGR EFAFDLKLVA PKLPPFDVPM GRTEASWLRE
LVLRGALDRY GLPQENPAAY RQIEHELALI EQLEFPGYFL VVSDIVEFCR EQRILCQGRG
SAANSAVCFA LRITNADPVR YQLLFERFLA PERDGPPDID LDIESDRREE VIQYVYRKYG
RMHAAQVANV ISYRPRSAVR DVARALGYSP GQQDAWSKEI EHWGPLPEDS EIPEPVRELA
GELLGFPRHL GIHSGGMVIC HRPVGEVCPV EWARMPGRTV LQWDKDDCAE VGLVKFDLLG
LGMLSALHYA IDMTLEHHGI EVDLGELDLN DDAVYEMLRR ADAVGVFQVE SRAQLATLPR
LKPREFYDLV VEVALIRPGP IQGGSVHPYI RRRNGLEDWD FEHPSMAGAL KKTLGVPLFQ
EQLMQLAVDV AGFSAAEADQ LRRAMGAKRS EERMERLRGR LFEGMAAKGI SGELAERIYQ
RMLAFANYGF PESHALSFAL LVFASAWFKH YYPAVFCAAL LKAQPMGFYS PQSLVADARR
HGVRVRGPDV NASRAQADLE PDADSEGKRA VRLGLASVRK LGESAGERLV MERAENGPYV
DMADVARRTQ LTAAQMEALA TAGAFGCFGL SRREALWNAA AAAGDRPDRL PGTTASAAAP
ALPGMDGVEV AAADVWATGV SPDSFPLQFV RARLDELGAI PADRLSEVEH GSRVLVGGAV
THRQRPATAG GVTFLNLEDE TGMVNVMCSP GLWARYRKVG RTSAALLVRG IVERAEGVIN
LRADRLQKLE VRIPSTSRDF H
//
