ID A0A1H4ILQ0_9PSEU Unreviewed; 1101 AA.
AC A0A1H4ILQ0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=SAMN04489727_0947 {ECO:0000313|EMBL:SEB34228.1};
OS Amycolatopsis tolypomycina.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=208445 {ECO:0000313|EMBL:SEB34228.1, ECO:0000313|Proteomes:UP000199622};
RN [1] {ECO:0000313|EMBL:SEB34228.1, ECO:0000313|Proteomes:UP000199622}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44544 {ECO:0000313|EMBL:SEB34228.1,
RC ECO:0000313|Proteomes:UP000199622};
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|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; FNSO01000002; SEB34228.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H4ILQ0; -.
DR STRING; 208445.SAMN04489727_0947; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000199622; 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:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd04485; DnaE_OBF; 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; 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};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01902}.
FT DOMAIN 62..129
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT REGION 17..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1101 AA; 120983 MW; 1390D50ABF6D0D0B CRC64;
MGWNNPPVRW TDLARTLAGG VPPGDHGDSP AWGRHREGYR RPGDLPTRRN DDGAETVRVP
YAELHCHSNF SFLDGASHPE ELVEEAARLQ LDAIALTDHD GMYGVVRFAE AARELGVDTV
FGTELSFGLQ GPQNGVPDPE GEHLLLLARG DQGYRALCRA ITAGQIHHQA EKGRPIYDLG
AVAEEVAGQC VVLTGCRKGA VRSALVTHGP AAAAEKLEEL IDRFGRDNVY VELTDHRQPL
DSTHNDLLTQ LAGELNLPTV ATTAAHYARP ERAPLADALA AIRARRGIDE LEGWLPAAGT
AFLRSGAEMD VLFRRYPGAV RRSALLGMEC AFPLKLIAPE LPPFDVPDGY TETTYLRHLT
EEGAKERFKG KAHQEKANEQ IEHELAIIEE LGFPGYFLIV WDIVRFCNDN DILCQGRGSA
ANSAVCYALG ITKVDSVAYE LLFERFLAPD RDGYPDIDLD IESDRREEAI QYVFRKHGRL
RTAQVANVIT YRARSAVRDA ARALGYSPGQ QDAWSKQIDR WGSLQSTEKD HDHDIPDDVV
QLAFALEDFP RHLGIHSGGM VMCAEPVSQV VPVEWARMEN RSVIQWEKED CAAAGLVKFD
LLGLGMLSAL HYMIDLVAGY KGEKVDLAEL DLADEKIYDM LCRADAIGVF QVESRAQLAT
LPRLQPREFY DLAVEVALIR PGPIQGGSVH PYIRRKQGRE KWTYDHPLLK KALHKTKGVP
LFQEQMMQIA LDVANFTAAE ADQLRHAMGS KRSDRKMERL REGFLAGAAA NGVDDELAQK
IFLKLKAFAN FGFPESHALS FAHLVFSSAY FKFYHPDAFL AGLLRAQPMG FYSPQSLVAD
ARRHDVTVHG PDINRSLPHA TLEAGTGKFH DVRTGLSTVR KIGEDLAKRI VAEREANGEY
RDLADVARRV RLTTPQLEAL ATAGAFAGFG GDRRQALWIA GAVAGERPEK LPGLVGAPAP
VLPGMDGLDV AAADVWATGV SPDSYPTQFI RDRLDELGVV PASGLAELDD GARVLVGGAV
THRQRPATAA GVTFLNIEDE TGMVNVICTL GLWQRYHRVA RGSPALLIRG VLEKADGVVS
VLAHRVEPLP MRIKAKSRDF R
//
