ID A0A1B0ZRF0_9RHOB Unreviewed; 964 AA.
AC A0A1B0ZRF0;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
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 ECO:0000313|EMBL:ANP36720.1};
GN ORFNames=JL2886_01812 {ECO:0000313|EMBL:ANP36720.1};
OS Phaeobacter gallaeciensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Phaeobacter.
OX NCBI_TaxID=60890 {ECO:0000313|EMBL:ANP36720.1, ECO:0000313|Proteomes:UP000092565};
RN [1] {ECO:0000313|EMBL:ANP36720.1, ECO:0000313|Proteomes:UP000092565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JL2886 {ECO:0000313|EMBL:ANP36720.1,
RC ECO:0000313|Proteomes:UP000092565};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-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; CP015124; ANP36720.1; -; Genomic_DNA.
DR RefSeq; WP_065271653.1; NZ_JARCJU010000010.1.
DR AlphaFoldDB; A0A1B0ZRF0; -.
DR PATRIC; fig|60890.4.peg.1769; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000092565; 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; 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; IPR003141; Pol/His_phosphatase_N.
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 SMART; SM00481; POLIIIAc; 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:UP000092565};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01902}.
FT DOMAIN 3..93
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 964 AA; 107166 MW; C844BF0CFB1E6574 CRC64;
MSAEFAILSN FTFLTGASHP EEYVERAVAL GIEALAIADE NSVAGIVRAH SHCRDIARRV
AERQAWDRDN ALIGPPRPAD VPPAPSFPIY AVPRLIPAAR LVFANAPPLI ALPEDRMGWG
SLCRLISAGR LRAEKGACHL ELADLLEQGE RLHLLLLPPA EHLPGGAGGW APHMEALTRR
FAGRVHLMMA PAYDGRDGRR FARLEEQANA LNLPTIASAA PRMHHGARRR LADVLSAIRL
RCRVEDLGRA ALANGEQRLR APHEMQRIFR GHEGALTRAQ DLAARLTFSL DELRYDYPDE
GLEGETPSAR LRRLAEEGLI WRYPAGAPPK VRDMLEHELT LIARLKYEPY FLTVRDIVDF
ARSRGILCQG RGSAANSVVC YCLGVTSVSP ETGTMVFERF VSEARDEPPD IDVDFEHERR
EEVIQWIYDR YGRHRAGLCA TVIHYRGKRA IREVGRAMGL SEDTIAAMSS QLWGSFDRSG
GGDARLREIG LDPDAPRLRQ TLDLVGQIIG FPRHLSQHVG GFIITAGRLD ELVPIENATM
EGRTVICWDK DDIDALGILK VDVLSLGMLT CIRKAFDLMR QHHRLDYALA TLPPEDPAVY
DMLCRADSIG VFQVESRAQM NFLPRMRPRN FYDLVIEVAI IRPGPIQGDM VHPYIRRRNG
EEPVEFPSDA LGEVLGKTMG VPLFQEQAMQ IAMVGAGFTP EQADRLRRSL ATFNKHGNVS
EFRSLFLRGM ARNGYDAEFS ERCFSQIEGF GAYGFPESHA ASFALLVYAS AWIKCHHPGI
FACALLNSQP MGFYAPAQIV RDARAHGVEV RPICINASYW DNVMEPDGQG GLALRLGFRQ
IKGLSDEDVS WLTAARGNGY TEVQDVWRKA GLPPPVIERL AEADAFAVLG LSRREALWQA
KAITAKKPLP LFERELEGEA IDEPTAHLPQ MTLGEEVVED YVALRLSLRA HPVALLRHLL
TPEG
//
