ID A0A1H1RFW7_9MICO Unreviewed; 1151 AA.
AC A0A1H1RFW7;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=SAMN04489721_1161 {ECO:0000313|EMBL:SDS34644.1};
OS Agromyces flavus.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Agromyces.
OX NCBI_TaxID=589382 {ECO:0000313|EMBL:SDS34644.1, ECO:0000313|Proteomes:UP000199482};
RN [1] {ECO:0000313|Proteomes:UP000199482}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CPCC 202695 {ECO:0000313|Proteomes:UP000199482};
RA Varghese N., Submissions S.;
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; LT629755; SDS34644.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H1RFW7; -.
DR STRING; 589382.SAMN04489721_1161; -.
DR Proteomes; UP000199482; Chromosome i.
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 InterPro; IPR010994; RuvA_2-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.
DR SUPFAM; SSF47781; RuvA domain 2-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 63..131
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT REGION 16..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 884..913
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1151 AA; 127055 MW; 0A251BC470DABBD3 CRC64;
MGWNNPEIPW SELERRLSDR QRPGGSKVLA DGGDSPGWSR KRHPYRPSHD ADERPAGPVV
PYAELHAHST FSFLDGASGP ERLVEEAHRL GLAGIAITDH DGFYGVVRFA EAAESYPELD
TVFGAELSFG LTEPQMGAAD PEGEHLLVLA AGEEGYHRLA AAITAGQLAG GEKGRPVYDL
EQLAERADGH WVIPTGCRKG AVRRALAGEG GADAAWRELD RLVALFGRDH VVVELTDHGD
PLDQVRNDAL AELAARARVP VLATNAVHYA TPGEHRLASA LAAVRARRSL DELDGWLPAT
DGLHLRSGAE MLARFDRYPG AVAHSVTLAR DLSFRLRSAR PKLPRQQVPD GHTPMSWLRE
LVWAGADRRY PGLPDHVRDR LAKELDVIEQ KDFPGYFLIV HDLVQEARRR GILCQGRGSA
ANSAVCYVLD ITGVDSIFYE LPFERFLSSL RDEEPDIDVD FDSDRREEII QYVYGKYGRH
NAAQVANVIS YRPKGAVRDM AKALGYSTGR QDAWSRQVER WGAVVETQDH DIPDAVVELA
EQLLTFPRHL GIHSGGMVLT DRPVGEVCPI EHARMEDRTV LQWDKDDCAW MGLVKFDLLG
LGMLAALQYT FDLVREHTGE HWELATIPKE EPAVYDMLCR ADSIGVFQVE SRAQMGTLPR
LKPRCFYDLV VEIALIRPGP VQGGAVHPYI RRRTGEEQVS YLHPKLEPVL RRTLGVPLFQ
EQLMQMAVAV GDCDAADADL LRRAMGSKRG VEKIERLRAK LYDGMARNGI EPDVADSIYE
KIEAFANFGF AESHAISFGL LVYASSWLKL HYPAAFLAAL LRAQPMGFYS PHTLTADARR
HGVELLRPDL ARSGVNAGLE PIGAAGSDEP ATDAAAEASG IRRPTGMPEC ARVTQPPVGE
FDRDAPDRSG EHRRDGAFAV RLGLADVTSI GEKVAERIVA EREQHGPYRD MADLSRRADL
DAAQLEALAA AGAFECFDLQ PRQALWLAGE AAQDRADYLP GAVVVVQPPL LPILNDAEQV
VYDLWATGIS PDDHPIRHVR ERLDARGVVR IDLLREAESG RRIEVGGVVT HRQRPATASG
ITFMNLEDES GTLNVIASVG VWTRYRRIAR EAPAMVVRGI LERSREGVVN LVADRFEPLT
VSTTNRSRDF R
//
