ID A0A1I1IWG2_9BURK Unreviewed; 1173 AA.
AC A0A1I1IWG2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=SAMN05216321_104187 {ECO:0000313|EMBL:SFC40679.1};
OS Cupriavidus sp. OV038.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=1855313 {ECO:0000313|EMBL:SFC40679.1, ECO:0000313|Proteomes:UP000199583};
RN [1] {ECO:0000313|EMBL:SFC40679.1, ECO:0000313|Proteomes:UP000199583}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OV038 {ECO:0000313|EMBL:SFC40679.1,
RC ECO:0000313|Proteomes:UP000199583};
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; FOKX01000004; SFC40679.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1IWG2; -.
DR Proteomes; UP000199583; 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; 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; IPR004365; NA-bd_OB_tRNA.
DR InterPro; IPR004013; PHP_dom.
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.
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 20..223
FT /note="PHP"
FT /evidence="ECO:0000259|Pfam:PF02811"
FT DOMAIN 405..660
FT /note="Bacterial DNA polymerase III alpha subunit NTPase"
FT /evidence="ECO:0000259|Pfam:PF07733"
FT DOMAIN 663..833
FT /note="DNA polymerase III alpha subunit finger"
FT /evidence="ECO:0000259|Pfam:PF17657"
FT DOMAIN 913..1002
FT /note="DNA polymerase helix-hairpin-helix motif"
FT /evidence="ECO:0000259|Pfam:PF14579"
FT DOMAIN 1083..1157
FT /note="OB"
FT /evidence="ECO:0000259|Pfam:PF01336"
FT REGION 107..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..125
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1173 AA; 130629 MW; 911556499709F277 CRC64;
MLSSLPGLSS LLPSLPDYAE LHCVSNFTFL TGASHPQELI ARAFQLGYSG LALTDECSVA
GTARAHHAIK VLREEMWEAV ARSARRLAAG QADGEFDDAE LVHAFTPDGM EGMDDVDDME
EGDPDALPLI GDHPDDHPDD HPGDHPDDDP DAAAHRHRVL EARAAAADAF NVILGSRFTL
TASPVQPPEP YAMPMPPPRL LLLAQNREGF GNLCEFITLG RTRAEKGSYL LYPSDLASPE
PDQAHLRGMP DCLAILLPDY CADPDVLRAQ ALWCRETFGT RVWIALELLQ GHAEALHRTR
LQAVSAETGV PLVAAGAVTM HVRSRKPLAD VLTAIRLGQP LPACGMALAP NAEAHLRMRQ
VVSRLYPREA LAQTLKIADQ CRFSLDTLRY EYPEELVPDG ETPISYLRKE VERGSRERFP
HGMEPEWEAQ LEGELELIEE KHYEPFFLTV HDIVRFARQR GILCQGRGSA ANSLVCYCLH
ITEVSPEQAN LLFGRFLSRE RDEPPDIDVD FEHQRREEVI QYIYEKYGRH RAALAASLIT
YRSRSALRDV GRALGIDPSV VEQVVKGQAW WDGGTAFLER ITRYGLDPDS PAVRQWASLT
EQLRGFPRHL SQHVGGFVIA RHKLSRLVPI ENAAMADRSV IQWDKDDLES LGLLKVDVLA
LGMLTAIRRA LAMIPNPEPE RAGLPCRMED LPETDDATYD MICKADTVGV FQIESRAQQS
MLPRLQPRKY YDLVVEVAIV RPGPIQGGMV HPYLKRREAL RRTGKLPTYF NDVIRRVLGR
TLGVPIFQEQ VMQLAIDAAG FTPGQADQLR RSMAAWRRRG DLKKHQDALV RALTTRGYPE
SFALAICKQI EGFGEYGFPE SHAASFAKLV YVSAWLKCHH PDAFLCGLLN SHPMGFYSPS
QLVQDARRHD VVTQPVDVTV SGWESALEAR RPGQRYRDVR LGLGRVRGMR EDAALRIEAA
RAERPFESVE DLARRAGLDK HDIDVLAAAD ALVSLAGHRR QARWLARGAA VQSVHRDLLH
EAPPAEAELL LPEPKIGEDV AADYASLGLS LKCHPLTLLR RRLTALKFLT AQQLSRLGNG
RRVRACGIVT VRQRPSTANG TIFTSIEDET GPINVIIWPD LVERQRKEVL GAKLLGVIGT
WQRQGEVRHL VAQELVDLSP LLGKLMAESR DFH
//