ID A0A1I7KYL6_9BURK Unreviewed; 1100 AA.
AC A0A1I7KYL6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=SAMN05216350_11442 {ECO:0000313|EMBL:SFV02384.1};
OS Polaromonas sp. YR568.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas.
OX NCBI_TaxID=1855301 {ECO:0000313|EMBL:SFV02384.1, ECO:0000313|Proteomes:UP000217451};
RN [1] {ECO:0000313|EMBL:SFV02384.1, ECO:0000313|Proteomes:UP000217451}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YR568 {ECO:0000313|EMBL:SFV02384.1,
RC ECO:0000313|Proteomes:UP000217451};
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; FPBM01000014; SFV02384.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I7KYL6; -.
DR STRING; 1855301.SAMN05216350_11442; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000217451; 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 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 16..83
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1100 AA; 122686 MW; 3ACB302E08BD6E5C CRC64;
MLPDDLSETL RLPDYAELHA LSNFSFQRGA SHAQELVERA AELGYRAAAI TDECSVAGVV
RAHEAAKKTG FKLLPGAEFL VQAQNGHEAF RLVVLPHNAT GWGNLCEFIT TARQVGDTIE
KGSYRVALGE TDFSVLAHCE VLLSPLPGAI DSEALCAHAQ WAVTHFGGAA WLAVELLQGM
DDALRLAQLR EVGRRTGIAL VAAGNVLMHI RSRKPLHDVL TAIKLGCTVH ECGFELQANA
EAHMRHRMKL AEVYPRDLLG ATLEVAGRCR FNLDEIRNLY RYPQEDIVPA AETPAFCLRR
LAWQGAQKRY RRRIPHKIRR QVSKELALIE ELGYEMYFIT VRDIVRFARS ENILCQGRGS
AANSAVCYCL EVTAIDPSES DLLFERFISR ERREPPDIDV DFEHERREEV IQYIYEKYGH
DRAAIAATVI SYRSRSAVRD VGKALGIDTA TVELYAKEHF WFDGSEVMEE KIREAEVQAD
VGPVLQWLQL SRLLMAVYPE PKDEIAETGD RKKREKERPA FPRHLSQHVG GFVLTQGKLT
RLVPVQPASM EDRRIIQWDK DDLEAIGLMK VDVLALGMLS AIRRCLEMVN RIRRPNIPLE
MHTLPLEEEQ TYDMICEADT TGVFQIESRA QMSMLPRLRP RNYYDLVVEV AIVRPGPIQG
GMVHPYLKAR DVKRKEGKVP SEYPALDPAL ERTLGIPIFQ EQVMQIAIIA ADFTPGEADG
LRRSMAAWKR KGGVGHYHGR LVNAMVKNGY APEFAERIFS QIRGFGDYGF PESHAASFAK
LVYVSCWLKC HEPACFLAAL VNSQPMGFYA PAQLVQDARR HGVEVRAVDV MHSDWDCTLE
PAENTPLPQY PGIEENQPAV RLGLRLVAGL SEAAVTRLVQ ARADAPFTST EDLVSRAQLG
SQEVNALAAA DALLPLAGHR RQQVWEASAI KPAPLLLKSV PTHETPLALP DTPEGENILF
DYNATGLTLR RHPLALLRER LARRGLLTAS ELNALPDGQE VAGCGIVTVR QQPQTANGTI
FVTLEDETGP VNVIVWKSLR EEQRAELLHS RLLAVHGVWQ RSEESGTAKG YGAVRNLVAS
RLEDLTPLLG RLGTSSRDFH
//
