ID A0A1E4IVV0_9BURK Unreviewed; 1117 AA.
AC A0A1E4IVV0;
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|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=ABS94_23400 {ECO:0000313|EMBL:ODU14242.1};
OS Variovorax sp. SCN 67-85.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1660152 {ECO:0000313|EMBL:ODU14242.1, ECO:0000313|Proteomes:UP000094461};
RN [1] {ECO:0000313|EMBL:ODU14242.1, ECO:0000313|Proteomes:UP000094461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26031303; DOI=10.1111/1462-2920.12936;
RA Kantor R.S., van Zyl A.W., van Hille R.P., Thomas B.C., Harrison S.T.,
RA Banfield J.F.;
RT "Bioreactor microbial ecosystems for thiocyanate and cyanide degradation
RT unravelled with genome-resolved metagenomics.";
RL Environ. Microbiol. 17:4929-4941(2015).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ODU14242.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MEFM01000028; ODU14242.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E4IVV0; -.
DR Proteomes; UP000094461; 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 36..124
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1117 AA; 125798 MW; 05143218C29DD352 CRC64;
MPELSGKQES RRQPAKVHAL PVPLRRPPAL TLPDYAELHC LTNFSFQRGA STPEEMVERA
YQLGYKALAI TDECSVAGIV RAHVCLRGME HKLDEYEREH PDEPKIPRNP TFRLLFGSEF
QFERFRLVVI ANDTEGWGNL CEFITAARNT ELPKGEYRVG WEESDVASLQ HCQILFVPNR
NPGGAMDKAT LHEDLLAARA LYGENLWLAV ELFNELDDDL WLVTLMEVGE QAGVPLVAAG
DVHMHARSCK PLHDVLTAVR EGKTVAECGF ALQSNAQRHL RPRMRLAEIH LRRMLENTLA
VAGRCNFDPE VIRENYKYPL ETLGSDETPA QTLVRKTWEG ARGRYPEGIP DKVRAQVQKE
LDIIIDLKYE MFFLTVENIV SFARSQKILC QGRGSSANSA VCFCLGITAI DPTKGHLLFE
RFLSRERHEP PDIDVDFEHQ RREEVIQYIY AKYGRHRAAI AAVVICYRSR SALRDVGKAI
GIDERLIDEF AKDHYWFDDT VLGEQLRQAQ ARVGVVEDEL KLVHWIEMTQ KLKGFPRHLS
QHVGGFVLTH TRLTRLVPVE KASMKDRSVI QWEKDDLEAM GMLKVDVLAL GMLSAIRRGL
EHMNRWRGST IEMHQIPNDD QKVFDMICDA DTIGVFQIES RAQMSMLPRL KPRTYEDLVI
EVAIVRPGPI QGGMVHPYLK QRERVRKGLP IHYEKEELRE ALERTLGIPI FQEQVMQIAM
IAAKFTADEA DQLRRAMAAW KRKGGLGKFH DKLVNGMTLN GYKASFAEAI FKQVMGFGDY
GFPESHAASF ALLVTVSSWL KNYEPACFLA ALLDSQPMGF YSPSQLVQDA RRHGVEVRPV
DVTRSDFDTT LEAREPDAPR PSGIDERYAD RLGNENQPAV RLGLNRIAGF SAGGVERLLK
ARAAAPFTST EDLALRAELE GKDMAALAAA DALMSLSGHR RQQVWDATAQ RRAPALLRGV
PINEQALLLP AASEGEEIVG DYASLRLTLR RHPLALLRPR LARMKLMSAA ELRSVPNGQT
ARACGIVKGR QRPQTANGTI FVTLEDETGN VNVIVWSHVI EAWREPLLKS HLLAVQGTWQ
RDDETGGKVQ HLVATGFKDL TPLMGRLAQS NTSRDFH
//
