ID A0A147GQB0_9BURK Unreviewed; 1119 AA.
AC A0A147GQB0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
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=NS331_18520 {ECO:0000313|EMBL:KTT16408.1};
OS Pseudacidovorax intermedius.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Pseudacidovorax.
OX NCBI_TaxID=433924 {ECO:0000313|EMBL:KTT16408.1, ECO:0000313|Proteomes:UP000072741};
RN [1] {ECO:0000313|EMBL:KTT16408.1, ECO:0000313|Proteomes:UP000072741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NS331 {ECO:0000313|EMBL:KTT16408.1,
RC ECO:0000313|Proteomes:UP000072741};
RX PubMed=26793183;
RA Midha S., Bansal K., Sharma S., Kumar N., Patil P.P., Chaudhry V.,
RA Patil P.B.;
RT "Genomic Resource of Rice Seed Associated Bacteria.";
RL Front. Microbiol. 6:1551-1551(2016).
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:KTT16408.1}.
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DR EMBL; LDSL01000126; KTT16408.1; -; Genomic_DNA.
DR RefSeq; WP_058643425.1; NZ_LDSL01000126.1.
DR AlphaFoldDB; A0A147GQB0; -.
DR PATRIC; fig|433924.3.peg.687; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000072741; 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; 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 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}; Reference proteome {ECO:0000313|Proteomes:UP000072741};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01902}.
FT DOMAIN 40..148
FT /note="PHP"
FT /evidence="ECO:0000259|Pfam:PF02811"
FT DOMAIN 335..592
FT /note="Bacterial DNA polymerase III alpha subunit NTPase"
FT /evidence="ECO:0000259|Pfam:PF07733"
FT DOMAIN 595..764
FT /note="DNA polymerase III alpha subunit finger"
FT /evidence="ECO:0000259|Pfam:PF17657"
FT DOMAIN 837..944
FT /note="DNA polymerase helix-hairpin-helix motif"
FT /evidence="ECO:0000259|Pfam:PF14579"
FT DOMAIN 1023..1087
FT /note="OB"
FT /evidence="ECO:0000259|Pfam:PF01336"
SQ SEQUENCE 1119 AA; 123982 MW; 698745FA82A830B1 CRC64;
MPELSLKDEE ARRQRRLAAV GAGLPASAPT AASPLPAYAE LHALSNFSFQ RGASHPWELA
VRAWQLGYAA IAITDECSVA GVVRAVSGLR MWREEREEDG LPLPPHPEPQ LIFGSEFDFG
RFRLVVLAHD LEGWGHLCQY ISAARMHEDI AKGDYRASLA DAAGLLHCDI LCVPRRRSGE
PIDEAALHAD LAAVAALFAP RADGEPGPLW LAVELFHEAD DALWLQVLQR AGEATGLPLV
AAGDVHMHLR SRKPLQDVLT AVRQGRPVAD CGFALQPNAE RHLRSRARLA GLYPADLLVR
TLLIAGRCHF DLQEIRKQYV YPQEVIGSGE TPAQTLIRKT WEGAQARYPE GVPDKVHAQI
QTELDLILDL DYEMFFLTVE DIVAFARREG ILCQGRGSSA NSAVCYCLGI TAVNPEDGNL
LFERFISRER AEPPDIDVDF EHDRREEVIQ YIYRTYGRER AAIAAVVISY RSRSALRDAG
KALGVDERLV DAFARDHYWF DDPMLDERLE AAMARAGVRE DPFRLRLWIG LANELRGFPR
HLSQHVGGFV LTQGPLTRLV PVEKASMEAR SIIQWDKDDL DEVGMFKVDV LALGMLSCIR
RALDMVNGWR GTAHQMHQLP TDDPRVYDMI GRADTVGVFQ IESRAQMSML PRLRPRNYYD
LVIEVAIVRP GPIQGGMVHP YLKNRAKVER GQKIELRYPQ LEPALQRTLG VPIFQEQVMQ
IAMIAAGFSA GQADRLRRAM AAWRRTGHME RFYGPLVKGM VDNGYDEDFA KAIFQQIQGF
GEYGFPESHA ASFAKLVTVS SWLKCYEPAC FLAAILNAQP MGFYTPSQLI QDAVRHGVQV
RPVDVHRSDR FCTLEPADAD GPAPAAPWAE SAAQALPGQP AVRLGLRHVK GLSPAAVARL
VEARAQAPFT STGDLARRAG LGTAEMALLA GADALRALAG HRRQQVWEAT ASHRAPALLR
GAPIHESPLA LPAAEEGEEI VGDYASLGFS LRRHPLALLR PRLARWRLSS AEELRAMPGG
MPVRACGIVT VRQRPGTAKG TVFVTLEDET GAVNVVVWAR VAEQWREPLL KSQLLAVRGT
WQRDRETGGK VCHLVAEGMR DLTPLLGRLA RENRSRDFH
//
