ID A0A1X7JKZ4_9BURK Unreviewed; 1218 AA.
AC A0A1X7JKZ4;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=SAMN06265784_102789 {ECO:0000313|EMBL:SMG28683.1};
OS Paraburkholderia susongensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=1515439 {ECO:0000313|EMBL:SMG28683.1, ECO:0000313|Proteomes:UP000193228};
RN [1] {ECO:0000313|Proteomes:UP000193228}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 29540 {ECO:0000313|Proteomes:UP000193228};
RA Varghese N., Submissions S.;
RL Submitted (APR-2017) 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; FXAT01000002; SMG28683.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X7JKZ4; -.
DR STRING; 1515439.SAMN06265784_102789; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000193228; 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 22..135
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT REGION 78..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1138..1191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..92
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1176..1191
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1218 AA; 135398 MW; CBF6F1C1457C80C6 CRC64;
MTTSAPSISS QQTLAAHLPT YAELHCLTNF SFLRGASHPH ELVEQAMSLG YSALAITDEC
SLAGVVRAYT ALKEIEEEQE RQGKEREEQA RKAAQAAASS QDASGASASS QEPTSDEALK
PVPHLIIGSE FNLTDADGKP FCTLVALAIN RNGYGNLAEL ITLARSRADK GSYRIGPQDF
TDALSHLEHL RGLPDCVLML VPQRTATLSH TLRCAHWLAS FAAQRAWIAL ELWQTGSDDL
QIDALRMISK ESGLPLVAAG GVLMHVRSRK PLQDTMTAIG RGTPLSACGH ALEANAERHM
RTRVRLGKLY PRDTLEETLR IAALCRFSLK ELQYEYPEEL VPAGESPSSY LRKLVMAGAM
ERWPGGMDLK RIQQIEKELG LIADLKYEKY FLTVHDIVSF ARSRNILCQG RGSAANSVVC
YCLHVTEIDP VSMNMLIERF ISRARNEPPD IDVDFEHQRR EEVIQYIYAK YGRHRAALTA
SLITYRSRSA LKDVGKALGL EASLIERISK SQQWWDGPDA VAAYLAEAGF DASSHITQNL
IRLTRELRNF PRHLSQHVGG FVIAKDRLSR LVPIENASMK DRSVIEWDKD DIDALKLLKV
DVLALGMLSA IRRALEFVAL RRGFPVFRMQ DIPREDRAVY EMCGHADTIG VFQIESRAQQ
SMLPRLKPNA YYDLVIEVAI VRPGPIQGGM VHPYLRRKQG LEPVDYAKDE LRPVLERTLG
VPIFQEQVMH LAMVAAKYTG EQADRLRRAM AAWRRSGNLA KYQKDLTNRM LARGYEQAFI
ERICKQIEGF GEYGFPESHA ASFALLVYLS AWLKRYEPAA FLAGLLNSQP LGFYSPSQLV
QDARRHGVQV LPPDVTLSDW ESTFERRNAE GLRIVADQTH LRRQYAVLSA QQLRYLSLPS
LKVSRTIRRA AQRLSARVFQ PSSTYGSRGP AVRIGMHLIK GLAQEAAERI MAARREAPFA
DVDDLARRAA LTRRELEALA AANALTRIAG HRREAWWAVT AQHTVPKLLR DAPIAEAPLA
LPRASEHREI VDDYASLGLT LNRHPLALLR ARLAQQRFRT AAELAACRHG TMARACGIVT
VRQRPGTANG TVFVSIEDET GSINVIVWPS LVEKQRKALL GSSLLAVYGV VQRDDGVTTG
GDRAGNVSPA VSATNVNRRA REDAGSRGGG TSRTSGRGET RRKPGRKQQG EVVHLVAHRL
EDYSAWLGEL ATTSRDFH
//
