ID A0A255DKE9_9MYCO Unreviewed; 1098 AA.
AC A0A255DKE9;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=CG716_10260 {ECO:0000313|EMBL:OYN79846.1};
OS Mycolicibacterium sphagni.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=1786 {ECO:0000313|EMBL:OYN79846.1, ECO:0000313|Proteomes:UP000216063};
RN [1] {ECO:0000313|EMBL:OYN79846.1, ECO:0000313|Proteomes:UP000216063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33027 {ECO:0000313|EMBL:OYN79846.1,
RC ECO:0000313|Proteomes:UP000216063};
RA Tortoli E., Trovato A., Cirillo D.M.;
RT "The new phylogeny of genus Mycobacterium.";
RL Submitted (JUL-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}.
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:OYN79846.1}.
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DR EMBL; NOZR01000007; OYN79846.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A255DKE9; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000216063; 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 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 63..130
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1098 AA; 119091 MW; D59105D302B294AD CRC64;
MSWFNGPPSW SEMERVLNGK PRRPGLSLGE SHTDGGDSPA WSRHREPYEP PGERPVRSAV
PYAELHAHSA YSFLDGASTP EELVEEAARL DLRAIALTDH DGLYGVVRFA EAAKELDMRT
VFGAELSLSN TARTELPDPP GPHLLVLARG PEGYRRLSRQ LSAAHLAGGE KGKPRYDYNS
LTEAAGGHWH ILTGCRKGHV RQALSEGGPQ AAAAALADLV DRFGRDRVSI ELSCHGDPLD
DERNAALAAL APRFGVGVVA TTAAHFAEPS RGRLAMAMGA IRARQSLDEA AGWLAPLGGS
HLRSGDEMAR LFARYPEAVS AAADLGEQCA FGLALIAPQL PPYPDVPSGE TEDSWLRELV
MVGAARRYGP RAGAPEAYAQ IERELDIIAA LKFPGYFLVV HDITRFCREN DILCQGRGSA
ANSAVCYALG VTAVDPIANE LLFERFLSPA RDGPPDIDID IESDLREKAI QYVYDRYGRD
YAAQVANVIT YRGKSAVRDM ARALGFSQGQ QDAWSKQISH WHSGADSPDV EGIPGPVVEL
ATQIKNLPRH MGIHSGGMVI CDRPIADVCP VEWARMENRS VLQWDKDDCA AIGLVKFDML
GLGMLSALHY VIDLVAEHKG IEVDLARLDL AEPAVYEMLQ KADSVGVFQV ESRAQMATLP
RLKPRVFYDL VVEVALIRPG PIQGGSVHPY IKRRNGLEPV TYDHPSMEPA LRKTLGVPLF
QEQLMQLAVD CAGFSAAEAD QLRRAMGSKR STEKMRRLRD RFYAGMAQRH GITGEIAERI
YEKLEAFANF GFPESHSLSF ASLVYYSSWF KLHHPAAFCA ALLRAQPMGF YSPQSLVADA
RRHGVVVHGP DVNASLAHPT LENSGLDVRL GLGAVRHIGG ELAQRIVDAR DAGGPYTSLM
DLTGRVQLSV PQTEALATAG ALGCFSVTRR EGLWAAGAAA TQRPDRLPGV GSSSQVPSLP
GMTEVELAAA DVWATGVSPD SYPTQFLRED LDTMGVLPAD RLLDVPDGSR VLIAGAVTHR
QRPATAQGVT FMNIEDETGM VNVLCTPGVW ARHRKLAQTA SALLIRGQVQ NATGAVTVVA
ERMGRITLKV GSRSRDFR
//
