ID A0A2A2A397_9CORY Unreviewed; 1045 AA.
AC A0A2A2A397;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=CKJ84_05055 {ECO:0000313|EMBL:PAT15621.1};
OS Corynebacterium sp. NML 120412.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=2029401 {ECO:0000313|EMBL:PAT15621.1, ECO:0000313|Proteomes:UP000218861};
RN [1] {ECO:0000313|EMBL:PAT15621.1, ECO:0000313|Proteomes:UP000218861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NML 120412 {ECO:0000313|EMBL:PAT15621.1,
RC ECO:0000313|Proteomes:UP000218861};
RA Bernier A.-M., Burdz T., Bernard K.;
RT "Whole genome sequences of 6 clinical strains closest to Corynebacterium
RT imitans.";
RL Submitted (AUG-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:PAT15621.1}.
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DR EMBL; NSGL01000001; PAT15621.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2A397; -.
DR Proteomes; UP000218861; 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; cd07431; PHP_PolIIIA; 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 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.
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 50..117
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1045 AA; 114034 MW; 4475A02929A5EDCA CRC64;
MRFNGGAPLS WSKLERILSG AETAAPVPVQ HTAPAQSPQR VSSTSRVPFA ELHAVSAYNF
LSGASEPEEM VARASALGVE TLALLDRDGF YGAVKFAEAA AAAGVGTVFG AELTLDGRVL
PVIARGPEGY KRLSHLMAEA HMATREKDKV AYPPLELIGE ELGGTCVVLA GWQWTEEKGA
IDRLVDAFGP GNLVREYEVS MTPQDAEHHE LLDRHDTLPA IVTAAPGAAT REHARLAQAK
RALARRDSLA QANGYLHPMG ANWLRSGEQL ARMLPGCEDA LAYTVELAKQ CAFTLNLVAP
ELPRFDTPDG RSEMEHLRAL TLASAKLRYA SWSEEVRAKA LAQIRYELDV IQELNFPGYF
LIVHDFVEFC RRENILCQGR GSAANSAVCF ALGITNAEPI SAGLLFERFL SPDREGPPDI
DIDIESGRRE EVIQYVYAKY GRDNAAQVAN VITYRRKGAV RDAARALGYA QGAADGWAKG
VEEVPGSVDK LAAQFEGQPR HLGIHSGGMV ICDRPIADVV PVEWARMEGR SVVQWDKDDC
ASAGLVKFDM LGLGMLEALH HMIDLVRDTT GREVHLWELS LDDAHVYDML CRADAVGVFQ
VESRAQLGTL PRLKPRVFFD LVVEVALIRP GPIQGGSVHP YLRRRDGLEP VVYDHPVLEK
SLGKTLGIPL FQEQLMQIAV DAAGFSGREA DALRRAMGSK RSPAKMAALK ARFFRGCWET
NQIGEEVAEK LWTKIVAFAA YGFPESHSQS FASLVYFSAW FKRYYPAQFC VGLLRAQPMG
FYSPQSLIQD ARRHGVTVLP VSVNESGREA RCLDNETIRV GLNLVRGLGD AAADRVEAAQ
PFSGIPDLSR RAELKVEQVE ALARAGALDC FDVDRRQALW QAGVAATERE GMLPGLSAID
APALPGMNAF ELLAADVAAT GVTPDAQPME VLRDQLQAAG ILRAVDLKRV EDGTRVRIAG
VVTHRQRPHT AQGLTFLGME DETGLLNVMV SPGLWGRQRV LARTSRALIV RGIVQNATGA
VSVVADKFEP LEVGEWLSRG SRDFR
//