ID A0A1G8FM73_9NOCA Unreviewed; 1081 AA.
AC A0A1G8FM73;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=SAMN05444695_103328 {ECO:0000313|EMBL:SDH83197.1};
OS Rhodococcus triatomae.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=300028 {ECO:0000313|EMBL:SDH83197.1, ECO:0000313|Proteomes:UP000183263};
RN [1] {ECO:0000313|EMBL:SDH83197.1, ECO:0000313|Proteomes:UP000183263}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44892 {ECO:0000313|EMBL:SDH83197.1,
RC ECO:0000313|Proteomes:UP000183263};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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 ---------------------------------------------------------------------------
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; FNDN01000003; SDH83197.1; -; Genomic_DNA.
DR RefSeq; WP_072736600.1; NZ_FNDN01000003.1.
DR AlphaFoldDB; A0A1G8FM73; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000183263; 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}; Reference proteome {ECO:0000313|Proteomes:UP000183263};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01902}.
FT DOMAIN 59..126
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1081 AA; 117690 MW; D44F40626F2B6D0A CRC64;
MGWGNGPPTW AEMERVLSGR PGREPDSPGD GGDSPAWSRR RGEYRVGAAR RRTGAVPYAE
LHAHSAFSFL DGAASPEELV EEAAQLGLEA LALTDHDGFY GVVRFAEAAR EWGMPTVFGS
ELTLDDGHLL VLARGQEGYR RLSRQIAAAH LAGGAKGVLH YNLDELTEAA GGHWQILTGC
RKGHVRHALA ESGPDAAAVR LRELVDRFGA DRVTVELTRH GIPTDDERNA ALAALARSHG
LSTIASTAAH FARPEQRRLA MAMAAVGGRQ SLDDAVGRLP PTGGTHLRSG EEMAQLFARY
PEAVREAARL GLECAFDLDL IAPELPPFDV PDGYSEAGWL RELALTGAHR RYGTPAENSA
AYRQIEHELD VIETMDFPGY FLVVHDIVQF CKANDILCQG RGSAANSAVC FAIGITNVDP
VRNELLFERF LSPARDGPPD IDLDIESDRR EEAIQHVYTK YGRDYAAQVA NVITYRGKSA
VRDMARALGF SQGQQDAWSR QIGRWSGVDK ETGTDIPPAV LELAAQIEGY PRHLGIHSGG
MVICDRPIAD VCPVEWARME NRSVLQWDKD DCAAAGLVKF DLLGLGMLSA LHYMIDLAAQ
HKGIEVDLAQ LDLSETAVYE MLQRGDSVGV FQVESRAQMA TLPRLKPRRF YDLVVEVALI
RPGPIQGGSV HPYIRRRNKL EPVVYDHPCL EPSLQRTYGV PLFQEQLMQM AVDAAGFTPA
EADQLRRAMG SKRSTEKMER LRDRLYRGMR ELHGIEGEVA DRIYEKLYAF ANFGFPESHS
QSFASLVFYS SWFKLHHPAI FCAGLLRAQP MGFYTPQSLV ADARRHGVTV RGADVNASLA
HATVESEGTV VRLGLGEVRH IGEPLARRIV EARDRGGPFT SFLDLTGRVE LSVPQAESLA
TAGALGGVGL GRREALWAAG AAAGERSDRL PGLGASTRAP TLPGMSDVEL AAADVWATGV
SPDSYPTEFL RPQLDALGVI PAARLLDVPD GDRVLVGGAV THRQRPATAA GVTFVNLEDE
TGMVNVVCSV GVWAKYRKLA NTAAALLVRG KVQNAEGAVT VVADRLQLMD LRIRSKSRDF
R
//
