DNAE2_GLUOX
ID DNAE2_GLUOX Reviewed; 901 AA.
AC Q5HXU1;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Error-prone DNA polymerase;
DE EC=2.7.7.7;
GN Name=dnaE2; OrderedLocusNames=GOX2598;
OS Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans).
OG Plasmid pGOX1.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Gluconobacter.
OX NCBI_TaxID=290633;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=621H;
RX PubMed=15665824; DOI=10.1038/nbt1062;
RA Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F.,
RA Ehrenreich A., Gottschalk G., Deppenmeier U.;
RT "Complete genome sequence of the acetic acid bacterium Gluconobacter
RT oxydans.";
RL Nat. Biotechnol. 23:195-200(2005).
CC -!- FUNCTION: DNA polymerase involved in damage-induced mutagenesis and
CC translesion synthesis (TLS). It is not the major replicative DNA
CC polymerase (By similarity). {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-C family. DnaE2
CC subfamily. {ECO:0000305}.
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DR EMBL; CP000004; AAW59662.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5HXU1; -.
DR SMR; Q5HXU1; -.
DR STRING; 290633.GOX2598; -.
DR EnsemblBacteria; AAW59662; AAW59662; GOX2598.
DR KEGG; gox:GOX2598; -.
DR eggNOG; COG0587; Bacteria.
DR HOGENOM; CLU_001600_4_0_5; -.
DR OMA; VAKSHHW; -.
DR Proteomes; UP000006375; Plasmid pGOX1.
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-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR InterPro; IPR011708; DNA_pol3_alpha_NTPase_dom.
DR InterPro; IPR040982; DNA_pol3_finger.
DR InterPro; IPR023073; DNA_pol_error_prone.
DR InterPro; IPR029460; DNAPol_HHH.
DR InterPro; IPR004805; PolC_alpha.
DR PANTHER; PTHR32294; PTHR32294; 1.
DR PANTHER; PTHR32294:SF4; PTHR32294:SF4; 1.
DR Pfam; PF07733; DNA_pol3_alpha; 1.
DR Pfam; PF17657; DNA_pol3_finger; 1.
DR Pfam; PF14579; HHH_6; 1.
DR TIGRFAMs; TIGR00594; polc; 1.
PE 3: Inferred from homology;
KW Cytoplasm; DNA damage; DNA repair; DNA replication;
KW DNA-directed DNA polymerase; Nucleotidyltransferase; Plasmid;
KW Reference proteome; Transferase.
FT CHAIN 1..901
FT /note="Error-prone DNA polymerase"
FT /id="PRO_0000103380"
SQ SEQUENCE 901 AA; 100168 MW; 56F6240D81383D72 CRC64;
MAMYCEPRSE WWTRLPAPGG HRAWIACSSA LSRSAVLAGT PARLPVSTSA FLTHSFSVCA
EQPILLAIDT IAVQRDGCSP SCSRTRRTAR ERTSGENFFT GLLIRPSSQV NRSPLIPGRF
NPTETERTGE SAQETLTRLV QAALPRRYPA GAPPEVETQI AHELRLIGSL SYAPYFLTVN
TIVRHARSLG IVCQGRGSAA NSAVCYVLGI TSIDPVRSGL LFERFISTER QEPPDIDVDF
ESDRREEVIQ WIYRHYGRHR AALCATVQRY QPKGALREVG KVLGLPEDLT GQLSKHIASS
LADPDLCKAR AADLGLNLKD RRLSLTFHLA RLLLGFPRQL GTHPGGFVLT EDRLDELVPL
MPTAMDGRQI IVWDKDDIDV LRFMKVDVLG LGMLGCLRRG FELLHTVYQT RMDLAAIPAE
DPQTYRMVQK ADTLGTFQIE SRAQMSMLPR MKPATFYDLV IQVAIVRPGP IQGDMVHPYL
RRREKLEPVT YPSETLRGIL GKTLGVPLFQ EQAMQVAIHC AGFTPGEADQ LRRAMATFKM
TGGVSPFRDK LVNGMLANGY EQEFAEQTFA QLEGFGSYGF PESHAASFAL IAYASAWMKC
HYPDVFCAAL LNSQPMGFYA PSQIVQDAQR HGVEVRPICI NASRWDCTLE RGRNGRHAAV
RLGFRMVKGL ANGHGAALIA ARMPDYESID DVWRRADVPV AALKCLAEAD AFRVFGQMRR
AALWSIKGLA DTALPLFEAA DRGRNFPLPE VIEPEITLPM MSERASVHED YRATGLSLNG
HPVAFLREGL RKEGIVRCGD LPYLRDGRRI QLTGLVLMRQ RPGTANGTMF VTIEDETGTA
NLIVWKDVQE KYRRPLLASR LLACKGRLQK EGDVIHVVVL SLEDRTPLLQ GSEPLKARDF
R