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Database: UniProt
Entry: B2IJZ6_BEII9
LinkDB: B2IJZ6_BEII9
Original site: B2IJZ6_BEII9 
ID   B2IJZ6_BEII9            Unreviewed;      1090 AA.
AC   B2IJZ6;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   27-MAR-2024, entry version 96.
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   OrderedLocusNames=Bind_2802 {ECO:0000313|EMBL:ACB96371.1};
OS   Beijerinckia indica subsp. indica (strain ATCC 9039 / DSM 1715 / NCIMB
OS   8712).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Beijerinckiaceae; Beijerinckia.
OX   NCBI_TaxID=395963 {ECO:0000313|EMBL:ACB96371.1, ECO:0000313|Proteomes:UP000001695};
RN   [1] {ECO:0000313|Proteomes:UP000001695}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9039 / DSM 1715 / NCIMB 8712
RC   {ECO:0000313|Proteomes:UP000001695};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., LaButti K., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Mikhailova N., Dunfield P.F., Dedysh S.N.,
RA   Liesack W., Saw J.H., Alam M., Chen Y., Murrell J.C., Richardson P.;
RT   "Complete sequence of chromosome of Beijerinckia indica subsp. indica ATCC
RT   9039.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACB96371.1, ECO:0000313|Proteomes:UP000001695}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9039 / DSM 1715 / NCIMB 8712
RC   {ECO:0000313|Proteomes:UP000001695};
RX   PubMed=20601475; DOI=10.1128/JB.00656-10;
RA   Tamas I., Dedysh S.N., Liesack W., Stott M.B., Alam M., Murrell J.C.,
RA   Dunfield P.F.;
RT   "Complete genome sequence of Beijerinckia indica subsp. indica.";
RL   J. Bacteriol. 192:4532-4533(2010).
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; CP001016; ACB96371.1; -; Genomic_DNA.
DR   RefSeq; WP_012385722.1; NC_010581.1.
DR   AlphaFoldDB; B2IJZ6; -.
DR   STRING; 395963.Bind_2802; -.
DR   KEGG; bid:Bind_2802; -.
DR   eggNOG; COG0587; Bacteria.
DR   HOGENOM; CLU_001600_4_0_5; -.
DR   OrthoDB; 9803237at2; -.
DR   Proteomes; UP000001695; Chromosome.
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}; Reference proteome {ECO:0000313|Proteomes:UP000001695};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01902}.
FT   DOMAIN          8..75
FT                   /note="Polymerase/histidinol phosphatase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00481"
FT   REGION          1039..1072
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1058..1072
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1090 AA;  121954 MW;  15091B444EA48649 CRC64;
     MNRSARYAEL QVTSHFSFLR GASSCEELFA QAALLGIEAL AVVDRHSLAG IVRAHQAAKA
     TGIRLIIGCR LDLADGMSVL VYPTDRASYA RLCRLLSLGK QRGGKAQCHL DWLDLVAHGE
     GLLTILIAEK ADEICGLHLR RLHDTFKDRA YLALTLHRRP NDQLRLHQLA VLAARFRVPT
     VVTNDILFHE PARRILQDVV TCIRHGCTID EAGFRRERHA DRYLKPPEEM HRLFSLYPEA
     LARTLEITDR CQFSLEELTY QYPEEKTMPG LTAQEALTRL TLKGAADHYP EGVPDKVQAL
     LDHELELIAK LNYAPYFLTV NAIVHFAKTE GILCQGRGSA ANSAVCYVLG ITSIAPDQHD
     LLFERFVSEE RREPPDIDVD FEHERREIVI QWIYKTYGRD RAALCATVIR YRAKGALRDV
     GKALGLPEDL LTMLSSQTWV WSKQGLDVKS AKELNLNLDD PRLRLTLDLA RELIGTPRHL
     SQHPGGFVLT HDRLDELVPI EPAAMTDRQV IEWDKDDIEV LKFMKVDVLA LGMLSCMKRS
     FNLLAEHKKL ALALTSIPSE DPHTYAMIQR ADTIGVFQIE SRAQMSMLPR LKPKTFYDLV
     IEVAIVRPGP IQGDMVHPYL RRREGKEDPD LPRAELKNVL EKTLGVPLFQ EQAMRIAIEC
     AGFTPGEADQ LRRSMATFKH TGTINTFKDK LVNGMVANGY EHAFAERIFH QLEGFGSYGF
     PESHAASFAL LAYASSWIKC WHPDVFCAAL LNSQPMGFYA PAQIVRDARN HGVEIRPVCV
     NHSHWDCTLE ATGDEKRFAL RLGMRMVKRL SNQDAATIVA AKADQPFLSI EDLWHRAGVP
     VSALVALAEA DAFAPTFGIA RRKALWTIKA LRDNPLPLFA AASAREAAFV SEIREPAVTL
     TPMAAGGEVV EDYVSVGLTL REHPIAFLRG DLARRRIATC AEVIHARDRC WIETAGLVLV
     RQRPGSAKGV IFITIEDETG IANLVIWPKL YEKHRRIIHG ARMIAARGPI QREGDVVHLV
     VRHLTDLSGD LASVIHREDT APPSAGSAGI GSHKSLVRHP ADSSKTRQPH GLLALDERPH
     QIRVKTRDFH
//
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