ID   DNAE2_AGRVS             Reviewed;        1097 AA.
AC   B9JWL2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Error-prone DNA polymerase {ECO:0000255|HAMAP-Rule:MF_01902};
DE            EC=2.7.7.7 {ECO:0000255|HAMAP-Rule:MF_01902};
GN   Name=dnaE2 {ECO:0000255|HAMAP-Rule:MF_01902}; OrderedLocusNames=Avi_2294;
OS   Agrobacterium vitis (strain S4 / ATCC BAA-846) (Rhizobium vitis (strain
OS   S4)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium.
OX   NCBI_TaxID=311402;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S4 / ATCC BAA-846;
RX   PubMed=19251847; DOI=10.1128/jb.01779-08;
RA   Slater S.C., Goldman B.S., Goodner B., Setubal J.C., Farrand S.K.,
RA   Nester E.W., Burr T.J., Banta L., Dickerman A.W., Paulsen I., Otten L.,
RA   Suen G., Welch R., Almeida N.F., Arnold F., Burton O.T., Du Z., Ewing A.,
RA   Godsy E., Heisel S., Houmiel K.L., Jhaveri J., Lu J., Miller N.M.,
RA   Norton S., Chen Q., Phoolcharoen W., Ohlin V., Ondrusek D., Pride N.,
RA   Stricklin S.L., Sun J., Wheeler C., Wilson L., Zhu H., Wood D.W.;
RT   "Genome sequences of three Agrobacterium biovars help elucidate the
RT   evolution of multichromosome genomes in bacteria.";
RL   J. Bacteriol. 191:2501-2511(2009).
CC   -!- FUNCTION: DNA polymerase involved in damage-induced mutagenesis and
CC       translesion synthesis (TLS). It is not the major replicative DNA
CC       polymerase. {ECO:0000255|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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01902};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01902}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-C family. DnaE2
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01902}.
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DR   EMBL; CP000633; ACM36640.1; -; Genomic_DNA.
DR   RefSeq; WP_015916061.1; NC_011989.1.
DR   AlphaFoldDB; B9JWL2; -.
DR   SMR; B9JWL2; -.
DR   STRING; 311402.Avi_2294; -.
DR   EnsemblBacteria; ACM36640; ACM36640; Avi_2294.
DR   KEGG; avi:Avi_2294; -.
DR   eggNOG; COG0587; Bacteria.
DR   HOGENOM; CLU_001600_4_0_5; -.
DR   OMA; HVEAREQ; -.
DR   OrthoDB; 561611at2; -.
DR   Proteomes; UP000001596; Chromosome 1.
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:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
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; DNA_pol_error_prone.
DR   InterPro; IPR029460; DNAPol_HHH.
DR   InterPro; IPR004013; PHP_dom.
DR   InterPro; IPR003141; Pol/His_phosphatase_N.
DR   InterPro; IPR016195; Pol/histidinol_Pase-like.
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   Pfam; PF02811; PHP; 1.
DR   SMART; SM00481; POLIIIAc; 1.
DR   SUPFAM; SSF89550; SSF89550; 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; Reference proteome;
KW   Transferase.
FT   CHAIN           1..1097
FT                   /note="Error-prone DNA polymerase"
FT                   /id="PRO_1000188729"
FT   REGION          1037..1097
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1058..1082
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1097 AA;  123486 MW;  5E29BF10DDB54856 CRC64;
     MRYAELQVTT HFSFLRGASS AIELFETAKS LGIDAIGVVD RNSLAGIVRA LEASRATGVR
     LVVGCRLDLQ DGMSILVYPT DRTAYSRLAR LITLGKGRGG KDNCILMLDD IAQYGEGLLG
     ILVPDLADDT CAVQLRKMAE VFGDLAYLSL CLRRRPNDQL RLHELSNMAT RFKVKTVVTN
     DVLFHEPGRR QLQDIVTCIR NNTTIDTVGF ERERHADRYL KPPEEMERLF PRYRQALRRT
     MEIVDRCKFS LEELTYQYPE EAIVPRKTAQ ESLEHYVWQC VPDRYPQGLP PKTLQIIRHE
     LDLIHKMKYA PYFLTVFSIV RFARAKGILC QGRGSAANSA VCYILGVTSI DPETNNLLFE
     RFVSQERDEP PDIDVDFEHE RREEVIQWIY KTYGKEKAAL CATVNRYRAK GAIRDVGKAL
     GLPEDLIKAL SSGMWSWSQE TSDRNVRELN LNPDDRRLTL TLQLAQQLMG APRHLGQHPG
     GFVLTHDRLD DLVPIEPSTM EDRQIIEWDK DDVEALKFMK VDVLALGMLT CMSKVFALIR
     EHKGDDLDLA KIRQEDKATY EMICKADTLG TFQIESRAQM AMLPRLKPKT FYDLVVQVAI
     VRPGPIQGDM VHPYLRRREK KEDVDYPTPE LEAVLGKTLG VPLFQESAMR VAMVCAGFTG
     GEADQLRKSM ATFKFTGGVS RFKEKLVSGM VKNGYTPEFA EKTFSRLEGF GSYGFPESHA
     ASFALIAYAS NYVKCHFPDV FCAALLNSQP MGFYAPAQIV GDARAHGVEV RPVCVNRSRW
     DCTLERIGTT QQHAVRLGMR MVKGLVVADV ARIVAARMNG PFDSVDDMWR RSGVPAASLV
     ELAHADAFQP SLKLARRDVL WAIKALRDEP LPLFAAAAER EMKTIAEQNE PEVELRQMTK
     GHNVVEDYGH IGLTLRDHPI AFLRTDLAKR NIVTCEEAMT ARDGRWVITA GLVLVRQKPG
     SAKGVMFITI EDETGPANIV VWPKLFEKRR RIVLGSSMMA IHGRIQREGE VVHLIAQQLF
     DLTSDLSGLA DRDMEFKLPT GRGDEFAHGS PGGGDSRDRS PPKPRDIVVP LCRARHKGID
     PEPETMPSAF PKPRDFR