ID   DNAE2_XANAC             Reviewed;        1083 AA.
AC   Q8PN74;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 2.
DT   25-MAY-2022, entry version 108.
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=XAC1199;
OS   Xanthomonas axonopodis pv. citri (strain 306).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=190486;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=306;
RX   PubMed=12024217; DOI=10.1038/417459a;
RA   da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA   Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA   Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA   Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA   Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA   Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA   Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA   Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA   Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA   Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA   Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA   Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA   Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA   Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT   specificities.";
RL   Nature 417:459-463(2002).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM36071.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE008923; AAM36071.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_040107586.1; NC_003919.1.
DR   AlphaFoldDB; Q8PN74; -.
DR   SMR; Q8PN74; -.
DR   STRING; 190486.XAC1199; -.
DR   EnsemblBacteria; AAM36071; AAM36071; XAC1199.
DR   KEGG; xac:XAC1199; -.
DR   eggNOG; COG0587; Bacteria.
DR   HOGENOM; CLU_001600_4_0_6; -.
DR   OMA; NSWPMGF; -.
DR   Proteomes; UP000000576; 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: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; Transferase.
FT   CHAIN           1..1083
FT                   /note="Error-prone DNA polymerase"
FT                   /id="PRO_0000103404"
SQ   SEQUENCE   1083 AA;  120563 MW;  BFC1F06ADB9281A3 CRC64;
     MSWDDAIDGV DRDTPGGRMP RAWNVAARLR AANDDIVHAQ QADGLPAYAE LHCLSDFSFL
     RGASSAEQLF ARAQQCGYSA LAITDECSLA GIVRGLEASR ATGVRLIVGS EFTLVDGTRF
     VLLVENAHGY PQLCGLITTA RRAASKGAYR LDRAEVQAQF RDVAPGVFAL WLPGAQPQAE
     QGAWLQQVFG ERAFLAVELH REQDDVARLH VLQALAQQLG MTALASGDVH MAQRRERIVQ
     DTLTAIRHTL PLAECGAHLF RNGERHLRTR RALGNIYPDA LLQATVELAQ RCTFDISKIS
     YTYPRELVPE GHTPTSYLRQ LTEAGIRRRW PGGITAKVRE DIEKELALIA LKKYEAFFLT
     VQDVVRFARE QNILCQGRGS SANSAVCYAL GITAVNPDET RLLMARFLSE KRDEPPDIDV
     DFEHERREEV LQYVYSKYGR ERAALAATVI CYRGKSAVRD VAKAFGLPPD QIALLANCYG
     WGNGETPMDQ RIEEAGFDLA NPLINKILAV TEHLRDHPRH LSQHVGGFVI SDEPLSLLVP
     VENAAMANRT IIQWDKDDLE TMKLLKVDCL ALGMLTCIRK TLDLVRGHRG RNYSIATLPG
     GDAPTYKMIQ RADTVGVFQI ESRAQMAMLP RLKPAAFYDL VIEVAIVRPG PIQGDMVHPY
     LRRRQGREEV NYPSPAVEDI LKPTLGVPLF QEQVMELLMH AADYSEDEAD NLRRSMAAWR
     RGGDMEQHRT RVRERMQGKG YASSFIDQIF EQIKGFGSYG FPQSHAASFA KLVYASCWLK
     RHEPAAFACG LLNAQPMGFY SASQIVQDAR RGSPERERVE VLPVDVLHSD WDNTLVGGRP
     WRSAADPGEQ PAIRLGMRQV AGLSQVVAQR IVAARTQRAF ADIGDLCLRA ALDEKARLAL
     AEAGALQGMV GNRNAARWAM AGVEARCPLL PGSPEERPVE FEAPRAGEEI LADYRSVGLS
     LRQHPMALLR PQMRQRRILG LRELQGRRHG SGVHVAGLVT QRQRPATAKG TIFVTLEDEQ
     GMINVIVWSH LALRRRRALL ESRLLAVRGR WERVDGVEHL IAGDLYDLSN LLGDMQLPSR
     DFH