ID   DNAE2_CUTAK             Reviewed;        1134 AA.
AC   Q6A780;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   25-MAY-2022, entry version 117.
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=PPA1650;
OS   Cutibacterium acnes (strain DSM 16379 / KPA171202) (Propionibacterium
OS   acnes).
OC   Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae;
OC   Cutibacterium.
OX   NCBI_TaxID=267747;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16379 / KPA171202;
RX   PubMed=15286373; DOI=10.1126/science.1100330;
RA   Brueggemann H., Henne A., Hoster F., Liesegang H., Wiezer A.,
RA   Strittmatter A., Hujer S., Duerre P., Gottschalk G.;
RT   "The complete genome sequence of Propionibacterium acnes, a commensal of
RT   human skin.";
RL   Science 305:671-673(2004).
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; AE017283; AAT83385.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6A780; -.
DR   SMR; Q6A780; -.
DR   STRING; 267747.PPA1650; -.
DR   EnsemblBacteria; AAT83385; AAT83385; PPA1650.
DR   KEGG; pac:PPA1650; -.
DR   eggNOG; COG0587; Bacteria.
DR   HOGENOM; CLU_001600_4_0_11; -.
DR   OMA; NSWPMGF; -.
DR   Proteomes; UP000000603; 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..1134
FT                   /note="Error-prone DNA polymerase"
FT                   /id="PRO_0000103387"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        17..33
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1134 AA;  124661 MW;  8D2F6F71B5B6D5B3 CRC64;
     MSYHNPPIPW RELEGRISGR PAPHGHQESH ADQVGYRHVR KPFDRHPVRP EGPVVPYAEL
     HCHSSYSFLD GASNPEDLVI RAVELGLSGL ALTDHDGLYG VVRMAEAAEA CGLSTIIGSE
     LSIGVPEPQN GVADPVGSHL LVLANGPEGY RRLAEALTDA YLVEGGRKGR PVHDLDHLAE
     VADGHWTVLT GCRKGAVRQG LVKGMLQAEA ELRRLVDLFG IDNVLVELTD HRAPTDSRDN
     DLLAELASRH SLLTVATTAA HYAGAEQFEL ACALSAVRAR RSLDEMDGWL PPGPVARLRS
     GAEMADLFSR HRDAVDNTVA VAERTAFHLK SVRPRLPDQK VPDGHTPISW LRHLVEEGRR
     ACYGDDPVAK DRLATELDLI EDRGFAGYFL IVSDIVEFAQ SQGILCQGRG SAAASAVCYV
     LGITVVDPVF YGLPFERFLS VLREEEPDID VDFDARRREE VIQYVYAKYG RRNAAQVADV
     ITYRPRSAVR DMAKALGYSQ GQQDAWSRQM ERRSVPPLPH DPDGPEIPDD VTTLAQQVMG
     LPRHLGIHSA GMVLTREPVG RICPIEPARM FGRTVLQWDK EDCAWMGLVK FDLLGLGMLS
     ALSISFDLIS QHCGRFWTLA SIPRNEPGVY DMLCRGDSIG VFQVESRAQI GALPRLKPRC
     FYDLAVEIGL IRPGPVQGGA VHPYIRRRTG VEPVTYPHPL LEPVLERTLG IPLFQEQLMQ
     MATTVGNCTA ADADLLRRAM GSKRGVERID SLRTKLFEGM AANGIDDDTA QGIYARIESF
     ANFGFAESHA LSFAGLVYTS AWIKLHYPAV FLAALLRSQP MGFYSSATLV ADARRHGVVT
     RRPDVARSSV GADLELLDAC CEELGSEELE TGIDECLHDH DESEIGAFDP NRDDGDHRRD
     THFAVRLGLS DVSGINIETA TRIVEERERE SFASLDDLAR RVDLSGEEVE ALALAGAFDD
     LVGSRRGALW QIGQINGVAP GQLDVQVVTQ PPLLPEPTQM ELLGDDLRAT GISTADHPVR
     QVRDALNRRG VVQVDRLDGV ETRRRIEVAG VVTHRQRPGT AGGVTFLNLE DETGLLNVIV
     TPGAWRHYRR VARTSRALVV RGILERGDEG VMSLQADRLE ALDLSVPTKS RDFR